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  • Animals  (591)
  • Molecular Sequence Data  (248)
  • American Association for the Advancement of Science (AAAS)  (702)
  • American Institute of Physics (AIP)
  • 1995-1999  (702)
  • 1990-1994
  • 1945-1949
  • 1996  (702)
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  • American Association for the Advancement of Science (AAAS)  (702)
  • American Institute of Physics (AIP)
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  • 1995-1999  (702)
  • 1990-1994
  • 1945-1949
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  • 101
    Publication Date: 1996-04-05
    Description: The rotavirus nonstructural glycoprotein NSP4 is an intracellular receptor that mediates the acquisition of a transient membrane envelope as subviral particles bud into the endoplasmic reticulum. NSP4 also causes an increase in intracellular calcium in insect cells. Purified NSP4 or a peptide corresponding to NSP4 residues 114 to 135 induced diarrhea in young (6 to 10 days old) CD1 mice. This disease response was age-dependent, dose-dependent, and specific. Electrophysiologic data from intestinal mucosa showed that the NSP4 114-135 peptide potentiates chloride secretion by a calcium-dependent signaling pathway. Diarrhea is induced when NSP4, acting as a viral enterotoxin, triggers a signal transduction pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ball, J M -- Tian, P -- Zeng, C Q -- Morris, A P -- Estes, M K -- DK 30144/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 Apr 5;272(5258):101-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8600515" target="_blank"〉PubMed〈/a〉
    Keywords: *Aging ; Amino Acid Sequence ; Animals ; Calcium/metabolism ; Carbachol/pharmacology ; Chlorides/metabolism ; Colforsin/pharmacology ; Diarrhea/*etiology/prevention & control/virology ; Enterotoxins/*toxicity ; Glycoproteins/immunology/*toxicity ; Immune Sera/administration & dosage ; Immunization ; In Vitro Techniques ; Intestinal Mucosa/drug effects/secretion ; Mice ; Molecular Sequence Data ; Peptide Fragments/toxicity ; Receptors, Virus ; Rotavirus/*pathogenicity ; Rotavirus Infections/prevention & control/*virology ; Signal Transduction ; Toxins, Biological ; Viral Nonstructural Proteins/immunology/*toxicity
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  • 102
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-04-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1996 Apr 19;272(5260):349.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602520" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Clocks ; *Circadian Rhythm ; Cricetinae ; Culture Techniques ; Humans ; Melatonin/*biosynthesis ; Mesocricetus ; Retina/metabolism/*physiology ; Suprachiasmatic Nucleus/physiology
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  • 103
    Publication Date: 1996-04-19
    Description: Nitric oxide (NO) is associated with broad-spectrum antimicrobial activity of particular importance in infections caused by intracellular pathogens. An insertion mutation in the metL gene of Salmonella typhimurium conferred specific hypersusceptibility to S-nitrosothiol NO-donor compounds and attenuated virulence of the organism in mice. The metL gene product catalyzes two proximal metabolic steps required for homocysteine biosynthesis. S-Nitrosothiol resistance was restored by exogenous homocysteine or introduction of the metL gene on a plasmid. Measurement of expression of the homocysteine-sensitive metH gene indicated that S-nitrosothiols may directly deplete intracellular homocysteine. Homocysteine may act as an endogenous NO antagonist in diverse processes including infection, atherosclerosis, and neurologic disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉De Groote, M A -- Testerman, T -- Xu, Y -- Stauffer, G -- Fang, F C -- AI32463/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Apr 19;272(5260):414-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Colorado Health Sciences Center, Denver, CO 80262, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602531" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aspartokinase Homoserine Dehydrogenase/genetics/*metabolism ; Base Sequence ; Drug Resistance, Microbial ; Female ; Glutathione/analogs & derivatives/pharmacology ; Homocysteine/metabolism/pharmacology/*physiology ; *Mercaptoethanol ; Mice ; Mice, Inbred C3H ; Microbial Sensitivity Tests ; Molecular Sequence Data ; Mutagenesis, Insertional ; Nitric Oxide/*antagonists & inhibitors/metabolism ; Nitroso Compounds/pharmacology ; S-Nitrosoglutathione ; *S-Nitrosothiols ; Salmonella Infections, Animal/microbiology ; Salmonella typhimurium/cytology/drug effects/pathogenicity/*physiology ; Virulence
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  • 104
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-01-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1996 Jan 5;271(5245):32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539594" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Eritrea ; *Fossils ; History, Ancient ; Hominidae/*anatomy & histology ; Humans ; Skull/*anatomy & histology
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  • 105
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-01-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1996 Jan 5;271(5245):33.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539595" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*embryology/genetics ; *Caenorhabditis elegans Proteins ; *Embryonic Development ; Female ; Fertilization ; Genes, Helminth ; Helminth Proteins/genetics/*physiology ; Male ; Mutation ; *Nuclear Proteins ; Oocytes/physiology ; Spermatozoa/*chemistry/physiology
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  • 106
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-01-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560255" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Archaea/classification ; Bacteria/classification ; Cyanobacteria ; Enzymes/*chemistry ; *Eukaryotic Cells/classification/enzymology ; *Evolution, Molecular ; Fossils ; Phylogeny ; *Prokaryotic Cells/classification/enzymology
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  • 107
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-02-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1056-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599078" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Fungal Proteins/chemistry/*physiology ; GTP-Binding Proteins/*physiology ; *GTPase-Activating Proteins ; Humans ; Phosphoproteins/chemistry/*physiology ; Proteins/chemistry/*physiology ; *RGS Proteins ; *Saccharomyces cerevisiae Proteins ; *Signal Transduction
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  • 108
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-02-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1996 Feb 2;271(5249):594-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8571119" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Culture Techniques ; Cells, Cultured ; Female ; Fertilization in Vitro ; Granulosa Cells/cytology/*physiology ; Mice ; Oocytes/cytology/*physiology ; *Oogenesis ; Organ Culture Techniques ; Ovary/physiology
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  • 109
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-01-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):447.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560254" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; BCG Vaccine/genetics/*immunology/therapeutic use ; Bacterial Proteins/immunology ; Cytokines/*biosynthesis/genetics/immunology ; Genetic Engineering ; Humans ; Mice ; Mycobacterium tuberculosis/immunology ; Neoplasms/therapy ; T-Lymphocytes/immunology ; Tuberculosis/immunology/prevention & control ; Vaccines, Synthetic/genetics/*immunology/therapeutic use
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  • 110
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-07-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, M -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):183.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8668994" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier Proteins/chemistry/*metabolism ; Crystallography, X-Ray ; DNA-Binding Proteins/chemistry/*metabolism ; *Gene Expression Regulation ; Genetic Therapy ; Growth Hormone/*genetics ; Heat-Shock Proteins/chemistry/*metabolism ; Humans ; *Immunophilins ; Mice ; *Phosphotransferases (Alcohol Group Acceptor) ; Polyenes/chemistry/*metabolism ; Sirolimus ; TOR Serine-Threonine Kinases ; Tacrolimus Binding Proteins
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  • 111
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-03-15
    Description: Phosphorylated products of phosphatidylinositol play critical roles in the regulation of membrane traffic, in addition to their classical roles as second messengers in signal transduction at the cell surface. Growing evidence suggests that phosphorylation-dephosphorylation of the polar heads of phosphoinositides (polyphosphorylated inositol lipids) in specific intracellular locations signals either the recruitment or the activation of proteins essential for vesicular transport. Cross talk between phosphatidylinositol metabolites and guanosine triphosphatases is an important feature of these regulatory mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉De Camilli, P -- Emr, S D -- McPherson, P S -- Novick, P -- CA-46128/CA/NCI NIH HHS/ -- CA-58689/CA/NCI NIH HHS/ -- GM-32703/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1533-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599109" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport ; Cell Membrane/*metabolism ; Coated Vesicles/metabolism ; Endocytosis ; Exocytosis ; GTP Phosphohydrolases/metabolism ; Golgi Apparatus/metabolism ; Inositol Phosphates/*metabolism ; Intracellular Membranes/*metabolism ; Membrane Proteins/*metabolism ; Phosphatidylinositols/*metabolism ; Phosphorylation ; Yeasts/metabolism
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  • 112
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-10-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lander, E S -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):536-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge, MA 02142, USA. lander@genome.wi.mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8928008" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bioethics ; DNA/genetics ; Gene Expression ; Genetic Techniques ; Genetic Variation ; *Human Genome Project ; Humans ; Mice ; *Molecular Biology/education ; Proteins/chemistry/metabolism ; RNA/genetics ; Sequence Analysis, DNA
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  • 113
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-11-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1306.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8966602" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Clocks ; Bombyx/genetics/*metabolism ; Brain/metabolism ; Cell Nucleus/metabolism ; *Circadian Rhythm ; Cloning, Molecular ; *Drosophila Proteins ; Drosophila melanogaster/genetics/metabolism ; Gene Expression Regulation ; Genes, Insect ; Neurons/*metabolism ; Nuclear Proteins/genetics/*metabolism ; Period Circadian Proteins ; Proteins/genetics/metabolism ; RNA, Antisense/metabolism ; RNA, Messenger/metabolism
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  • 114
    Publication Date: 1996-08-23
    Description: Bruton's tyrosine kinase (BTK) is a member of the SRC-related TEC family of protein tyrosine kinases (PTKs). DT-40 lymphoma B cells, rendered BTK-deficient through targeted disruption of the btk gene by homologous recombination knockout, did not undergo radiation-induced apoptosis, but cells with disrupted lyn or syk genes did. Introduction of the wild-type, or a SRC homology 2 domain or a plecstrin homology domain mutant (but not a kinase domain mutant), human btk gene into BTK-deficient cells restored the apoptotic response to radiation. Thus, BTK is the PTK responsible for triggering radiation-induced apoptosis of lymphoma B cells, and its kinase domain is indispensable for the apoptotic response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Uckun, F M -- Waddick, K G -- Mahajan, S -- Jun, X -- Takata, M -- Bolen, J -- Kurosaki, T -- R01-CA-42111/CA/NCI NIH HHS/ -- R01-CA-42633/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 23;273(5278):1096-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Signal Transduction Laboratory, Biotherapy Institute, University of Minnesota, Roseville, MN 55113, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688094" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; B-Lymphocytes/cytology/enzymology/*radiation effects ; Chickens ; Gamma Rays ; Gene Targeting ; Humans ; Immunoglobulin M/immunology ; Lymphoma, B-Cell/enzymology/*pathology ; Phosphorylation ; Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; Receptors, Antigen, B-Cell/immunology/physiology ; Tumor Cells, Cultured ; src Homology Domains
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  • 115
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-05-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gura, T -- New York, N.Y. -- Science. 1996 May 17;272(5264):954-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638140" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/physiopathology ; Animals ; Asthma/physiopathology ; Chemokine CCL11 ; Chemokine CCL2/isolation & purification/physiology ; Chemokines/antagonists & inhibitors/isolation & purification/*physiology ; *Chemokines, CC ; Chemotactic Factors, Eosinophil/isolation & purification/physiology ; Chemotaxis, Leukocyte ; Cytokines/isolation & purification/physiology ; Humans ; Inflammation/drug therapy/*immunology/physiopathology ; Interleukin-8/isolation & purification/physiology ; Monocytes/physiology ; Neoplasms/physiopathology ; Neutrophils/physiology ; Respiratory Distress Syndrome, Adult/physiopathology
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  • 116
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-05-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Landfield, P W -- McEwan, B S -- Sapolsky, R M -- Meaney, M J -- New York, N.Y. -- Science. 1996 May 31;272(5266):1249-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650531" target="_blank"〉PubMed〈/a〉
    Keywords: *Aging ; Animals ; Cell Count ; Cell Death ; Hippocampus/*cytology ; Humans ; Memory Disorders/etiology ; Neurons/*cytology ; Rats
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  • 117
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-06-21
    Description: The human beta T cell receptor (TCR) locus, comprising a complex family of genes, has been sequenced. The locus contains two types of coding elements--TCR elements (65 variable gene segments and two clusters of diversity, joining, and constant segments) and eight trypsinogen genes --that constitute 4.6 percent of the DNA. Genome-wide interspersed repeats and locus-specific repeats span 30 and 47 percent, respectively, of the 685-kilobase sequence. A comparison of the germline variable elements with their approximately 300 complementary DNA counterparts reveals marked differential patterns of variable gene expression, the importance of exonuclease activity in generating TCR diversity, and the predominant tendency for only functional variable elements to be present in complementary DNA libraries.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rowen, L -- Koop, B F -- Hood, L -- New York, N.Y. -- Science. 1996 Jun 21;272(5269):1755-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biotechnology, University of Washington, Seattle 98195-7730, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650574" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Biological Evolution ; Chromosomes, Human, Pair 7 ; Chromosomes, Human, Pair 9 ; DNA, Complementary/genetics ; Exons ; Genetic Variation ; Humans ; Introns ; Molecular Sequence Data ; *Multigene Family ; Polymorphism, Genetic ; Promoter Regions, Genetic ; Pseudogenes ; RNA Splicing ; Receptors, Antigen, T-Cell, alpha-beta/*genetics ; Repetitive Sequences, Nucleic Acid ; Translocation, Genetic ; Trypsinogen/genetics
