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  • Cell Line  (131)
  • Chemistry
  • American Association for the Advancement of Science (AAAS)  (133)
  • 2000-2004  (133)
  • 2003  (54)
  • 2002  (79)
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  • American Association for the Advancement of Science (AAAS)  (133)
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  • 2000-2004  (133)
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  • 1
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    Patent law. Natural substances and patentable inventions (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Demaine, Linda J -- Fellmeth, Aaron X -- New York, N.Y. -- Science. 2003 May 30;300(5624):1375-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉RAND, Santa Monica, CA 90401, USA. demaine@rand.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12775825" target="_blank"〉PubMed〈/a〉
    Keywords: Aluminum Oxide ; Chemical Phenomena ; Chemistry ; Natural Science Disciplines ; Patents as Topic/*legislation & jurisprudence ; Plant Extracts ; Plant Roots ; Titanium ; United States
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-26
    Description: The active-site cysteine of peroxiredoxins is selectively oxidized to cysteine sulfinic acid during catalysis, which leads to inactivation of peroxidase activity. This oxidation was thought to be irreversible. However, by metabolic labeling of mammalian cells with 35S, we show that the sulfinic form of peroxiredoxin I, produced during the exposure of cells to H2O2, is rapidly reduced to the catalytically active thiol form. The mammalian cells' ability to reduce protein sulfinic acid might serve as a mechanism to repair oxidatively damaged proteins or represent a new type of cyclic modification by which the function of various proteins is regulated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Woo, Hyun Ae -- Chae, Ho Zoon -- Hwang, Sung Chul -- Yang, Kap-Seok -- Kang, Sang Won -- Kim, Kanghwa -- Rhee, Sue Goo -- New York, N.Y. -- Science. 2003 Apr 25;300(5619):653-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Cell Signaling Research and Division of Molecular Life Sciences, Ewha Womans University, Seoul 120-750, Korea.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12714748" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Catalysis ; Cell Line ; Cycloheximide/pharmacology ; Cysteine/*analogs & derivatives/*metabolism ; Dimerization ; HeLa Cells ; Humans ; Hydrogen Peroxide/*metabolism ; Methionine/metabolism ; Mice ; Neurotransmitter Agents ; Oxidation-Reduction ; Peroxidases/chemistry/*metabolism ; Peroxiredoxins ; Protein Synthesis Inhibitors/pharmacology ; Spectrometry, Mass, Electrospray Ionization ; Sulfhydryl Compounds/metabolism ; Sulfinic Acids/metabolism ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Insulin staining of ES cell progeny from insulin uptake (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-01-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rajagopal, Jayaraj -- Anderson, William J -- Kume, Shoen -- Martinez, Olga I -- Melton, Douglas A -- New York, N.Y. -- Science. 2003 Jan 17;299(5605):363.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Howard Hughes Medical Institute, Harvard University, 7 Divinity Avenue, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12532008" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/immunology ; Apoptosis ; Cell Differentiation ; Cell Line ; Embryo, Mammalian/*cytology ; Humans ; Insulin/*analysis/genetics/immunology/*metabolism ; Islets of Langerhans/*cytology/metabolism ; Mice ; Microscopy, Confocal ; RNA, Messenger/genetics/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Stem Cells/*cytology/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Single molecule profiling of alternative pre-mRNA splicing (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-09
    Description: Alternative pre-messenger RNA splicing is an important mechanism for generating protein diversity and may explain in part how mammalian complexity arises from a surprisingly small complement of genes. Here, we describe "digital polony exon profiling,"a single molecule-based technology for studying complex alternative pre-messenger RNA splicing. This technology allows researchers to monitor the combinatorial diversity of exon inclusion in individual transcripts. A minisequencing strategy provides single nucleotide resolution, and the digital nature of the technology allows quantitation of individual splicing variants. Digital polony exon profiling can be used to investigate the physiological and pathological roles of alternately spliced messenger RNAs, as well as the mechanisms by which these messenger RNAs are produced.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhu, Jun -- Shendure, Jay -- Mitra, Robi D -- Church, George M -- 5U54GM62119/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Aug 8;301(5634):836-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12907803" target="_blank"〉PubMed〈/a〉
    Keywords: Acrylamide ; *Alternative Splicing ; Animals ; Antigens, CD44/genetics ; Brain/metabolism ; Cell Line ; Cell Line, Transformed ; Cyclic AMP Response Element-Binding Protein ; *Exons ; Humans ; Mice ; Microtubule-Associated Proteins/genetics ; Nerve Tissue Proteins/genetics ; Polymerase Chain Reaction/*methods ; Polymorphism, Single Nucleotide ; Protein Isoforms ; RNA Precursors/*genetics/metabolism ; RNA-Binding Proteins ; SMN Complex Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-01
    Description: The mechanisms that determine how folding attempts are interrupted to target folding-incompetent proteins for endoplasmic reticulum-associated degradation (ERAD) are poorly defined. Here the alpha-mannosidase I-like protein EDEM was shown to extract misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. EDEM overexpression resulted in faster release of folding-incompetent proteins from the calnexin cycle and earlier onset of degradation, whereas EDEM down-regulation prolonged folding attempts and delayed ERAD. Up-regulation of EDEM during ER stress may promote cell recovery by clearing the calnexin cycle and by accelerating ERAD of terminally misfolded polypeptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Molinari, Maurizio -- Calanca, Verena -- Galli, Carmela -- Lucca, Paola -- Paganetti, Paolo -- New York, N.Y. -- Science. 2003 Feb 28;299(5611):1397-400.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Research in Biomedicine, CH-6500 Bellinzona, Switzerland. Maurizio.molinari@irb.unisi.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12610306" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid Endopeptidases/chemistry/*metabolism ; Calnexin/*metabolism ; Cell Line ; Down-Regulation ; Electrophoresis, Polyacrylamide Gel ; Endoplasmic Reticulum/*metabolism ; Glycoproteins/chemistry/*metabolism ; Glycosylation ; Humans ; Kinetics ; Membrane Proteins/*metabolism ; Molecular Weight ; Polysaccharides/metabolism ; Protein Conformation ; Protein Folding ; RNA Interference ; Transfection ; Up-Regulation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    A B cell-based sensor for rapid identification of pathogens (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-12
    Description: We report the use of genetically engineered cells in a pathogen identification sensor. This sensor uses B lymphocytes that have been engineered to emit light within seconds of exposure to specific bacteria and viruses. We demonstrated rapid screening of relevant samples and identification of a variety of pathogens at very low levels. Because of its speed, sensitivity, and specificity, this pathogen identification technology could prove useful for medical diagnostics, biowarfare defense, food- and water-quality monitoring, and other applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rider, Todd H -- Petrovick, Martha S -- Nargi, Frances E -- Harper, James D -- Schwoebel, Eric D -- Mathews, Richard H -- Blanchard, David J -- Bortolin, Laura T -- Young, Albert M -- Chen, Jianzhu -- Hollis, Mark A -- New York, N.Y. -- Science. 2003 Jul 11;301(5630):213-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Massachusetts Institute of Technology Lincoln Laboratory, Lexington, MA 02420, USA. thor@ll.mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12855808" target="_blank"〉PubMed〈/a〉
    Keywords: Aequorin/biosynthesis ; Antibodies, Bacterial/immunology ; Antibodies, Viral/immunology ; *B-Lymphocytes/immunology ; Bacillus anthracis/immunology/isolation & purification ; Bacteria/immunology/*isolation & purification ; *Bacteriological Techniques ; *Biosensing Techniques ; Cell Line ; Colony Count, Microbial ; Encephalitis Virus, Venezuelan Equine/immunology/isolation & purification ; Escherichia coli O157/immunology/isolation & purification ; Foot-and-Mouth Disease Virus/immunology/isolation & purification ; Immunoglobulin Variable Region/immunology ; Light ; Receptors, Antigen, B-Cell/immunology ; Sensitivity and Specificity ; Time Factors ; Transfection ; Viruses/immunology/*isolation & purification ; Yersinia pestis/immunology/isolation & purification
    Print ISSN: 0036-8075
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  • 7
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    TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-07
    Description: Insulin resistance is a major hallmark in the development of type II diabetes, which is characterized by the failure of insulin to promote glucose uptake in muscle and to suppress glucose production in liver. The serine-threonine kinase Akt (PKB) is a principal target of insulin signaling that inhibits hepatic glucose output when glucose is available from food. Here we show that TRB3, a mammalian homolog of Drosophila tribbles, functions as a negative modulator of Akt. TRB3 expression is induced in liver under fasting conditions, and TRB3 disrupts insulin signaling by binding directly to Akt and blocking activation of the kinase. Amounts of TRB3 RNA and protein were increased in livers of db/db diabetic mice compared with those in wild-type mice. Hepatic overexpression of TRB3 in amounts comparable to those in db/db mice promoted hyperglycemia and glucose intolerance. Our results suggest that, by interfering with Akt activation, TRB3 contributes to insulin resistance in individuals with susceptibility to type II diabetes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Du, Keyong -- Herzig, Stephan -- Kulkarni, Rohit N -- Montminy, Marc -- New York, N.Y. -- Science. 2003 Jun 6;300(5625):1574-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Peptide Biology Laboratories, Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037-1002, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12791994" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/genetics/physiology ; Amino Acid Substitution ; Animals ; Blood Glucose/metabolism ; Cell Cycle Proteins/genetics/*metabolism ; Cell Line ; Diabetes Mellitus/genetics/metabolism ; Enzyme Activation ; Fasting ; Genetic Vectors ; Glucose/metabolism ; Glucose Intolerance ; Glycogen Synthase Kinase 3/metabolism ; Humans ; Insulin/blood/*metabolism ; Insulin Resistance ; Insulin-Like Growth Factor I/pharmacology ; Liver/*metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Phosphorylation ; Polymerase Chain Reaction ; Protein-Serine-Threonine Kinases/metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-akt ; RNA Interference ; Rats ; Repressor Proteins ; Signal Transduction ; Transfection ; Transgenes ; Tumor Cells, Cultured ; Two-Hybrid System Techniques
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Control of nutrient-sensitive transcription programs by the unconventional prefoldin URI (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-11-15
    Description: Prefoldins (PFDs) are members of a recently identified, small-molecular weight protein family able to assemble into molecular chaperone complexes. Here we describe an unusually large member of this family, termed URI, that forms complexes with other small-molecular weight PFDs and with RPB5, a shared subunit of all three RNA polymerases. Functional analysis of the yeast and human orthologs of URI revealed that both are targets of nutrient signaling and participate in gene expression controlled by the TOR kinase. Thus, URI is a component of a signaling pathway that coordinates nutrient availability with gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gstaiger, Matthias -- Luke, Brian -- Hess, Daniel -- Oakeley, Edward J -- Wirbelauer, Christiane -- Blondel, Marc -- Vigneron, Marc -- Peter, Matthias -- Krek, Wilhelm -- New York, N.Y. -- Science. 2003 Nov 14;302(5648):1208-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich Miescher Institut, Maulbeerstrasse 66, CH-4058 Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14615539" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/*metabolism ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Line ; DNA-Binding Proteins/metabolism ; DNA-Directed RNA Polymerases/metabolism ; GATA Transcription Factors ; *Gene Expression Regulation/drug effects ; Humans ; *Intracellular Signaling Peptides and Proteins ; Molecular Sequence Data ; Phosphorylation ; Protein Kinases/metabolism ; Protein Subunits/metabolism ; RNA Interference ; Repressor Proteins/metabolism ; Saccharomyces cerevisiae/*genetics/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; *Signal Transduction ; Sirolimus/pharmacology ; TOR Serine-Threonine Kinases ; Trans-Activators/metabolism ; Transcription Factors/metabolism ; *Transcription, Genetic/drug effects ; Transfection
    Print ISSN: 0036-8075
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  • 9
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    A conserved domain in axonal targeting of Kv1 (Shaker) voltage-gated potassium channels (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-02
    Description: Axonal voltage-gated potassium (Kv1) channels regulate action-potential invasion and hence transmitter release. Although evolutionarily conserved, what mediates their axonal targeting is not known. We found that Kv1 axonal targeting required its T1 tetramerization domain. When fused to unpolarized CD4 or dendritic transferrin receptor, T1 promoted their axonal surface expression. Moreover, T1 mutations eliminating Kvbeta association compromised axonal targeting, but not surface expression, of CD4-T1 fusion proteins. Thus, proper association of Kvbeta with the Kv1 T1 domain is essential for axonal targeting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, Chen -- Jan, Yuh Nung -- Jan, Lily Yeh -- New York, N.Y. -- Science. 2003 Aug 1;301(5633):646-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Departments of Physiology and Biochemistry, University of California, San Francisco, CA 94143-0725, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12893943" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Substitution ; Animals ; Antigens, CD4/metabolism ; Axons/*metabolism ; Biopolymers ; COS Cells ; Cell Line ; Cell Membrane/metabolism ; Cell Polarity ; Cells, Cultured ; Dendrites/metabolism ; Endocytosis ; Hippocampus/cytology ; Humans ; Kv1.2 Potassium Channel ; Models, Molecular ; Mutagenesis ; Neurons/metabolism ; Potassium Channels/*chemistry/*metabolism ; *Potassium Channels, Voltage-Gated ; *Protein Structure, Tertiary ; Receptors, Transferrin/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Shaker Superfamily of Potassium Channels ; Shal Potassium Channels ; Transfection
    Print ISSN: 0036-8075
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  • 10
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    Cell therapy of alpha-sarcoglycan null dystrophic mice through intra-arterial delivery of mesoangioblasts (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-12
    Description: Preclinical or clinical trials for muscular dystrophies have met with modest success, mainly because of inefficient delivery of viral vectors or donor cells to dystrophic muscles. We report here that intra-arterial delivery of wild-type mesoangioblasts, a class of vessel-associated stem cells, corrects morphologically and functionally the dystrophic phenotype of virtually all downstream muscles in adult immunocompetent alpha-sarcoglycan (alpha-SG) null mice, a model organism for limb-girdle muscular dystrophy. When mesoangioblasts isolated from juvenile dystrophic mice and transduced with a lentiviral vector expressing alpha-SG were injected into the femoral artery of dystrophic mice, they reconstituted skeletal muscle in a manner similar to that seen in wild-type cells. The success of this protocol was mainly due to widespread distribution of donor stem cells through the capillary network, a distinct advantage of this strategy over previous approaches.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sampaolesi, Maurilio -- Torrente, Yvan -- Innocenzi, Anna -- Tonlorenzi, Rossana -- D'Antona, Giuseppe -- Pellegrino, M Antonietta -- Barresi, Rita -- Bresolin, Nereo -- De Angelis, M Gabriella Cusella -- Campbell, Kevin P -- Bottinelli, Roberto -- Cossu, Giulio -- 1322/Telethon/Italy -- 463/BI/Telethon/Italy -- New York, N.Y. -- Science. 2003 Jul 25;301(5632):487-92. Epub 2003 Jul 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stem Cell Research Institute, H. S. Raffaele, Via Olgettina 58, 20132 Milan, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12855815" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Vessels/cytology/embryology ; Cell Differentiation ; Cell Line ; Cell Movement ; Cytoskeletal Proteins/*genetics/*metabolism ; Dystrophin/metabolism ; Endothelium, Vascular/physiology ; Female ; Femoral Artery ; Genetic Vectors ; Lentivirus/genetics ; Locomotion ; Male ; Membrane Glycoproteins/*genetics/*metabolism ; Mesoderm/cytology ; Mice ; Mice, Knockout ; Mice, Transgenic ; Muscle Contraction ; Muscle Fibers, Skeletal/cytology/physiology ; Muscle, Skeletal/cytology/metabolism/pathology/*physiology ; Muscular Dystrophy, Animal/metabolism/pathology/*therapy ; Regeneration ; Sarcoglycans ; *Stem Cell Transplantation ; Stem Cells/*physiology ; Transfection
    Print ISSN: 0036-8075
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  • 11
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    Dishevelled 2 recruits beta-arrestin 2 to mediate Wnt5A-stimulated endocytosis of Frizzled 4 (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-06
    Description: Wnt proteins, regulators of development in many organisms, bind to seven transmembrane-spanning (7TMS) receptors called frizzleds, thereby recruiting the cytoplasmic molecule dishevelled (Dvl) to the plasma membrane.Frizzled-mediated endocytosis of Wg (a Drosophila Wnt protein) and lysosomal degradation may regulate the formation of morphogen gradients. Endocytosis of Frizzled 4 (Fz4) in human embryonic kidney 293 cells was dependent on added Wnt5A protein and was accomplished by the multifunctional adaptor protein beta-arrestin 2 (betaarr2), which was recruited to Fz4 by binding to phosphorylated Dvl2. These findings provide a previously unrecognized mechanism for receptor recruitment of beta-arrestin and demonstrate that Dvl plays an important role in the endocytosis of frizzled, as well as in promoting signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Wei -- ten Berge, Derk -- Brown, Jeff -- Ahn, Seungkirl -- Hu, Liaoyuan A -- Miller, William E -- Caron, Marc G -- Barak, Larry S -- Nusse, Roel -- Lefkowitz, Robert J -- HL 16037/HL/NHLBI NIH HHS/ -- HL 61365/HL/NHLBI NIH HHS/ -- NS 19576/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2003 Sep 5;301(5638):1391-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Departments of Medicine and Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12958364" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Animals ; Arrestins/genetics/*metabolism ; Cell Line ; Cell Membrane/metabolism ; Clathrin/metabolism ; Cytoplasm/metabolism ; *Endocytosis ; Frizzled Receptors ; Humans ; Mice ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Kinase C/antagonists & inhibitors/metabolism ; Proteins/genetics/*metabolism ; Proto-Oncogene Proteins/*metabolism/pharmacology ; RNA, Small Interfering ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Wnt Proteins
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  • 12
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    The BRCT domain is a phospho-protein binding domain (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-10-25
    Description: The carboxyl-terminal domain (BRCT) of the Breast Cancer Gene 1 (BRCA1) protein is an evolutionarily conserved module that exists in a large number of proteins from prokaryotes to eukaryotes. Although most BRCT domain-containing proteins participate in DNA-damage checkpoint or DNA-repair pathways, or both, the function of the BRCT domain is not fully understood. We show that the BRCA1 BRCT domain directly interacts with phosphorylated BRCA1-Associated Carboxyl-terminal Helicase (BACH1). This specific interaction between BRCA1 and phosphorylated BACH1 is cell cycle regulated and is required for DNA damage-induced checkpoint control during the transition from G2 to M phase of the cell cycle. Further, we show that two other BRCT domains interact with their respective physiological partners in a phosphorylation-dependent manner. Thirteen additional BRCT domains also preferentially bind phospho-peptides rather than nonphosphorylated control peptides. These data imply that the BRCT domain is a phospho-protein binding domain involved in cell cycle control.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, Xiaochun -- Chini, Claudia Christiano Silva -- He, Miao -- Mer, Georges -- Chen, Junjie -- CA89239/CA/NCI NIH HHS/ -- CA92312/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2003 Oct 24;302(5645):639-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oncology, Mayo Clinic and Foundation, Rochester, MN 55905, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14576433" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; BRCA1 Protein/*chemistry/*metabolism ; Carrier Proteins/chemistry/metabolism ; Cell Cycle ; *Cell Cycle Proteins ; Cell Line ; DNA Damage ; DNA Repair ; *DNA-Binding Proteins ; E2F Transcription Factors ; G2 Phase ; Humans ; Mitosis ; Mutation ; Nuclear Proteins ; Peptide Library ; Phosphoprotein Phosphatases/chemistry/metabolism ; Phosphoproteins/chemistry/genetics/*metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Protein Binding ; Protein Structure, Tertiary ; RNA Helicases/chemistry/genetics/*metabolism ; RNA Polymerase II/metabolism ; RNA, Small Interfering ; Recombinant Fusion Proteins/chemistry/metabolism ; Transcription Factors/metabolism ; Transfection ; Tumor Cells, Cultured
