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  • Amino Acid Sequence  (65)
  • Signal Transduction  (65)
  • American Association for the Advancement of Science (AAAS)  (117)
  • 2000-2004  (117)
  • 2000  (117)
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  • American Association for the Advancement of Science (AAAS)  (117)
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  • 2000-2004  (117)
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  • 1
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    Bacteriophytochromes: phytochrome-like photoreceptors from nonphotosynthetic eubacteria (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-05
    Description: Phytochromes are a family of photoreceptors used by green plants to entrain their development to the light environment. The distribution of these chromoproteins has been expanded beyond photoautotrophs with the discovery of phytochrome-like proteins in the nonphotosynthetic eubacteria Deinococcus radiodurans and Pseudomonas aeruginosa. Like plant phytochromes, the D. radiodurans receptor covalently binds linear tetrapyrroles autocatalytically to generate a photochromic holoprotein. However, the attachment site is distinct, using a histidine to potentially form a Schiff base linkage. Sequence homology and mutational analysis suggest that D. radiodurans bacteriophytochrome functions as a light-regulated histidine kinase, which helps protect the bacterium from visible light.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S J -- Vener, A V -- Vierstra, R D -- New York, N.Y. -- Science. 1999 Dec 24;286(5449):2517-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetics, Cellular and Molecular Biology Program and Department of Horticulture, University of Wisconsin-Madison, 1575 Linden Drive, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10617469" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Bacterial Proteins/chemistry/genetics/*metabolism ; Biliverdine/analogs & derivatives/metabolism ; Binding Sites ; Gram-Positive Cocci/genetics/*metabolism ; Histidine/metabolism ; Light ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Photoreceptors, Microbial/chemistry/genetics/*metabolism ; Phytochrome/metabolism ; Protein Kinases/chemistry/genetics/*metabolism ; Pseudomonas aeruginosa/*metabolism ; Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Molecular biology. The mad ways of meiosis (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-05
    Description: Reproductive cells that are destined to become sperm or egg undergo meiotic division during which the chromosome number is halved. As Sluder and McCollum explain in their Perspective, new findings (Shonn et al.) in yeast show that there is a spindle checkpoint that operates during meiosis to ensure that an equal number of replicated chromosomes arrives at each pole of the cell. One of the components of this meiotic spindle checkpoint turns out to be Mad2, which gives the signal to halt meiosis if it looks like unequal chromosome segregation is taking place.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sluder, G -- McCollum, D -- New York, N.Y. -- Science. 2000 Jul 14;289(5477):254-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA. greenfield.sluder@umassmed.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10917849" target="_blank"〉PubMed〈/a〉
    Keywords: Calcium-Binding Proteins/physiology ; *Carrier Proteins ; Cell Cycle Proteins ; Chromosome Aberrations ; Chromosome Disorders ; Chromosome Segregation ; Fungal Proteins/physiology ; Humans ; Meiosis/*physiology ; Nuclear Proteins ; Saccharomycetales/genetics/physiology ; Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Selective inhibition of NF-kappaB activation by a peptide that blocks the interaction of NEMO with the IkappaB kinase complex (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-09-01
    Description: Activation of the transcription factor nuclear factor (NF)-kappaB by proinflammatory stimuli leads to increased expression of genes involved in inflammation. Activation of NF-kappaB requires the activity of an inhibitor of kappaB (IkappaB)-kinase (IKK) complex containing two kinases (IKKalpha and IKKbeta) and the regulatory protein NEMO (NF-kappaB essential modifier). An amino-terminal alpha-helical region of NEMO associated with a carboxyl-terminal segment of IKKalpha and IKKbeta that we term the NEMO-binding domain (NBD). A cell-permeable NBD peptide blocked association of NEMO with the IKK complex and inhibited cytokine-induced NF-kappaB activation and NF-kappaB-dependent gene expression. The peptide also ameliorated inflammatory responses in two experimental mouse models of acute inflammation. The NBD provides a target for the development of drugs that would block proinflammatory activation of the IKK complex without inhibiting basal NF-kappaB activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉May, M J -- D'Acquisto, F -- Madge, L A -- Glockner, J -- Pober, J S -- Ghosh, S -- AI 33443/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Sep 1;289(5484):1550-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Immunobiology and Department of Molecular Biophysics and Biochemistry, 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/10968790" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anti-Inflammatory Agents, Non-Steroidal/chemistry/pharmacology ; COS Cells ; Cells, Cultured ; E-Selectin/biosynthesis/genetics ; Endothelium, Vascular/metabolism ; Gene Expression Regulation ; HeLa Cells ; Humans ; I-kappa B Kinase ; Inflammation/drug therapy ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; NF-kappa B/*metabolism ; Peptides/chemistry/*pharmacology ; Point Mutation ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    A potassium channel protein encoded by chlorella virus PBCV-1 (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-04