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  • 118
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-02-09
    Description: The reaper gene (rpr) is important for the activation of apoptosis in Drosophila. To investigate whether rpr expression is sufficient to induce apoptosis, transgenic flies were generated that express rpr complementary DNA or the rpr open reading frame in cells that normally live. Transcription of rpr from a heat-inducible promoter rapidly caused wide-spread ectopic apoptosis and organismal death. Ectopic overexpression of rpr in the developing retina resulted in eye ablation. The occurrence of cell death was highly sensitive to the dosage of the transgene. Because cell death induced by the protein encoded by rpr (RPR) could be blocked by the baculovirus p35 protein, RPR appears to activate a death program mediated by a ced-3/ICE (interleukin-1 converting enzyme)-like protease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉White, K -- Tahaoglu, E -- Steller, H -- New York, N.Y. -- Science. 1996 Feb 9;271(5250):805-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cutaneous Biology Research Center, Massachusetts General Hospital, Charlestown 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8628996" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; *Apoptosis ; Caspase 1 ; Cysteine Endopeptidases/metabolism ; DNA, Complementary/genetics ; Drosophila/cytology/embryology/*genetics ; *Drosophila Proteins ; Gene Dosage ; Gene Expression ; *Genes, Insect ; Hot Temperature ; Inhibitor of Apoptosis Proteins ; Mutation ; Open Reading Frames ; Peptides/*genetics/physiology ; Photoreceptor Cells, Invertebrate/cytology ; Transgenes ; Viral Proteins/genetics/physiology
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  • 119
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-06-28
    Description: Activated epidermal growth factor (EGF) receptors induce the formation of various complexes of intracellular signaling proteins that are mediated by SRC homology 2 (SH2) and SH3 domains. The activated receptors are also rapidly internalized into the endocytotic compartment and degraded in lysosomes. EGF stimulation of canine epithelial cells induced a rapid and transient association of the SH3-SH2-SH3 protein GRB2 with dynamin, a guanosine triphosphatase that regulates endocytosis. Disruption of GRB2 interactions by microinjection of a peptide corresponding to the GRB2 SH2 domain or its phosphopeptide ligand blocked EGF receptor endocytosis; other SH2 domains that bind EGF receptors or antibodies that neutralize RAS did not. Both activation and termination of EGF signaling appear to be regulated by the diverse interactions of GRB2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Z -- Moran, M F -- New York, N.Y. -- Science. 1996 Jun 28;272(5270):1935-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Banting and Best Department of Medical Research, University of Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658166" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Animals ; Antibodies, Monoclonal ; Cell Line ; Dogs ; Dynamins ; *Endocytosis/drug effects ; Epidermal Growth Factor/pharmacology ; GRB2 Adaptor Protein ; GTP Phosphohydrolases/metabolism ; Microinjections ; Peptide Fragments/pharmacology ; Proteins/*metabolism ; Receptor, Epidermal Growth Factor/*metabolism ; Receptors, Transferrin/metabolism ; Recombinant Fusion Proteins/pharmacology ; Signal Transduction ; ras Proteins/immunology/physiology ; src Homology Domains/physiology
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  • 120
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-03-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bork, P -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1431-2; author reply 1434-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596918" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amino Acid Sequence ; Animals ; DNA, Complementary ; Female ; Frameshifting, Ribosomal ; Humans ; Male ; Molecular Sequence Data ; Protein Sorting Signals/chemistry ; Protein-Tyrosine Kinases/*chemistry/genetics ; Proto-Oncogene Proteins/*chemistry/genetics ; Receptor Protein-Tyrosine Kinases/*chemistry/genetics ; Sequence Alignment ; Sperm-Ovum Interactions ; Spermatozoa/*chemistry
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  • 121
    Publication Date: 1996-07-05
    Description: The Caenorhabditis elegans LIN-12 and GLP-1 proteins are members of the LIN-12/Notch family of receptors for intercellular signals that specify cell fate. Evidence presented here suggests that the intracellular domains of LIN-12 and GLP-1 interact with the C. elegans EMB-5 protein and that the emb-5 gene functions in the same pathway as the lin-12 and glp-1 genes. EMB-5 is similar in sequence to a yeast protein that controls chromatin structure. Hence, a direct consequence of LIN-12 or GLP-1 activation may be an alteration of chromatin structure that produces changes in transcriptional activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hubbard, E J -- Dong, Q -- Greenwald, I -- GM37602/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 5;273(5271):112-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University College of Physicians and Surgeons, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658178" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*cytology/embryology/genetics/*metabolism ; *Caenorhabditis elegans Proteins ; Cell Lineage ; Chromatin/metabolism ; Gene Expression Regulation, Developmental ; Genes, Helminth ; Helminth Proteins/genetics/*metabolism ; Meiosis ; Membrane Proteins/genetics/*metabolism ; Mitosis ; Mutation ; Receptors, Notch ; *Signal Transduction ; Temperature ; Transcription Factors/genetics/*metabolism
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  • 122
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-04-05
    Description: Innate immunity has been considered only to provide rapid, incomplete antimicrobial host defense until the slower, more definitive acquired immune response develops. However, innate immunity may have an additional role in determining which antigens the acquired immune system responds to and the nature of that response. Knowledge of the molecules and pathways involved may create new therapeutic options for infectious and autoimmune diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fearon, D T -- Locksley, R M -- AI26918/AI/NIAID NIH HHS/ -- AI30663/AI/NIAID NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1996 Apr 5;272(5258):50-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Immunology Unit, Department of Medicine, University of Cambridge School of Clinical Medicine, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8600536" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibody Formation ; Antigens/immunology ; Autoimmune Diseases/immunology/therapy ; B-Lymphocytes/immunology ; Cytokines/immunology ; Humans ; Immunity, Active/*immunology ; Immunity, Innate/*immunology ; Immunotherapy ; Infection/immunology/therapy ; T-Lymphocytes/immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 123
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-04-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bothwell, M -- New York, N.Y. -- Science. 1996 Apr 26;272(5261):506-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Washington, Seattle, WA 98192, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614797" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; NF-kappa B/physiology ; Nerve Growth Factors/pharmacology ; Neurons/cytology ; Receptor, Nerve Growth Factor ; Receptors, Nerve Growth Factor/*physiology ; Receptors, Tumor Necrosis Factor/physiology ; Schwann Cells/*physiology ; *Signal Transduction ; Tumor Necrosis Factor-alpha/physiology
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  • 124
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-03-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickelgren, I -- New York, N.Y. -- Science. 1996 Mar 1;271(5253):1229-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638100" target="_blank"〉PubMed〈/a〉
    Keywords: *Aging ; Animals ; Cell Count ; Cell Death ; Hippocampus/*cytology ; Humans ; Memory Disorders/*etiology ; Neurons/*cytology ; Pyramidal Cells/*cytology ; Rats
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  • 125
    Publication Date: 1996-04-12
    Description: Very few of the enzymes required for eukaryotic precursor ribosomal RNA (pre-rRNA) processing have been identified. Ribonuclease (RNase) MRP was characterized as a nuclease that cleaves mitochondrial replication primers, but it is predominantly nucleolar. Previous genetic evidence revealed that this ribonucleoprotein is required, directly or indirectly, for cleavage of the yeast pre-rRNA in vivo at site A3. Here, an in vitro processing system that accurately reproduces this cleavage is described. Biochemical purification and the use of extracts depleted of the MRP RNA demonstrate that endonucleolytic cleavage of the pre-rRNA is directly mediated by RNase MRP. This establishes a role for RNase MRP in the nucleolus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lygerou, Z -- Allmang, C -- Tollervey, D -- Seraphin, B -- New York, N.Y. -- Science. 1996 Apr 12;272(5259):268-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602511" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Nucleolus/enzymology ; Endoribonucleases/isolation & purification/*metabolism ; Molecular Sequence Data ; RNA Precursors/*metabolism ; *RNA Processing, Post-Transcriptional ; RNA, Ribosomal/*metabolism ; Ribonucleoproteins/metabolism ; Saccharomyces cerevisiae/*enzymology
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  • 126
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-10-11
    Description: In Saccharomyces cerevisiae, MAD2 is required for mitotic arrest if the spindle assembly is perturbed. The human homolog of MAD2 was isolated and shown to be a necessary component of the mitotic checkpoint in HeLa cells by antibody electroporation experiments. Human, or Homo sapiens, MAD2 (hsMAD2) was localized at the kinetochore after chromosome condensation but was no longer observed at the kinetochore in metaphase, suggesting that MAD2 might monitor the completeness of the spindle-kinetochore attachment. Finally, T47D, a human breast tumor cell line that is sensitive to taxol and nocodazole, had reduced MAD2 expression and failed to arrest in mitosis after nocodazole treatment. Thus, defects in the mitotic checkpoint may contribute to the sensitivity of certain tumors to mitotic spindle inhibitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Y -- Benezra, R -- P30-CA-08748/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):246-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Genetics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8824189" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anaphase ; *Calcium-Binding Proteins ; Carrier Proteins/chemistry/*genetics/*metabolism ; Cell Cycle Proteins ; Electroporation ; HeLa Cells ; Humans ; Interphase ; Kinetochores/*metabolism ; Mad2 Proteins ; Metaphase ; *Mitosis ; Molecular Sequence Data ; Nocodazole/pharmacology ; Paclitaxel/pharmacology ; Repressor Proteins ; Spindle Apparatus/drug effects/*metabolism ; Tumor Cells, Cultured
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  • 127
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-05-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Birchler, J A -- New York, N.Y. -- Science. 1996 May 24;272(5265):1190-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638167" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA-Binding Proteins/genetics/metabolism ; *Dosage Compensation, Genetic ; Drosophila/*genetics ; Drosophila Proteins ; Female ; Male ; Nuclear Proteins/genetics/metabolism ; Transcription Factors/genetics/metabolism ; X Chromosome/*genetics/metabolism
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  • 128
    Publication Date: 1996-02-02
    Description: The Rho guanosine 5'-triphosphatase (GTPase) cycles between the active guanosine triphosphate (GTP)-bound form and the inactive guanosine diphosphate-bound form and regulates cell adhesion and cytokinesis, but how it exerts these actions is unknown. The yeast two-hybrid system was used to clone a complementary DNA for a protein (designated Rhophilin) that specifically bound to GTP-Rho. The Rho-binding domain of this protein has 40 percent identity with a putative regulatory domain of a protein kinase, PKN. PKN itself bound to GTP-Rho and was activated by this binding both in vitro and in vivo. This study indicates that a serine-threonine protein kinase is a Rho effector and presents an amino acid sequence motif for binding to GTP-Rho that may be shared by a family of Rho target proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watanabe, G -- Saito, Y -- Madaule, P -- Ishizaki, T -- Fujisawa, K -- Morii, N -- Mukai, H -- Ono, Y -- Kakizuka, A -- Narumiya, S -- New York, N.Y. -- Science. 1996 Feb 2;271(5249):645-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Kyoto University Faculty of Medicine, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8571126" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; Enzyme Activation ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/chemistry/*metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Membrane Proteins/*metabolism ; Mice ; Molecular Sequence Data ; Phosphorylation ; Protein Kinase C/chemistry/*metabolism ; *Protein-Serine-Threonine Kinases ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Signal Transduction ; ras Proteins ; *rho GTP-Binding Proteins ; rhoA GTP-Binding Protein ; rhoB GTP-Binding Protein
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  • 129
    Publication Date: 1996-08-09
    Description: alpha2-Adrenergic receptors (alpha2ARs) present in the brainstem decrease blood pressure and are targets for clinically effective antihypertensive drugs. The existence of three alpha2AR subtypes, the lack of subtype-specific ligands, and the cross-reactivity of alpha2AR agonists with imidazoline receptors has precluded an understanding of the role of individual alpha2AR subtypes in the hypotensive response. Gene targeting was used to introduce a point mutation into the alpha2aAR subtype in the mouse genome. The hypotensive response to alpha2AR agonists was lost in the mutant mice, demonstrating that the alpha2aAR subtype plays a principal role in this response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacMillan, L B -- Hein, L -- Smith, M S -- Piascik, M T -- Limbird, L E -- HL38120/HL/NHLBI NIH HHS/ -- HL43671/HL/NHLBI NIH HHS/ -- HL48638/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 9;273(5276):801-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8670421" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic alpha-2 Receptor Agonists ; Adrenergic alpha-Agonists/pharmacology ; Animals ; Antihypertensive Agents/pharmacology ; Base Sequence ; Blood Pressure/drug effects/*physiology ; Brain Stem/physiology ; Brimonidine Tartrate ; Gene Targeting ; Heart Rate/drug effects/physiology ; Imidazoles/pharmacology ; Medetomidine ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Point Mutation ; Quinoxalines/pharmacology ; Receptors, Adrenergic, alpha-2/genetics/metabolism/*physiology