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  • 13
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    VDAC2 inhibits BAK activation and mitochondrial apoptosis (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-26
    Description: The multidomain proapoptotic molecules BAK or BAX are required to initiate the mitochondrial pathway of apoptosis. How cells maintain the potentially lethal proapoptotic effector BAK in a monomeric inactive conformation at mitochondria is unknown. In viable cells, we found BAK complexed with mitochondrial outer-membrane protein VDAC2, a VDAC isoform present in low abundance that interacts specifically with the inactive conformer of BAK. Cells deficient in VDAC2, but not cells lacking the more abundant VDAC1, exhibited enhanced BAK oligomerization and were more susceptible to apoptotic death. Conversely, overexpression of VDAC2 selectively prevented BAK activation and inhibited the mitochondrial apoptotic pathway. Death signals activate "BH3-only" molecules such as tBID, BIM, or BAD, which displace VDAC2 from BAK, enabling homo-oligomerization of BAK and apoptosis. Thus, VDAC2, an isoform restricted to mammals, regulates the activity of BAK and provides a connection between mitochondrial physiology and the core apoptotic pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheng, Emily H Y -- Sheiko, Tatiana V -- Fisher, Jill K -- Craigen, William J -- Korsmeyer, Stanley J -- NS42319/NS/NINDS NIH HHS/ -- R37CA50239/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2003 Jul 25;301(5632):513-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12881569" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; BH3 Interacting Domain Death Agonist Protein ; Biopolymers ; Carrier Proteins/metabolism/pharmacology ; Cell Line ; Cells, Cultured ; Etoposide/pharmacology ; Humans ; Intracellular Membranes/metabolism ; Jurkat Cells ; Membrane Proteins/chemistry/genetics/*metabolism ; Mice ; Mice, Inbred C57BL ; Mitochondria/*metabolism ; Mitochondria, Liver/metabolism ; Porins/genetics/isolation & purification/*metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Proto-Oncogene Proteins/metabolism ; *Proto-Oncogene Proteins c-bcl-2 ; Recombinant Proteins/pharmacology ; Staurosporine/pharmacology ; Voltage-Dependent Anion Channel 1 ; Voltage-Dependent Anion Channel 2 ; Voltage-Dependent Anion Channels ; bcl-2 Homologous Antagonist-Killer Protein ; bcl-2-Associated X Protein
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 14
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    LRP: role in vascular wall integrity and protection from atherosclerosis (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-12
    Description: Vascular smooth muscle cell (SMC) proliferation and migration are important events in the development of atherosclerosis. The low-density lipoprotein receptor-related protein (LRP1) mediates suppression of SMC migration induced by platelet-derived growth factor (PDGF). Here we show that LRP1 forms a complex with the PDGF receptor (PDGFR). Inactivation of LRP1 in vascular SMCs of mice causes PDGFR overexpression and abnormal activation of PDGFR signaling, resulting in disruption of the elastic layer, SMC proliferation, aneurysm formation, and marked susceptibility to cholesterol-induced atherosclerosis. The development of these abnormalities was reduced by treatment with Gleevec, an inhibitor of PDGF signaling. Thus, LRP1 has a pivotal role in protecting vascular wall integrity and preventing atherosclerosis by controlling PDGFR activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boucher, Philippe -- Gotthardt, Michael -- Li, Wei-Ping -- Anderson, Richard G W -- Herz, Joachim -- GM 52016/GM/NIGMS NIH HHS/ -- HL20948/HL/NHLBI NIH HHS/ -- HL63762/HL/NHLBI NIH HHS/ -- NS43408/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2003 Apr 11;300(5617):329-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9046, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12690199" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta/cytology/metabolism/*pathology ; Arteriosclerosis/*pathology/physiopathology/*prevention & control ; Benzamides ; Cattle ; Cell Division ; Cell Line ; Cholesterol, Dietary/administration & dosage ; Diet, Atherogenic ; Elastin/analysis ; Enzyme Inhibitors/pharmacology ; Imatinib Mesylate ; Ligands ; Low Density Lipoprotein Receptor-Related ; Protein-1/genetics/metabolism/*physiology ; Mesenteric Arteries/cytology/pathology ; Mice ; Mice, Knockout ; Mice, Transgenic ; Muscle, Smooth, Vascular/cytology/*metabolism/pathology ; Myocytes, Smooth Muscle/*metabolism/physiology ; Phosphorylation ; Piperazines/pharmacology ; Platelet-Derived Growth Factor/metabolism/pharmacology ; Proto-Oncogene Proteins c-sis ; Pyrimidines/pharmacology ; Receptor, Platelet-Derived Growth Factor beta/metabolism ; Signal Transduction
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 15
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    Glycosylation restores survival of chilled blood platelets (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-13
    Description: Cooling of blood platelets clusters the von Willebrand factor receptor complex. Macrophage alphaMbeta2 integrins bind to the GPIbalpha subunit of the clustered complex, resulting in rapid clearance of transfused, cooled platelets. This precludes refrigeration of platelets for transfusion, but the current practice of room temperature storage has major drawbacks. We document that alphaMbeta2 is a lectin that recognizes exposed beta-N-acetylglucosamine residues of N-linked glycans on GPIbalpha. Enzymatic galactosylation of chilled platelets blocks alphaMbeta2 recognition, prolonging the circulation of functional cooled platelets. Platelet-associated galactosyltransferase produces efficient galactosylation when uridine diphosphate-galactose is added, affording a potentially simple method for storing platelets in the cold.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffmeister, Karin M -- Josefsson, Emma C -- Isaac, Natasha A -- Clausen, Henrik -- Hartwig, John H -- Stossel, Thomas P -- HL19429/HL/NHLBI NIH HHS/ -- HL56949/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2003 Sep 12;301(5639):1531-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Hematology, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA. khoffmeister@rics.bwh.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12970565" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylglucosamine/metabolism/pharmacology ; Animals ; Blood Platelets/metabolism/*physiology ; Blood Preservation ; Carbohydrate Conformation ; Cell Line ; Cell Survival ; *Cold Temperature ; Female ; Galactose/*metabolism ; Galactosyltransferases/metabolism ; Glycosylation ; Humans ; Lectins/metabolism ; Ligands ; Macrophage-1 Antigen/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Monosaccharides/pharmacology ; Phagocytosis/drug effects ; Platelet Aggregation ; Platelet Glycoprotein GPIb-IX Complex/metabolism ; *Platelet Membrane Glycoproteins ; Platelet Transfusion ; Refrigeration ; Uridine Diphosphate Galactose/metabolism ; von Willebrand Factor/metabolism
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  • 16
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    Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-10-18
    Description: Human immunodeficiency virus-1 (HIV-1) Vif is essential for viral evasion of host antiviral factor CEM15/APOBEC3G. We report that Vif interacts with cellular proteins Cul5, elongins B and C, and Rbx1 to form an Skp1-cullin-F-box (SCF)-like complex. The ability of Vif to suppress antiviral activity of APOBEC3G was specifically dependent on Cul5-SCF function, allowing Vif to interact with APOBEC3G and induce its ubiquitination and degradation. A Vif mutant that interacted with APOBEC3G but not with Cul5-SCF was functionally inactive. The Cul5-SCF was also required for Vif function in distantly related simian immunodeficiency virus mac. These results indicate that the conserved Cul5-SCF pathway used by Vif is a potential target for antiviral development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, Xianghui -- Yu, Yunkai -- Liu, Bindong -- Luo, Kun -- Kong, Wei -- Mao, Panyong -- Yu, Xiao-Fang -- 1S10-RR14702/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2003 Nov 7;302(5647):1056-60. Epub 2003 Oct 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology and Immunology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14564014" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier Proteins/genetics/metabolism ; Cell Line ; Cullin Proteins/genetics/*metabolism ; Cytidine Deaminase ; Gene Products, vif/genetics/*metabolism ; HIV-1/genetics/*physiology ; Humans ; Mutation ; Nucleoside Deaminases ; Proteins/*metabolism ; Repressor Proteins ; Transcription Factors/genetics/metabolism ; Transfection ; Ubiquitin/*metabolism ; Virus Replication ; vif Gene Products, Human Immunodeficiency Virus
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  • 17
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    Embryonic stem cells. Stem cell programs (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-10
    Description: The availability of human embryonic stem cell lines provides an important tool for scientists to explore the fundamental mechanisms that regulate differentiation into specific cell types. When more is known about the mechanisms that govern these processes, human embryonic stem cells may be clinically useful in generating cell types that have been damaged or depleted by a variety of human diseases. The NIH is actively pursuing a variety of initiatives to promote this developing research field, while continuing and expanding its long-standing investment in adult stem cells and research.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zerhouni, Elias -- New York, N.Y. -- Science. 2003 May 9;300(5621):911-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12738840" target="_blank"〉PubMed〈/a〉
    Keywords: Advisory Committees ; Cell Culture Techniques ; Cell Line ; Education ; *Embryo Research ; Embryo, Mammalian/*cytology ; Expressed Sequence Tags ; Financing, Government ; Humans ; Internet ; *National Institutes of Health (U.S.) ; Patents as Topic ; Research Support as Topic ; *Stem Cells/cytology/physiology ; United States
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  • 18
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    Disruption of the epithelial apical-junctional complex by Helicobacter pylori CagA (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-31
    Description: Helicobacter pylori translocates the protein CagA into gastric epithelial cells and has been linked to peptic ulcer disease and gastric carcinoma. We show that injected CagA associates with the epithelial tight-junction scaffolding protein ZO-1 and the transmembrane protein junctional adhesion molecule, causing an ectopic assembly of tight-junction components at sites of bacterial attachment, and altering the composition and function of the apical-junctional complex. Long-term CagA delivery to polarized epithelia caused a disruption of the epithelial barrier function and dysplastic alterations in epithelial cell morphology. CagA appears to target H. pylori to host cell intercellular junctions and to disrupt junction-mediated functions.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3369828/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3369828/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amieva, Manuel R -- Vogelmann, Roger -- Covacci, Antonello -- Tompkins, Lucy S -- Nelson, W James -- Falkow, Stanley -- AI38459/AI/NIAID NIH HHS/ -- CA92229/CA/NCI NIH HHS/ -- DDC DK56339/DC/NIDCD NIH HHS/ -- R01 GM035527/GM/NIGMS NIH HHS/ -- R01GM35227/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 May 30;300(5624):1430-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA. amieva@stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12775840" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Bacterial/genetics/*metabolism ; Bacterial Adhesion ; Bacterial Proteins/genetics/*metabolism ; Cell Adhesion Molecules/metabolism ; Cell Line ; Cell Polarity ; Cell Size ; Dogs ; Epithelial Cells/cytology/metabolism/*microbiology/ultrastructure ; Gastric Mucosa ; Helicobacter pylori/*pathogenicity/physiology ; Humans ; Intracellular Signaling Peptides and Proteins ; Junctional Adhesion Molecules ; Membrane Proteins/metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatases/metabolism ; Tight Junctions/*microbiology/physiology/*ultrastructure ; Tumor Cells, Cultured ; Zonula Occludens-1 Protein
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  • 19
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    Talin binding to integrin beta tails: a final common step in integrin activation (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-10-04
    Description: Control of integrin affinity for ligands (integrin activation) is essential for normal cell adhesion, migration, and assembly of an extracellular matrix. Integrin activation is usually mediated through the integrin beta subunit cytoplasmic tail and can be regulated by many different biochemical signaling pathways. We report that specific binding of the cytoskeletal protein talin to integrin beta subunit cytoplasmic tails leads to the conformational rearrangements of integrin extracellular domains that increase their affinity. Thus, regulated binding of talin to integrin beta tails is a final common element of cellular signaling cascades that control integrin activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tadokoro, Seiji -- Shattil, Sanford J -- Eto, Koji -- Tai, Vera -- Liddington, Robert C -- de Pereda, Jose M -- Ginsberg, Mark H -- Calderwood, David A -- New York, N.Y. -- Science. 2003 Oct 3;302(5642):103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, The Scripps Research Institute, The Burnham Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14526080" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Antibodies, Monoclonal/immunology ; Antigens, CD29/chemistry/metabolism ; Cell Line ; Fibronectins/metabolism ; Humans ; Integrin beta Chains/chemistry/*metabolism ; Integrin beta3/chemistry/metabolism ; Molecular Sequence Data ; Mutation ; Platelet Glycoprotein GPIIb-IIIa Complex/chemistry/immunology/metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; RNA, Small Interfering ; Recombinant Proteins/metabolism ; *Signal Transduction ; Talin/*metabolism ; Transfection
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  • 20
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    Dilated cardiomyopathy and heart failure caused by a mutation in phospholamban (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-01
    Description: Molecular etiologies of heart failure, an emerging cardiovascular epidemic affecting 4.7 million Americans and costing 17.8 billion health-care dollars annually, remain poorly understood. Here we report that an inherited human dilated cardiomyopathy with refractory congestive heart failure is caused by a dominant Arg --〉 Cys missense mutation at residue 9 (R9C) in phospholamban (PLN), a transmembrane phosphoprotein that inhibits the cardiac sarcoplasmic reticular Ca2+-adenosine triphosphatase (SERCA2a) pump. Transgenic PLN(R9C) mice recapitulated human heart failure with premature death. Cellular and biochemical studies revealed that, unlike wild-type PLN, PLN(R9C) did not directly inhibit SERCA2a. Rather, PLN(R9C) trapped protein kinase A (PKA), which blocked PKA-mediated phosphorylation of wild-type PLN and in turn delayed decay of calcium transients in myocytes. These results indicate that myocellular calcium dysregulation can initiate human heart failure-a finding that may lead to therapeutic opportunities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schmitt, Joachim P -- Kamisago, Mitsuhiro -- Asahi, Michio -- Li, Guo Hua -- Ahmad, Ferhaan -- Mende, Ulrike -- Kranias, Evangelia G -- MacLennan, David H -- Seidman, J G -- Seidman, Christine E -- New York, N.Y. -- Science. 2003 Feb 28;299(5611):1410-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School and Howard Hughes Medical Institute, 200 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12610310" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Calcium/metabolism ; Calcium Signaling ; Calcium-Binding Proteins/chemistry/*genetics/*physiology ; Calcium-Transporting ATPases/antagonists & inhibitors/metabolism ; Cardiomegaly ; Cardiomyopathy, Dilated/*genetics/pathology/physiopathology ; Cell Line ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Female ; Heart Failure/*genetics/pathology/physiopathology ; Heart Ventricles/metabolism/pathology ; Humans ; Lod Score ; Male ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Muscle Cells/metabolism/physiology ; *Mutation, Missense ; Myocardial Contraction ; Myocardium/pathology ; Pedigree ; Phosphorylation ; Sarcoplasmic Reticulum Calcium-Transporting ATPases
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  • 21
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    Listeria intracellular growth and virulence require host-derived lipoic acid (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-10-18
    Description: Listeria monocytogenes is a Gram-positive intracytosolic pathogen that causes severe disease in pregnant and immunocompromised individuals. We found that L. monocytogenes lacking the lipoate protein ligase LplA1 was defective for growth specifically in the host cytosol and was less virulent in animals by a factor of 300. A major target for LplA1, the E2 subunit of pyruvate dehydrogenase (PDH), lacked a critical lipoyl modification when the DeltalplA1 strain was grown intracellularly, which suggests that abortive growth was due to loss of PDH function. Thus, the use of host-derived lipoic acid may be a critical process for in vivo replication of bacterial pathogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Riordan, Mary -- Moors, Marlena A -- Portnoy, Daniel A -- AI29619/AI/NIAID NIH HHS/ -- R01 AI027655/AI/NIAID NIH HHS/ -- R01 AI27655/AI/NIAID NIH HHS/ -- R37 AI029619/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2003 Oct 17;302(5644):462-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, School of Public Health, University of California, Berkeley, CA 94720-3202, USA. oriordan@umich.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14564012" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Culture Media ; Cytosol/microbiology ; Dihydrolipoyllysine-Residue Acetyltransferase ; Gene Deletion ; Lethal Dose 50 ; Listeria monocytogenes/genetics/*growth & development/metabolism/*pathogenicity ; Listeriosis/microbiology ; Macrophages/metabolism/*microbiology ; Mice ; Mice, Inbred BALB C ; Mutation ; Open Reading Frames ; Peptide Synthases/genetics/metabolism ; Pyruvate Dehydrogenase Complex/metabolism ; Thioctic Acid/*metabolism ; Virulence
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  • 22
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    Requirement of mammalian Timeless for circadian rhythmicity (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-10-18
    Description: Despite a central circadian role in Drosophila for the transcriptional regulator Timeless (dTim), the relevance of mammalian Timeless (mTim) remains equivocal. Conditional knockdown of mTim protein expression in the rat suprachiasmatic nucleus (SCN) disrupted SCN neuronal activity rhythms, and altered levels of known core clock elements. Full-length mTim protein (mTIM-fl) exhibited a 24-hour oscillation, where as a truncated isoform (mTIM-s) was constitutively expressed. mTIM-fl associated with the mammalian clock Period proteins (mPERs) in oscillating SCN cells. These data suggest that mTim is required for rhythmicity and is a functional homolog of dTim on the negative-feedback arm of the mammalian molecular clockwork.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barnes, Jessica W -- Tischkau, Shelley A -- Barnes, Jeffrey A -- Mitchell, Jennifer W -- Burgoon, Penny W -- Hickok, Jason R -- Gillette, Martha U -- GM07143/GM/NIGMS NIH HHS/ -- HL67007/HL/NHLBI NIH HHS/ -- NS10170/NS/NINDS NIH HHS/ -- NS11134/NS/NINDS NIH HHS/ -- NS11158/NS/NINDS NIH HHS/ -- NS22155/NS/NINDS NIH HHS/ -- NS35859/NS/NINDS NIH HHS/ -- R01 HL067007/HL/NHLBI NIH HHS/ -- R01 NS022155/NS/NINDS NIH HHS/ -- R01 NS035859/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2003 Oct 17;302(5644):439-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Structural Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14564007" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Clocks ; Cell Cycle Proteins ; Cell Line ; *Circadian Rhythm ; Cryptochromes ; *Drosophila Proteins ; Electrophysiology ; *Eye Proteins ; Flavoproteins/metabolism ; Humans ; In Vitro Techniques ; Intracellular Signaling Peptides and Proteins ; Neurons/physiology ; Nuclear Proteins/metabolism ; Oligonucleotides, Antisense/pharmacology ; Period Circadian Proteins ; *Photoreceptor Cells, Invertebrate ; RNA Interference ; RNA, Messenger/genetics/metabolism ; Rats ; Rats, Inbred Strains ; Receptors, G-Protein-Coupled ; Reverse Transcriptase Polymerase Chain Reaction ; Suprachiasmatic Nucleus/*physiology ; Transcription Factors/chemistry/genetics/*metabolism ; Transfection
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  • 23