    Description: The large chlorella virus PBCV-1, which contains double-stranded DNA (dsDNA), encodes a 94-codon open reading frame (ORF) that contains a motif resembling the signature sequence of the pore domain of potassium channel proteins. Phylogenetic analyses of the encoded protein, Kcv, indicate a previously unidentified type of potassium channel. The messenger RNA encoded by the ORF leads to functional expression of a potassium-selective conductance in Xenopus laevis oocytes. The channel blockers amantadine and barium, but not cesium, inhibit this conductance, in addition to virus plaque formation. Thus, PBCV-1 encodes the first known viral protein that functions as a potassium-selective channel and is essential in the virus life cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Plugge, B -- Gazzarrini, S -- Nelson, M -- Cerana, R -- Van Etten, J L -- Derst, C -- DiFrancesco, D -- Moroni, A -- Thiel, G -- 971/Telethon/Italy -- GM32441/GM/NIGMS NIH HHS/ -- GM41333/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Mar 3;287(5458):1641-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Albrecht-von-Haller-Institut fur Pflanzenwissenschaften, Universitat Gottingen, 37073 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10698737" target="_blank"〉PubMed〈/a〉
    Keywords: Amantadine/pharmacology ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Barium/pharmacology ; Cesium/pharmacology ; Chlorella/virology ; Isoelectric Point ; Molecular Sequence Data ; Molecular Weight ; Oocytes ; Patch-Clamp Techniques ; Phycodnaviridae/chemistry/drug effects/*genetics/*physiology ; Potassium/metabolism ; Potassium Channels/*chemistry/genetics/*physiology ; RNA, Messenger/genetics/metabolism ; Recombinant Proteins/metabolism ; Sodium/metabolism ; Viral Plaque Assay ; *Viral Proteins ; Virus Replication/drug effects ; Xenopus laevis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 5
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    Functional requirement for class I MHC in CNS development and plasticity (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-12-16
    Description: Class I major histocompatibility complex (class I MHC) molecules, known to be important for immune responses to antigen, are expressed also by neurons that undergo activity-dependent, long-term structural and synaptic modifications. Here, we show that in mice genetically deficient for cell surface class I MHC or for a class I MHC receptor component, CD3zeta, refinement of connections between retina and central targets during development is incomplete. In the hippocampus of adult mutants, N-methyl-D-aspartate receptor-dependent long-term potentiation (LTP) is enhanced, and long-term depression (LTD) is absent. Specific class I MHC messenger RNAs are expressed by distinct mosaics of neurons, reflecting a potential for diverse neuronal functions. These results demonstrate an important role for these molecules in the activity-dependent remodeling and plasticity of connections in the developing and mature mammalian central nervous system (CNS).〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2175035/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2175035/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huh, G S -- Boulanger, L M -- Du, H -- Riquelme, P A -- Brotz, T M -- Shatz, C J -- 1F32EY07016/EY/NEI NIH HHS/ -- EY06912/EY/NEI NIH HHS/ -- F32 EY007016/EY/NEI NIH HHS/ -- F32 EY007016-02/EY/NEI NIH HHS/ -- F32 EY007016-03/EY/NEI NIH HHS/ -- MH48108/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2000 Dec 15;290(5499):2155-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, 220 Longwood Avenue, Boston, MA 02115, USA. gshuh@alum.mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11118151" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD3/genetics/*physiology ; Brain/growth & development/*physiology ; Excitatory Postsynaptic Potentials ; Gene Expression Profiling ; Genes, MHC Class I ; Geniculate Bodies/physiology ; Hippocampus/growth & development/physiology ; Histocompatibility Antigens Class I/genetics/*physiology ; In Situ Hybridization ; Long-Term Potentiation ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Mice, Mutant Strains ; Neural Pathways ; *Neuronal Plasticity ; Neurons/*physiology ; Receptors, GABA-A/metabolism ; Receptors, N-Methyl-D-Aspartate/metabolism ; Retina/growth & development/physiology ; Retinal Ganglion Cells/physiology ; Signal Transduction ; Synapses/*physiology ; Synaptic Transmission ; Visual Pathways
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 6
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    Reversal of antipsychotic-induced working memory deficits by short-term dopamine D1 receptor stimulation (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-17