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  • 130
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-10-25
    Description: Human leukocyte antigen (HLA)-DM is a critical participant in antigen presentation that catalyzes the release of class II-associated invariant chain-derived peptides (CLIP) from newly synthesized class II histocompatibility molecules, freeing the peptide-binding site for acquisition of antigenic peptides. The mechanism for the selective release of CLIP but not other peptides is unknown. DM was found to enhance the rate of peptide dissociation to an extent directly proportional to the intrinsic rate of peptide dissociation from HLA-DR, regardless of peptide sequence. Thus, CLIP is rapidly released in the presence of DM, because its intrinsic rate of dissociation is relatively high. In antigen presentation, DM has the potential to markedly enhance the rate of peptide exchange, favoring the presentation of peptides with slower intrinsic rates of dissociation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weber, D A -- Evavold, B D -- Jensen, P E -- AI30554/AI/NIAID NIH HHS/ -- AI33614/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):618-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, GA 30322, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849454" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigen Presentation ; Antigens, Differentiation, B-Lymphocyte/*metabolism ; Binding Sites ; HLA-D Antigens/*metabolism ; HLA-DR Antigens/immunology/*metabolism ; Histocompatibility Antigens Class II/*metabolism ; Humans ; Kinetics ; Molecular Sequence Data ; Peptides/immunology/*metabolism ; Recombinant Fusion Proteins/metabolism
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  • 131
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-11-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, N -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1302.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8966600" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD95/*physiology ; *Apoptosis ; Fas Ligand Protein ; Humans ; Melanoma/chemistry/*immunology ; Membrane Glycoproteins/analysis/*physiology ; Mice ; T-Lymphocytes, Cytotoxic/*cytology/immunology ; Tumor Cells, Cultured ; *Tumor Escape
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  • 132
    Publication Date: 1996-02-23
    Description: Human CD2 locus control region (LCR) sequences are shown here to be essential for establishing an open chromatin configuration. Transgenic mice carrying an hCD2 mini-gene attached only to the 3' CD2 transcriptional enhancer exhibited variegated expression when the transgene integrated in the centromere. In contrast, mice carrying a transgene with additional 3' sequences showed no variegation even when the latter integrated in centromeric positions. This result suggests that LCRs operate by ensuring an open chromatin configuration and that a short region, with no enhancer activity, functions in the establishment, maintenance, or both of an open chromatin domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Festenstein, R -- Tolaini, M -- Corbella, P -- Mamalaki, C -- Parrington, J -- Fox, M -- Miliou, A -- Jones, M -- Kioussis, D -- TGT06S01/Telethon/Italy -- TGT95000/Telethon/Italy -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1123-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Immunology, National Institute for Medical Research, The Ridgeway, London, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599090" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD2/analysis/*genetics ; Centromere/genetics ; Enhancer Elements, Genetic ; *Gene Expression Regulation ; Heterochromatin/*genetics ; Humans ; In Situ Hybridization, Fluorescence ; Mice ; Mice, Transgenic ; *Regulatory Sequences, Nucleic Acid ; T-Lymphocytes/*immunology ; *Transgenes
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  • 133
    Publication Date: 1996-05-24
    Description: The entorhinal cortex provides the major cortical input to the hippocampus, and both structures have been implicated in memory processes. The dynamics of neuronal circuits in the entorhinal-hippocampal system were studied in slices by optical imaging with high spatial and temporal resolution. Reverberation of neural activity was detected in the entorhinal cortex and was more prominent when the inhibition due to gamma-aminobutyric acid was slightly suppressed. Neural activity was transferred in a frequency-dependent way from the entorhinal cortex to the hippocampus. The entorhinal neuronal circuit could contribute to memory processes by holding information and selectively gating the entry of information into the hippocampus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Iijima, T -- Witter, M P -- Ichikawa, M -- Tominaga, T -- Kajiwara, R -- Matsumoto, G -- New York, N.Y. -- Science. 1996 May 24;272(5265):1176-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular and Cellular Neuroscience Section, Electrotechnical Laboratory, Ibaraki, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638163" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bicuculline/pharmacology ; Electric Stimulation ; Entorhinal Cortex/*physiology ; GABA Antagonists/pharmacology ; Hippocampus/*physiology ; Image Processing, Computer-Assisted ; In Vitro Techniques ; Male ; Memory/*physiology ; Microscopy, Fluorescence ; Neural Pathways ; Rats ; Rats, Wistar ; Synaptic Transmission/drug effects
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  • 134
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-06-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, N -- New York, N.Y. -- Science. 1996 Jun 7;272(5267):1416-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8633226" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD36/metabolism ; Chondroitin Sulfates/*metabolism ; Erythrocytes/metabolism/*parasitology ; Female ; Genes, Protozoan ; Humans ; Malaria/immunology/*parasitology ; Malaria, Falciparum/immunology/parasitology ; Placenta/*parasitology ; Plasmodium/genetics/*physiology ; Plasmodium falciparum/genetics/physiology ; Pregnancy ; Pregnancy Complications, Parasitic/immunology/*parasitology
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  • 135
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-01-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Iyengar, R -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):461-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Mount Sinai School of Medicine, City University of New York, NY 10029, USA. iyengar@msvax.mssm.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560257" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Division ; Cell Survival ; Cell Transformation, Neoplastic ; Cyclic AMP/*metabolism ; Long-Term Potentiation ; Nerve Growth Factors/physiology ; Neurons/cytology ; *Signal Transduction
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  • 136
    Publication Date: 1996-08-09
    Description: Physiological signaling pathways both diverge and converge-a single neurotransmitter can have multiple effects and multiple transmitters can have the same effects-in the same target cell. Divergence couples the effects of a transmitter together in a relatively fixed ratio. Different physiological circumstances may require a different ratio, however; the coupling must be made modifiable. This can be achieved through convergence. If two transmitters couple the effects in different ratios, then combinations of the transmitters can yield all intermediate ratios of the effects, thus functionally uncoupling them. This mechanism is analyzed in a well-understood, simple invertebrate neuromuscular circuit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brezina, V -- Orekhova, I V -- Weiss, K R -- GM320099/GM/NIGMS NIH HHS/ -- K21 MH00987/MH/NIMH NIH HHS/ -- MH36730/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 9;273(5276):806-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8670423" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aplysia ; Calcium/metabolism ; Models, Neurological ; Motor Neurons/physiology ; *Muscle Contraction ; Muscle Relaxation ; Muscles/*physiology ; Neurotransmitter Agents/*metabolism ; Potassium/metabolism ; *Signal Transduction
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  • 137
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-03-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, N -- New York, N.Y. -- Science. 1996 Mar 1;271(5253):1234.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638102" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD28/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; *Clonal Anergy ; Interleukin-2/biosynthesis ; Mice ; Mitogen-Activated Protein Kinase 1 ; Mitogen-Activated Protein Kinase 3 ; *Mitogen-Activated Protein Kinases ; Proto-Oncogene Proteins p21(ras)/*metabolism ; Receptors, Antigen, T-Cell/immunology ; *Signal Transduction ; T-Lymphocytes/*immunology/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 138
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-05-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobson, R H -- Tjian, R -- New York, N.Y. -- Science. 1996 May 10;272(5263):827-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, Berkeley 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8629011" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crystallography, X-Ray ; DNA/*chemistry/metabolism ; DNA-Binding Proteins/*chemistry/metabolism ; Humans ; Models, Molecular ; Nucleic Acid Conformation ; Protein Conformation ; Protein Structure, Secondary ; TATA Box ; TATA-Box Binding Protein ; Transcription Factor TFIIA ; Transcription Factor TFIID ; Transcription Factors/*chemistry/genetics/*metabolism ; *Transcription, Genetic
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  • 139
    Publication Date: 1996-09-06
    Description: Subdivision of the limb primordia of Drosophila into anterior and posterior compartments triggers cell interactions that pattern the legs and wings. A comparable compartment-based mechanism is used to pattern the dorsal-ventral axis of the wing. Evidence is presented here for a mechanism based on cell interaction, rather than on compartment formation, that distinguishes dorsal from ventral in the leg. Mutual repression by Wingless and Decapentaplegic signaling systems generates a stable regulatory circuit by which each gene maintains its own expression in a spatially restricted domain. Compartment-independent patterning mechanisms may be used by other organisms during development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brook, W J -- Cohen, S M -- New York, N.Y. -- Science. 1996 Sep 6;273(5280):1373-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Meyerhofstr 1, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703069" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Cell Lineage ; Drosophila/*genetics/growth & development ; *Drosophila Proteins ; Extremities/growth & development ; *Gene Expression Regulation, Developmental ; *Genes, Insect ; Insect Hormones/*genetics/physiology ; Molecular Sequence Data ; Morphogenesis ; Proto-Oncogene Proteins/*genetics/physiology ; Signal Transduction ; Wnt1 Protein
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 140
    Publication Date: 1996-12-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seiwert, S D -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1636-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Seattle Biomedical Research Institute, Seattle, WA 98109, USA. seiwert@u.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8984633" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Awards and Prizes ; Evolution, Molecular ; History, 20th Century ; *Molecular Biology/history ; *RNA Editing ; RNA Precursors/genetics/metabolism ; RNA, Guide/genetics/metabolism ; RNA, Protozoan/genetics/metabolism ; Trypanosomatina/genetics ; United States
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 141
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-03-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, N -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1365-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596907" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Game Theory ; Genes ; Genetics, Population ; Humans ; *Models, Biological ; Models, Genetic ; Mutation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 142
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-11-01
    Description: The neurotransmitter functions of nitric oxide are dependent on dynamic regulation of its biosynthetic enzyme, neuronal nitric oxide synthase (nNOS). By means of a yeast two-hybrid screen, a 10-kilodalton protein was identified that physically interacts with and inhibits the activity of nNOS. This inhibitor, designated PIN, appears to be one of the most conserved proteins in nature, showing 92 percent amino acid identity with the nematode and rat homologs. Binding of PIN destabilizes the nNOS dimer, a conformation necessary for activity. These results suggest that PIN may regulate numerous biological processes through its effects on nitric oxide synthase activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jaffrey, S R -- Snyder, S H -- DA00074/DA/NIDA NIH HHS/ -- GM-07309/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 1;274(5288):774-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8864115" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/genetics/*metabolism/pharmacology ; Cell Line ; Cyclic GMP/metabolism ; Dimerization ; *Drosophila Proteins ; Dyneins ; Enzyme Inhibitors/chemistry/*metabolism/pharmacology ; Humans ; Molecular Sequence Data ; Molecular Weight ; Neurons/enzymology ; Nitric Oxide Synthase/*antagonists & inhibitors/metabolism ; Rats ; Recombinant Fusion Proteins/metabolism/pharmacology ; Saccharomyces cerevisiae ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 143
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-05-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, I A -- New York, N.Y. -- Science. 1996 May 17;272(5264):973-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638141" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen Presentation ; Antigens/chemistry/*metabolism ; Antigens, Differentiation, B-Lymphocyte/chemistry/*metabolism ; HLA-DR1 Antigen/chemistry/metabolism ; Histocompatibility Antigens Class II/chemistry/immunology/*metabolism ; Humans ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Mice ; Models, Molecular ; Protein Conformation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 144