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    Biotechnology. Stem cells lose market luster (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-03-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2003 Mar 21;299(5614):1830-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12649456" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Australia ; Biotechnology/*economics/manpower ; Cell Line ; Clinical Trials as Topic ; Cloning, Organism/*economics ; Commerce ; Embryo Research/*economics ; Embryo, Mammalian/*cytology ; Financing, Government ; Humans ; *Investments ; Research Personnel ; Research Support as Topic ; *Stem Cells ; United States
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  • 24
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    Cleavage of Arabidopsis PBS1 by a bacterial type III effector (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-30
    Description: Plant disease-resistance (R) proteins are thought to function as receptors for ligands produced directly or indirectly by pathogen avirulence (Avr) proteins. The biochemical functions of most Avr proteins are unknown, and the mechanisms by which they activate R proteins have not been determined. In Arabidopsis, resistance to Pseudomonas syringae strains expressing AvrPphB requires RPS5, a member of the class of R proteins that have a predicted nucleotide-binding site and leucine-rich repeats, and PBS1, a protein kinase. AvrPphB was found to proteolytically cleave PBS1, and this cleavage was required for RPS5-mediated resistance, which indicates that AvrPphB is detected indirectly via its enzymatic activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shao, Feng -- Golstein, Catherine -- Ade, Jules -- Stoutemyer, Mark -- Dixon, Jack E -- Innes, Roger W -- DK18849/DK/NIDDK NIH HHS/ -- GM46451/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Aug 29;301(5637):1230-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Medical School and Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12947197" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/genetics/*metabolism/microbiology ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Bacterial Proteins/chemistry/genetics/*metabolism ; Carrier Proteins/genetics/metabolism ; Cell Line ; Cysteine Endopeptidases/chemistry/genetics/*metabolism ; Genes, Bacterial ; Genes, Plant ; Genetic Complementation Test ; Humans ; Models, Biological ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Plant Diseases/*microbiology ; Plant Extracts/metabolism ; Plant Proteins/genetics/metabolism ; Plants, Genetically Modified ; Precipitin Tests ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Pseudomonas/*metabolism ; Recombinant Proteins/metabolism ; Tobacco/genetics/metabolism ; Transformation, Genetic
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    Hypermutation of HIV-1 DNA in the absence of the Vif protein (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lecossier, Denise -- Bouchonnet, Francine -- Clavel, Francois -- Hance, Allan J -- New York, N.Y. -- Science. 2003 May 16;300(5622):1112.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INSERM U552, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12750511" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; Cytidine Deaminase ; DNA Mutational Analysis ; DNA, Viral/biosynthesis/*genetics ; Gene Products, vif/*physiology ; HIV-1/genetics/*physiology ; HeLa Cells ; Humans ; Molecular Sequence Data ; *Mutation ; Nucleoside Deaminases ; Proteins/physiology ; Repressor Proteins ; Virion/genetics/physiology ; Virus Replication ; vif Gene Products, Human Immunodeficiency Virus
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Nod1 detects a unique muropeptide from gram-negative bacterial peptidoglycan (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-07
    Description: Although the role of Toll-like receptors in extracellular bacterial sensing has been investigated intensively, intracellular detection of bacteria through Nod molecules remains largely uncharacterized. Here, we show that human Nod1 specifically detects a unique diaminopimelate-containing N-acetylglucosamine-N-acetylmuramic acid (GlcNAc-MurNAc) tripeptide motif found in Gram-negative bacterial peptidoglycan, resulting in activation of the transcription factor NF-kappaB pathway. Moreover, we show that in epithelial cells (which represent the first line of defense against invasive pathogens), Nod1is indispensable for intracellular Gram-negative bacterial sensing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Girardin, Stephen E -- Boneca, Ivo G -- Carneiro, Leticia A M -- Antignac, Aude -- Jehanno, Muguette -- Viala, Jerome -- Tedin, Karsten -- Taha, Muhamed-Kheir -- Labigne, Agnes -- Zahringer, Ulrich -- Coyle, Anthony J -- DiStefano, Peter S -- Bertin, John -- Sansonetti, Philippe J -- Philpott, Dana J -- New York, N.Y. -- Science. 2003 Jun 6;300(5625):1584-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite de Pathogenie Microbienne Moleculaire, INSERM U389, Institut Pasteur, 28, Rue du Dr. Roux, 75724Paris Cedex 15, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12791997" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Amino Acid Motifs ; Animals ; Antigens, Differentiation/metabolism ; Carrier Proteins/chemistry/metabolism/*physiology ; Cell Line ; Cytoplasm/microbiology ; Epithelial Cells/metabolism/microbiology ; Gram-Negative Bacteria/*chemistry/immunology ; Gram-Positive Bacteria/chemistry/immunology ; Humans ; Immunity, Innate ; Interleukin-8/metabolism ; *Intracellular Signaling Peptides and Proteins ; Lipopolysaccharides/pharmacology ; Mice ; Myeloid Differentiation Factor 88 ; NF-kappa B/chemistry/metabolism ; Nod1 Signaling Adaptor Protein ; Nod2 Signaling Adaptor Protein ; Oligopeptides/*analysis/chemistry ; Peptidoglycan/*chemistry/pharmacology ; Protein Structure, Tertiary ; Receptors, Immunologic/metabolism ; Signal Transduction ; Trisaccharides/*analysis/chemistry
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    Selective trafficking of non-cell-autonomous proteins mediated by NtNCAPP1 (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-01-18
    Description: In plants, cell-to-cell communication is mediated by plasmodesmata and involves the trafficking of non-cell-autonomous proteins (NCAPs). A component in this pathway, Nicotiana tabacum NON-CELL-AUTONOMOUS PATHWAY PROTEIN1 (NtNCAPP1), was affinity purified and cloned. Protein overlay assays and in vivo studies showed that NtNCAPP1 is located on the endoplasmic reticulum at the cell periphery and displays specificity in its interaction with NCAPs. Deletion of the NtNCAPP1 amino-terminal transmembrane domain produced a dominant-negative mutant that blocked the trafficking of specific NCAPs. Transgenic tobacco plants expressing this mutant form of NtNCAPP1 and plants in which the NtNCAPP1 gene was silenced were compromised in their ability to regulate leaf and floral development. These results support a model in which NCAP delivery to plasmodesmata is both selective and regulated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Jung-Youn -- Yoo, Byung-Chun -- Rojas, Maria R -- Gomez-Ospina, Natalia -- Staehelin, L Andrew -- Lucas, William J -- GM18639/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Jan 17;299(5605):392-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Plant Biology, Division of Biological Sciences, University of California, 1 Shields Avenue, Davis, CA 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12532017" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Communication ; Cell Line ; Cloning, Molecular ; Cytoplasm/metabolism ; Endoplasmic Reticulum/metabolism ; Flowers/growth & development ; Gene Silencing ; Green Fluorescent Proteins ; Immunohistochemistry ; Luminescent Proteins/metabolism ; Molecular Sequence Data ; Mutation ; Phenotype ; Plant Leaves/growth & development ; Plant Proteins/chemistry/genetics/*isolation & purification/*metabolism ; Plants, Genetically Modified ; Plasmodesmata/*metabolism ; Protein Transport ; Recombinant Fusion Proteins/metabolism ; Tobacco/genetics/growth & development/*metabolism ; Tobacco Mosaic Virus ; Viral Proteins/metabolism
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    Chimeric nucleases stimulate gene targeting in human cells (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Porteus, Matthew H -- Baltimore, David -- R01-GM39458/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 May 2;300(5620):763.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, California Institute of Technology, Pasadena CA 91125, USA. matthew.porteus@UTSouthwestern.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12730593" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; DNA/metabolism ; Deoxyribonucleases, Type II Site-Specific/chemistry/genetics/*metabolism ; Dimerization ; Gene Targeting/*methods ; Green Fluorescent Proteins ; Humans ; Luminescent Proteins/genetics ; Mutation ; Nuclear Localization Signals ; Recombinant Fusion Proteins/chemistry/*metabolism ; Recombination, Genetic ; Saccharomyces cerevisiae Proteins ; Transfection ; *Zinc Fingers
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Predominant autoantibody production by early human B cell precursors (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-16
    Description: During B lymphocyte development, antibodies are assembled by random gene segment reassortment to produce a vast number of specificities. A potential disadvantage of this process is that some of the antibodies produced are self-reactive. We determined the prevalence of self-reactive antibody formation and its regulation in human B cells. A majority (55 to 75%) of all antibodies expressed by early immature B cells displayed self-reactivity, including polyreactive and anti-nuclear specificities. Most of these autoantibodies were removed from the population at two discrete checkpoints during B cell development. Inefficient checkpoint regulation would lead to substantial increases in circulating autoantibodies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wardemann, Hedda -- Yurasov, Sergey -- Schaefer, Anne -- Young, James W -- Meffre, Eric -- Nussenzweig, Michel C -- New York, N.Y. -- Science. 2003 Sep 5;301(5638):1374-7. Epub 2003 Aug 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Immunology, Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12920303" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Antinuclear/biosynthesis/immunology ; Antibody Diversity ; Antibody Specificity ; Autoantibodies/*biosynthesis/immunology ; B-Lymphocytes/cytology/*immunology/physiology ; Cell Differentiation ; Cell Line ; Complementarity Determining Regions/chemistry/immunology ; Cytosol/immunology ; Genes, Immunoglobulin ; Humans ; Immunoglobulin Heavy Chains/chemistry/immunology ; Recombination, Genetic ; Selection, Genetic ; Tumor Cells, Cultured
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    The birth of an alternatively spliced exon: 3' splice-site selection in Alu exons (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-24
    Description: Alu repetitive elements can be inserted into mature messenger RNAs via a splicing-mediated process termed exonization. To understand the molecular basis and the regulation of the process of turning intronic Alus into new exons, we compiled and analyzed a data set of human exonized Alus. We revealed a mechanism that governs 3' splice-site selection in these exons during alternative splicing. On the basis of these findings, we identified mutations that activated the exonization of a silent intronic Alu.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lev-Maor, Galit -- Sorek, Rotem -- Shomron, Noam -- Ast, Gil -- New York, N.Y. -- Science. 2003 May 23;300(5623):1288-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics and Molecular Medicine, Sackler Faculty of Medicine, Tel Aviv University, Ramat Aviv 69978, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12764196" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Deaminase/genetics ; *Alternative Splicing ; Alu Elements/*genetics ; Cell Line ; Cloning, Molecular ; DNA, Antisense ; Dinucleoside Phosphates/genetics ; *Exons ; Genome, Human ; Glucosyltransferases/genetics ; Humans ; Introns ; Mutagenesis, Site-Directed ; Point Mutation ; Polymerase Chain Reaction ; RNA-Binding Proteins ; Ribonucleoproteins, Small Nuclear/genetics/physiology ; Spliceosomes/metabolism ; Transfection ; Tumor Cells, Cultured
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    Inhibition of neuroepithelial patched-induced apoptosis by sonic hedgehog (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-09
    Description: During early development in vertebrates, Sonic hedgehog (Shh) is produced by the notochord and the floor plate. A ventrodorsal gradient of Shh directs ventrodorsal patterning of the neural tube. However, Shh is also required for the survival of neuroepithelial cells. We show that Patched (Ptc) induces apoptotic cell death unless its ligand Shh is present to block the signal. Moreover, the blockade of Ptc-induced cell death partly rescues the chick spinal cord defect provoked by Shh deprivation. Thus, the proapoptotic activity of unbound Ptc and the positive effect of Shh-bound Ptc on cell differentiation probably cooperate to achieve the appropriate spinal cord development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thibert, Chantal -- Teillet, Marie-Aimee -- Lapointe, Francoise -- Mazelin, Laetitia -- Le Douarin, Nicole M -- Mehlen, Patrick -- New York, N.Y. -- Science. 2003 Aug 8;301(5634):843-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Apoptosis/Differentiation Laboratory, "La Ligue," Molecular and Cellular Genetic Center, CNRS Unite Mixte Recherche (UMR) 5534, University of Lyon, 69622 Villeurbanne, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12907805" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Caspase 3 ; Caspases/metabolism ; Cell Differentiation ; Cell Line ; Central Nervous System/cytology/*embryology/metabolism ; Chick Embryo ; Electroporation ; Epithelial Cells/cytology/metabolism ; Hedgehog Proteins ; Humans ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins/chemistry/genetics/*metabolism ; Mice ; Mutation ; Protein Binding ; Protein Structure, Tertiary ; Rats ; Receptors, Cell Surface ; Signal Transduction ; Spinal Cord/cytology/embryology ; Trans-Activators/genetics/*metabolism ; Transfection
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    Screening for nitric oxide-dependent protein-protein interactions (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-02
    Description: Because nitric oxide (NO) may be a ubiquitous regulator of cellular signaling, we have modified the yeast two-hybrid system to explore the possibility of NO-dependent protein-protein interactions. We screened for binding partners of procaspase-3, a protein implicated in apoptotic signaling pathways, and identified multiple NO-dependent interactions.Two such interactions, with acid sphingomyelinase and NO synthase, were shown to occur in mammalian cells dependent on endogenous NO. Nitrosylation may thus provide a broad-based mechanism for regulating interactions between proteins. If so, systematic proteomic analyses in which redox state and NO bioavailability are carefully controlled will reveal a large array of novel interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsumoto, Akio -- Comatas, Karrie E -- Liu, Limin -- Stamler, Jonathan S -- New York, N.Y. -- Science. 2003 Aug 1;301(5633):657-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12893946" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Caspase 3 ; Caspases/*metabolism ; Cell Line ; Enzyme Inhibitors/pharmacology ; Enzyme Precursors/*metabolism ; Escherichia coli/genetics/growth & development ; Gene Library ; Humans ; Hydrogen Peroxide/metabolism ; Lysosomes/enzymology ; Mitochondria/enzymology ; Nitric Oxide/*metabolism/pharmacology ; Nitric Oxide Donors/pharmacology ; Nitric Oxide Synthase/antagonists & inhibitors/*metabolism ; Nitric Oxide Synthase Type I ; Nitric Oxide Synthase Type II ; Nitric Oxide Synthase Type III ; Oxidation-Reduction ; Precipitin Tests ; *Protein Binding ; Signal Transduction ; Sphingomyelin Phosphodiesterase/*metabolism ; Transfection ; Transformation, Bacterial ; Triazenes/pharmacology ; Two-Hybrid System Techniques ; beta-Galactosidase/metabolism ; omega-N-Methylarginine/pharmacology
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    European Union. E.U. stem cell debate ends in a draw (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2003 Dec 12;302(5652):1872-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14671253" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; *Embryo Research/economics/legislation & jurisprudence ; Embryo, Mammalian/*cytology ; *European Union ; *Guidelines as Topic ; Humans ; Research Support as Topic ; *Stem Cells
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    Stem cells. Visiting German profs could face jail (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2003 Aug 1;301(5633):577.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12893913" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Embryo Research/*legislation & jurisprudence ; Embryo, Mammalian/*cytology ; *Faculty ; Germany ; Government ; Humans ; Jurisprudence ; Private Sector ; Public Sector ; Research Personnel/*legislation & jurisprudence ; *Stem Cells
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    Genome-wide survey of human alternative pre-mRNA splicing with exon junction microarrays (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-20
    Description: Alternative pre-messenger RNA (pre-mRNA) splicing plays important roles in development, physiology, and disease, and more than half of human genes are alternatively spliced. To understand the biological roles and regulation of alternative splicing across different tissues and stages of development, systematic methods are needed. Here, we demonstrate the use of microarrays to monitor splicing at every exon-exon junction in more than 10,000 multi-exon human genes in 52 tissues and cell lines. These genome-wide data provide experimental evidence and tissue distributions for thousands of known and novel alternative splicing events. Adding to previous studies, the results indicate that at least 74% of human multi-exon genes are alternatively spliced.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, Jason M -- Castle, John -- Garrett-Engele, Philip -- Kan, Zhengyan -- Loerch, Patrick M -- Armour, Christopher D -- Santos, Ralph -- Schadt, Eric E -- Stoughton, Roland -- Shoemaker, Daniel D -- New York, N.Y. -- Science. 2003 Dec 19;302(5653):2141-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rosetta Inpharmatics LLC, Merck & Co., Inc., 12040 115th Avenue N.E., Kirkland, WA 98034, USA. jason_johnson@merck.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14684825" target="_blank"〉PubMed〈/a〉
    Keywords: *Alternative Splicing ; Amyloid beta-Protein Precursor/analysis/genetics ; Cell Line ; DNA, Complementary ; *Exons ; Expressed Sequence Tags ; *Genome, Human ; Humans ; Hydroxymethylglutaryl CoA Reductases/analysis/genetics ; Molecular Sequence Data ; *Oligonucleotide Array Sequence Analysis ; *Phosphoric Monoester Hydrolases ; Protein Isoforms/analysis ; Proteins/analysis/genetics ; RNA Precursors/*genetics ; ROC Curve ; Reverse Transcriptase Polymerase Chain Reaction ; Tissue Distribution
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    Triggering the interferon antiviral response through an IKK-related pathway (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-19
    Description: Rapid induction of type I interferon expression, a central event in establishing the innate antiviral response, requires cooperative activation of numerous transcription factors. Although signaling pathways that activate the transcription factors nuclear factor kappaB and ATF-2/c-Jun have been well characterized, activation of the interferon regulatory factors IRF-3 and IRF-7 has remained a critical missing link in understanding interferon signaling. We report here that the IkappaB kinase (IKK)-related kinases IKKepsilon and TANK-binding kinase 1 are components of the virus-activated kinase that phosphorylate IRF-3 and IRF-7. These studies illustrate an essential role for an IKK-related kinase pathway in triggering the host antiviral response to viral infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharma, Sonia -- tenOever, Benjamin R -- Grandvaux, Nathalie -- Zhou, Guo-Ping -- Lin, Rongtuan -- Hiscott, John -- New York, N.Y. -- Science. 2003 May 16;300(5622):1148-51. Epub 2003 Apr 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lady Davis Institute for Medical Research-Jewish General Hospital, Departments of Microbiology and Immunology and Medicine, McGill University, Montreal, Quebec H3T 1E2, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12702806" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; DNA-Binding Proteins/metabolism ; Enzyme Activation ; Gene Expression Regulation, Viral ; Hepacivirus/immunology/*physiology ; Humans ; I-kappa B Kinase ; Interferon Regulatory Factor-3 ; Interferon Regulatory Factor-7 ; Interferon Type I/*biosynthesis/genetics ; Phosphorylation ; Promoter Regions, Genetic ; Protein-Serine-Threonine Kinases/*metabolism ; RNA, Small Interfering/metabolism ; Transcription Factors/metabolism
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    Regulation of cell polarity and protrusion formation by targeting RhoA for degradation (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-06