    Description: Chronic blockade of dopamine D2 receptors, a common mechanism of action for antipsychotic drugs, down-regulates D1 receptors in the prefrontal cortex and, as shown here, produces severe impairments in working memory. These deficits were reversed in monkeys by short-term coadministration of a D1 agonist, ABT 431, and this improvement was sustained for more than a year after cessation of D1 treatment. These findings indicate that pharmacological modulation of the D1 signaling pathway can produce long-lasting changes in functional circuits underlying working memory. Resetting this pathway by brief exposure to the agonist may provide a valuable strategy for therapeutic intervention in schizophrenia and other dopamine dysfunctional states.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castner, S A -- Williams, G V -- Goldman-Rakic, P S -- P01DA10160/DA/NIDA NIH HHS/ -- P50MH44866/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2000 Mar 17;287(5460):2020-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Neurobiology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10720329" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antipsychotic Agents/*pharmacology ; Cyclic AMP/metabolism ; Dopamine/metabolism ; Dopamine Agonists/*pharmacology ; Dopamine Antagonists/pharmacology ; Down-Regulation ; Female ; Haloperidol/*pharmacology ; Haplorhini ; Memory/*drug effects ; Prefrontal Cortex/drug effects/metabolism ; Psychomotor Performance/drug effects ; Pyridines/*pharmacology ; Receptors, Dopamine D1/agonists/*metabolism ; Signal Transduction ; Tetrahydronaphthalenes/*pharmacology ; Time Factors
    Print ISSN: 0036-8075
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  • 7
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    Activation of the DNA replication checkpoint through RNA synthesis by primase (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-09-23
    Description: When DNA replication is inhibited during the synthesis (S) phase of the cell cycle, a signaling pathway (checkpoint) is activated that serves to prevent mitosis from initiating before completion of replication. This replication checkpoint acts by down-regulating the activity of the mitotic inducer cdc2-cyclin B. Here, we report the relation between chromatin structure and induction of the replication checkpoint. Chromatin was competent to initiate a checkpoint response only after the DNA was unwound and DNA polymerase alpha had been loaded. Checkpoint induction did not require new DNA synthesis on the unwound template strand but did require RNA primer synthesis by primase. These findings identify the RNA portion of the primer as an important component of the signal that activates the replication checkpoint.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Michael, W M -- Ott, R -- Fanning, E -- Newport, J -- 52948/PHS HHS/ -- R01GM33523-16/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Sep 22;289(5487):2133-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla, CA 92093-0349, USA. matt@mcb.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11000117" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aphidicolin/pharmacology ; *CDC2-CDC28 Kinases ; Carrier Proteins/metabolism ; Chromatin/*metabolism ; Cyclin E/metabolism ; Cyclin-Dependent Kinase 2 ; Cyclin-Dependent Kinases/metabolism ; DNA Helicases/metabolism ; DNA Polymerase I/antagonists & inhibitors/metabolism ; DNA Primase/*metabolism ; *DNA Replication/drug effects ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/metabolism ; Mitosis ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; RNA/*biosynthesis ; Recombinant Proteins/metabolism ; S Phase ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Xenopus ; Xenopus Proteins
    Print ISSN: 0036-8075
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  • 8
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    Neurobiology. Receptors as kissing cousins (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-04-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milligan, G -- New York, N.Y. -- Science. 2000 Apr 7;288(5463):65-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, Scotland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10766637" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclase Inhibitors ; Adenylyl Cyclases/metabolism ; Animals ; Cell Line ; Cerebral Cortex/metabolism ; Corpus Striatum/metabolism ; Dimerization ; Energy Transfer ; Fluorescence ; GTP-Binding Proteins/*metabolism ; Ligands ; Rats ; Receptor Cross-Talk ; Receptors, Dopamine D1/metabolism ; Receptors, Dopamine D2/agonists/*metabolism ; Receptors, Dopamine D5 ; Receptors, GABA-A/metabolism ; Receptors, Somatostatin/agonists/*metabolism ; Signal Transduction ; Somatostatin/metabolism
    Print ISSN: 0036-8075
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  • 9
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    Two-amino acid molecular switch in an epithelial morphogen that regulates binding to two distinct receptors (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-20