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-10-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1996 Oct 18;274(5286):342-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8927990" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1B Proteins/*genetics/metabolism ; Adenoviruses, Human/genetics/*physiology ; Animals ; Clinical Trials, Phase I as Topic ; Cytopathogenic Effect, Viral ; Genes, Viral ; *Genes, p53 ; Head and Neck Neoplasms/*therapy/virology ; Humans ; Mice ; Mutation ; Neoplasm Transplantation ; Neoplasms, Experimental/*therapy/virology ; Tumor Suppressor Protein p53/metabolism ; Virus Replication
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  • 145
    Publication Date: 1996-01-05
    Description: The molecular origin of the exceptional mechanical properties of spider silk is unclear. This paper presents solid-state 2H nuclear magnetic resonance data from unoriented, oriented, and supercontracted fibers, indicating that the crystalline fraction of dragline silk consists of two types of alanine-rich regions, one that is highly oriented and one that is poorly oriented and less densely packed. A new model for the molecular-level structure of individual silk molecules and their arrangement in the fibers is proposed. These data suggest that it will be necessary to control the secondary structure of individual polymer molecules in order to obtain optimum properties in bio-inspired polymers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simmons, A H -- Michal, C A -- Jelinski, L W -- New York, N.Y. -- Science. 1996 Jan 5;271(5245):84-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Advanced Technology in Biotechnology, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539605" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine/analysis ; Algorithms ; Amino Acid Sequence ; Animals ; Crystallization ; Crystallography, X-Ray ; *Fibroins ; Glycine/analysis ; *Insect Proteins ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Peptides/analysis ; Protein Conformation ; Protein Structure, Secondary ; Proteins/*chemistry ; Silk ; Spiders/*chemistry
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 146
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-06-14
    Description: Mitogen-activated protein kinase (MAPK) cascades, termed MAPK modules, channel extracellular signals into specific cellular responses. Chimeric molecules were constructed between p38 and p44 MAPKs, which transduce stress and growth factor signals, respectively. A discrete region of 40 residues located in the amono-terminal p38MAPK lobe directed the specificity of response to extracellular signals, whereas the p44MAPK chimera, expressed in vivo, redirected stress signals into early mitogenic responses, demonstrating the functional independence of these domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brunet, A -- Pouyssegur, J -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1652-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre de Biochemie-CNRS, UMR134, Parc Valrose, Faculte des Sciences, Nice, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658140" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anisomycin/pharmacology ; Binding Sites ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/*metabolism ; Cell Division ; Cell Line ; Cricetinae ; Cricetulus ; Enzyme Activation ; Gene Expression Regulation ; Genes, fos ; Growth Substances/metabolism ; Mice ; Mitogen-Activated Protein Kinase 3 ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Phosphorylation/drug effects ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Recombinant Fusion Proteins/genetics/metabolism ; Ribosomal Protein S6 Kinases ; Signal Transduction ; Sorbitol/pharmacology ; Substrate Specificity ; p38 Mitogen-Activated Protein Kinases
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  • 147
    Publication Date: 1996-12-06
    Description: The obesity syndrome of ob/ob mice results from lack of leptin, a hormone released by fat cells that acts in the brain to suppress feeding and stimulate metabolism. Neuropeptide Y (NPY) is a neuromodulator implicated in the control of energy balance and is overproduced in the hypothalamus of ob/ob mice. To determine the role of NPY in the response to leptin deficiency, ob/ob mice deficient for NPY were generated. In the absence of NPY, ob/ob mice are less obese because of reduced food intake and increased energy expenditure, and are less severely affected by diabetes, sterility, and somatotropic defects. These results suggest that NPY is a central effector of leptin deficiency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erickson, J C -- Hollopeter, G -- Palmiter, R D -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1704-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry, University of Washington, Box 357370, Seattle, WA 98195-7370, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8939859" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/pathology ; Animals ; Blood Glucose/analysis ; Body Composition ; Body Height ; Body Weight ; Diabetes Mellitus/etiology ; Diabetes Mellitus, Type 2/etiology ; Eating ; Energy Metabolism ; Female ; Fertility ; Insulin-Like Growth Factor I/metabolism ; Leptin ; Male ; Mice ; Mice, Mutant Strains ; Mice, Obese ; Neuropeptide Y/deficiency/genetics/*physiology ; Obesity/pathology/*physiopathology ; Oxygen Consumption ; Proteins/genetics/*physiology ; RNA, Messenger/metabolism
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  • 148
    Publication Date: 1996-12-20
    Description: The human Kv1.5 potassium channel (hKv1.5) contains proline-rich sequences identical to those that bind to Src homology 3 (SH3) domains. Direct association of the Src tyrosine kinase with cloned hKv1.5 and native hKv1.5 in human myocardium was observed. This interaction was mediated by the proline-rich motif of hKv1.5 and the SH3 domain of Src. Furthermore, hKv1.5 was tyrosine phosphorylated, and the channel current was suppressed, in cells coexpressing v-Src. These results provide direct biochemical evidence for a signaling complex composed of a potassium channel and a protein tyrosine kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmes, T C -- Fadool, D A -- Ren, R -- Levitan, I B -- F32 NS009952/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 20;274(5295):2089-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Volen Center for Complex Systems, Brandeis University, Waltham, MA 02254, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8953041" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Line ; Cloning, Molecular ; Humans ; Kv1.5 Potassium Channel ; Molecular Sequence Data ; Myocardium/chemistry ; Oncogene Protein pp60(v-src)/metabolism ; Patch-Clamp Techniques ; Phosphorylation ; Phosphotyrosine/metabolism ; Potassium Channels/chemistry/*metabolism ; *Potassium Channels, Voltage-Gated ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transfection ; src Homology Domains/*physiology ; src-Family Kinases/chemistry/*metabolism
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  • 149
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-05-03
    Description: Heart formation requires complex interactions among cells from multiple embryonic origins. Recent studies have begun to reveal the genetic pathways that control cardiac morphogenesis. Many of the genes within these pathways are conserved across vast phylogenetic distances, which has allowed cardiac development to be dissected in organisms ranging from flies to mammals. Studies of cardiac development have also revealed the molecular defects underlying several congenital cardiac malformations in humans and may ultimately provide opportunities for genetic testing and intervention.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olson, E N -- Srivastava, D -- New York, N.Y. -- Science. 1996 May 3;272(5262):671-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Oncology, University of Texas Southwestern Medical Center, Dallas, 75235-9148, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614825" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; *Gene Expression Regulation, Developmental ; Genes ; Genes, Regulator ; Heart/*embryology ; Heart Conduction System/embryology ; Heart Defects, Congenital/embryology/*genetics/pathology ; Humans ; Morphogenesis ; Mutation ; Myocardium/cytology ; Neural Crest/cytology ; Transcription Factors/physiology ; Transcription, Genetic
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  • 150
    Publication Date: 1996-01-05
    Description: A complete and accurate set of experimental crystallographic phases to a resolution of 1.8 angstroms was obtained for a 230-residue dimeric fragment of rat mannose-binding protein A with the use of multiwavelength anomalous dispersion (MAD) phasing. An accurate image of the crystal structure could thus be obtained without resort to phases calculated from a model. Partially reduced disulfide bonds, local disorder, and differences in the mobility of chemically equivalent molecules are apparent in the experimental electron density map. A solvation layer is visible that includes well-ordered sites of hydration around polar and charged protein atoms, as well as diffuse, partially disordered solvent shells around exposed hydrophobic groups. Because the experimental phases and the resulting electron density map are free from the influence of a model, they provide a stringent test of theoretical models of macromolecular solvation, motion, and conformational heterogeneity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burling, F T -- Weis, W I -- Flaherty, K M -- Brunger, A T -- GM50565/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 5;271(5245):72-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Yale University, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539602" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier Proteins/*chemistry ; Chemistry, Physical ; Crystallization ; *Crystallography, X-Ray ; Hydrogen Bonding ; Mannose/*metabolism ; *Mannose-Binding Lectin ; Models, Molecular ; Molecular Sequence Data ; Physicochemical Phenomena ; *Protein Conformation ; Rats ; Solvents ; Water
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  • 151
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-05-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1996 May 17;272(5264):949-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638138" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*genetics ; Animals ; Biological Clocks/*genetics ; Caenorhabditis elegans/*genetics/physiology ; *Genes, Helminth ; Longevity/genetics ; Mutation
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  • 152
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-11-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1996 Nov 8;274(5289):908-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8966566" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Inversion ; *Chromosomes, Human, Pair 16 ; Genetic Research ; History, 20th Century ; Human Genome Project ; Humans ; Leukemia, Myelomonocytic, Acute/*genetics ; Mice ; National Institutes of Health (U.S.) ; *Scientific Misconduct ; United States
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  • 153
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-11-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joffe, M -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1285-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8966591" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Drug Synergism ; Estradiol/metabolism ; Estrogens, Non-Steroidal/metabolism/*pharmacology ; Humans ; Insecticides/metabolism/*pharmacology ; Polychlorinated Biphenyls/metabolism/*pharmacology ; Rats ; Receptors, Estrogen/drug effects/*metabolism
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  • 154
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-06-07
    Description: Women are particularly susceptible to malaria during first and second pregnancies, even though they may have developed immunity over years of residence in endemic areas. Plasmodium falciparum-infected red blood cells (IRBCs) were obtained from human placentas. These IRBCs bound to purified chondroitin sulfate A (CSA) but not to other extracellular matrix proteins or to other known IRBC receptors. IRBCs from nonpregnant donors did not bind to CSA. Placental IRBCs adhered to sections of fresh-frozen human placenta with an anatomic distribution similar to that of naturally infected placentas, and this adhesion was competitively inhibited by purified CSA. Thus, adhesion to CSA appears to select for a subpopulation of parasites that causes maternal malaria.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fried, M -- Duffy, P E -- New York, N.Y. -- Science. 1996 Jun 7;272(5267):1502-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉U.S. Army Medical Research Unit-Kenya, Kisumu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8633247" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesiveness ; Adolescent ; Adult ; Animals ; Antigens, CD36/metabolism ; Chondroitin Lyases/pharmacology ; Chondroitin Sulfates/*metabolism ; Erythrocytes/metabolism/*parasitology ; Extracellular Matrix Proteins/metabolism ; Female ; Humans ; Malaria, Falciparum/*parasitology ; Placenta/*parasitology ; Plasmodium falciparum/*physiology ; Pregnancy ; Pregnancy Complications, Parasitic/*parasitology
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  • 155
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-09-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1996 Sep 20;273(5282):1652.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8830407" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Animals ; Child ; Colombia ; Controlled Clinical Trials as Topic ; Humans ; *Malaria Vaccines/immunology ; Malaria, Falciparum/*prevention & control ; Plasmodium falciparum/*immunology ; Protozoan Proteins/*immunology ; *Recombinant Proteins ; Thailand ; Vaccines, Synthetic/immunology ; World Health Organization
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 156
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-08-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sollner-Webb, B -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1182-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biological Chemistry Department, Johns Hopkins University School of Medicine, Baltimore, MD 22105, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8787123" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Models, Genetic ; *RNA Editing ; RNA Precursors/*metabolism ; RNA, Guide/*metabolism ; RNA, Messenger/*metabolism ; RNA, Protozoan/metabolism ; Trypanosomatina/*genetics/metabolism ; Uridine Monophosphate/*metabolism
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  • 157
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-11-08
    Description: Whole-cell recordings from optic tectal neurons in Xenopus tadpoles were used to study the maturation of a glutamatergic synapse. The first glutamatergic transmission is mediated only by N-methyl-D-aspartate (NMDA) receptors and is silent at resting potentials. More mature synapses acquire transmission by alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) receptors. This maturational program is mimicked by postsynaptic expression of constitutively active calcium-calmodulin-dependent protein kinase II (CaMKII). Newly formed synapses may be silent unless sufficient depolarization is provided by coincident activity that could activate postsynaptic CaMKII, resulting in the appearance of AMPA responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, G -- Malinow, R -- Cline, H T -- New York, N.Y. -- Science. 1996 Nov 8;274(5289):972-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA. cline@cshl.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8875937" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/*metabolism ; Evoked Potentials ; Glutamates/*physiology ; In Vitro Techniques ; N-Methylaspartate/metabolism ; Neurons/cytology/enzymology/physiology/virology ; Patch-Clamp Techniques ; Receptors, AMPA/*physiology ; Receptors, N-Methyl-D-Aspartate/*physiology ; Recombinant Proteins/metabolism ; Superior Colliculi/cytology/physiology ; Synapses/*physiology ; *Synaptic Transmission ; Xenopus ; alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid/metabolism