    Description: The Rho family of small guanosine triphosphatases regulates actin cytoskeleton dynamics that underlie cellular functions such as cell shape changes, migration, and polarity. We found that Smurf1, a HECT domain E3 ubiquitin ligase, regulated cell polarity and protrusive activity and was required to maintain the transformed morphology and motility of a tumor cell. Atypical protein kinase C zeta (PKCzeta), an effector of the Cdc42/Rac1-PAR6 polarity complex, recruited Smurf1 to cellular protrusions, where it controlled the local level of RhoA. Smurf1 thus links the polarity complex to degradation of RhoA in lamellipodia and filopodia to prevent RhoA signaling during dynamic membrane movements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Hong-Rui -- Zhang, Yue -- Ozdamar, Barish -- Ogunjimi, Abiodun A -- Alexandrova, Evguenia -- Thomsen, Gerald H -- Wrana, Jeffrey L -- HD32429/HD/NICHD NIH HHS/ -- R01 HD032429/HD/NICHD NIH HHS/ -- R01 HD032429-06/HD/NICHD NIH HHS/ -- R01 HD032429-07/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2003 Dec 5;302(5651):1775-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto M56 1x5, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14657501" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Line, Tumor ; Cell Membrane/metabolism/physiology ; *Cell Movement ; *Cell Polarity ; Cell Size ; Cell Transformation, Neoplastic ; Cytoskeleton/ultrastructure ; Guanine Nucleotide Exchange Factors/metabolism ; Humans ; Intercellular Junctions/metabolism ; Mice ; NIH 3T3 Cells ; Protein Kinase C/metabolism ; Protein Structure, Tertiary ; Pseudopodia/*metabolism/ultrastructure ; RNA, Small Interfering ; Signal Transduction ; Transfection ; Ubiquitin-Protein Ligases/chemistry/genetics/*metabolism ; cdc42 GTP-Binding Protein/metabolism ; rhoA GTP-Binding Protein/genetics/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    RNA leaching of transcription factors disrupts transcription in myotonic dystrophy (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-06
    Description: Myotonic dystrophy type 1 (DM1) is caused by a CUGn expansion (n approximately 50 to 5000) in the 3' untranslated region of the mRNA of the DM protein kinase gene. We show that mutant RNA binds and sequesters transcription factors (TFs), with up to 90% depletion of selected TFs from active chromatin. Diverse genes are consequently reduced in expression, including the ion transporter CIC-1, which has been implicated in myotonia. When TF specificity protein 1 (Sp1) was overexpressed in DM1-affected cells, low levels of messenger RNA for CIC-1 were restored to normal. Transcription factor leaching from chromatin by mutant RNA provides a potentially unifying pathomechanistic explanation for this disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ebralidze, A -- Wang, Y -- Petkova, V -- Ebralidse, K -- Junghans, R P -- New York, N.Y. -- Science. 2004 Jan 16;303(5656):383-7. Epub 2003 Dec 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biotherapeutics Development Lab, Harvard Institute of Human Genetics, Harvard Medical School and Division of Hematology-Oncology, Beth Israel Deaconess Medical Center, 4 Blackfan Circle, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14657503" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cell Line ; Cell Nucleus/metabolism ; Chloride Channels/genetics ; Chromatin/metabolism ; DNA-Binding Proteins/genetics/metabolism ; Humans ; Muscle Cells/*metabolism ; Mutation ; Myotonic Dystrophy/*genetics ; Myotonin-Protein Kinase ; Promoter Regions, Genetic ; Protein-Serine-Threonine Kinases/*genetics ; RNA/genetics/*metabolism ; RNA Splicing ; RNA, Messenger/genetics/metabolism ; Receptors, IgG/genetics ; Receptors, Retinoic Acid/genetics/metabolism ; Ribonucleoproteins/metabolism ; STAT1 Transcription Factor ; STAT3 Transcription Factor ; Sp1 Transcription Factor/genetics/metabolism ; Sp3 Transcription Factor ; Trans-Activators/genetics/metabolism ; Transcription Factors/genetics/*metabolism ; *Transcription, Genetic
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    EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-01
    Description: Terminally misfolded proteins in the endoplasmic reticulum (ER) are retrotranslocated to the cytoplasm and degraded by proteasomes through a mechanism known as ER-associated degradation (ERAD). EDEM, a postulated Man8B-binding protein, accelerates the degradation of misfolded proteins in the ER. Here, EDEM was shown to interact with calnexin, but not with calreticulin, through its transmembrane region. Both binding of substrates to calnexin and their release from calnexin were required for ERAD to occur. Overexpression of EDEM accelerated ERAD by promoting the release of terminally misfolded proteins from calnexin. Thus, EDEM appeared to function in the ERAD pathway by accepting substrates from calnexin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oda, Yukako -- Hosokawa, Nobuko -- Wada, Ikuo -- Nagata, Kazuhiro -- New York, N.Y. -- Science. 2003 Feb 28;299(5611):1394-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606-8397, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12610305" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcysteine/*analogs & derivatives/pharmacology ; Calnexin/*metabolism ; Calreticulin/metabolism ; Cell Line ; Endoplasmic Reticulum/*metabolism ; Glycoproteins/chemistry/*metabolism ; Humans ; Indolizines/pharmacology ; Membrane Proteins/*metabolism ; Precipitin Tests ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Transport ; Recombinant Fusion Proteins/metabolism ; Transfection ; alpha 1-Antitrypsin/chemistry/*metabolism
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    Design and chemical synthesis of a homogeneous polymer-modified erythropoiesis protein (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-02-08
    Description: We report the design and total chemical synthesis of "synthetic erythropoiesis protein" (SEP), a 51-kilodalton protein-polymer construct consisting of a 166-amino-acid polypeptide chain and two covalently attached, branched, and monodisperse polymer moieties that are negatively charged. The ability to control the chemistry allowed us to synthesize a macromolecule of precisely defined covalent structure. SEP was homogeneous as shown by high-resolution analytical techniques, with a mass of 50,825 +/-10 daltons by electrospray mass spectrometry, and with a pI of 5.0. In cell and animal assays for erythropoiesis, SEP displayed potent biological activity and had significantly prolonged duration of action in vivo. These chemical methods are a powerful tool in the rational design of protein constructs with potential therapeutic applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kochendoerfer, Gerd G -- Chen, Shiah-Yun -- Mao, Feng -- Cressman, Sonya -- Traviglia, Stacey -- Shao, Haiyan -- Hunter, Christie L -- Low, Donald W -- Cagle, E Neil -- Carnevali, Maia -- Gueriguian, Vincent -- Keogh, Peter J -- Porter, Heather -- Stratton, Stephen M -- Wiedeke, M Con -- Wilken, Jill -- Tang, Jie -- Levy, Jay J -- Miranda, Les P -- Crnogorac, Milan M -- Kalbag, Suresh -- Botti, Paolo -- Schindler-Horvat, Janice -- Savatski, Laura -- Adamson, John W -- Kung, Ada -- Kent, Stephen B H -- Bradburne, James A -- New York, N.Y. -- Science. 2003 Feb 7;299(5608):884-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gryphon Therapeutics, 250 East Grand Avenue, Suite 90, South San Francisco, CA 94080, USA. Gkochendoerfer@gryphonRX.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12574628" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Circular Dichroism ; *Drug Design ; Drug Stability ; Electrophoresis, Polyacrylamide Gel ; *Erythropoiesis ; Erythropoietin/chemistry/pharmacology ; Hematocrit ; Humans ; Isoelectric Point ; Mice ; Molecular Sequence Data ; Molecular Structure ; Molecular Weight ; *Polymers/*chemical synthesis/*chemistry/pharmacokinetics/pharmacology ; Protein Folding ; Proteins/*chemical synthesis/*chemistry/pharmacokinetics/pharmacology ; Rats ; Receptors, Erythropoietin/drug effects/metabolism ; Recombinant Proteins ; Spectrometry, Mass, Electrospray Ionization
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    FACT facilitates transcription-dependent nucleosome alteration (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-23
    Description: The FACT (facilitates chromatin transcription) complex is required for transcript elongation through nucleosomes by RNA polymerase II (Pol II) in vitro. Here, we show that FACT facilitates Pol II-driven transcription by destabilizing nucleosomal structure so that one histone H2A-H2B dimer is removed during enzyme passage. We also demonstrate that FACT possesses intrinsic histone chaperone activity and can deposit core histones onto DNA. Importantly, FACT activity requires both of its constituent subunits and is dependent on the highly acidic C terminus of its larger subunit, Spt16. These findings define the mechanism by which Pol II can transcribe through chromatin without disrupting its epigenetic status.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Belotserkovskaya, Rimma -- Oh, Sangtaek -- Bondarenko, Vladimir A -- Orphanides, George -- Studitsky, Vasily M -- Reinberg, Danny -- GM37120/GM/NIGMS NIH HHS/ -- GM58650/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Aug 22;301(5636):1090-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry, Division of Nucleic Acids Enzymology, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway, NJ 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12934006" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Cycle Proteins/chemistry/metabolism ; Cell Line ; DNA/metabolism ; DNA-Binding Proteins/chemistry/metabolism ; Dimerization ; HeLa Cells ; High Mobility Group Proteins/chemistry/metabolism ; Histones/metabolism ; Humans ; Models, Genetic ; Molecular Chaperones/chemistry/metabolism ; Molecular Sequence Data ; Nucleosomes/*metabolism ; Protein Binding ; Protein Subunits ; RNA Polymerase II/*metabolism ; Recombinant Proteins/chemistry/metabolism ; Templates, Genetic ; Transcription Factors/chemistry/metabolism ; *Transcription, Genetic ; Transcriptional Elongation Factors/chemistry/*metabolism
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    Biochemistry. An overoxidation journey with a return ticket (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Georgiou, George -- Masip, Lluis -- New York, N.Y. -- Science. 2003 Apr 25;300(5619):592-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering, Biomedical Engineering and Institute for Cell and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA. gg@che.utexas.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12714731" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; Antioxidants/*metabolism ; Bacteria/enzymology ; Catalysis ; Cell Line ; Cysteine/*analogs & derivatives/metabolism ; Erythrocytes/enzymology ; Evolution, Molecular ; Humans ; Hydrogen Peroxide/*metabolism ; Models, Biological ; Neurotransmitter Agents ; Oxidation-Reduction ; Peroxidases/*chemistry/*metabolism ; Peroxiredoxins ; Protein Conformation ; Protein Structure, Secondary ; *Signal Transduction ; Sulfenic Acids/metabolism ; Sulfinic Acids/metabolism
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    Embryonic stem cells. Key questions loom over effort to energize research (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-01-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- Holden, Constance -- New York, N.Y. -- Science. 2003 Jan 24;299(5606):493-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12543947" target="_blank"〉PubMed〈/a〉
    Keywords: Access to Information ; Advisory Committees ; Animals ; Biological Specimen Banks ; Cell Culture Techniques ; Cell Line ; Chimera ; *Embryo Research/ethics ; Embryo, Mammalian/*cytology ; Guidelines as Topic ; Humans ; International Cooperation ; Internet ; Mice ; Pluripotent Stem Cells ; *Stem Cells
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    Transport of dsRNA into cells by the transmembrane protein SID-1 (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-13
    Description: RNA interference (RNAi) spreads systemically in plants and nematodes to silence gene expression distant from the site of initiation. We previously identified a gene, sid-1, essential for systemic but not cell-autonomous RNAi in Caenorhabditis elegans. Here, we demonstrate that SID-1 is a multispan transmembrane protein that sensitizes Drosophila cells to soaking RNAi with a potency that is dependent on double-stranded RNA (dsRNA) length. Further analyses revealed that SID-1 enables passive cellular uptake of dsRNA. These data indicate that systemic RNAi in C. elegans involves SID-1-mediated intercellular transport of dsRNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feinberg, Evan H -- Hunter, Craig P -- R01 GM069891/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Sep 12;301(5639):1545-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12970568" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Biological Transport ; Caenorhabditis elegans/*genetics ; Caenorhabditis elegans Proteins/chemistry/*metabolism ; Cell Line ; Diffusion ; Drosophila ; Membrane Proteins/chemistry/*metabolism ; *RNA Interference ; RNA, Double-Stranded/chemistry/genetics/*metabolism ; Recombinant Proteins/metabolism ; Transfection
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    Spread of HTLV-I between lymphocytes by virus-induced polarization of the cytoskeleton (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-02-18
    Description: Cell contact is required for efficient transmission of human T cell leukemia virus- type 1 (HTLV-I) between cells and between individuals, because naturally infected lymphocytes produce virtually no cell-free infectious HTLV-I particles. However, the mechanism of cell-to-cell spread of HTLV-I is not understood. We show here that cell contact rapidly induces polarization of the cytoskeleton of the infected cell to the cell-cell junction. HTLV-I core (Gag protein) complexes and the HTLV-I genome accumulate at the cell-cell junction and are then transferred to the uninfected cell. Other lymphotropic viruses, such as HIV-1, may similarly subvert normal T cell physiology to allow efficient propagation between cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Igakura, Tadahiko -- Stinchcombe, Jane C -- Goon, Peter K C -- Taylor, Graham P -- Weber, Jonathan N -- Griffiths, Gillian M -- Tanaka, Yuetsu -- Osame, Mitsuhiro -- Bangham, Charles R M -- New York, N.Y. -- Science. 2003 Mar 14;299(5613):1713-6. Epub 2003 Feb 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Imperial College London, St. Mary's Campus, Norfolk Place, London W2 1PG, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12589003" target="_blank"〉PubMed〈/a〉
    Keywords: CD4-Positive T-Lymphocytes/immunology/ultrastructure/virology ; CD8-Positive T-Lymphocytes/immunology/ultrastructure/virology ; Cell Adhesion Molecules/metabolism ; Cell Communication ; Cell Line ; *Cell Polarity ; Extracellular Space/virology ; Gene Products, env/metabolism ; Gene Products, gag/metabolism ; Genome, Viral ; HTLV-I Infections/virology ; Human T-lymphotropic virus 1/genetics/*physiology ; Humans ; In Situ Hybridization, Fluorescence ; Intercellular Junctions/*physiology/ultrastructure/virology ; Microscopy, Confocal ; Microtubule-Organizing Center/*physiology/ultrastructure ; Microtubules/physiology ; Nucleocapsid Proteins/metabolism ; Peptide Nucleic Acids ; Receptors, Antigen, T-Cell/immunology ; T-Lymphocytes/immunology/*ultrastructure/*virology ; Talin/metabolism ; Virion/physiology
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    Identification of a testicular odorant receptor mediating human sperm chemotaxis (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-29
    Description: Although it has been known for some time that olfactory receptors (ORs) reside in spermatozoa, the function of these ORs is unknown. Here, we identified, cloned, and functionally expressed a previously undescribed human testicular OR, hOR17-4. With the use of ratiofluorometric imaging, Ca2+ signals were induced by a small subset of applied chemical stimuli, establishing the molecular receptive fields for the recombinantly expressed receptor in human embryonic kidney (HEK) 293 cells and the native receptor in human spermatozoa. Bourgeonal was a powerful agonist for both recombinant and native receptor types, as well as a strong chemoattractant in subsequent behavioral bioassays. In contrast, undecanal was a potent OR antagonist to bourgeonal and related compounds. Taken together, these results indicate that hOR17-4 functions in human sperm chemotaxis and may be a critical component of the fertilization process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Spehr, Marc -- Gisselmann, Gunter -- Poplawski, Alexandra -- Riffell, Jeffrey A -- Wetzel, Christian H -- Zimmer, Richard K -- Hatt, Hanns -- New York, N.Y. -- Science. 2003 Mar 28;299(5615):2054-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Physiology, Ruhr University Bochum, 150 University Street, D-44780 Bochum, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12663925" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Aldehydes/chemistry/metabolism/pharmacology ; Binding Sites ; Calcium/metabolism ; Calcium Signaling ; Cell Line ; Chemotactic Factors/chemistry/metabolism/*pharmacology ; *Chemotaxis ; Cloning, Molecular ; Dose-Response Relationship, Drug ; Fertilization ; Gene Expression Profiling ; Humans ; Ligands ; Male ; Molecular Structure ; Odors ; Receptors, Odorant/chemistry/genetics/*physiology ; Recombinant Fusion Proteins/metabolism ; Seminal Plasma Proteins/genetics/*physiology ; *Sperm Motility/drug effects ; Spermatozoa/drug effects/*physiology ; Testis/*metabolism ; Type C Phospholipases/metabolism
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    Cell signaling. beta-arrestin--not just for G protein-coupled receptors (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Spiegel, Allen -- New York, N.Y. -- Science. 2003 Sep 5;301(5638):1338-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA. spiegela@extra.niddk.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12958351" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Animals ; Arrestins/*metabolism ; Cell Line ; Cell Membrane/metabolism ; Clathrin/metabolism ; Coated Pits, Cell-Membrane/metabolism ; Down-Regulation ; Drosophila ; *Endocytosis ; Frizzled Receptors ; GTP-Binding Proteins/metabolism ; Humans ; Mice ; Phosphoproteins/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases ; Proteins/*metabolism ; Proteoglycans/metabolism ; Proto-Oncogene Proteins/metabolism ; Receptors, Cell Surface/*metabolism ; Receptors, Transforming Growth Factor beta/metabolism ; *Signal Transduction ; Transforming Growth Factor beta/metabolism ; Wnt Proteins
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    Cell biology. NO says yes to mitochondria (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-02-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, Guy C -- New York, N.Y. -- Science. 2003 Feb 7;299(5608):838-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Cambridge University, Cambridge CB2 1QW, UK. gcb@mole.bio.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12574611" target="_blank"〉PubMed〈/a〉
    Keywords: Adipocytes/metabolism/ultrastructure ; Adipose Tissue, Brown/cytology/metabolism/ultrastructure ; Animals ; Cell Differentiation ; Cell Line ; Cyclic GMP/metabolism ; Energy Metabolism ; Gene Expression Regulation ; Mice ; Mice, Transgenic ; Mitochondria/*metabolism ; Muscles/metabolism/ultrastructure ; Nitric Oxide/*physiology ; Nitric Oxide Synthase/*metabolism ; Nitric Oxide Synthase Type II ; Nitric Oxide Synthase Type III ; Oxygen Consumption ; Rats ; Transcription Factors/metabolism ; Up-Regulation ; Weight Gain
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    Redistribution of intracellular oxygen in hypoxia by nitric oxide: effect on HIF1alpha (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-13
    Description: Cells exposed to low oxygen concentrations respond by initiating defense mechanisms, including the stabilization of hypoxia-inducible factor (HIF) 1alpha, a transcription factor that upregulates genes such as those involved in glycolysis and angiogenesis. Nitric oxide and other inhibitors of mitochondrial respiration prevent the stabilization of HIF1alpha during hypoxia. In studies of cultured cells, we show that this effect is a result of an increase in prolyl hydroxylase-dependent degradation of HIF1alpha. With the use of Renilla luciferase to detect intracellular oxygen concentrations, we also demonstrate that, upon inhibition of mitochondrial respiration in hypoxia, oxygen is redistributed toward nonrespiratory oxygen-dependent targets such as prolyl hydroxylases so that they do not register hypoxia. Thus, the signaling consequences of hypoxia may be profoundly modified by nitric oxide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hagen, Thilo -- Taylor, Cormac T -- Lam, Francis -- Moncada, Salvador -- New York, N.Y. -- Science. 2003 Dec 12;302(5652):1975-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wolfson Institute for Biomedical Research, University College London, Gower Street, London WC1E 6BT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14671307" target="_blank"〉PubMed〈/a〉
    Keywords: Antioxidants/pharmacology ; *Cell Hypoxia ; Cell Line ; *Cell Respiration/drug effects ; Cycloheximide/pharmacology ; Cysteine Proteinase Inhibitors/pharmacology ; HeLa Cells ; Humans ; Hypoxia-Inducible Factor 1, alpha Subunit ; Leupeptins/*pharmacology ; Luciferases/metabolism ; Methacrylates ; Mitochondria/*metabolism ; Nitric Oxide/pharmacology/*physiology ; Nitric Oxide Donors/pharmacology ; Oxygen/*metabolism ; Procollagen-Proline Dioxygenase/metabolism ; Protein Synthesis Inhibitors/pharmacology ; Reactive Oxygen Species/metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Thiazoles/pharmacology ; Transcription Factors/*metabolism ; Transfection ; Triazenes/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    R2D2, a bridge between the initiation and effector steps of the Drosophila RNAi pathway (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-27