    Description: Ectodysplasin, a member of the tumor necrosis factor family, is encoded by the anhidrotic ectodermal dysplasia (EDA) gene. Mutations in EDA give rise to a clinical syndrome characterized by loss of hair, sweat glands, and teeth. EDA-A1 and EDA-A2 are two isoforms of ectodysplasin that differ only by an insertion of two amino acids. This insertion functions to determine receptor binding specificity, such that EDA-A1 binds only the receptor EDAR, whereas EDA-A2 binds only the related, but distinct, X-linked ectodysplasin-A2 receptor (XEDAR). In situ binding and organ culture studies indicate that EDA-A1 and EDA-A2 are differentially expressed and play a role in epidermal morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yan, M -- Wang, L C -- Hymowitz, S G -- Schilbach, S -- Lee, J -- Goddard, A -- de Vos, A M -- Gao, W Q -- Dixit, V M -- New York, N.Y. -- Science. 2000 Oct 20;290(5491):523-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Oncology, Genentech, 1 DNA Way, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11039935" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Binding Sites ; Cell Line ; DNA-Binding Proteins/metabolism ; Ectodermal Dysplasia/genetics ; Ectodysplasins ; Epidermis/embryology/*metabolism ; Humans ; *I-kappa B Proteins ; In Situ Hybridization ; Ligands ; Membrane Proteins/*chemistry/*metabolism ; Mice ; Models, Molecular ; Molecular Sequence Data ; Morphogenesis ; NF-kappa B/metabolism ; Phosphorylation ; Point Mutation ; Protein Conformation ; Proteins/metabolism ; Receptors, Cell Surface/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; TNF Receptor-Associated Factor 6 ; Transfection
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  • 10
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    Localization of the G protein betagamma complex in living cells during chemotaxis (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-02-11
    Description: Gradients of chemoattractants elicit signaling events at the leading edge of a cell even though chemoattractant receptors are uniformly distributed on the cell surface. In highly polarized Dictyostelium discoideum amoebas, membrane-associated betagamma subunits of heterotrimeric guanine nucleotide-binding proteins (G proteins) were localized in a shallow anterior-posterior gradient. A uniformly applied chemoattractant generated binding sites for pleckstrin homology (PH) domains on the inner surface of the membrane in a pattern similar to that of the Gbetagamma subunits. Loss of cell polarity resulted in uniform distribution of both the Gbetagamma subunits and the sensitivity of PH domain recruitment. These observations indicate that Gbetagamma subunits are not sufficiently localized to restrict signaling events to the leading edge but that their distribution may determine the relative chemotactic sensitivity of polarized cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jin, T -- Zhang, N -- Long, Y -- Parent, C A -- Devreotes, P N -- GM-28007/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Feb 11;287(5455):1034-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, 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/10669414" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cell Membrane/metabolism ; Cell Polarity ; Chemotactic Factors/pharmacology ; Chemotaxis/*physiology ; Cyclic AMP/pharmacology ; Dictyostelium/metabolism/*physiology ; *GTP-Binding Protein beta Subunits ; *GTP-Binding Protein gamma Subunits ; GTP-Binding Proteins/*metabolism ; *Heterotrimeric GTP-Binding Proteins ; Recombinant Fusion Proteins/metabolism ; Signal Transduction
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  • 11
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    Genetic suppression of polyglutamine toxicity in Drosophila (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-10
    Description: A Drosophila model for Huntington's and other polyglutamine diseases was used to screen for genetic factors modifying the degeneration caused by expression of polyglutamine in the eye. Among 7000 P-element insertions, several suppressor strains were isolated, two of which led to the discovery of the suppressor genes described here. The predicted product of one, dHDJ1, is homologous to human heat shock protein 40/HDJ1. That of the second, dTPR2, is homologous to the human tetratricopeptide repeat protein 2. Each of these molecules contains a chaperone-related J domain. Their suppression of polyglutamine toxicity was verified in transgenic flies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kazemi-Esfarjani, P -- Benzer, S -- New York, N.Y. -- Science. 2000 Mar 10;287(5459):1837-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA. parsa@its.caltech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10710314" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Cloning, Molecular ; Crosses, Genetic ; DNA Transposable Elements ; Disease Models, Animal ; *Drosophila Proteins ; Drosophila melanogaster/anatomy & histology/embryology/*genetics/metabolism ; Expressed Sequence Tags ; Eye/metabolism ; Eye Abnormalities ; Female ; Genes, Insect ; *Genes, Suppressor ; HSP40 Heat-Shock Proteins ; Heat-Shock Proteins/chemistry/*genetics/physiology ; Male ; Molecular Sequence Data ; *Nerve Degeneration ; Neurodegenerative Diseases ; Peptides/genetics/*metabolism ; Phenotype ; Proteins/chemistry ; Repetitive Sequences, Nucleic Acid ; Retina/metabolism ; Suppression, Genetic
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  • 12