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  • 158
    Publication Date: 1996-02-09
    Description: Bruton's tyrosine kinase (BTK) is pivotal in B cell activation and development through its participation in the signaling pathways of multiple hematopoietic receptors. The mechanisms controlling BTK activation were studied here by examination of the biochemical consequences of an interaction between BTK and SRC family kinases. This interaction of BTK with SRC kinases transphosphorylated BTK on tyrosine at residue 551, which led to BTK activation. BTK then autophosphorylated at a second site. The same two sites were phosphorylated upon B cell antigen receptor cross-linking. The activated BTK was predominantly membrane-associated, which suggests that BTK integrates distinct receptor signals resulting in SRC kinase activation and BTK membrane targeting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rawlings, D J -- Scharenberg, A M -- Park, H -- Wahl, M I -- Lin, S -- Kato, R M -- Fluckiger, A C -- Witte, O N -- Kinet, J P -- AR01912/AR/NIAMS NIH HHS/ -- AR36834/AR/NIAMS NIH HHS/ -- CA09120-20/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Feb 9;271(5250):822-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, University of California, Los Angeles 90095-1662, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8629002" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; B-Lymphocytes/*enzymology ; Cell Line, Transformed ; Cell Membrane/enzymology ; Enzyme Activation ; Immunoglobulin M/immunology ; Lymphocyte Activation ; Mice ; Mutation ; Phosphopeptides/analysis ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; Receptors, Antigen, B-Cell/metabolism ; Signal Transduction ; src-Family Kinases/*metabolism
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  • 159
    Publication Date: 1996-11-15
    Description: An evolutionary change in development was studied in two closely related ascidian species, one exhibiting a conventional tadpole larva and the other a modified tailless larva. Interspecific hybridization restores chordate features to the tailless larva. The zinc finger gene Manx is expressed in cells that generate chordate features in the tailed species but is down-regulated in the tailless species. Manx expression is restored in hybrid embryos. Antisense oligodeoxynucleotide treatment inhibited Manx expression and chordate features in hybrid embryos, which suggests that Manx is required for development of the chordate larval phenotype in ascidians.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Swalla, B J -- Jeffery, W R -- HD-13970/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1205-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Vanderbilt University, Nashville, TN 37235, USA. swallabj@ctrvax.vanderbilt.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8895472" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chordata, Nonvertebrate/*embryology/genetics ; *Gene Expression Regulation, Developmental ; Hybridization, Genetic ; In Situ Hybridization ; Larva/growth & development ; Notochord/embryology ; Oligonucleotides, Antisense/metabolism/pharmacology ; RNA, Messenger/genetics/metabolism ; Tail/embryology ; Thionucleotides/metabolism/pharmacology ; Transcription Factors/*genetics ; Up-Regulation ; Urochordata/*embryology/*genetics ; Zinc Fingers/*genetics
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  • 160
    Publication Date: 1996-03-29
    Description: The cystic fibrosis transmembrane conductance regulator (CFTR) is a chloride ion channel regulated by protein kinase A and adenosine triphosphate (ATP). Loss of CFTR-mediated chloride ion conductance from the apical plasma membrane of epithelial cells is a primary physiological lesion in cystic fibrosis. CFTR has also been suggested to function an an ATP channel, although the size of the ATP anion is much larger than the estimated size of the CFTR pore. ATP was not conducted through CFTR in intact organs, polarized human lung cell lines, stably transfected mammalian cell lines, or planar lipid bilayers reconstituted with CFTR protein. These findings suggest that ATP permeation through the CFTR is unlikely to contribute to the normal function of CFTR or to the pathogenesis of cystic fibrosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reddy, M M -- Quinton, P M -- Haws, C -- Wine, J J -- Grygorczyk, R -- Tabcharani, J A -- Hanrahan, J W -- Gunderson, K L -- Kopito, R R -- DK43994/DK/NIDDK NIH HHS/ -- DK45913/DK/NIDDK NIH HHS/ -- HL42368/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1876-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biomedical Sciences, University of California, Riverside, 92521, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596959" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/*metabolism ; Animals ; CHO Cells ; Cell Line ; Cell Membrane/metabolism ; Cell Polarity ; Chlorides/metabolism ; Cricetinae ; Cystic Fibrosis Transmembrane Conductance Regulator/*metabolism ; Humans ; Lipid Bilayers/metabolism ; Lung/cytology/metabolism ; Patch-Clamp Techniques ; Recombinant Proteins/metabolism
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  • 161
    Publication Date: 1996-12-13
    Description: Hominid fossils from Ngandong and Sambungmacan, Central Java, are considered the most morphologically advanced representatives of Homo erectus. Electron spin resonance (ESR) and mass spectrometric U-series dating of fossil bovid teeth collected from the hominid-bearing levels at these sites gave mean ages of 27 +/- 2 to 53.3 +/- 4 thousand years ago; the range in ages reflects uncertainties in uranium migration histories. These ages are 20,000 to 400,000 years younger than previous age estimates for these hominids and indicate that H. erectus may have survived on Java at least 250,000 years longer than on the Asian mainland, and perhaps 1 million years longer than in Africa. The new ages raise the possibility that H. erectus overlapped in time with anatomically modern humans (H. sapiens) in Southeast Asia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Swisher, C C 3rd -- Rink, W J -- Anton, S C -- Schwarcz, H P -- Curtis, G H -- Suprijo, A -- Widiasmoro -- New York, N.Y. -- Science. 1996 Dec 13;274(5294):1870-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Berkeley Geochronology Center, 2455 Ridge Road, Berkeley, CA 94709 USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8943192" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Animals ; Asia, Southeastern ; Australia ; Cattle ; Dental Enamel/chemistry ; Dentin/chemistry ; Electron Spin Resonance Spectroscopy ; *Fossils ; History, Ancient ; *Hominidae ; Humans ; Indonesia ; Mass Spectrometry ; Paleodontology ; *Paleontology ; Uranium/analysis
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  • 162
    Publication Date: 1996-02-23
    Description: Transmembrane signaling by bacterial chemotaxis receptors appears to require a conformational change within a receptor dimer. Dimers were engineered of the cytoplasmic domain of the Escherichia coli aspartate receptor that stimulated the kinase CheA in vitro. The folding free energy of the leucine-zipper dimerization domain was harnessed to twist the dimer interface of the receptor, which markedly affected the extent of CheA activation. Response to this twist was attenuated by modification of receptor regulatory sites, in the same manner as adaptation resets sensitivity to ligand in vivo. These results suggest that the normal allosteric activation of the chemotaxis receptor has been mimicked in a system that lacks both ligand-binding and transmembrane domains. The most stimulatory receptor dimer formed a species of tetrameric size.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cochran, A G -- Kim, P S -- T32 AI07348-07/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1113-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599087" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry/*metabolism ; Chemoreceptor Cells ; Chemotaxis ; Cytoplasm/metabolism ; Enzyme Activation ; Escherichia coli/*metabolism ; *Escherichia coli Proteins ; Leucine Zippers ; Ligands ; Membrane Proteins/chemistry/*metabolism ; Methylation ; Molecular Sequence Data ; Phosphorylation ; Protein Conformation ; Protein Kinases/metabolism ; Protein Structure, Secondary ; Receptors, Amino Acid/chemistry/*metabolism ; *Receptors, Cell Surface ; Recombinant Fusion Proteins/chemistry/metabolism ; *Signal Transduction
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  • 163
    Publication Date: 1996-01-05
    Description: Developing insects repeatedly shed their cuticle by means of a stereotyped behavior called ecdysis, thought to be initiated by the brain peptide eclosion hormone. Here an ecdysis-triggering hormone, Mas-ETH, is described from the tobacco hornworm Manduca sexta. Mas-ETH contains 26 amino acids and is produced by a segmentally distributed endocrine system of epitracheal glands (EGs). The EGs undergo a marked reduction in volume, appearance, and immunohistochemical staining during ecdysis, at which time Mas-ETH is found in the hemolymph. Injection of EGs extract or synthetic Mas-ETH into pharate larvae, pupae, or adults initiates preecdysis within 2 to 10 minutes, followed by ecdysis. Sensitivity to injected Mas-ETH appears much earlier before ecdysis and occurs with shorter latency than that reported for eclosion hormone. The isolated central nervous system responds to Mas-ETH, but not to eclosion hormone, with patterned motor bursting corresponding to in vivo preecdysis and ecdysis. Mas-ETH may be an immediate blood-borne trigger for ecdysis through a direct action on the nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zitnan, D -- Kingan, T G -- Hermesman, J L -- Adams, M E -- New York, N.Y. -- Science. 1996 Jan 5;271(5245):88-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomology, University of California, Riverside 92521, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539606" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Central Nervous System/drug effects/physiology ; Endocrine Glands/chemistry/cytology/physiology ; Hemolymph/chemistry ; Insect Hormones/chemistry/isolation & purification/pharmacology/*physiology ; Larva/physiology ; Manduca/*chemistry/physiology ; Molecular Sequence Data ; Molecular Weight ; *Molting ; Motor Neurons/drug effects/physiology ; Peptides/chemistry/isolation & purification/pharmacology/*physiology ; Pupa/physiology
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  • 164
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-06-14
    Description: As a model for studying the generation of antibody diversity, a gene-targeted mouse was produced that is hemizygous for a rearranged V(D)J segment at the immunoglobulin (Ig) heavy chain locus, the other allele being nonfunctional. The mouse also has no functional kappa light chain allele. The heavy chain, when paired with any lambda light chain, is specific for the hapten (4-hydroxy-3-nitrophenyl) acetyl (NP). The primary repertoire of this quasi-monoclonal mouse is monospecific, but somatic hypermutation and secondary rearrangements change the specificity of 20 percent of the antigen receptors on B cells. The serum concentrations of the Ig isotypes are similar to those in nontransgenic littermates, but less than half of the serum IgM binds to NP, and none of the other isotypes do. Thus, neither network interactions nor random activation of a small fraction of the B cell population can account for serum Ig concentrations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cascalho, M -- Ma, A -- Lee, S -- Masat, L -- Wabl, M -- 1R01 GM37699/GM/NIGMS NIH HHS/ -- P60 AR20684/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1649-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of California, San Francisco 94143-0670, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658139" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/*genetics/immunology ; *Antigens, CD ; Antigens, CD43 ; Antigens, CD45/immunology ; B-Lymphocytes/cytology/immunology ; Base Sequence ; Cell Line ; Cloning, Molecular ; Dna ; Flow Cytometry ; Gene Rearrangement, B-Lymphocyte, Heavy Chain ; Haptens/immunology ; Immunoglobulin Heavy Chains/*genetics/immunology ; Immunoglobulin Isotypes/genetics ; Immunoglobulin J-Chains/genetics ; Immunoglobulin Light Chains/genetics/immunology ; Immunoglobulin Variable Region/genetics ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mice, Knockout/genetics/*immunology ; Molecular Sequence Data ; Nitrophenols/immunology ; Phenylacetates ; Recombinant Proteins/genetics/immunology ; Sialoglycoproteins/immunology
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  • 165
    Publication Date: 1996-10-25
    Description: Metabotropic glutamate receptors (mGluRs) regulate transmitter release at mammalian central synapses. However, because of the difficulty of recording from mammalian presynaptic terminals, the mechanism underlying mGluR-mediated presynaptic inhibition is not known. Here, simultaneous recordings from a giant presynaptic terminal, the calyx of Held, and its postsynaptic target in the medial nucleus of the trapezoid body were obtained in rat brainstem slices. Agonists of mGluRs suppressed a high voltage-activated P/Q-type calcium conductance in the presynaptic terminal, thereby inhibiting transmitter release at this glutamatergic synapse. Because several forms of presynaptic modulation and plasticity are mediated by mGluRs, this identification of a target ion channel is a first step toward elucidation of their molecular mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takahashi, T -- Forsythe, I D -- Tsujimoto, T -- Barnes-Davies, M -- Onodera, K -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):594-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurophysiology, Institute for Brain Research, Faculty of Medicine, University of Tokyo, Tokyo 113, Japan. ttakahas-tky@umin.u-tokyo.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849448" target="_blank"〉PubMed〈/a〉
    Keywords: Aminobutyrates/pharmacology ; Animals ; Brain Stem ; Cadmium/pharmacology ; Calcium/*metabolism ; Calcium Channel Blockers/pharmacology ; Calcium Channels/drug effects/*metabolism ; Excitatory Amino Acid Agonists/pharmacology ; In Vitro Techniques ; Neurotransmitter Agents/metabolism ; Patch-Clamp Techniques ; Potassium/metabolism ; Potassium Channels/drug effects/metabolism ; Presynaptic Terminals/*metabolism ; Rats ; Rats, Wistar ; Receptors, Metabotropic Glutamate/agonists/*metabolism ; Synapses/*metabolism ; *Synaptic Transmission
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  • 166
    Publication Date: 1996-11-22