    Description: The RNA interference (RNAi) pathway is initiated by processing long double-stranded RNA into small interfering RNA (siRNA). The siRNA-generating enzyme was purified from Drosophila S2cells and consists of two stoichiometric subunits: Dicer-2(DCR-2) and a previously unknown protein that we named R2D2. R2D2 is homologous to the Caenorhabditis elegans RNAi protein RDE-4. Association with R2D2 does not affect the enzymatic activity of DCR-2. Rather, the DCR-2/R2D2 complex, but not DCR-2 alone, binds to siRNA and enhances sequence-specific messenger RNA degradation mediated by the RNA-initiated silencing complex (RISC). These results indicate that R2D2 bridges the initiation and effector steps of the Drosophila RNAi pathway by facilitating siRNA passage from Dicer to RISC.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Qinghua -- Rand, Tim A -- Kalidas, Savitha -- Du, Fenghe -- Kim, Hyun-Eui -- Smith, Dean P -- Wang, Xiaodong -- DC02539/DC/NIDCD NIH HHS/ -- New York, N.Y. -- Science. 2003 Sep 26;301(5641):1921-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14512631" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Argonaute Proteins ; Biotinylation ; Caenorhabditis elegans/genetics/metabolism ; Caenorhabditis elegans Proteins/chemistry ; Cell Line ; Chemical Precipitation ; Drosophila Proteins/chemistry/genetics/*isolation & purification/*metabolism ; Drosophila melanogaster/*genetics/metabolism ; Electrophoretic Mobility Shift Assay ; Endoribonucleases/genetics/isolation & purification/*metabolism ; Kinetics ; Molecular Sequence Data ; Mutation ; Protein Structure, Tertiary ; RNA Helicases/genetics/*isolation & purification/*metabolism ; *RNA Interference ; RNA, Double-Stranded/metabolism ; RNA, Messenger/metabolism ; RNA, Small Interfering/*metabolism ; RNA-Binding Proteins/chemistry/genetics/isolation & purification/*metabolism ; RNA-Induced Silencing Complex/isolation & purification/metabolism ; Recombinant Proteins/metabolism ; Ribonuclease III
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    Inactivation of TNF signaling by rationally designed dominant-negative TNF variants (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-27
    Description: Tumor necrosis factor (TNF) is a key regulator of inflammatory responses and has been implicated in many pathological conditions. We used structure-based design to engineer variant TNF proteins that rapidly form heterotrimers with native TNF to give complexes that neither bind to nor stimulate signaling through TNF receptors. Thus, TNF is inactivated by sequestration. Dominant-negative TNFs represent a possible approach to anti-inflammatory biotherapeutics, and experiments in animal models show that the strategy can attenuate TNF-mediated pathology. Similar rational design could be used to engineer inhibitors of additional TNF superfamily cytokines as well as other multimeric ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steed, Paul M -- Tansey, Malu G -- Zalevsky, Jonathan -- Zhukovsky, Eugene A -- Desjarlais, John R -- Szymkowski, David E -- Abbott, Christina -- Carmichael, David -- Chan, Cheryl -- Cherry, Lisa -- Cheung, Peter -- Chirino, Arthur J -- Chung, Hyo H -- Doberstein, Stephen K -- Eivazi, Araz -- Filikov, Anton V -- Gao, Sarah X -- Hubert, Rene S -- Hwang, Marian -- Hyun, Linus -- Kashi, Sandhya -- Kim, Alice -- Kim, Esther -- Kung, James -- Martinez, Sabrina P -- Muchhal, Umesh S -- Nguyen, Duc-Hanh T -- O'Brien, Christopher -- O'Keefe, Donald -- Singer, Karen -- Vafa, Omid -- Vielmetter, Jost -- Yoder, Sean C -- Dahiyat, Bassil I -- New York, N.Y. -- Science. 2003 Sep 26;301(5641):1895-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Xencor, 111 West Lemon Avenue, Monrovia, CA 91016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14512626" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Antigens, CD/metabolism ; Apoptosis ; Arthritis, Experimental/drug therapy ; Biopolymers ; Caspases/metabolism ; Cell Line ; Cell Nucleus/metabolism ; Computer Simulation ; Disease Progression ; Enzyme-Linked Immunosorbent Assay ; Female ; Galactosamine/pharmacology ; HeLa Cells ; Humans ; Liver/drug effects ; NF-kappa B/metabolism ; Point Mutation ; *Protein Engineering ; Rats ; Receptors, Tumor Necrosis Factor/metabolism ; Receptors, Tumor Necrosis Factor, Type I ; Receptors, Tumor Necrosis Factor, Type II ; *Signal Transduction ; Transcription Factor RelA ; Transcription, Genetic ; Tumor Necrosis Factor-alpha/*antagonists & ; inhibitors/genetics/metabolism/*pharmacology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    German science. Stem cell project wins final approval (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-01-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steghaus-Kovac, Sabine -- New York, N.Y. -- Science. 2003 Jan 3;299(5603):31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12511625" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; *Embryo Research ; Embryo, Mammalian/*cytology ; Germany ; Humans ; Research Support as Topic ; *Stem Cells
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    A mule cloned from fetal cells by nuclear transfer (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Woods, Gordon L -- White, Kenneth L -- Vanderwall, Dirk K -- Li, Guang-Peng -- Aston, Kenneth I -- Bunch, Thomas D -- Meerdo, Lora N -- Pate, Barry J -- New York, N.Y. -- Science. 2003 Aug 22;301(5636):1063. Epub 2003 May 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Northwest Equine Reproduction Laboratory, Department of Animal and Veterinary Science, University of Idaho, Moscow, ID 83844, USA. gwoods@uidaho.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12775846" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Cell Line ; *Cloning, Organism ; Embryo Transfer ; Embryo, Mammalian ; Embryonic and Fetal Development ; Equidae/*embryology/*genetics ; Female ; Fibroblasts ; Horses ; Male ; *Nuclear Transfer Techniques ; Oocytes/metabolism ; Pregnancy
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Beta-arrestin 2 mediates endocytosis of type III TGF-beta receptor and down-regulation of its signaling (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-06
    Description: beta-Arrestins bind to activated seven transmembrane-spanning (7TMS) receptors (G protein-coupled receptors) after the receptors are phosphorylated by G protein-coupled receptor kinases (GRKs), thereby regulating their signaling and internalization. Here, we demonstrate an unexpected and analogous role of beta-arrestin 2 (betaarr2) for the single transmembrane-spanning type III transforming growth factor-beta (TGF-beta) receptor (TbetaRIII, also referred to as betaglycan). Binding of betaarr2 to TbetaRIII was also triggered by phosphorylation of the receptor on its cytoplasmic domain (likely at threonine 841). However, such phosphorylation was mediated by the type II TGF-beta receptor (TbetaRII), which is itself a kinase, rather than by a GRK. Association with betaarr2 led to internalization of both receptors and down-regulation of TGF-beta signaling. Thus, the regulatory actions of beta-arrestins are broader than previously appreciated, extending to the TGF-beta receptor family as well.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Wei -- Kirkbride, Kellye C -- How, Tam -- Nelson, Christopher D -- Mo, Jinyao -- Frederick, Joshua P -- Wang, Xiao-Fan -- Lefkowitz, Robert J -- Blobe, Gerard C -- CA 75368/CA/NCI NIH HHS/ -- CA 91816/CA/NCI NIH HHS/ -- HL 16037/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2003 Sep 5;301(5638):1394-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Duke University Medical Center, Departments of Medicine and Biochemistry, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12958365" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Arrestins/genetics/*metabolism ; Cell Line ; Cell Membrane/metabolism ; Cytoplasm/metabolism ; Down-Regulation ; *Endocytosis ; Humans ; Keratinocytes/metabolism ; Mice ; Mice, Knockout ; Molecular Sequence Data ; Mutagenesis ; Phosphorylation ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases ; Proteoglycans/chemistry/genetics/*metabolism ; RNA, Small Interfering ; Receptors, Transforming Growth Factor beta/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Transfection ; Transforming Growth Factor beta ; Transforming Growth Factor beta1
    Print ISSN: 0036-8075
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    Direct recognition of cytomegalovirus by activating and inhibitory NK cell receptors (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-16
    Description: Natural killer (NK) cells express inhibitory receptors for major histocompatibility complex (MHC) class I antigens, preventing attack against healthy cells. Mouse cytomegalovirus (MCMV) encodes an MHC-like protein (m157) that binds to an inhibitory NK cell receptor in certain MCMV-susceptible mice. In MCMV-resistant mice, this viral protein engages a related activating receptor (Ly49H) and confers host protection. These activating and inhibitory receptors are highly homologous, suggesting the possibility that one evolved from the other in response to selective pressure imposed by the pathogen.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arase, Hisashi -- Mocarski, Edward S -- Campbell, Ann E -- Hill, Ann B -- Lanier, Lewis L -- AI30363/AI/NIAID NIH HHS/ -- CA89294/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 May 17;296(5571):1323-6. Epub 2002 Apr 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology and the Cancer Research Institute, University of California San Francisco, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11950999" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Antigens, Ly/chemistry/genetics/*immunology/metabolism ; Cell Line ; Coculture Techniques ; Disease Susceptibility ; Evolution, Molecular ; Herpesviridae Infections/*immunology ; Histocompatibility Antigens Class I/immunology ; Hybridomas ; Immunity, Innate ; Interferon-gamma/biosynthesis ; Killer Cells, Natural/*immunology ; Lectins, C-Type ; Ligands ; Lymphocyte Activation ; Membrane Glycoproteins/chemistry/genetics/*immunology/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Inbred Strains ; Muromegalovirus/genetics/*immunology/metabolism ; NK Cell Lectin-Like Receptor Subfamily A ; Protein Binding ; Receptors, Immunologic/chemistry/genetics/*immunology/metabolism ; Receptors, NK Cell Lectin-Like ; Recombinant Fusion Proteins/metabolism ; Transfection ; Viral Proteins/chemistry/genetics/*immunology/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Genetics. Please don't call it cloning! (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogelstein, Bert -- Alberts, Bruce -- Shine, Kenneth -- New York, N.Y. -- Science. 2002 Feb 15;295(5558):1237.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Kimmel Cancer Center at Johns Hopkins University, Baltimore, MD 21231, USA. vogelbe@welch.jhu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11847324" target="_blank"〉PubMed〈/a〉
    Keywords: Bioethical Issues ; Cell Line ; *Cloning, Organism/legislation & jurisprudence ; Embryo Research ; Embryo, Mammalian/*cytology ; Humans ; *Nuclear Transfer Techniques ; *Stem Cells ; *Terminology as Topic ; United States
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    Inhibition of excess nodal signaling during mouse gastrulation by the transcriptional corepressor DRAP1 (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-10
    Description: The formation and patterning of mesoderm during mammalian gastrulation require the activity of Nodal, a secreted mesoderm-inducing factor of the transforming growth factor-beta (TGF-beta) family. Here we show that the transcriptional corepressor DRAP1 has a very specific role in regulation of Nodal activity during mouse embryogenesis. We find that loss of Drap1 leads to severe gastrulation defects that are consistent with increased expression of Nodal and can be partially suppressed by Nodal heterozygosity. Biochemical studies indicate that DRAP1 interacts with and inhibits DNA binding by the winged-helix transcription factor FoxH1 (FAST), a critical component of a positive feedback loop for Nodal activity. We propose that DRAP1 limits the spread of a morphogenetic signal by down-modulating the response to the Nodal autoregulatory loop.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Iratni, Rabah -- Yan, Yu-Ting -- Chen, Canhe -- Ding, Jixiang -- Zhang, Yi -- Price, Sandy M -- Reinberg, Danny -- Shen, Michael M -- New York, N.Y. -- Science. 2002 Dec 6;298(5600):1996-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry, Division of Nucleic Acids Enzymology, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12471260" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Cell Line ; Crosses, Genetic ; DNA/metabolism ; DNA-Binding Proteins/metabolism ; *Embryonic and Fetal Development ; Female ; Forkhead Transcription Factors ; Gastrula/*physiology ; Gene Expression Regulation, Developmental ; Gene Targeting ; Heterozygote ; In Situ Hybridization ; Left-Right Determination Factors ; Male ; Mesoderm/cytology/physiology ; Mice ; Morphogenesis ; Mutation ; Nodal Protein ; Phenotype ; Protein Binding ; RNA Interference ; Recombinant Fusion Proteins/metabolism ; Repressor Proteins/genetics/*metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; *Signal Transduction ; Transcription Factors/metabolism ; Transforming Growth Factor beta/genetics/*metabolism
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    Historical essay. The early years of HIV/AIDS (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gallo, Robert C -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1728-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Human Virology and Department of Microbiology and Immunology, University of Maryland, Baltimore, MD 21201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12459576" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Serodiagnosis/history ; Acquired Immunodeficiency Syndrome/diagnosis/*history/immunology/virology ; CD4-Positive T-Lymphocytes/virology ; Cell Line ; Cells, Cultured ; France ; *HIV/classification/isolation & purification/physiology ; History, 20th Century ; Human T-lymphotropic virus 1/isolation & purification/physiology ; Human T-lymphotropic virus 2/isolation & purification/physiology ; Humans ; Interleukin-2/history/isolation & purification/physiology ; Patents as Topic/history ; RNA-Directed DNA Polymerase/history/isolation & purification/metabolism ; United States ; Virus Cultivation
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    An essential role of N-terminal arginylation in cardiovascular development (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-07-06
    Description: The enzymatic conjugation of arginine to the N-termini of proteins is a part of the ubiquitin-dependent N-end rule pathway of protein degradation. In mammals, three N-terminal residues-aspartate, glutamate, and cysteine-are substrates for arginylation. The mouse ATE1 gene encodes a family of Arg-tRNA-protein transferases (R-transferases) that mediate N-terminal arginylation. We constructed ATE1-lacking mouse strains and found that ATE1-/- embryos die with defects in heart development and in angiogenic remodeling of the early vascular plexus. Through biochemical analyses, we show that N-terminal cysteine, in contrast to N-terminal aspartate and glutamate, is oxidized before its arginylation by R-transferase, suggesting that the arginylation branch of the N-end rule pathway functions as an oxygen sensor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kwon, Yong Tae -- Kashina, Anna S -- Davydov, Ilia V -- Hu, Rong-Gui -- An, Jee Young -- Seo, Jai Wha -- Du, Fangyong -- Varshavsky, Alexander -- GM31530/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jul 5;297(5578):96-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, 147-75, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12098698" target="_blank"〉PubMed〈/a〉
    Keywords: Alkylation ; Aminoacyltransferases/*genetics/*metabolism ; Animals ; Aorta/embryology ; Arginine/*metabolism ; Aspartic Acid/metabolism ; Blood Vessels/*embryology ; Cell Line ; Cysteic Acid/metabolism ; Cysteine/metabolism ; Female ; Glutamic Acid/metabolism ; Heart/*embryology ; Heart Defects, Congenital/embryology ; Heart Septal Defects/embryology ; Hypoxia-Inducible Factor 1, alpha Subunit ; Male ; Mice ; Mice, Inbred C57BL ; Neovascularization, Physiologic ; Oxidation-Reduction ; Proteins/*metabolism ; Pulmonary Artery/embryology ; RGS Proteins/metabolism ; Recombinant Proteins/metabolism ; Sulfinic Acids/metabolism ; Transcription Factors/metabolism ; Transfection
    Print ISSN: 0036-8075
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    Toll-like receptor 4-dependent activation of dendritic cells by beta-defensin 2 (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-02
    Description: beta-Defensins are small antimicrobial peptides of the innate immune system produced in response to microbial infection of mucosal tissue and skin. We demonstrate that murine beta-defensin 2 (mDF2beta) acts directly on immature dendritic cells as an endogenous ligand for Toll-like receptor 4 (TLR-4), inducing up-regulation of costimulatory molecules and dendritic cell maturation. These events, in turn, trigger robust, type 1 polarized adaptive immune responses in vivo, suggesting that mDF2beta may play an important role in immunosurveillance against pathogens and, possibly, self antigens or tumor antigens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biragyn, Arya -- Ruffini, Pier Adelchi -- Leifer, Cynthia A -- Klyushnenkova, Elena -- Shakhov, Alexander -- Chertov, Oleg -- Shirakawa, Aiko K -- Farber, Joshua M -- Segal, David M -- Oppenheim, Joost J -- Kwak, Larry W -- N0L-CO-12400/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 1;298(5595):1025-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Experimental Transplantation and Immunology Branch, National Cancer Institute, Bethesda, MD 20892, USA. arya@mail.ncifcrf.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12411706" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Neoplasm/immunology ; Cancer Vaccines/immunology ; Cell Line ; Cytokines/biosynthesis ; Dendritic Cells/*immunology ; *Drosophila Proteins ; Female ; Humans ; Interferon-alpha/physiology ; Ligands ; Lipopolysaccharides/immunology/pharmacology ; Lymphocyte Culture Test, Mixed ; Membrane Glycoproteins/genetics/*physiology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Mice, Inbred C57BL ; Neoplasms/immunology/therapy ; Receptors, CCR6 ; Receptors, Cell Surface/genetics/*physiology ; Receptors, Chemokine/metabolism ; Recombinant Fusion Proteins/pharmacology ; Signal Transduction ; Toll-Like Receptor 4 ; Toll-Like Receptors ; Transfection ; beta-Defensins/pharmacology/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    An LRR receptor kinase involved in perception of a peptide plant hormone, phytosulfokine (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-25
    Description: The sulfated peptide phytosulfokine (PSK) is an intercellular signal that plays a key role in cellular dedifferentiation and proliferation in plants. Using ligand-based affinity chromatography, we purified a 120-kilodalton membrane protein, specifically interacting with PSK, from carrot microsomal fractions. The corresponding complementary DNA encodes a 1021-amino acid receptor kinase that contains extracellular leucine-rich repeats, a single transmembrane domain, and a cytoplasmic kinase domain. Overexpression of this receptor kinase in carrot cells caused enhanced callus growth in response to PSK and a substantial increase in the number of tritium-labeled PSK binding sites, suggesting that PSK and this receptor kinase act as a ligand-receptor pair.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsubayashi, Yoshikatsu -- Ogawa, Mari -- Morita, Akiko -- Sakagami, Youji -- New York, N.Y. -- Science. 2002 May 24;296(5572):1470-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate School of Bio-Agricultural Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan. matsu@agr.nagoya-u.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12029134" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding, Competitive ; Cell Line ; Chromatography, Affinity ; DNA, Complementary ; Daucus carota/cytology/*enzymology/genetics/growth & development ; Genes, Plant ; Glycosylation ; Leucine ; Ligands ; Microsomes/enzymology ; Molecular Sequence Data ; Molecular Weight ; Peptide Hormones ; *Plant Growth Regulators ; Plant Proteins/*chemistry/genetics/isolation & purification/*metabolism ; Plants, Genetically Modified ; Polymerase Chain Reaction ; Protein Structure, Tertiary ; Receptors, Cell Surface/*chemistry/genetics/isolation & purification/*metabolism ; Repetitive Sequences, Amino Acid
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    Partitioning of the matrix fraction of the Golgi apparatus during mitosis in animal cells (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-02
    Description: The Golgi apparatus is partitioned during mitosis in animal cells by a process of fragmentation, dispersal, and reassembly in each daughter cell. We fractionated the Golgi apparatus in vivo using the drug brefeldin A or a dominant-negative mutant of the Sar1p protein. After these treatments, Golgi enzymes moved back to the endoplasmic reticulum, leaving behind a matrix of Golgi structural proteins. Under these conditions, cells still entered and exited mitosis normally, and their Golgi matrix partitioned in a manner very similar to that of the complete organelle. Thus, the matrix may be the partitioning unit of the Golgi apparatus and may carry the Golgi enzyme-containing membranes into the daughter cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seemann, Joachim -- Pypaert, Marc -- Taguchi, Tomohiko -- Malsam, Jorg -- Warren, Graham -- New York, N.Y. -- Science. 2002 Feb 1;295(5556):848-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Ludwig Institute for Cancer Research, Yale University School of Medicine, 333 Cedar Street, Post Office Box 208002, New Haven, CT 06520-8002, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11823640" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase ; Animals ; Autoantigens ; Brefeldin A/pharmacology ; Cell Line ; Endoplasmic Reticulum/enzymology ; Golgi Apparatus/*metabolism/ultrastructure ; HeLa Cells ; Humans ; Interphase ; Intracellular Membranes/metabolism/ultrastructure ; Mannosidases/metabolism ; Membrane Proteins/metabolism ; Metaphase ; Microscopy, Electron ; Microscopy, Fluorescence ; *Mitosis ; Monomeric GTP-Binding Proteins/pharmacology ; N-Acetylglucosaminyltransferases/metabolism ; Protein Disulfide-Isomerases/metabolism ; Rats ; *Saccharomyces cerevisiae Proteins ; Telophase ; Vesicular Transport Proteins