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    Surface expression of HLA-E, an inhibitor of natural killer cells, enhanced by human cytomegalovirus gpUL40 (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-02-11
    Description: The nonclassical major histocompatibility complex (MHC) class I molecule HLA-E inhibits natural killer (NK) cell-mediated lysis by interacting with CD94/NKG2A receptors. Surface expression of HLA-E depends on binding of conserved peptides derived from MHC class I molecules. The same peptide is present in the leader sequence of the human cytomegalovirus (HCMV) glycoprotein UL40 (gpUL40). It is shown that, independently of the transporter associated with antigen processing, gpUL40 can up-regulate expression of HLA-E, which protects targets from NK cell lysis. While classical MHC class I molecules are down-regulated, HLA-E is up-regulated by HCMV. Induction of HLA-E surface expression by gpUL40 may represent an escape route for HCMV.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomasec, P -- Braud, V M -- Rickards, C -- Powell, M B -- McSharry, B P -- Gadola, S -- Cerundolo, V -- Borysiewicz, L K -- McMichael, A J -- Wilkinson, G W -- New York, N.Y. -- Science. 2000 Feb 11;287(5455):1031.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Wales College of Medicine, Cardiff CF14 4XN, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10669413" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; *Antigens, CD ; Cell Line ; Cell Membrane/immunology ; Cells, Cultured ; Conserved Sequence ; Cytomegalovirus/genetics/immunology/*metabolism ; Cytotoxicity, Immunologic ; Down-Regulation ; HLA Antigens/immunology/*metabolism ; Histocompatibility Antigens Class I/immunology/*metabolism ; Humans ; Killer Cells, Natural/*immunology ; Molecular Sequence Data ; Open Reading Frames ; Protein Sorting Signals/chemistry/*metabolism ; Receptors, Immunologic/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Transfection ; Up-Regulation ; Viral Proteins/chemistry/genetics/*metabolism
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  • 13
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    A structural framework for deciphering the link between I-Ag7 and autoimmune diabetes (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-04-25
    Description: Susceptibility to murine and human insulin-dependent diabetes mellitus correlates strongly with major histocompatibility complex (MHC) class II I-A or HLA-DQ alleles that lack an aspartic acid at position beta57. I-Ag7 lacks this aspartate and is the only class II allele expressed by the nonobese diabetic mouse. The crystal structure of I-Ag7 was determined at 2.6 angstrom resolution as a complex with a high-affinity peptide from the autoantigen glutamic acid decarboxylase (GAD) 65. I-Ag7 has a substantially wider peptide-binding groove around beta57, which accounts for distinct peptide preferences compared with other MHC class II alleles. Loss of Asp(beta57) leads to an oxyanion hole in I-Ag7 that can be filled by peptide carboxyl residues or, perhaps, through interaction with the T cell receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corper, A L -- Stratmann, T -- Apostolopoulos, V -- Scott, C A -- Garcia, K C -- Kang, A S -- Wilson, I A -- Teyton, L -- CA58896/CA/NCI NIH HHS/ -- DK55037/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2000 Apr 21;288(5465):505-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10775108" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Aspartic Acid/chemistry ; Crystallography, X-Ray ; Diabetes Mellitus, Type 1/*immunology ; Drosophila melanogaster ; *Genes, MHC Class II ; Glutamate Decarboxylase/metabolism ; Histocompatibility Antigens Class II/*chemistry/genetics/metabolism ; Humans ; Hydrogen Bonding ; Mice ; Mice, Inbred NOD ; Models, Molecular ; Molecular Sequence Data ; Peptide Library ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Receptors, Antigen, T-Cell/metabolism ; Recombinant Proteins/chemistry/metabolism
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  • 14
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    Structure of the RNA polymerase domain of E. coli primase (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-31
    Description: All cellular organisms use specialized RNA polymerases called "primases" to synthesize RNA primers for the initiation of DNA replication. The high-resolution crystal structure of a primase, comprising the catalytic core of the Escherichia coli DnaG protein, was determined. The core structure contains an active-site architecture that is unrelated to other DNA or RNA polymerase palm folds, but is instead related to the "toprim" fold. On the basis of the structure, it is likely that DnaG binds nucleic acid in a groove clustered with invariant residues and that DnaG is positioned within the replisome to accept single-stranded DNA directly from the replicative helicase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keck, J L -- Roche, D D -- Lynch, A S -- Berger, J M -- New York, N.Y. -- Science. 2000 Mar 31;287(5462):2482-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, 229 Stanley Hall, no. 3206, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10741967" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; DNA Helicases/chemistry/metabolism ; DNA Primase/*chemistry/*metabolism ; DNA Replication ; DNA, Bacterial/metabolism ; DNA, Single-Stranded/*metabolism ; DNA-Directed RNA Polymerases/*chemistry/metabolism ; Escherichia coli/*enzymology/metabolism ; Metals/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA/biosynthesis ; Recombinant Proteins/chemistry/metabolism ; Templates, Genetic