    Description: Large macromolecular assemblies have evolved as a means of compartmentalizing reactions in organisms lacking membrane-bounded compartments. A tricorn-shaped protease was isolated from the archaeon Thermoplasma and was shown to form a multisubunit proteolytic complex. The 120-kilodalton monomer assembled to form a hexameric toroid that could assemble further into a capsid structure. Tricorn protease appeared to act as the core of a proteolytic system; when it interacted with several smaller proteins, it displayed multicatalytic activities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tamura, T -- Tamura, N -- Cejka, Z -- Hegerl, R -- Lottspeich, F -- Baumeister, W -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1385-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8910281" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cloning, Molecular ; Cysteine Endopeptidases/metabolism ; Endopeptidases/*chemistry/genetics/isolation & purification/*metabolism ; Genes, Bacterial ; Microscopy, Electron ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Multienzyme Complexes/metabolism ; Peptides/metabolism ; Proteasome Endopeptidase Complex ; *Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; Substrate Specificity ; Thermoplasma/*enzymology
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  • 167
    Publication Date: 1996-02-16
    Description: Variants of lambda repressor and cytochrome b562 translated from messenger RNAs without stop codons were modified by carboxyl terminal addition of an ssrA-encoded peptide tag and subsequently degraded by carboxyl terminal-specific proteases present in both the cytoplasm and periplasm of Escherichia coli. The tag appears to be added to the carboxyl terminus of the nascent polypeptide chain by cotranslational switching of the ribosome from the damaged messenger RNA to ssrA RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keiler, K C -- Waller, P R -- Sauer, R T -- AI-15706/AI/NIAID NIH HHS/ -- AI-16892/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 16;271(5251):990-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139-4307, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8584937" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine ; Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Codon, Terminator ; Cytochrome b Group/genetics/*metabolism ; *DNA-Binding Proteins ; Endopeptidases/metabolism ; Escherichia coli/genetics/metabolism ; *Escherichia coli Proteins ; Molecular Sequence Data ; Peptides/metabolism ; Protein Biosynthesis ; *Protein Processing, Post-Translational ; RNA, Bacterial/genetics/*metabolism ; RNA, Messenger/genetics/*metabolism ; Repressor Proteins/genetics/*metabolism ; Viral Proteins ; Viral Regulatory and Accessory Proteins
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  • 168
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-03-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taubes, G -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1493-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599100" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*metabolism ; Amino Acid Sequence ; Amyloid beta-Peptides/*chemistry/metabolism ; Amyloid beta-Protein Precursor/chemistry/genetics/metabolism ; Amyloidosis/*metabolism ; Animals ; Brain Chemistry ; Humans ; Prealbumin/chemistry/genetics ; Prion Diseases/*metabolism ; *Protein Folding
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  • 169
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-11-15
    Description: The generation of distinct neuronal cell types in appropriate numbers and at precise positions underlies the assembly of neural circuits that encode animal behavior. Despite the complexity of the vertebrate central nervous system, advances have been made in defining the principles that control the diversification and patterning of its component cells. A combination of molecular genetic, biochemical, and embryological assays has begun to reveal the identity and mechanism of action of molecules that induce and pattern neural tissue and the role of transcription factors in establishing generic and specific neuronal fates. Some of these advances are discussed here, focusing on the spinal cord as a model system for analyzing the molecular control of central nervous system development in vertebrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanabe, Y -- Jessell, T M -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1115-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Center for Neurobiology and Behavior, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8895454" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Body Patterning ; Cell Differentiation ; Ectoderm/cytology/physiology ; *Embryonic Induction ; Gene Expression Regulation, Developmental ; Motor Neurons/cytology/physiology ; Neurons/*cytology/physiology ; Notochord/physiology ; Signal Transduction ; Spinal Cord/cytology/*embryology ; Transcription Factors/physiology
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  • 170
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-05-03
    Description: Interdigital cell death leads to regression of soft tissue between embryonic digits in many vertebrates. Although the signals that regulate interdigital apoptosis are not known, BMPs--signaling molecules of the transforming growth factor-beta superfamily--are expressed interdigitally. A dominant negative type I BMP receptor (dnBMPR-IB) was used here to block BMP signaling. Expression of dnBMPR in chicken embryonic hind limbs greatly reduced interdigital apoptosis and resulted in webbed feet. In addition, scales were transformed into feathers. The similarity of the webbing to webbed duck feet led to studies that indicate that BMPs are not expressed in the duck interdigit. These results indicate BMP signaling actively mediates cell death in the embryonic limb.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zou, H -- Niswander, L -- New York, N.Y. -- Science. 1996 May 3;272(5262):738-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614838" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Bone Morphogenetic Protein Receptors, Type I ; Bone Morphogenetic Proteins ; Chick Embryo ; Ducks ; Feathers/cytology/*embryology ; Foot/embryology ; Gene Expression ; Hindlimb/cytology/*embryology ; In Situ Hybridization ; Mesoderm/metabolism ; Mice ; Mutagenesis, Site-Directed ; Phenotype ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Proteins/genetics/*physiology ; RNA/genetics/metabolism ; Receptors, Growth Factor/genetics/*metabolism ; *Signal Transduction ; Transfection
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  • 171
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-05-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McKean, K A -- Nunney, L -- Zuk, M -- New York, N.Y. -- Science. 1996 May 3;272(5262):634-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614814" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Humans ; Immune System/*physiology ; Immune Tolerance ; Selection, Genetic ; Self Tolerance ; Virus Diseases/*immunology ; Viruses/*immunology
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  • 172
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-07-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, Jocelyn -- New York, N.Y. -- Science. 1996 Jul 5;273(5271):39.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11644816" target="_blank"〉PubMed〈/a〉
    Keywords: *Animal Experimentation ; *Animal Rights ; *Animal Welfare ; Animals ; *Politics ; *Primates ; United States
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  • 173
    Publication Date: 1996-06-28
    Description: A chloroplast RNA polymerase sigma factor is encoded by a nuclear gene, sigA, in the red alga Cyanidium caldarium RK-1. The encoded protein functions as an RNA polymerase sigma factor in vitro and it is localized to the chloroplast in vivo. SigA shows high sequence similarity to the sigma factors of cyanobacteria, which is indicative of the ancestral endosymbiotic event and subsequent transfer of the sigA gene to the nuclear genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanaka, K -- Oikawa, K -- Ohta, N -- Kuroiwa, H -- Kuroiwa, T -- Takahashi, H -- New York, N.Y. -- Science. 1996 Jun 28;272(5270):1932-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular and Cellular Biosciences, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658165" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Blotting, Southern ; Cell Nucleus/genetics ; Chloroplasts/*enzymology/genetics ; DNA-Directed RNA Polymerases/chemistry/*genetics/isolation & ; purification/metabolism ; Molecular Sequence Data ; Recombinant Proteins/isolation & purification/metabolism ; Rhodophyta/enzymology/*genetics/ultrastructure ; Sequence Alignment ; Sigma Factor/chemistry/*genetics/isolation & purification/metabolism
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  • 174
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-08-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 1996 Aug 2;273(5275):577-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8701307" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; Genetics, Behavioral ; Maternal Behavior/*physiology ; Mice ; Mice, Knockout/genetics/*physiology ; Neurons/metabolism ; Preoptic Area/metabolism/physiology ; Proto-Oncogene Proteins c-fos/*genetics/physiology
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  • 175
    Publication Date: 1996-01-26
    Description: High density lipoprotein (HDL) and low density lipoprotein (LDL) are cholesterol transport particles whose plasma concentrations are directly (LDL) and inversely (HDL) correlated with risk for atherosclerosis. LDL catabolism involves cellular uptake and degradation of the entire particle by a well-characterized receptor. HDL, in contrast, selectively delivers its cholesterol, but not protein, to cells by unknown receptors. Here it is shown that the class B scavenger receptor SR-BI is an HDL receptor. SR-BI binds HDL with high affinity, is expressed primarily in liver and nonplacental steroidogenic tissues, and mediates selective cholesterol uptake by a mechanism distinct from the classic LDL receptor pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Acton, S -- Rigotti, A -- Landschulz, K T -- Xu, S -- Hobbs, H H -- Krieger, M -- HL09047/HL/NHLBI NIH HHS/ -- HL41484/HL/NHLBI NIH HHS/ -- HL52212/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):518-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560269" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Glands/metabolism ; Animals ; Antigens, CD36/genetics/*metabolism ; CHO Cells ; *Carrier Proteins ; Cholesterol/metabolism ; Cholesterol Esters/*metabolism ; Cricetinae ; Female ; Fluorescent Dyes/metabolism ; Lipoproteins, HDL/*metabolism ; Liver/metabolism ; *Membrane Proteins ; Mice ; Molecular Sequence Data ; Ovary/metabolism ; *RNA-Binding Proteins ; *Receptors, Immunologic ; Receptors, LDL/metabolism ; Receptors, Lipoprotein/*metabolism ; Receptors, Scavenger ; Scavenger Receptors, Class B ; Thiazines/metabolism ; Transfection
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  • 176
    Publication Date: 1996-07-12
    Description: The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP.RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kimura, K -- Ito, M -- Amano, M -- Chihara, K -- Fukata, Y -- Nakafuku, M -- Yamamori, B -- Feng, J -- Nakano, T -- Okawa, K -- Iwamatsu, A -- Kaibuchi, K -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):245-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Signal Transduction, Nara Institute of Science and Technology, Ikoma 630-01, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662509" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Actins/metabolism ; Amino Acid Sequence ; Animals ; Cattle ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/*metabolism ; Intracellular Signaling Peptides and Proteins ; Isopropyl Thiogalactoside/pharmacology ; Mice ; Molecular Sequence Data ; Muscle Contraction ; Muscle, Smooth/physiology ; Myosin Light Chains/metabolism ; Myosin-Light-Chain Phosphatase ; Oxazoles/pharmacology ; Phosphoprotein Phosphatases/*antagonists & inhibitors/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/*metabolism ; rho-Associated Kinases ; rhoA GTP-Binding Protein
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  • 177
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-04-05
    Description: The immune system can remember, sometimes for a lifetime, the identity of a pathogen. Understanding how this is accomplished has fascinated immunologists and microbiologists for many years, but there is still considerable debate regarding the mechanisms by which long-term immunity is maintained. Some of the controversy stems from a failure to distinguish between effector and memory cells and to define their roles in conferring protection against disease. Here the current understanding of the cellular basis of immune memory is reviewed and the relative contributions made to protective immunity by memory and effector T and B cells are examined.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ahmed, R -- Gray, D -- AI-30048/AI/NIAID NIH HHS/ -- NS-21496/NS/NINDS NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1996 Apr 5;272(5258):54-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Emory Vaccine Center, Emory University School of Medicine, Atlanta, GA, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8600537" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibody Formation ; Antigens/immunology ; B-Lymphocytes/cytology/*immunology ; CD4-Positive T-Lymphocytes/cytology/immunology ; CD8-Positive T-Lymphocytes/cytology/immunology ; Cell Differentiation ; Cell Lineage ; Humans ; Immunologic Memory/*immunology ; Infection/immunology ; Lymphocyte Activation ; Plasma Cells/immunology ; Receptors, Antigen, T-Cell/immunology ; T-Lymphocytes/cytology/*immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 178
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-01-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tautz, D -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):160-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zoologisches Institut, Universitat Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539613" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; DNA-Binding Proteins/*genetics ; Drosophila/drug effects/*genetics ; *Drosophila Proteins ; Ether/pharmacology ; *Genes, Homeobox ; Genes, Insect ; *Genes, Regulator ; Homeodomain Proteins/*genetics ; Homeostasis ; Mutation ; *Polymorphism, Genetic ; *Transcription Factors
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  • 179
    Publication Date: 1996-02-09