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    Divergent regulation of dihydrofolate reductase between malaria parasite and human host (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-20
    Description: For half a century, successful antifolate therapy against Plasmodium falciparum malaria has been attributed to host-parasite differences in drug binding to dihydrofolate reductase-thymidylate synthase (DHFR-TS). Selectivity may also arise through previously unappreciated differences in regulation of this drug target. The DHFR-TS of Plasmodium binds its cognate messenger RNA (mRNA) and inhibits its own translation. However, unlike translational regulation of DHFR or TS in humans, DHFR-TS mRNA binding is not coupled to enzyme active sites. Thus, antifolate treatment does not relieve translational inhibition and parasites cannot replenish dead enzyme.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3830934/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3830934/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Kai -- Rathod, Pradipsinh K -- AI26912/AI/NIAID NIH HHS/ -- AI40956/AI/NIAID NIH HHS/ -- R01 AI026912/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):545-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, The Catholic University of America, Washington, DC 20064, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964483" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antimalarials/pharmacology ; Catalytic Domain ; Cell Line ; Folic Acid Antagonists/*pharmacology ; Host-Parasite Interactions ; Humans ; Multienzyme Complexes/chemistry/*genetics/*metabolism ; Plasmodium falciparum/*enzymology/genetics ; Protein Biosynthesis ; RNA, Messenger/genetics/metabolism ; RNA, Protozoan/genetics/metabolism ; Recombinant Proteins/genetics/metabolism ; Tetrahydrofolate Dehydrogenase/chemistry/*genetics/*metabolism ; Thymidylate Synthase/chemistry/*genetics/*metabolism ; Triazines/pharmacology
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    A heat-sensitive TRP channel expressed in keratinocytes (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-23
    Description: Mechanical and thermal cues stimulate a specialized group of sensory neurons that terminate in the skin. Three members of the transient receptor potential (TRP) family of channels are expressed in subsets of these neurons and are activated at distinct physiological temperatures. Here, we describe the cloning and characterization of a novel thermosensitive TRP channel. TRPV3 has a unique threshold: It is activated at innocuous (warm) temperatures and shows an increased response at noxious temperatures. TRPV3 is specifically expressed in keratinocytes; hence, skin cells are capable of detecting heat via molecules similar to those in heat-sensing neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peier, Andrea M -- Reeve, Alison J -- Andersson, David A -- Moqrich, Aziz -- Earley, Taryn J -- Hergarden, Anne C -- Story, Gina M -- Colley, Sian -- Hogenesch, John B -- McIntyre, Peter -- Bevan, Stuart -- Patapoutian, Ardem -- New York, N.Y. -- Science. 2002 Jun 14;296(5575):2046-9. Epub 2002 May 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genomics Institute of the Novartis Research Foundation, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12016205" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Newborn ; Blotting, Northern ; CHO Cells ; Capsaicin/*analogs & derivatives/pharmacology ; *Cation Transport Proteins ; Cell Line ; Cells, Cultured ; Cloning, Molecular ; Cricetinae ; Epidermis/cytology/innervation/metabolism ; Ganglia, Spinal/metabolism ; *Hot Temperature ; Humans ; In Situ Hybridization ; Ion Channels/chemistry/genetics/*metabolism ; Keratinocytes/*metabolism ; Membrane Potentials ; Mice ; Molecular Sequence Data ; Nerve Endings/physiology ; Neurons/physiology ; Patch-Clamp Techniques ; RNA, Messenger/genetics/metabolism ; Ruthenium Red/pharmacology ; Signal Transduction ; Spinal Cord/metabolism ; TRPV Cation Channels ; Temperature
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    Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-20
    Description: Simian virus 40 (SV40) utilizes endocytosis through caveolae for infectious entry into host cells. We found that after binding to caveolae, virus particles induced transient breakdown of actin stress fibers. Actin was then recruited to virus-loaded caveolae as actin patches that served as sites for actin "tail" formation. Dynamin II was also transiently recruited. These events depended on the presence of cholesterol and on the activation of tyrosine kinases that phosphorylated proteins in caveolae. They were necessary for formation of caveolae-derived endocytic vesicles and for infection of the cell. Thus, caveolar endocytosis is ligand-triggered and involves extensive rearrangement of the actin cytoskeleton.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pelkmans, Lucas -- Puntener, Daniel -- Helenius, Ari -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):535-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Swiss Federal Institute of Technology Zurich (ETHZ), HPM1 Building, ETH Honggerberg, CH-8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964480" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*physiology/ultrastructure ; Actins/*metabolism ; Animals ; Bicyclo Compounds, Heterocyclic/pharmacology ; Caveolae/*metabolism/ultrastructure/virology ; Caveolin 1 ; Caveolins/metabolism ; Cell Line ; Cholesterol/physiology ; *Depsipeptides ; Dynamins ; *Endocytosis ; GTP Phosphohydrolases/genetics/*metabolism ; Haplorhini ; Peptides, Cyclic/pharmacology ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/antagonists & inhibitors/metabolism ; Recombinant Fusion Proteins/metabolism ; Simian virus 40/*physiology ; Stress Fibers/metabolism ; Thiazoles/pharmacology ; Thiazolidines ; Transport Vesicles/metabolism
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    Embryonic stem cells. Australian agreement allows new lines (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dayton, Leigh -- New York, N.Y. -- Science. 2002 Apr 12;296(5566):238.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11951010" target="_blank"〉PubMed〈/a〉
    Keywords: Australia ; Cell Line ; Cloning, Organism/*legislation & jurisprudence ; Embryo Disposition ; *Embryo Research ; Embryo, Mammalian/*cytology ; Ethics Committees ; Fertilization in Vitro ; *Government Regulation ; Humans ; Research/*legislation & jurisprudence ; *Stem Cells
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Senescence induced by altered telomere state, not telomere loss (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-03-30
    Description: Primary human cells in culture invariably stop dividing and enter a state of growth arrest called replicative senescence. This transition is induced by programmed telomere shortening, but the underlying mechanisms are unclear. Here, we report that overexpression of TRF2, a telomeric DNA binding protein, increased the rate of telomere shortening in primary cells without accelerating senescence. TRF2 reduced the senescence setpoint, defined as telomere length at senescence, from 7 to 4 kilobases. TRF2 protected critically short telomeres from fusion and repressed chromosome-end fusions in presenescent cultures, which explains the ability of TRF2 to delay senescence. Thus, replicative senescence is induced by a change in the protected status of shortened telomeres rather than by a complete loss of telomeric DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karlseder, Jan -- Smogorzewska, Agata -- de Lange, Titia -- AG16643/AG/NIA NIH HHS/ -- CA76027/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 29;295(5564):2446-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Cell Biology and Genetics, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11923537" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Polyomavirus Transforming/genetics/metabolism ; *Cell Aging ; *Cell Division ; Cell Line ; Cells, Cultured ; DNA/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Humans ; Oncogene Proteins, Viral/genetics/metabolism ; Papillomavirus E7 Proteins ; *Repressor Proteins ; Retinoblastoma Protein/metabolism ; Retroviridae/genetics ; Telomere/metabolism/*physiology ; Telomeric Repeat Binding Protein 2 ; Transformation, Genetic ; Tumor Suppressor Protein p53/metabolism
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    Large-scale transcriptional activity in chromosomes 21 and 22 (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-05-04
    Description: The sequences of the human chromosomes 21 and 22 indicate that there are approximately 770 well-characterized and predicted genes. In this study, empirically derived maps identifying active areas of RNA transcription on these chromosomes have been constructed with the use of cytosolic polyadenylated RNA obtained from 11 human cell lines. Oligonucleotide arrays containing probes spaced on average every 35 base pairs along these chromosomes were used. When compared with the sequence annotations available for these chromosomes, it is noted that as much as an order of magnitude more of the genomic sequence is transcribed than accounted for by the predicted and characterized exons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kapranov, Philipp -- Cawley, Simon E -- Drenkow, Jorg -- Bekiranov, Stefan -- Strausberg, Robert L -- Fodor, Stephen P A -- Gingeras, Thomas R -- New York, N.Y. -- Science. 2002 May 3;296(5569):916-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Affymetrix, Santa Clara, CA 95051, USA., National Cancer Institute, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11988577" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Cell Nucleus/metabolism ; Chromosomes, Human, Pair 21/*genetics ; Chromosomes, Human, Pair 22/*genetics ; Computational Biology ; Contig Mapping ; Cytosol/metabolism ; DNA, Complementary ; DiGeorge Syndrome/genetics ; Exons ; Humans ; Oligonucleotide Array Sequence Analysis ; Oligonucleotide Probes ; *Physical Chromosome Mapping ; Polymerase Chain Reaction ; RNA, Messenger/*genetics/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; *Transcription, Genetic ; Tumor Cells, Cultured
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    Spider silk fibers spun from soluble recombinant silk produced in mammalian cells (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-01-19
    Description: Spider silks are protein-based "biopolymer" filaments or threads secreted by specialized epithelial cells as concentrated soluble precursors of highly repetitive primary sequences. Spider dragline silk is a flexible, lightweight fiber of extraordinary strength and toughness comparable to that of synthetic high-performance fibers. We sought to "biomimic" the process of spider silk production by expressing in mammalian cells the dragline silk genes (ADF-3/MaSpII and MaSpI) of two spider species. We produced soluble recombinant (rc)-dragline silk proteins with molecular masses of 60 to 140 kilodaltons. We demonstrated the wet spinning of silk monofilaments spun from a concentrated aqueous solution of soluble rc-spider silk protein (ADF-3; 60 kilodaltons) under modest shear and coagulation conditions. The spun fibers were water insoluble with a fine diameter (10 to 40 micrometers) and exhibited toughness and modulus values comparable to those of native dragline silks but with lower tenacity. Dope solutions with rc-silk protein concentrations 〉20% and postspinning draw were necessary to achieve improved mechanical properties of the spun fibers. Fiber properties correlated with finer fiber diameter and increased birefringence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lazaris, Anthoula -- Arcidiacono, Steven -- Huang, Yue -- Zhou, Jiang-Feng -- Duguay, Francois -- Chretien, Nathalie -- Welsh, Elizabeth A -- Soares, Jason W -- Karatzas, Costas N -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):472-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nexia Biotechnologies, Vaudreuil-Dorion, Quebec J7V 8P5, Canada. alazaris@nexiabiotech.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799236" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Biopolymers ; Birefringence ; Cattle ; Cell Line ; Cloning, Molecular ; Cricetinae ; Culture Media, Conditioned ; DNA, Complementary ; Elasticity ; Epithelial Cells/metabolism ; *Fibroins ; Materials Testing ; Mechanics ; Molecular Sequence Data ; Molecular Weight ; *Protein Biosynthesis ; Protein Structure, Secondary ; Proteins/chemistry/*genetics/isolation & purification ; Recombinant Proteins/biosynthesis/chemistry/isolation & purification ; Solubility ; Spiders/*genetics/metabolism ; Stress, Mechanical ; Tensile Strength ; Water
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    Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-07
    Description: The Golgi-localized, gamma-ear-containing, adenosine diphosphate ribosylation factor-binding proteins (GGAs) are multidomain proteins that bind mannose 6-phosphate receptors (MPRs) in the Golgi and have an essential role in lysosomal enzyme sorting. Here the GGAs and the coat protein adaptor protein-1 (AP-1) were shown to colocalize in clathrin-coated buds of the trans-Golgi networks of mouse L cells and human HeLa cells. Binding studies revealed a direct interaction between the hinge domains of the GGAs and the gamma-ear domain of AP-1. Further, AP-1 contained bound casein kinase-2 that phosphorylated GGA1 and GGA3, thereby causing autoinhibition. This could induce the directed transfer of the MPRs from GGAs to AP-1. MPRs that are defective in binding to GGAs are poorly incorporated into AP-1-containing clathrin-coated vesicles. Thus, the GGAs and AP-1 interact to package MPRs into AP-1-containing coated vesicles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doray, Balraj -- Ghosh, Pradipta -- Griffith, Janice -- Geuze, Hans J -- Kornfeld, Stuart -- R01 CA-08759/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 6;297(5587):1700-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12215646" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factors/*metabolism ; Adaptor Proteins, Vesicular Transport ; Animals ; Biological Transport ; Carrier Proteins/*metabolism ; Cattle ; Cell Line ; Clathrin-Coated Vesicles/metabolism ; HeLa Cells ; Humans ; L Cells (Cell Line) ; Membrane Proteins/*metabolism ; Mice ; Mutation ; Phosphorylation ; Protein Binding ; Receptor, IGF Type 2/genetics/*metabolism ; Recombinant Proteins/metabolism ; trans-Golgi Network/*metabolism
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    Materials science. Mammalian cells spin a spidery new yarn (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, Robert F -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):419-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799209" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biopolymers ; Cattle ; Cell Line ; Cricetinae ; Epithelial Cells/metabolism ; *Fibroins ; Genes ; Mechanics ; Molecular Weight ; *Protein Biosynthesis ; Proteins/chemistry/*genetics/isolation & purification ; Recombinant Proteins/biosynthesis/chemistry ; Spiders/*genetics
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    MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-02-16
    Description: Phosphorylation of mitogen-activated protein kinases (MAPKs) on specific tyrosine and threonine sites by MAP kinase kinases (MAPKKs) is thought to be the sole activation mechanism. Here, we report an unexpected activation mechanism for p38alpha MAPK that does not involve the prototypic kinase cascade. Rather it depends on interaction of p38alpha with TAB1 [transforming growth factor-beta-activated protein kinase 1 (TAK1)-binding protein 1] leading to autophosphorylation and activation of p38alpha. We detected formation of a TRAF6-TAB1-p38alpha complex and showed stimulus-specific TAB1-dependent and TAB1-independent p38alpha activation. These findings suggest that alternative activation pathways contribute to the biological responses of p38alpha to various stimuli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ge, Baoxue -- Gram, Hermann -- Di Padova, Franco -- Huang, Betty -- New, Liguo -- Ulevitch, Richard J -- Luo, Ying -- Han, Jiahuai -- AI41637/AI/NIAID NIH HHS/ -- HL07195/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 15;295(5558):1291-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11847341" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Binding Sites ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Line ; *Drosophila Proteins ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Humans ; Imidazoles/pharmacology ; *Intracellular Signaling Peptides and Proteins ; MAP Kinase Kinase 6 ; *MAP Kinase Signaling System ; Membrane Glycoproteins/metabolism ; Mitogen-Activated Protein Kinase 14 ; Mitogen-Activated Protein Kinase Kinases/metabolism ; Mitogen-Activated Protein Kinases/antagonists & ; inhibitors/chemistry/genetics/*metabolism ; Mutation ; Peptide Mapping ; Peroxynitrous Acid/pharmacology ; Phosphorylation ; Proteins/metabolism ; Pyridines/pharmacology ; Receptors, Cell Surface/metabolism ; Recombinant Fusion Proteins/metabolism ; TNF Receptor-Associated Factor 6 ; Toll-Like Receptors ; Tumor Necrosis Factor-alpha/pharmacology ; Two-Hybrid System Techniques ; p38 Mitogen-Activated Protein Kinases
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    Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-02
    Description: The hypoxia-inducible factors (HIFs) 1alpha and 2alpha are key mammalian transcription factors that exhibit dramatic increases in both protein stability and intrinsic transcriptional potency during low-oxygen stress. This increased stability is due to the absence of proline hydroxylation, which in normoxia promotes binding of HIF to the von Hippel-Lindau (VHL tumor suppressor) ubiquitin ligase. We now show that hypoxic induction of the COOH-terminal transactivation domain (CAD) of HIF occurs through abrogation of hydroxylation of a conserved asparagine in the CAD. Inhibitors of Fe(II)- and 2-oxoglutarate-dependent dioxygenases prevented hydroxylation of the Asn, thus allowing the CAD to interact with the p300 transcription coactivator. Replacement of the conserved Asn by Ala resulted in constitutive p300 interaction and strong transcriptional activity. Full induction of HIF-1alpha and -2alpha, therefore, relies on the abrogation of both Pro and Asn hydroxylation, which during normoxia occur at the degradation and COOH-terminal transactivation domains, respectively.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lando, David -- Peet, Daniel J -- Whelan, Dean A -- Gorman, Jeffrey J -- Whitelaw, Murray L -- New York, N.Y. -- Science. 2002 Feb 1;295(5556):858-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biosciences (Biochemistry), Adelaide University, SA 5005, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11823643" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Asparagine/*metabolism ; Basic Helix-Loop-Helix Transcription Factors ; Cell Hypoxia/*physiology ; Cell Line ; Humans ; Hydroxylation ; Hypoxia-Inducible Factor 1, alpha Subunit ; Mass Spectrometry ; Mice ; Mixed Function Oxygenases/metabolism ; Molecular Sequence Data ; Mutation ; Oxygen/*physiology ; Proline/metabolism ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; Trans-Activators/chemistry/genetics/*metabolism ; Transcription Factors/chemistry/genetics/*metabolism ; *Transcriptional Activation
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    Distinct effects of T-bet in TH1 lineage commitment and IFN-gamma production in CD4 and CD8 T cells (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-12
    Description: T-bet is a member of the T-box family of transcription factors that appears to regulate lineage commitment in CD4 T helper (TH) lymphocytes in part by activating the hallmark TH1 cytokine, interferon-gamma (IFN-gamma). IFN-gamma is also produced by natural killer (NK) cells and most prominently by CD8 cytotoxic T cells, and is vital for the control of microbial pathogens. Although T-bet is expressed in all these cell types, it is required for control of IFN-gamma production in CD4 and NK cells, but not in CD8 cells. This difference is also apparent in the function of these cell subsets. Thus, the regulation of a single cytokine, IFN-gamma, is controlled by distinct transcriptional mechanisms within the T cell lineage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Szabo, Susanne J -- Sullivan, Brandon M -- Stemmann, Claudia -- Satoskar, Abhay R -- Sleckman, Barry P -- Glimcher, Laurie H -- New York, N.Y. -- Science. 2002 Jan 11;295(5553):338-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11786644" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CD4-Positive T-Lymphocytes/*immunology/physiology ; Cell Differentiation ; Cell Line ; Cell Lineage ; Cytotoxicity, Immunologic ; Gene Targeting ; Immunization ; Immunoglobulin G/biosynthesis ; Interferon-gamma/*biosynthesis ; Interleukin-4/biosynthesis ; Interleukin-5/biosynthesis ; Killer Cells, Natural/immunology/metabolism ; Leishmania major ; Leishmaniasis, Cutaneous/immunology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; T-Box Domain Proteins ; T-Lymphocytes, Cytotoxic/*immunology ; Th1 Cells/*immunology ; Transcription Factors/deficiency/*genetics/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Transcriptional regulation of cortical neuron migration by POU domain factors (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-23