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  • 15
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    CikA, a bacteriophytochrome that resets the cyanobacterial circadian clock (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-05
    Description: The circadian oscillator of the cyanobacterium Synechococcus elongatus, like those in eukaryotes, is entrained by environmental cues. Inactivation of the gene cikA (circadian input kinase) shortens the circadian period of gene expression rhythms in S. elongatus by approximately 2 hours, changes the phasing of a subset of rhythms, and nearly abolishes resetting of phase by a pulse of darkness. The CikA protein sequence reveals that it is a divergent bacteriophytochrome with characteristic histidine protein kinase motifs and a cryptic response regulator motif. CikA is likely a key component of a pathway that provides environmental input to the circadian oscillator in S. elongatus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schmitz, O -- Katayama, M -- Williams, S B -- Kondo, T -- Golden, S S -- GM37040/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Aug 4;289(5480):765-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Texas A&M University, College Station, TX 77843-3258, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10926536" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Motifs ; Amino Acid Sequence ; *Bacterial Proteins ; *Biological Clocks/genetics/physiology ; *Circadian Rhythm/genetics/physiology ; Cyanobacteria/genetics/*physiology ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Genes, Reporter ; Luminescent Measurements ; Molecular Sequence Data ; Mutation ; Phenotype ; Protein Kinases/chemistry/*genetics/physiology ; Sequence Alignment
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    Neuroscience. A new look at how neurons compute (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 2000 Sep 29;289(5488):2256-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11041785" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chloride Channels/metabolism ; Chlorides/metabolism ; Culture Techniques ; Dendrites/physiology ; Motion Perception/*physiology ; Neural Inhibition ; Patch-Clamp Techniques ; Rabbits ; Retinal Ganglion Cells/*physiology ; Signal Transduction ; Sodium Channels/metabolism
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  • 17
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    The incredible life and times of biological cells (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-09-23
    Description: In this month's essay, Paul Nurse recapitulates the ontogeny of one of the most important theories in the history of biology, the cell theory, which proposes that all forms of life are composed of cells. Along the way, he lays out the wondrous molecular complexities and processes that he and others have discovered in the course of their studies of the lives of cells. In particular, Nurse focuses on the mechanisms and controls of cell reproduction that ultimately allow growth, development, and evolution to occur.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nurse, P -- New York, N.Y. -- Science. 2000 Sep 8;289(5485):1711-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Imperial Cancer Research Fund, London, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11001740" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Biological Evolution ; Catalysis ; Cell Biology/*history ; *Cell Cycle ; Cell Division ; *Cell Physiological Phenomena ; DNA Replication ; Energy Metabolism ; Enzymes/metabolism ; Genes ; History, 17th Century ; History, 18th Century ; History, 19th Century ; History, 20th Century ; Humans ; Neoplasms/genetics/pathology ; Organelles/metabolism ; Signal Transduction
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  • 18
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    Crystal structure of the ribonucleoprotein core of the signal recognition particle (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-02-26
    Description: The signal recognition particle (SRP), a protein-RNA complex conserved in all three kingdoms of life, recognizes and transports specific proteins to cellular membranes for insertion or secretion. We describe here the 1.8 angstrom crystal structure of the universal core of the SRP, revealing protein recognition of a distorted RNA minor groove. Nucleotide analog interference mapping demonstrates the biological importance of observed interactions, and genetic results show that this core is functional in vivo. The structure explains why the conserved residues in the protein and RNA are required for SRP assembly and defines a signal sequence recognition surface composed of both protein and RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Batey, R T -- Rambo, R P -- Lucast, L -- Rha, B -- Doudna, J A -- New York, N.Y. -- Science. 2000 Feb 18;287(5456):1232-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University, New Haven, CT 06511, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10678824" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Base Pairing ; Binding Sites ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Escherichia coli/chemistry/genetics/metabolism ; *Escherichia coli Proteins ; Guanosine Triphosphate/metabolism ; Hydrogen Bonding ; Magnesium/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Potassium/metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA, Bacterial/*chemistry/genetics/metabolism ; Signal Recognition Particle/*chemistry/metabolism ; Transformation, Bacterial ; Water/metabolism