    Description: Mast cells originate from hematopoietic stem cells, but the mast cell-committed precursor has not been identified. In the study presented here, a cell population in murine fetal blood that fulfills the criteria of progenitor mastocytes was identified. It is defined by the phenotype Thy-1loc-Kithi, contains cytoplasmic granules, and expresses RNAs encoding mast cell-associated proteases but lacks expression of the high-affinity immunoglobulin E receptor. Thy-1loc-Kithi cells generated functionally competent mast cells at high frequencies in vitro but lacked developmental potential for other hematopoietic lineages. When transferred intraperitoneally, this population reconstituted the peritoneal mast cell compartment of genetically mast cell-deficient W/Wv mice to wild-type levels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rodewald, H R -- Dessing, M -- Dvorak, A M -- Galli, S J -- AI-33372/AI/NIAID NIH HHS/ -- AI/CA-23990/AI/NIAID NIH HHS/ -- CA/AI-72074/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 9;271(5250):818-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Basel Institute for Immunology, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8629001" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Thy-1/analysis ; Base Sequence ; Cell Lineage ; Cell Transplantation ; Cells, Cultured ; Cytoplasmic Granules/ultrastructure ; Endopeptidases/genetics/metabolism ; Fetal Blood ; Hematopoietic Stem Cells/*cytology/physiology/ultrastructure ; Immunophenotyping ; Interleukin-3/pharmacology ; Mast Cells/*cytology/physiology/ultrastructure ; Mice ; Molecular Sequence Data ; Peritoneal Cavity/cytology ; Proto-Oncogene Proteins c-kit/analysis ; RNA, Messenger/genetics/metabolism ; Receptors, IgE/analysis/genetics ; Stem Cell Factor/pharmacology
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  • 180
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-08-09
    Description: In axons, cytoskeletal constituents move by slow transport. However, it remains controversial whether axonal neurofilaments are dynamic structures in which only subunits are transported or whether filaments assemble in the proximal axon and are transported intact as polymers to the axon terminus. To investigate the form neurofilament proteins take during transport, neurons of transgenic mice lacking axonal neurofilaments were infected with a recombinant adenoviral vector encoding epitope-tagged neurofilament M. Confocal and electron microscopy revealed that the virally encoded neurofilament M was transported in unpolymerized form along axonal microtubules. Thus, neurofilament proteins are probably transported as subunits or small oligomers along microtubules, which are major routes for slow axonal transport.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Terada, S -- Nakata, T -- Peterson, A C -- Hirokawa, N -- New York, N.Y. -- Science. 1996 Aug 9;273(5276):784-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Brain Research, Faculty of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8670416" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/genetics ; Animals ; *Axonal Transport ; Axons/chemistry/*metabolism/ultrastructure ; Ganglia, Spinal/virology ; Genetic Vectors ; Mice ; Mice, Transgenic ; Microscopy, Confocal ; Microscopy, Immunoelectron ; Microtubules/*metabolism ; Neurofilament Proteins/analysis/*metabolism ; Proto-Oncogene Proteins c-myc/genetics/metabolism ; Recombinant Proteins/metabolism ; Sciatic Nerve/chemistry/ultrastructure
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  • 181
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-06-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldberg, A M -- Zurlo, J -- Rudacille, D -- New York, N.Y. -- Science. 1996 Jun 7;272(5267):1403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8633221" target="_blank"〉PubMed〈/a〉
    Keywords: *Animal Experimentation ; *Animal Testing Alternatives ; *Animal Welfare ; Animals ; *Animals, Laboratory ; *Research Design ; Stress, Psychological
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  • 182
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-04-19
    Description: Many of the cell fate decisions in precursor B cells and more mature B cells are controlled by membrane immunoglobulin (Ig)M heavy chain (mu) and the Ig alpha-Ig beta signal transducers. The role of Ig beta in regulating early B cell development was examined in mice that lack Ig beta (Ig beta-/-). These mice had a complete block in B cell development at the immature CD43+B220+ stage. Immunoglobulin heavy chain diversity (DH) and joining (JH) segments rearranged, but variable (VH) to DJH recombination and immunoglobulin messenger RNA expression were compromised. These experiments define an unexpected, early requirement for Ig(beta) to produce B cells that can complete VDJH recombination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gong, S -- Nussenzweig, M C -- New York, N.Y. -- Science. 1996 Apr 19;272(5260):411-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602530" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/genetics/*physiology ; Antigens, CD79 ; B-Lymphocytes/cytology/*immunology ; Gene Expression ; *Gene Rearrangement, B-Lymphocyte, Heavy Chain ; Gene Targeting ; Genes, Immunoglobulin ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin Joining Region/genetics ; Immunoglobulin Light Chains/*genetics ; Immunoglobulin Variable Region/genetics ; Immunoglobulin mu-Chains/biosynthesis/genetics/physiology ; Lymph Nodes ; Mice ; Mice, Inbred C57BL ; Mutation ; RNA, Messenger/genetics ; Receptors, Antigen, B-Cell/physiology ; *Recombination, Genetic ; Signal Transduction
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  • 183
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-11-15
    Description: Neuronal growth cones navigate over long distances along specific pathways to find their correct targets. The mechanisms and molecules that direct this pathfinding are the topics of this review. Growth cones appear to be guided by at least four different mechanisms: contact attraction, chemoattraction, contact repulsion, and chemorepulsion. Evidence is accumulating that these mechanisms act simultaneously and in a coordinated manner to direct pathfinding and that they are mediated by mechanistically and evolutionarily conserved ligand-receptor systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tessier-Lavigne, M -- Goodman, C S -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1123-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy, Howard Hughes Medical Institute, University of California, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8895455" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/*physiology ; Biological Evolution ; Cell Adhesion Molecules, Neuronal/physiology ; Cell Communication ; Cell Movement ; Humans ; Ligands ; Nerve Growth Factors/physiology ; Nerve Tissue Proteins/physiology ; Nervous System/*embryology ; Neural Pathways/*embryology ; Receptors, Cell Surface/physiology
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  • 184
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-10-11
    Description: Hedgehog (Hh) proteins comprise a family of secreted signaling molecules essential for patterning a variety of structures in animal embryogenesis. During biosynthesis, Hh undergoes an autocleavage reaction, mediated by its carboxyl-terminal domain, that produces a lipid-modified amino-terminal fragment responsible for all known Hh signaling activity. Here it is reported that cholesterol is the lipophilic moiety covalently attached to the amino-terminal signaling domain during autoprocessing and that the carboxyl-terminal domain acts as an intramolecular cholesterol transferase. This use of cholesterol to modify embryonic signaling proteins may account for some of the effects of perturbed cholesterol biosynthesis on animal development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Porter, J A -- Young, K E -- Beachy, P A -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):255-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8824192" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cells, Cultured ; Cholesterol/*metabolism ; Dithiothreitol/pharmacology ; Drosophila ; *Drosophila Proteins ; *Embryonic Induction ; Embryonic and Fetal Development ; Hedgehog Proteins ; Humans ; Protein Processing, Post-Translational ; Proteins/genetics/*metabolism ; Signal Transduction ; *Trans-Activators
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  • 185
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-08-23
    Description: Although neurons in primary visual cortex are sensitive to the spatial distribution and intensity of light, their responses have not been thought to correlate with the perception of brightness. Indeed, primary visual cortex is often described as an initial processing stage that sends information to higher cortical areas where perception of brightness, color, and form occurs. However, a significant percentage of neurons in primary visual cortex were shown to respond in a manner correlated with perceived brightness, rather than responding strictly to the light level in the receptive fields of the cells. This finding suggests that even at the first stage of visual cortical processing, spatial integration of information yields perceptual qualities that are only indirectly related to the pattern of illumination of the retina.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rossi, A F -- Rittenhouse, C D -- Paradiso, M A -- New York, N.Y. -- Science. 1996 Aug 23;273(5278):1104-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Brown University, Providence, RI 02912, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688096" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cats ; Color Perception ; *Contrast Sensitivity ; Form Perception ; Humans ; Light ; Neurons/physiology ; Visual Cortex/*physiology ; *Visual Perception
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  • 186
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-03-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldman, M -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1821-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Surgical and Radiological Sciences, University of California, Davis 95616-8742, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596947" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animals ; Carcinogens ; Child ; Dose-Response Relationship, Radiation ; Humans ; Neoplasms/*chemically induced ; *Neoplasms, Radiation-Induced ; Radiation Dosage ; Risk Assessment
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  • 187
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-05-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 1996 May 10;272(5263):805.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8629005" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Contraceptive Agents, Female/adverse effects ; Disease Models, Animal ; Epithelium/drug effects/virology ; Female ; HIV Infections/transmission/virology ; Haplorhini ; Humans ; Levonorgestrel/adverse effects ; Medroxyprogesterone Acetate/adverse effects ; Progesterone/*pharmacology ; Risk Factors ; Simian Acquired Immunodeficiency Syndrome/*transmission/virology ; Simian Immunodeficiency Virus/physiology ; Vagina/*drug effects/virology
    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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  • 188
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-03-15
    Description: Active transport of proteins and RNAs between the nucleus and cytoplasm is a major process in eukaryotic cells. Recently, factors that recognize transport substrates and mediate nuclear import or export have been characterized, revealing interactions that target substrates to the nuclear pore complexes, through which translocation occurs. Translocation requires energy, and for the import process this energy is at least partly consumed by the action of the small guanosine triphosphatase Ran. In the first half of the review, some of the well-established general background information on nucleocytoplasmic transport is discussed. The second half describes recent information on the mechanistic details of nuclear import and export as well as major unresolved issues such as how directionality is conferred on either import or export. The whole review is slanted toward discussion of metazoan cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gorlich, D -- Mattaj, I W -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1513-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome/Cancer Research Campaign Institute, Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599106" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Transport, Active ; Cell Nucleus/*metabolism ; Cytoplasm/*metabolism ; GTP-Binding Proteins/metabolism ; Humans ; Karyopherins ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; Protein Sorting Signals/metabolism ; Proteins/*metabolism ; RNA/*metabolism ; RNA Cap-Binding Proteins ; RNA-Binding Proteins/metabolism ; ran GTP-Binding Protein
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  • 189
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-07-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corey, D P -- Garcia-Anoveros, J -- New York, N.Y. -- Science. 1996 Jul 19;273(5273):323-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8685718" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Caenorhabditis elegans/genetics/*physiology ; Genes, Helminth ; Helminth Proteins/chemistry/genetics/*physiology ; Molecular Sequence Data ; Muscle Contraction ; Mutation ; Phenotype ; Sensation/genetics/*physiology ; Sodium Channels/chemistry/genetics/*physiology ; Touch/genetics/physiology
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  • 190
    Publication Date: 1996-03-08
    Description: Glutamic acid-203 of the alpha subunit of transducin (alphaT) resides within a domain that undergoes a guanosine triphosphate (GTP)-induced conformational change that is essential for effector recognition. Changing the glutamic acid to an alanine in bovine alpha(T) yielded an alpha subunit (alpha(T)E203A) that was fully dependent on rhodopsin for GTP-guanosine diphosphate (GDP) exchange and showed GTP hydrolytic activity similar to that measured for wild-type alpha(T). However, unlike the wild-type protein, the GDP-bound form of alpha(T)E203A was constitutively active toward the effector of transducin, the cyclic guanosine monophosphate phosphodiesterase. Thus, the alpha(T)E203A mutant represents a short-circuited protein switch that no longer requires GTP for the activation of the effector target phosphodiesterase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mittal, R -- Erickson, J W -- Cerione, R A -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1413-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Cornell University, Ithaca, NY 14853-6401, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596913" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-GMP Phosphodiesterases/*metabolism ; Adenosine Diphosphate Ribose/metabolism ; Alanine/chemistry ; Animals ; Base Sequence ; Cattle ; Enzyme Activation ; Glutamic Acid/chemistry ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/*metabolism ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins ; Rhodopsin/metabolism ; Transducin/chemistry/genetics/*metabolism
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  • 191
    Publication Date: 1996-10-04