    Description: The identification of pathways mediated by the kinase Cdk5 and the ligand reelin has provided a conceptual framework for exploring the molecular mechanisms underlying proper lamination of the developing mammalian cerebral cortex. In this report, we identify a component of the regulation of Cdk5-mediated cortical lamination by genetic analysis of the roles of the class III POU domain transcription factors, Brn-1 and Brn-2, expressed during the development of the forebrain and coexpressed in most layer II-V cortical neurons. Brn-1 and Brn-2 appear to critically control the initiation of radial migration, redundantly regulating the cell-autonomous expression of the p35 and p39 regulatory subunits of Cdk5 in migrating cortical neurons, with Brn-1(-/-)/Brn-2(-/-) mice exhibiting cortical inversion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McEvilly, Robert J -- de Diaz, Marcela Ortiz -- Schonemann, Marcus D -- Hooshmand, Farideh -- Rosenfeld, Michael G -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1528-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department and School of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92037-0648, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859196" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/cytology/embryology/metabolism ; Cell Adhesion Molecules, Neuronal/genetics/metabolism ; Cell Line ; Cell Movement ; Cerebral Cortex/cytology/embryology/*metabolism ; Cyclin-Dependent Kinase 5 ; Cyclin-Dependent Kinases/metabolism ; Extracellular Matrix Proteins/genetics/metabolism ; Female ; Gene Targeting ; Hippocampus/cytology/embryology/metabolism ; Homeodomain Proteins ; In Situ Hybridization ; Male ; Mice ; Mutation ; Nerve Tissue Proteins/genetics/metabolism ; Neurons/*physiology ; Neuropeptides/genetics/*physiology ; POU Domain Factors ; Serine Endopeptidases ; Trans-Activators/genetics/*physiology ; Transcription Factors/genetics/*physiology ; *Transcription, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Signal transduction. Decoding NF-kappaB signaling (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ting, Alice Y -- Endy, Drew -- New York, N.Y. -- Science. 2002 Nov 8;298(5596):1189-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12424362" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Nucleus/metabolism ; Chemokine CCL5/genetics ; Chemokine CXCL10 ; Chemokines, CXC/genetics ; Computer Simulation ; Cytoplasm/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Feedback, Physiological ; *Gene Expression Regulation ; Humans ; I-kappa B Proteins/genetics/*metabolism ; Mice ; Mice, Knockout ; Models, Biological ; NF-kappa B/*metabolism ; Proto-Oncogene Proteins/genetics/metabolism ; *Signal Transduction ; Tumor Necrosis Factor-alpha/metabolism/pharmacology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Embryonic stem cells. Stem cells not so stealthy after all (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-07-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2002 Jul 12;297(5579):175-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12114602" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Differentiation ; Cell Line ; Embryo, Mammalian/*cytology ; Genetic Engineering ; Graft Rejection ; HeLa Cells ; Histocompatibility Antigens Class I/*analysis ; Humans ; Nuclear Transfer Techniques ; Stem Cell Transplantation ; Stem Cells/*immunology ; Teratoma/immunology ; Tissue Banks ; Transplantation Immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Production of alpha-1,3-galactosyltransferase knockout pigs by nuclear transfer cloning (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-05
    Description: The presence of galactose alpha-1,3-galactose residues on the surface of pig cells is a major obstacle to successful xenotransplantation. Here, we report the production of four live pigs in which one allele of the alpha-1,3-galactosyltransferase locus has been knocked out. These pigs were produced by nuclear transfer technology; clonal fetal fibroblast cell lines were used as nuclear donors for embryos reconstructed with enucleated pig oocytes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lai, Liangxue -- Kolber-Simonds, Donna -- Park, Kwang-Wook -- Cheong, Hee-Tae -- Greenstein, Julia L -- Im, Gi-Sun -- Samuel, Melissa -- Bonk, Aaron -- Rieke, August -- Day, Billy N -- Murphy, Clifton N -- Carter, David B -- Hawley, Robert J -- Prather, Randall S -- R44 RR15198/RR/NCRR NIH HHS/ -- T32 RR07004/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1089-92. Epub 2002 Jan 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Animal Science, University of Missouri, Columbia, MO 65211, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11778012" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; *Animals, Genetically Modified ; Cell Line ; *Cloning, Organism ; Embryo Transfer ; Female ; Fetus ; Fibroblasts ; Galactosyltransferases/*genetics ; *Gene Targeting ; Genetic Vectors ; Male ; Mutagenesis, Insertional ; Nuclear Transfer Techniques ; Pregnancy ; Recombination, Genetic ; Swine ; Swine, Miniature/embryology/*genetics ; Transfection
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    SynCAM, a synaptic adhesion molecule that drives synapse assembly (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-31
    Description: Synapses, the junctions between nerve cells through which they communicate, are formed by the coordinated assembly and tight attachment of pre- and postsynaptic specializations. We now show that SynCAM is a brain-specific, immunoglobulin domain-containing protein that binds to intracellular PDZ-domain proteins and functions as a homophilic cell adhesion molecule at the synapse. Expression of the isolated cytoplasmic tail of SynCAM in neurons inhibited synapse assembly. Conversely, expression of full-length SynCAM in nonneuronal cells induced synapse formation by cocultured hippocampal neurons with normal release properties. Glutamatergic synaptic transmission was reconstituted in these nonneuronal cells by coexpressing glutamate receptors with SynCAM, which suggests that a single type of adhesion molecule and glutamate receptor are sufficient for a functional postsynaptic response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biederer, Thomas -- Sara, Yildirim -- Mozhayeva, Marina -- Atasoy, Deniz -- Liu, Xinran -- Kavalali, Ege T -- Sudhof, Thomas C -- New York, N.Y. -- Science. 2002 Aug 30;297(5586):1525-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Basic Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. Thomas.Biederer@UTSouthwestern.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12202822" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/cytology/*physiology ; Brain Chemistry ; Cell Adhesion Molecules/chemistry/isolation & purification/*physiology ; Cell Adhesion Molecules, Neuronal/chemistry/isolation & purification/*physiology ; Cell Line ; Coculture Techniques ; Exocytosis ; Humans ; Immunoglobulins ; Molecular Sequence Data ; Neurons/physiology ; Prosencephalon/chemistry/physiology ; Protein Structure, Tertiary ; Rats ; Receptors, AMPA/physiology ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Amino Acid ; Synapses/chemistry/*physiology ; Synaptic Transmission/physiology ; Transfection ; Tumor Suppressor Proteins
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    A stem cell molecular signature (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-14
    Description: Mechanisms regulating self-renewal and cell fate decisions in mammalian stem cells are poorly understood. We determined global gene expression profiles for mouse and human hematopoietic stem cells and other stages of the hematopoietic hierarchy. Murine and human hematopoietic stem cells share a number of expressed gene products, which define key conserved regulatory pathways in this developmental system. Moreover, in the mouse, a portion of the genetic program of hematopoietic stem cells is shared with embryonic and neural stem cells. This overlapping set of gene products represents a molecular signature of stem cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ivanova, Natalia B -- Dimos, John T -- Schaniel, Christoph -- Hackney, Jason A -- Moore, Kateri A -- Lemischka, Ihor R -- DK42989/DK/NIDDK NIH HHS/ -- DK54493/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 18;298(5593):601-4. Epub 2002 Sep 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12228721" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animals ; Cell Communication ; Cell Cycle ; Cell Differentiation ; Cell Line ; Cell Lineage ; Cell Separation ; Cells, Cultured ; Computational Biology ; Embryo, Mammalian/cytology ; Expressed Sequence Tags ; *Gene Expression ; *Gene Expression Profiling ; Genes, Homeobox ; Hematopoiesis ; Hematopoietic Stem Cell Transplantation ; Hematopoietic Stem Cells/*physiology ; Humans ; Mice ; Neurons/cytology ; Oligonucleotide Array Sequence Analysis ; Signal Transduction ; Stem Cells/*physiology ; Totipotent Stem Cells/*physiology ; Transcription, Genetic
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    Signal transduction. Scaffolding proteins--more than meets the eye (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, Gary -- New York, N.Y. -- Science. 2002 Feb 15;295(5558):1249-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Colorado Health Sciences Center, Denver, CO 80262, USA. gary.johnson@uchsc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11847330" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Amino Acid Motifs ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Carrier Proteins/chemistry/*metabolism ; Cell Line ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Humans ; Imidazoles/pharmacology ; *Intracellular Signaling Peptides and Proteins ; MAP Kinase Kinase 6 ; MAP Kinase Kinase Kinases/metabolism ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinase 14 ; Mitogen-Activated Protein Kinases/chemistry/*metabolism ; Phosphorylation ; Protein Binding ; Proteins/metabolism ; Pyridines/pharmacology ; Recombinant Proteins/metabolism ; TNF Receptor-Associated Factor 6 ; p38 Mitogen-Activated Protein Kinases
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    Role of Toxoplasma gondii myosin A in powering parasite gliding and host cell invasion (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-26
    Description: Obligate intracellular apicomplexan parasites rely on gliding motion powered by their actomyosin system to disperse throughout tissues and to penetrate host cells. Toxoplasma gondii myosin A has been implicated in this process, but direct proof has been lacking. We designed a genetic screen to generate a tetracycline-inducible transactivator system in T. gondii. The MyoA gene was disrupted in the presence of a second regulatable copy of MyoA. Conditional removal of this myosin caused severe impairment in host cell invasion and parasite spreading in cultured cells, and unambiguously established the pathogenic function of this motor in an animal model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meissner, Markus -- Schluter, Dirk -- Soldati, Dominique -- New York, N.Y. -- Science. 2002 Oct 25;298(5594):837-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Imperial College of Science, Technology and Medicine, Imperial College Road, London SW7 2AZ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12399593" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcimycin/pharmacology ; Calcium/metabolism ; Cell Line ; Cells, Cultured ; Exocytosis ; Genetic Vectors ; Humans ; Mice ; Movement ; Nonmuscle Myosin Type IIA/genetics/*physiology ; Organelles/metabolism ; Protozoan Proteins/genetics/physiology ; Tetracycline/pharmacology ; Toxoplasma/genetics/growth & development/*pathogenicity/*physiology ; Toxoplasmosis, Animal/*parasitology ; Trans-Activators/metabolism ; Transfection ; Transgenes ; Virulence ; Virulence Factors/*physiology
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    S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-17
    Description: Matrix metalloproteinases (MMPs) are implicated in the pathogenesis of neurodegenerative diseases and stroke. However, the mechanism of MMP activation remains unclear. We report that MMP activation involves S-nitrosylation. During cerebral ischemia in vivo, MMP-9 colocalized with neuronal nitric oxide synthase. S-Nitrosylation activated MMP-9 in vitro and induced neuronal apoptosis. Mass spectrometry identified the active derivative of MMP-9, both in vitro and in vivo, as a stable sulfinic or sulfonic acid, whose formation was triggered by S-nitrosylation. These findings suggest a potential extracellular proteolysis pathway to neuronal cell death in which S-nitrosylation activates MMPs, and further oxidation results in a stable posttranslational modification with pathological activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, Zezong -- Kaul, Marcus -- Yan, Boxu -- Kridel, Steven J -- Cui, Jiankun -- Strongin, Alex -- Smith, Jeffrey W -- Liddington, Robert C -- Lipton, Stuart A -- AR08505/AR/NIAMS NIH HHS/ -- P01 HD29587/HD/NICHD NIH HHS/ -- R01 AR42750/AR/NIAMS NIH HHS/ -- R01 CA 69306/CA/NCI NIH HHS/ -- R01 EY05477/EY/NEI NIH HHS/ -- R01 EY09024/EY/NEI NIH HHS/ -- R01 NS41207/NS/NINDS NIH HHS/ -- T32 AG00252/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 16;297(5584):1186-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Neuroscience and Aging, Program in Cell Adhesion and Extracellular Matrix Biology, The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12183632" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Brain Ischemia/*enzymology/pathology ; Cell Line ; Cells, Cultured ; Cerebral Cortex/blood supply/*enzymology/pathology ; Cysteine/*analogs & derivatives/metabolism/pharmacology ; Enzyme Activation ; Enzyme Precursors/genetics/metabolism ; Humans ; Matrix Metalloproteinase 9/chemistry/*metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Models, Molecular ; Neurons/*physiology ; Nitric Oxide/metabolism ; Nitric Oxide Synthase/antagonists & inhibitors/metabolism ; Nitric Oxide Synthase Type I ; Oxidation-Reduction ; Phenylmercuric Acetate/*analogs & derivatives/pharmacology ; Rats ; Recombinant Proteins/metabolism ; Reperfusion ; S-Nitrosothiols/*metabolism/pharmacology ; Signal Transduction ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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    Amphiphysin 2 (Bin1) and T-tubule biogenesis in muscle (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-17
    Description: In striated muscle, the plasma membrane forms tubular invaginations (transverse tubules or T-tubules) that function in depolarization-contraction coupling. Caveolin-3 and amphiphysin were implicated in their biogenesis. Amphiphysin isoforms have a putative role in membrane deformation at endocytic sites. An isoform of amphiphysin 2 concentrated at T-tubules induced tubular plasma membrane invaginations when expressed in nonmuscle cells. This property required exon 10, a phosphoinositide-binding module. In developing myotubes, amphiphysin 2 and caveolin-3 segregated in tubular and vesicular portions of the T-tubule system, respectively. These findings support a role of the bilayer-deforming properties of amphiphysin at T-tubules and, more generally, a physiological role of amphiphysin in membrane deformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Eunkyung -- Marcucci, Melissa -- Daniell, Laurie -- Pypaert, Marc -- Weisz, Ora A -- Ochoa, Gian-Carlo -- Farsad, Khashayar -- Wenk, Markus R -- De Camilli, Pietro -- CA46128/CA/NCI NIH HHS/ -- NS36251/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 16;297(5584):1193-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Howard Hughes Medical Institute, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12183633" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CHO Cells ; Caveolin 3 ; Caveolins/metabolism ; Cell Differentiation ; Cell Line ; Cell Membrane/metabolism ; Cell Membrane Structures/metabolism/*ultrastructure ; Cricetinae ; Dynamins ; Exons ; GTP Phosphohydrolases/metabolism ; Liposomes/metabolism ; Mice ; Microscopy, Electron ; Morphogenesis ; *Muscle Development ; Muscle, Skeletal/metabolism/*ultrastructure ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Phosphatidylinositol 4,5-Diphosphate/metabolism ; Protein Isoforms ; Protein Structure, Tertiary ; RNA, Small Interfering ; RNA, Untranslated/metabolism ; Recombinant Fusion Proteins/metabolism ; Transfection
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    DNA repair pathway stimulated by the forkhead transcription factor FOXO3a through the Gadd45 protein (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-20
    Description: The signaling pathway from phosphoinositide 3-kinase to the protein kinase Akt controls organismal life-span in invertebrates and cell survival and proliferation in mammals by inhibiting the activity of members of the FOXO family of transcription factors. We show that mammalian FOXO3a also functions at the G2 to M checkpoint in the cell cycle and triggers the repair of damaged DNA. By gene array analysis, FOXO3a was found to modulate the expression of several genes that regulate the cellular response to stress at the G2-M checkpoint. The growth arrest and DNA damage response gene Gadd45a appeared to be a direct target of FOXO3a that mediates part of FOXO3a's effects on DNA repair. These findings indicate that in mammals FOXO3a regulates the resistance of cells to stress by inducing DNA repair and thereby may also affect organismal life-span.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tran, Hien -- Brunet, Anne -- Grenier, Jill M -- Datta, Sandeep R -- Fornace, Albert J Jr -- DiStefano, Peter S -- Chiang, Lillian W -- Greenberg, Michael E -- NIHP30-HD18655/HD/NICHD NIH HHS/ -- P01-HD24926/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):530-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Children's Hospital and Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964479" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Chromones/pharmacology ; DNA Damage ; *DNA Repair ; DNA-Binding Proteins/genetics/*metabolism ; Forkhead Transcription Factors ; G2 Phase ; Gene Expression Profiling ; Gene Expression Regulation ; Genes, Reporter ; Humans ; Intracellular Signaling Peptides and Proteins ; Mitosis ; Morpholines/pharmacology ; Promoter Regions, Genetic ; Proteins/genetics/*metabolism ; Rats ; Recombinant Fusion Proteins/metabolism ; Tamoxifen/*analogs & derivatives/pharmacology ; Transcription Factors/genetics/*metabolism ; Transfection ; Ultraviolet Rays
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Tissue-specific regulation of retinal and pituitary precursor cell proliferation (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-07-20
    Description: Mammalian organogenesis requires the expansion of pluripotent precursor cells before the subsequent determination of specific cell types, but the tissue-specific molecular mechanisms that regulate the initial expansion of primordial cells remain poorly defined. We have genetically established that Six6 homeodomain factor, acting as a strong tissue-specific repressor, regulates early progenitor cell proliferation during mammalian retinogenesis and pituitary development. Six6, in association with Dach corepressors, regulates proliferation by directly repressing cyclin-dependent kinase inhibitors, including the p27Kip1 promoter. These data reveal a molecular mechanism by which a tissue-specific transcriptional repressor-corepressor complex can provide an organ-specific strategy for physiological expansion of precursor populations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Xue -- Perissi, Valentina -- Liu, Forrest -- Rose, David W -- Rosenfeld, Michael G -- 484/B/Telethon/Italy -- 5F32DK09814/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 16;297(5584):1180-3. Epub 2002 Jul 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Medicine, University of California, San Diego, School of Medicine, 9500 Gilman Drive, Room 345, La Jolla, CA 92093-0648, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12130660" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Cell Cycle ; Cell Cycle Proteins/genetics/metabolism ; *Cell Division ; Cell Line ; Cyclin-Dependent Kinase Inhibitor p27 ; Cyclin-Dependent Kinases/antagonists & inhibitors ; Embryo, Mammalian/cytology ; Eye Proteins/metabolism ; Homeodomain Proteins/*genetics/*metabolism ; Mice ; Nuclear Proteins/metabolism ; Organ Specificity ; Pituitary Gland/*cytology/embryology ; Promoter Regions, Genetic ; Proto-Oncogene Proteins/genetics/metabolism ; Recombinant Fusion Proteins/metabolism ; Repressor Proteins/metabolism ; Retina/*cytology/embryology ; Retinal Ganglion Cells/cytology/physiology ; Stem Cells/*physiology ; Trans-Activators/*genetics/*metabolism ; Transcription Factors ; Transcription, Genetic ; Transfection ; Tumor Suppressor Proteins/genetics/metabolism ; Up-Regulation
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Human cloning. U.N. split over full or partial cloning ban (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2002 Nov 15;298(5597):1316-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12434028" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; *Cloning, Organism ; Embryo, Mammalian/cytology ; Humans ; *International Cooperation ; *Research Embryo Creation ; *Stem Cells ; *United Nations
    Print ISSN: 0036-8075
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  • 88
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    Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-04