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  • 19
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    Requirement for DARPP-32 in progesterone-facilitated sexual receptivity in female rats and mice (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-02-11
    Description: DARPP-32, a dopamine- and adenosine 3',5'-monophosphate (cAMP)-regulated phosphoprotein (32 kilodaltons in size), is an obligate intermediate in progesterone (P)-facilitated sexual receptivity in female rats and mice. The facilitative effect of P on sexual receptivity in female rats was blocked by antisense oligonucleotides to DARPP-32. Homozygous mice carrying a null mutation for the DARPP-32 gene exhibited minimal levels of P-facilitated sexual receptivity when compared to their wild-type littermates. P significantly increased hypothalamic cAMP levels and cAMP-dependent protein kinase activity. These increases were not inhibited by a D1 subclass dopamine receptor antagonist. P also enhanced phosphorylation of DARPP-32 on threonine 34 in the hypothalamus of mice. DARPP-32 activation is thus an obligatory step in progestin receptor regulation of sexual receptivity in rats and mice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mani, S K -- Fienberg, A A -- O'Callaghan, J P -- Snyder, G L -- Allen, P B -- Dash, P K -- Moore, A N -- Mitchell, A J -- Bibb, J -- Greengard, P -- O'Malley, B W -- MH49662/MH/NIMH NIH HHS/ -- MH57442/MH/NIMH NIH HHS/ -- NS 35457/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 2000 Feb 11;287(5455):1053-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA. smani@bcm.tmc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10669419" target="_blank"〉PubMed〈/a〉
    Keywords: 2,3,4,5-Tetrahydro-7,8-dihydroxy-1-phenyl-1H-3-benzazepine/pharmacology ; Animals ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Dopamine/pharmacology ; Dopamine Agonists/pharmacology ; Dopamine and cAMP-Regulated Phosphoprotein 32 ; Female ; Hypothalamus/metabolism ; Injections, Intraventricular ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; *Nerve Tissue Proteins ; Oligonucleotides, Antisense/pharmacology ; Phosphoproteins/genetics/*metabolism ; Phosphorylation ; Posture ; Progesterone/*pharmacology ; Proteins/genetics/metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, Progesterone/metabolism ; Serotonin/pharmacology ; Sexual Behavior, Animal/*drug effects ; Signal Transduction
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  • 20
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    AIDS as a zoonosis: scientific and public health implications (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-01-29
    Description: Evidence of simian immunodeficiency virus (SIV) infection has been reported for 26 different species of African nonhuman primates. Two of these viruses, SIVcpz from chimpanzees and SIVsm from sooty mangabeys, are the cause of acquired immunodeficiency syndrome (AIDS) in humans. Together, they have been transmitted to humans on at least seven occasions. The implications of human infection by a diverse set of SIVs and of exposure to a plethora of additional human immunodeficiency virus-related viruses are discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hahn, B H -- Shaw, G M -- De Cock, K M -- Sharp, P M -- N01 AI 35338/AI/NIAID NIH HHS/ -- R01 AI 40951/AI/NIAID NIH HHS/ -- R01 AI 44596/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Jan 28;287(5453):607-14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Howard Hughes Medical Institute, University of Alabama at Birmingham, Birmingham, AL 35294, USA. bhahn@uab.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10649986" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/epidemiology/*transmission/virology ; Africa, Western/epidemiology ; Amino Acid Sequence ; Animals ; Disease Outbreaks ; Disease Reservoirs ; *HIV-1/genetics ; *HIV-2/genetics ; Haplorhini/*virology ; Humans ; Molecular Sequence Data ; Phylogeny ; Public Health ; Simian Acquired Immunodeficiency Syndrome/virology ; Simian Immunodeficiency Virus/classification/genetics/*physiology ; Species Specificity ; Zoonoses/*transmission
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    Bacterial rhodopsin: evidence for a new type of phototrophy in the sea (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-09-16