    Description: In response to visual stimulation, a subset of neurons in the striate and prestriate cortex displays synchronous rhythmic firing in the gamma frequency band (20 to 70 hertz). This finding has raised two fundamental questions: What is the functional significance of synchronous gamma-band activity and how is it generated? This report addresses the second of these two questions. By means of intracellular recording and staining of single cells in the cat striate cortex in vivo, a biophysically distinct class of pyramidal neuron termed "chattering cells" is described. These neurons are located in the superficial layers of the cortex, intrinsically generate 20- to 70-hertz repetitive burst firing in response to suprathreshold depolarizing current injection, and exhibit pronounced oscillations in membrane potential during visual stimulation that are largely absent during periods of spontaneous activity. These properties suggest that chattering cells may make a substantial intracortical contribution to the generation of synchronous cortical oscillations and thus participate in the recruitment of large populations of cells into synchronously firing assemblies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gray, C M -- McCormick, D A -- New York, N.Y. -- Science. 1996 Oct 4;274(5284):109-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Neuroscience, Section of Neurobiology, Physiology, and Behavior, University of California, Davis, CA 95616, USA. cmgray@ucdavis.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8810245" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Cats ; Electric Stimulation ; *Evoked Potentials, Visual ; Membrane Potentials ; Photic Stimulation ; Pyramidal Cells/cytology/*physiology ; Visual Cortex/cytology/*physiology
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  • 192
    Publication Date: 1996-08-23
    Description: Glutamate and aspartate are endogenous excitatory amino acid neurotransmitters widely distributed in the mammalian central nervous system. Aspartate was shown to induce a large membrane current sensitive to N-methyl-D-aspartate (NMDA) and non-NMDA receptor antagonists in Purkinje cells from mice lacking functional NMDA receptors (NR1(-/-)). This response was accompanied by high permeability to calcium. In contrast, no current was induced by aspartate in hippocampal neurons and cerebellar granule cells from NR1(-/-) mice. Several other glutamate receptor agonists failed to evoke this response. Thus, in Purkinje cells, aspartate activates a distinct response capable of contributing to synaptic plasticity through calcium permeability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yuzaki, M -- Forrest, D -- Curran, T -- Connor, J A -- P30CA21765/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 23;273(5278):1112-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Neurobiology, St. Jude Children's Research Hospital, 332 North Lauderdale, Memphis, TN 38105-2794, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688099" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aspartic Acid/*pharmacology ; Calcium/*metabolism ; Cerebellum/cytology/metabolism ; Excitatory Amino Acid Agonists/pharmacology ; Excitatory Amino Acid Antagonists/pharmacology ; Glutamic Acid/pharmacology ; Hippocampus/cytology/metabolism ; Homocysteine/analogs & derivatives/pharmacology ; Magnesium/pharmacology ; Mice ; Mice, Knockout ; N-Methylaspartate/pharmacology ; Neuronal Plasticity ; Neurons/drug effects/metabolism ; Patch-Clamp Techniques ; Permeability ; Purkinje Cells/drug effects/*metabolism ; Receptors, Amino Acid/drug effects/*metabolism ; Receptors, N-Methyl-D-Aspartate/agonists/antagonists & inhibitors/physiology
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  • 193
    Publication Date: 1996-07-26
    Description: B and T lymphocytes undergoing apoptosis in response to anti-immunoglobulin M antibodies and dexamethasone, respectively, were found to have increased amounts of messenger RNA for the inositol 1,4,5-trisphosphate receptor (IP3R) and increased amounts of IP3R protein. Immunohistochemical analysis revealed that the augmented receptor population was localized to the plasma membrane. Type 3 IP3R (IP3R3) was selectively increased during apoptosis, with no enhancement of type 1 IP3R (IP3R1). Expression of IP3R3 antisense constructs in S49 T cells blocked dexamethasone-induced apoptosis, whereas IP3R3 sense, IP3R1 sense, or IP3R1 antisense control constructs did not block cell death. Thus, the increases in IP3R3 may be causally related to apoptosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khan, A A -- Soloski, M J -- Sharp, A H -- Schilling, G -- Sabatini, D M -- Li, S H -- Ross, C A -- Snyder, S H -- AI-20922/AI/NIAID NIH HHS/ -- AI-37934/AI/NIAID NIH HHS/ -- MH43040/MH/NIMH NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Jul 26;273(5274):503-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662540" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Apoptosis ; B-Lymphocytes/*cytology/metabolism ; Base Sequence ; Calcium/metabolism ; Calcium Channels/genetics/immunology/*metabolism ; Cell Line ; Cell Membrane/metabolism ; Cells, Cultured ; DNA, Antisense ; Dexamethasone/pharmacology ; Immunoblotting ; Inositol 1,4,5-Trisphosphate/*metabolism ; Inositol 1,4,5-Trisphosphate Receptors ; Mice ; Molecular Sequence Data ; Receptors, Cytoplasmic and Nuclear/genetics/immunology/*metabolism ; T-Lymphocytes/*cytology/metabolism ; Transfection ; Tumor Cells, Cultured
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  • 194
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-12-06
    Description: Oscillations in the activity of cyclin-dependent kinases (CDKs) promote progression through the eukaryotic cell cycle. This review examines how proteolysis regulates CDK activity-by degrading CDK activators or inhibitors-and also how proteolysis may directly trigger the transition from metaphase to anaphase. Proteolysis during the cell cycle is mediated by two distinct ubiquitin-conjugation pathways. One pathway, requiring CDC34, initiates DNA replication by degrading a CDK inhibitor. The second pathway, involving a large protein complex called the anaphase-promoting complex or cyclosome, initiates chromosome segregation and exit from mitosis by degrading anaphase inhibitors and mitotic cyclins. Proteolysis therefore drives cell cycle progression not only by regulating CDK activity, but by directly influencing chromosome and spindle dynamics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, R W -- Deshaies, R J -- Peters, J M -- Kirschner, M W -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1652-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8939846" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase ; Anaphase-Promoting Complex-Cyclosome ; Animals ; *Cell Cycle ; Cell Cycle Proteins/metabolism ; Cell Division ; Cyclin-Dependent Kinases/antagonists & inhibitors/*metabolism ; Cyclins/metabolism ; Enzyme Inhibitors/metabolism ; Fungal Proteins/metabolism ; Fungi/cytology/metabolism ; G1 Phase ; Humans ; Ligases/metabolism ; Mitosis ; Proteins/*metabolism ; S Phase ; Ubiquitin-Conjugating Enzymes ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases ; Ubiquitins/metabolism
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  • 195
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-03-08
    Description: A class of dyes, BODIPY fluorophores, has been identified for automated DNA sequencing that has improved spectral characteristics compared with conventional fluorescein and rhodamine dyes. Single and double BODIPY dye primers were characterized in commercially available DNA sequencers and showed uniform electrophoretic mobilities and high fluorescence intensities. The improved physical properties of BODIPY dye primers were demonstrated by direct base-calling from the unprocessed fluorescent signals and improved heterozygote analyses of mixed-base populations. The high sensitivity of BODIPY dye primers requires at least 33 percent less reagent consumed per reaction than conventional dye primers, which should affect the costs of large genome-sequencing efforts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Metzker, M L -- Lu, J -- Gibbs, R A -- 1 P30 HG00210/HG/NHGRI NIH HHS/ -- 1 RO1 HG00823/HG/NHGRI NIH HHS/ -- AI07483/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1420-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596915" target="_blank"〉PubMed〈/a〉
    Keywords: Autoanalysis ; Base Sequence ; *Boron Compounds/chemistry ; DNA Primers ; Electrophoresis, Polyacrylamide Gel ; *Fluorescent Dyes/chemistry ; Molecular Sequence Data ; Sensitivity and Specificity ; Sequence Analysis, DNA/*methods ; Spectrometry, Fluorescence
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  • 196
    Publication Date: 1996-09-06
    Description: A chimeric oligonucleotide composed of DNA and modified RNA residues was used to direct correction of the mutation in the hemoglobin betaS allele. After introduction of the chimeric molecule into lymphoblastoid cells homozygous for the betaS mutation, there was a detectable level of gene conversion of the mutant allele to the normal sequence. The efficient and specific conversion directed by chimeric molecules may hold promise as a therapeutic method for the treatment of genetic diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cole-Strauss, A -- Yoon, K -- Xiang, Y -- Byrne, B C -- Rice, M C -- Gryn, J -- Holloman, W K -- Kmiec, E B -- New York, N.Y. -- Science. 1996 Sep 6;273(5280):1386-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Kimmel Cancer Center, Thomas Jefferson University, 233 South 10th Street, Philadelphia, PA 19107, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703073" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Anemia, Sickle Cell/*genetics/therapy ; Base Sequence ; Cells, Cultured ; *Gene Conversion ; Genetic Therapy ; Globins/genetics ; Hemoglobin, Sickle/*genetics ; Humans ; Lymphocytes ; Molecular Sequence Data ; Oligodeoxyribonucleotides/*genetics ; Oligoribonucleotides/*genetics ; Point Mutation ; Polymerase Chain Reaction ; Polymorphism, Restriction Fragment Length ; *Transfection
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  • 197
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-11-08
    Description: Mutations in the p53 tumor suppressor are among the most frequently observed genetic alterations in human cancer and map to the 200-amino acid core domain of the protein. The core domain contains the sequence-specific DNA binding activity and the in vitro 53BP2 protein binding activity of p53. The crystal structure of the p53 core domain bound to the 53BP2 protein, which contains an SH3 (Src homology 3) domain and four ankyrin repeats, revealed that (i) the SH3 domain binds the L3 loop of p53 in a manner distinct from that of previously characterized SH3-polyproline peptide complexes, and (ii) an ankyrin repeat, which forms an L-shaped structure consisting of a beta hairpin and two alpha helices, binds the L2 loop of p53. The structure of the complex shows that the 53BP2 binding site on the p53 core domain consists of evolutionarily conserved regions that are frequently mutated in cancer and that it overlaps the site of DNA binding. The six most frequently observed p53 mutations disrupt 53BP2 binding in vitro. The structure provides evidence that the 53BP2-p53 complex forms in vivo and may have a critical role in the p53 pathway of tumor suppression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gorina, S -- Pavletich, N P -- CA65698/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 8;274(5289):1001-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8875926" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Ankyrins/*chemistry ; Apoptosis Regulatory Proteins ; Binding Sites ; Carrier Proteins/*chemistry/metabolism ; Crystallography, X-Ray ; DNA/metabolism ; Humans ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Neoplasms/genetics ; Protein Binding ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism ; Tumor Suppressor Protein p53/*chemistry/genetics/metabolism ; *src Homology Domains
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  • 198
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-07-05
    Description: Changes in T lymphocyte populations underlie much of the age-related decline in the protective immune response. Aging leads to the replacement of virgin T cells by memory T cells and to the accumulation of cells with signal transduction defects. Studies of antibody gene assembly, accessory cell function, post-thymic T cell development, skewed selection of T cell receptor repertoire, and the clinical concomitants of immune senescence will shed new light on the causes and consequences of age-dependent immune failure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, R A -- New York, N.Y. -- Science. 1996 Jul 5;273(5271):70-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Michigan School of Medicine, University of Michigan Institute of Gerontology, Ann Arbor, 48109-0642, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658199" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Aged, 80 and over ; Aging/*immunology ; Animals ; Antibody Formation ; Antigen-Presenting Cells/immunology ; B-Lymphocytes/immunology ; Cytotoxicity, Immunologic ; Disease Susceptibility/immunology ; Humans ; Immune System/*immunology ; Immunologic Memory ; Killer Cells, Natural/immunology ; Longevity ; Receptors, Antigen, T-Cell/immunology ; T-Lymphocytes/*immunology
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  • 199
    Publication Date: 1996-05-03
    Description: A mouse model of familial hypertrophic cardiomyopathy (FHC) was generated by the introduction of an Arg 403 --〉 Gln mutation into the alpha cardiac myosin heavy chain (MHC) gene. Homozygous alpha MHC 403/403 mice died 7 days after birth, and sedentary heterozygous alpha MHC 403/+ mice survived for 1 year. Cardiac histopathology and dysfunction in the alpha MHC 403/+ mice resembled human FHC. Cardiac dysfunction preceded histopathologic changes, and myocyte disarray, hypertrophy, and fibrosis increased with age. Young male alpha MHC 403/+ mice showed more evidence of disease than did their female counterparts. Preliminary results suggested that exercise capacity may have been compromised in the alpha MHC 403/+ mice. This mouse model may help to define the natural history of FHC.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geisterfer-Lowrance, A A -- Christe, M -- Conner, D A -- Ingwall, J S -- Schoen, F J -- Seidman, C E -- Seidman, J G -- New York, N.Y. -- Science. 1996 May 3;272(5262):731-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical 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/8614836" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cardiac Output ; Cardiomyopathy, Hypertrophic/*genetics/pathology/physiopathology ; *Disease Models, Animal ; Female ; Gene Transfer Techniques ; Heart/*physiopathology ; Heterozygote ; Homozygote ; Humans ; Male ; Mice ; Mice, Mutant Strains ; Molecular Sequence Data ; Mutation ; Myocardium/chemistry/*pathology ; Myosin Heavy Chains/*genetics ; Physical Exertion ; Sex Characteristics ; Ventricular Function, Left
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  • 200
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-08-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Conn, P M -- Bowers, C Y -- New York, N.Y. -- Science. 1996 Aug 16;273(5277):923.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Oregon Regional Primate Research Center, Beaverton, OR 97006-3499, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8711477" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Growth Hormone/pharmacology/*secretion ; Growth Hormone-Releasing Hormone/metabolism ; Hormones/metabolism/pharmacology ; Humans ; Hypothalamus/metabolism ; Insulin-Like Growth Factor I/analysis ; Oligopeptides/*metabolism/pharmacology ; Receptors, Cell Surface/chemistry/*metabolism ; *Receptors, G-Protein-Coupled ; Receptors, Ghrelin ; Receptors, Neuropeptide/metabolism ; Receptors, Pituitary Hormone-Regulating Hormone/metabolism ; Recombinant Proteins/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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