    Description: Huntington's disease (HD) is an inherited neurodegenerative disease caused by expansion of a polyglutamine tract in the huntingtin protein. Transcriptional dysregulation has been implicated in HD pathogenesis. Here, we report that huntingtin interacts with the transcriptional activator Sp1 and coactivator TAFII130. Coexpression of Sp1 and TAFII130 in cultured striatal cells from wild-type and HD transgenic mice reverses the transcriptional inhibition of the dopamine D2 receptor gene caused by mutant huntingtin, as well as protects neurons from huntingtin-induced cellular toxicity. Furthermore, soluble mutant huntingtin inhibits Sp1 binding to DNA in postmortem brain tissues of both presymptomatic and affected HD patients. Understanding these early molecular events in HD may provide an opportunity to interfere with the effects of mutant huntingtin before the development of disease symptoms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dunah, Anthone W -- Jeong, Hyunkyung -- Griffin, April -- Kim, Yong-Man -- Standaert, David G -- Hersch, Steven M -- Mouradian, M Maral -- Young, Anne B -- Tanese, Naoko -- Krainc, Dimitri -- 5R37AG13617/AG/NIA NIH HHS/ -- AT00613/AT/NCCIH NIH HHS/ -- NS02174/NS/NINDS NIH HHS/ -- NS34361/NS/NINDS NIH HHS/ -- NS35255/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2238-43. Epub 2002 May 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Center for Aging, Genetics and Neurodegeneration, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11988536" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; Caudate Nucleus/metabolism ; Cell Death ; Cell Line ; Cell Nucleus/metabolism ; Cells, Cultured ; Corpus Striatum/cytology/embryology/metabolism ; DNA/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Down-Regulation ; Gene Expression Regulation ; Humans ; Huntington Disease/*genetics/metabolism ; Mice ; Mice, Transgenic ; Mutation ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Neurons/physiology ; Nuclear Proteins/chemistry/genetics/*metabolism ; Peptides ; Promoter Regions, Genetic ; Rats ; Receptors, Dopamine D2/genetics ; Solubility ; Sp1 Transcription Factor/chemistry/*metabolism ; *TATA-Binding Protein Associated Factors ; *Transcription Factor TFIID ; Transcription Factors/chemistry/*metabolism ; *Transcription, Genetic ; Transfection ; Trinucleotide Repeat Expansion ; Two-Hybrid System Techniques
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 89
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    Structural basis for gluten intolerance in celiac sprue (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-28
    Description: Celiac Sprue, a widely prevalent autoimmune disease of the small intestine, is induced in genetically susceptible individuals by exposure to dietary gluten. A 33-mer peptide was identified that has several characteristics suggesting it is the primary initiator of the inflammatory response to gluten in Celiac Sprue patients. In vitro and in vivo studies in rats and humans demonstrated that it is stable toward breakdown by all gastric, pancreatic, and intestinal brush-border membrane proteases. The peptide reacted with tissue transglutaminase, the major autoantigen in Celiac Sprue, with substantially greater selectivity than known natural substrates of this extracellular enzyme. It was a potent inducer of gut-derived human T cell lines from 14 of 14 Celiac Sprue patients. Homologs of this peptide were found in all food grains that are toxic to Celiac Sprue patients but are absent from all nontoxic food grains. The peptide could be detoxified in in vitro and in vivo assays by exposure to a bacterial prolyl endopeptidase, suggesting a strategy for oral peptidase supplement therapy for Celiac Sprue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shan, Lu -- Molberg, Oyvind -- Parrot, Isabelle -- Hausch, Felix -- Filiz, Ferda -- Gray, Gary M -- Sollid, Ludvig M -- Khosla, Chaitan -- R01 DK100619/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 27;297(5590):2275-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering, Stanford University, Stanford, CA 94305-5025, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351792" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Celiac Disease/*immunology/therapy ; Cell Line ; Edible Grain/chemistry ; Endopeptidases/metabolism ; Epitopes, T-Lymphocyte ; GTP-Binding Proteins/metabolism ; Gliadin/*chemistry/*immunology/metabolism ; HLA-DQ Antigens/immunology ; Humans ; Immunodominant Epitopes ; Intestinal Mucosa/enzymology/*immunology ; Intestine, Small/enzymology/*immunology ; Lymphocyte Activation ; Microvilli/enzymology ; Molecular Sequence Data ; Peptide Fragments/chemistry/immunology ; Rats ; Recombinant Proteins/chemistry/metabolism ; Sequence Homology, Amino Acid ; Serine Endopeptidases/administration & dosage/metabolism/therapeutic use ; T-Lymphocytes/*immunology ; Transglutaminases/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 90
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    Swedish research. New stem cell fund raises hackles (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2002 Oct 18;298(5593):517.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12386310" target="_blank"〉PubMed〈/a〉
    Keywords: *Biomedical Research ; Cell Line ; *Embryo Research ; Embryo, Mammalian/cytology ; Foundations ; Humans ; Peer Review, Research ; *Research Support as Topic ; *Stem Cells ; Sweden
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 91
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    A kinetic framework for a mammalian RNA polymerase in vivo (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-26
    Description: We have analyzed the kinetics of assembly and elongation of the mammalian RNA polymerase I complex on endogenous ribosomal genes in the nuclei of living cells with the use of in vivo microscopy. We show that components of the RNA polymerase I machinery are brought to ribosomal genes as distinct subunits and that assembly occurs via metastable intermediates. With the use of computational modeling of imaging data, we have determined the in vivo elongation time of the polymerase, and measurements of recruitment and incorporation frequencies show that incorporation of components into the assembling polymerase is inefficient. Our data provide a kinetic and mechanistic framework for the function of a mammalian RNA polymerase in living cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dundr, Miroslav -- Hoffmann-Rohrer, Urs -- Hu, Qiyue -- Grummt, Ingrid -- Rothblum, Lawrence I -- Phair, Robert D -- Misteli, Tom -- New York, N.Y. -- Science. 2002 Nov 22;298(5598):1623-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Cancer Institute (NCI), National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446911" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Catalytic Domain ; Cell Line ; Cell Nucleolus/metabolism ; Cell Nucleus/*metabolism ; Computer Simulation ; DNA, Ribosomal/genetics ; Fluorescence ; Fluorescence Recovery After Photobleaching ; Fluorescent Dyes ; Green Fluorescent Proteins ; Haplorhini ; Humans ; In Situ Hybridization, Fluorescence ; Kinetics ; Least-Squares Analysis ; Luminescent Proteins ; Microscopy ; Pol1 Transcription Initiation Complex Proteins/metabolism ; Probability ; Promoter Regions, Genetic ; Protein Subunits ; RNA Polymerase I/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Transcription, Genetic ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 92
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    Orc6 involved in DNA replication, chromosome segregation, and cytokinesis (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-10
    Description: Origin recognition complex (ORC) proteins serve as a landing pad for the assembly of a multiprotein prereplicative complex, which is required to initiate DNA replication. During mitosis, the smallest subunit of human ORC, Orc6, localizes to kinetochores and to a reticular-like structure around the cell periphery. As chromosomes segregate during anaphase, the reticular structures align along the plane of cell division and some Orc6 localizes to the midbody before cells separate. Silencing of Orc6 expression by small interfering RNA (siRNA) resulted in cells with multipolar spindles, aberrant mitosis, formation of multinucleated cells, and decreased DNA replication. Prolonged periods of Orc6 depletion caused a decrease in cell proliferation and increased cell death. These results implicate Orc6 as an essential gene that coordinates chromosome replication and segregation with cytokinesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prasanth, Supriya G -- Prasanth, Kannanganattu V -- Stillman, Bruce -- CA13106/CA/NCI NIH HHS/ -- P01 CA013106/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 9;297(5583):1026-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12169736" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bromodeoxyuridine/metabolism ; Cell Death ; *Cell Division ; Cell Line ; Cell Nucleus/metabolism ; Cells, Cultured ; Centromere/metabolism ; *Chromosome Segregation ; Chromosomes, Human/*metabolism ; *DNA Replication ; DNA-Binding Proteins/genetics/metabolism/*physiology ; Fluorescent Antibody Technique ; Gene Silencing ; Humans ; Kinetochores/metabolism ; Mitosis ; Origin Recognition Complex ; Phenotype ; Polyploidy ; RNA, Small Interfering ; RNA, Untranslated/metabolism/pharmacology ; Recombinant Fusion Proteins/analysis ; Saccharomyces cerevisiae Proteins ; Spindle Apparatus/ultrastructure ; Transfection ; Tumor Cells, Cultured
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    Stem cell research. Cloning pioneer heads toward human frontier (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):37-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364759" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; *Cloning, Organism/economics/legislation & jurisprudence ; Embryo, Mammalian/*cytology ; Ethics Committees, Research ; Great Britain ; History, 21st Century ; Humans ; Nuclear Transfer Techniques ; Patents as Topic ; Research ; Research Support as Topic ; *Stem Cells
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 94
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    Complete development of mosquito phases of the malaria parasite in vitro (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-26
    Description: Methods for reproducible in vitro development of the mosquito stages of malaria parasites to produce infective sporozoites have been elusive for over 40 years. We have cultured gametocytes of Plasmodium berghei through to infectious sporozoites with efficiencies similar to those recorded in vivo and without the need for salivary gland invasion. Oocysts developed extracellularly in a system whose essential elements include co-cultured Drosophila S2 cells, basement membrane matrix, and insect tissue culture medium. Sporozoite production required the presence of para-aminobenzoic acid. The entire life cycle of P. berghei, a useful model malaria parasite, can now be achieved in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Al-Olayan, Ebtesam M -- Beetsma, Annette L -- Butcher, Geoff A -- Sinden, Robert E -- Hurd, Hilary -- New York, N.Y. -- Science. 2002 Jan 25;295(5555):677-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Applied Entomology and Parasitology, School of Life Sciences, Keele University, Staffordshire ST5 5BG, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11809973" target="_blank"〉PubMed〈/a〉
    Keywords: 4-Aminobenzoic Acid/pharmacology ; Aedes ; Aerobiosis ; Animals ; Anopheles/parasitology ; Cell Line ; Coculture Techniques ; Collagen ; Culture Media ; Drosophila ; Drug Combinations ; Hydrogen-Ion Concentration ; Laminin ; Life Cycle Stages ; Malaria/parasitology ; Male ; Mice ; Plasmodium berghei/cytology/drug effects/*growth & development ; Proteoglycans
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  • 95
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    Systems analysis of Ran transport (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-19
    Description: The separate components of nucleocytoplasmic transport have been well characterized, including the key regulatory role of Ran, a guanine nucleotide triphosphatase. However, the overall system behavior in intact cells is difficult to analyze because the dynamics of these components are interdependent. We used a combined experimental and computational approach to study Ran transport in vivo. The resulting model provides the first quantitative picture of Ran flux between the nuclear and cytoplasmic compartments in eukaryotic cells. The model predicts that the Ran exchange factor RCC1, and not the flux capacity of the nuclear pore complex (NPC), is the crucial regulator of steady-state flux across the NPC. Moreover, it provides the first estimate of the total in vivo flux (520 molecules per NPC per second and predicts that the transport system is robust.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, Alicia E -- Slepchenko, Boris M -- Schaff, James C -- Loew, Leslie M -- Macara, Ian G -- GM-50526/GM/NIGMS NIH HHS/ -- NCRR-RR13186/RR/NCRR NIH HHS/ -- NIH-GM-20438/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):488-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Cell Signaling, Department of Pharmacology, University of Virginia, Charlottesville, VA 22908, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799242" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Animals ; *Cell Cycle Proteins ; Cell Line ; Cell Nucleus/metabolism ; *Computer Simulation ; Cricetinae ; Cytoplasm/metabolism ; Diffusion ; Fluorescence ; Guanine Nucleotide Exchange Factors/metabolism ; Guanosine Triphosphate/metabolism ; Kinetics ; Mathematics ; *Models, Biological ; Mutation ; Nuclear Pore/*metabolism ; *Nuclear Proteins ; Nucleocytoplasmic Transport Proteins/metabolism ; Recombinant Proteins/metabolism ; Temperature ; ran GTP-Binding Protein/genetics/*metabolism
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  • 96
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    Chemical ecology: missed opportunities? (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eisner, Thomas -- Berenbaum, May -- New York, N.Y. -- Science. 2002 Mar 15;295(5562):1973.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11896239" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biochemical Phenomena ; *Biochemistry ; *Biological Factors/chemistry ; *Biology ; Chemical Phenomena ; Chemistry ; *Ecology ; Ecosystem ; *Molecular Biology ; Research Support as Topic ; United States
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  • 97
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    Vitamin D receptor as an intestinal bile acid sensor (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-23
    Description: The vitamin D receptor (VDR) mediates the effects of the calcemic hormone 1alpha,25-dihydroxyvitamin D3 [1,25(OH)2D3]. We show that VDR also functions as a receptor for the secondary bile acid lithocholic acid (LCA), which is hepatotoxic and a potential enteric carcinogen. VDR is an order of magnitude more sensitive to LCA and its metabolites than are other nuclear receptors. Activation of VDR by LCA or vitamin D induced expression in vivo of CYP3A, a cytochrome P450 enzyme that detoxifies LCA in the liver and intestine. These studies offer a mechanism that may explain the proposed protective effects of vitamin D and its receptor against colon cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Makishima, Makoto -- Lu, Timothy T -- Xie, Wen -- Whitfield, G Kerr -- Domoto, Hideharu -- Evans, Ronald M -- Haussler, Mark R -- Mangelsdorf, David J -- New York, N.Y. -- Science. 2002 May 17;296(5571):1313-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9050, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12016314" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Aryl Hydrocarbon Hydroxylases ; Binding, Competitive ; COS Cells ; Cell Line ; Colonic Neoplasms/prevention & control ; Cytochrome P-450 CYP3A ; Cytochrome P-450 Enzyme System/genetics/metabolism ; DNA-Binding Proteins/metabolism ; Dimerization ; Gene Expression Regulation, Enzymologic ; Histone Acetyltransferases ; Humans ; Intestine, Small/*metabolism ; Ligands ; Lithocholic Acid/analogs & derivatives/*metabolism/pharmacology ; Male ; Mice ; Nuclear Receptor Coactivator 1 ; Oxidoreductases, N-Demethylating/genetics/metabolism ; Promoter Regions, Genetic ; Rats ; Receptors, Calcitriol/agonists/genetics/*metabolism ; Receptors, Cytoplasmic and Nuclear/metabolism ; Receptors, Steroid/metabolism ; Transcription Factors/metabolism ; Transfection
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    Biomedicine. Gluten and the gut-lessons for immune regulation (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schuppan, Detlef -- Hahn, Eckhart G -- New York, N.Y. -- Science. 2002 Sep 27;297(5590):2218-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉First Department of Medicine, University of Erlangen-Nuernberg, Ulmenweg 18, 91054 Erlangen, Germany. detlef.schuppan@med1.imed.uni-erlangen.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351776" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Celiac Disease/epidemiology/*immunology/therapy ; Cell Line ; Dendritic Cells/immunology ; Diet ; GTP-Binding Proteins/metabolism ; Gliadin/*immunology/metabolism ; Glutens/*analogs & derivatives/*immunology/metabolism ; HLA-DQ Antigens/*immunology ; Humans ; Intestines/enzymology/*immunology ; Lymphocyte Activation ; Mice ; Peptide Fragments/immunology/isolation & purification/metabolism ; Serine Endopeptidases/administration & dosage/metabolism ; T-Lymphocytes/*immunology ; Transglutaminases/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 99
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    Modulation of NMDA receptor-dependent calcium influx and gene expression through EphB receptors (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-19
    Description: Protein-protein interactions and calcium entry through the N-methyl-d-aspartate (NMDA)-type glutamate receptor regulate synaptic development and plasticity in the central nervous system. The EphB receptor tyrosine kinases are localized at excitatory synapses where they cluster and associate with NMDA receptors. We identified a mechanism whereby EphBs modulate NMDA receptor function. EphrinB2 activation of EphB in primary cortical neurons potentiates NMDA receptor-dependent influx of calcium. Treatment of cells with ephrinB2 led to NMDA receptor tyrosine phosphorylation through activation of the Src family of tyrosine kinases. These ephrinB2-dependent events result in enhanced NMDA receptor-dependent gene expression. Our findings indicate that ephrinB2 stimulation of EphB modulates the functional consequences of NMDA receptor activation and suggest a mechanism whereby activity-independent and activity-dependent signals converge to regulate the development and remodeling of synaptic connections.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takasu, Mari A -- Dalva, Matthew B -- Zigmond, Richard E -- Greenberg, Michael E -- CA43855/CA/NCI NIH HHS/ -- HD18655/HD/NICHD NIH HHS/ -- NS12651/NS/NINDS NIH HHS/ -- NS17512/NS/NINDS NIH HHS/ -- R01 NS045500/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):491-5. Epub 2001 Dec 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Children's Hospital, and the Department of Neurobiology, Harvard Medical School, 300 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799243" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain-Derived Neurotrophic Factor/pharmacology ; Calcium/*metabolism ; Cell Line ; Cells, Cultured ; Cerebral Cortex/cytology/embryology ; Cyclic AMP Response Element-Binding Protein/metabolism ; Ephrin-B2 ; *Gene Expression Regulation ; Genes, Reporter ; Glutamic Acid/metabolism ; Humans ; Immunoglobulin Fc Fragments ; Membrane Proteins/*metabolism/pharmacology ; Models, Neurological ; Mutation ; Neurons/*metabolism ; Phosphorylation ; Phosphotyrosine/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-fyn ; Rats ; Receptor Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; Receptor, EphB4 ; Receptors, Eph Family ; Receptors, N-Methyl-D-Aspartate/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism/pharmacology ; Signal Transduction ; Synapses/metabolism ; Transcription, Genetic ; src-Family Kinases/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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    Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-04
    Description: Many proteins associated with the plasma membrane are known to partition into submicroscopic sphingolipid- and cholesterol-rich domains called lipid rafts, but the determinants dictating this segregation of proteins in the membrane are poorly understood. We suppressed the tendency of Aequorea fluorescent proteins to dimerize and targeted these variants to the plasma membrane using several different types of lipid anchors. Fluorescence resonance energy transfer measurements in living cells revealed that acyl but not prenyl modifications promote clustering in lipid rafts. Thus the nature of the lipid anchor on a protein is sufficient to determine submicroscopic localization within the plasma membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zacharias, David A -- Violin, Jonathan D -- Newton, Alexandra C -- Tsien, Roger Y -- 2T32 GM07752/GM/NIGMS NIH HHS/ -- DK54441/DK/NIDDK NIH HHS/ -- NS27177/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 May 3;296(5569):913-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Biomedical Sciences Graduate Program, and, Howard Hughes Medical Institute, University of California, San Diego, La Jolla, CA 92093-0647, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11988576" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Animals ; Bacterial Proteins/chemistry/*metabolism ; Caveolin 1 ; Caveolins/metabolism ; Cell Line ; Detergents ; Dimerization ; Dogs ; Energy Transfer ; Fluorescence ; Green Fluorescent Proteins ; Luminescent Proteins/chemistry/*metabolism ; Membrane Microdomains/*metabolism ; Myristic Acid/metabolism ; Oligopeptides/chemistry/*metabolism ; Palmitic Acid/metabolism ; Protein Prenylation ; Recombinant Fusion Proteins/metabolism ; Solubility ; Spectrometry, Fluorescence ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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