    Description: Extremely halophilic archaea contain retinal-binding integral membrane proteins called bacteriorhodopsins that function as light-driven proton pumps. So far, bacteriorhodopsins capable of generating a chemiosmotic membrane potential in response to light have been demonstrated only in halophilic archaea. We describe here a type of rhodopsin derived from bacteria that was discovered through genomic analyses of naturally occuring marine bacterioplankton. The bacterial rhodopsin was encoded in the genome of an uncultivated gamma-proteobacterium and shared highest amino acid sequence similarity with archaeal rhodopsins. The protein was functionally expressed in Escherichia coli and bound retinal to form an active, light-driven proton pump. The new rhodopsin exhibited a photochemical reaction cycle with intermediates and kinetics characteristic of archaeal proton-pumping rhodopsins. Our results demonstrate that archaeal-like rhodopsins are broadly distributed among different taxa, including members of the domain Bacteria. Our data also indicate that a previously unsuspected mode of bacterially mediated light-driven energy generation may commonly occur in oceanic surface waters worldwide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beja, O -- Aravind, L -- Koonin, E V -- Suzuki, M T -- Hadd, A -- Nguyen, L P -- Jovanovich, S B -- Gates, C M -- Feldman, R A -- Spudich, J L -- Spudich, E N -- DeLong, E F -- HG01775-02S1/HG/NHGRI NIH HHS/ -- R01GM27750/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Sep 15;289(5486):1902-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Monterey Bay Aquarium Research Institute, Moss Landing, CA 95039-0628, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10988064" target="_blank"〉PubMed〈/a〉
    Keywords: Aerobiosis ; Amino Acid Sequence ; Archaea/classification/physiology ; Bacteria/genetics ; *Bacterial Physiological Phenomena ; Cloning, Molecular ; Escherichia coli ; Gammaproteobacteria/classification/genetics/*physiology ; Molecular Sequence Data ; Oceans and Seas ; Photochemistry ; Photosynthesis ; Phylogeny ; Phytoplankton/genetics/physiology ; Protein Binding ; Proton Pumps/physiology ; Retinaldehyde/metabolism ; Rhodopsin/*physiology ; Rhodopsins, Microbial ; *Water Microbiology
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  • 22
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    Molecular architecture and evolution of a modular spider silk protein gene (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-02-26
    Description: Spider flagelliform silk is one of the most elastic natural materials known. Extensive sequencing of spider silk genes has shown that the exons and introns of the flagelliform gene underwent intragenic concerted evolution. The intron sequences are more homogenized within a species than are the exons. This pattern can be explained by extreme mutation and recombination pressures on the internally repetitive exons. The iterated sequences within exons encode protein structures that are critical to the function of silks. Therefore, attributes that make silks exceptional biomaterials may also hinder the fixation of optimally adapted protein sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hayashi, C Y -- Lewis, R V -- New York, N.Y. -- Science. 2000 Feb 25;287(5457):1477-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, University of Wyoming, Laramie, WY 82071-3944, USA. hayashi@uwyo.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10688794" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Base Sequence ; Crossing Over, Genetic ; DNA/genetics ; DNA Replication ; *Evolution, Molecular ; *Exons ; Gene Conversion ; *Genes ; *Introns ; Molecular Sequence Data ; Mutation ; Proteins/chemistry/*genetics ; Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; Selection, Genetic ; Species Specificity ; Spiders/*genetics
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  • 23
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    Heterozygous germ line hCHK2 mutations in Li-Fraumeni syndrome (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-01-05
    Description: The hCHK2 gene encodes the human homolog of the yeast Cds1 and Rad53 G2 checkpoint kinases, whose activation in response to DNA damage prevents cellular entry into mitosis. Here, it is shown that heterozygous germ line mutations in hCHK2 occur in Li-Fraumeni syndrome, a highly penetrant familial cancer phenotype usually associated with inherited mutations in the TP53 gene. These observations suggest that hCHK2 is a tumor suppressor gene conferring predisposition to sarcoma, breast cancer, and brain tumors, and they also provide a link between the central role of p53 inactivation in human cancer and the well-defined G2 checkpoint in yeast.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bell, D W -- Varley, J M -- Szydlo, T E -- Kang, D H -- Wahrer, D C -- Shannon, K E -- Lubratovich, M -- Verselis, S J -- Isselbacher, K J -- Fraumeni, J F -- Birch, J M -- Li, F P -- Garber, J E -- Haber, D A -- New York, N.Y. -- Science. 1999 Dec 24;286(5449):2528-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Massachusetts General Hospital Center for Cancer Risk Analysis and Harvard Medical School, Building 149, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10617473" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Apoptosis ; Brain Neoplasms/genetics ; Breast Neoplasms/genetics ; Checkpoint Kinase 2 ; Female ; G1 Phase ; *G2 Phase ; *Genes, Tumor Suppressor ; Genes, p53 ; Genetic Predisposition to Disease ; *Germ-Line Mutation ; Heterozygote ; Humans ; Li-Fraumeni Syndrome/enzymology/*genetics/pathology ; Male ; Pedigree ; Polymorphism, Genetic ; Protein Kinases/genetics ; Protein-Serine-Threonine Kinases/*genetics/metabolism ; Sarcoma/genetics ; Signal Transduction ; Tumor Cells, Cultured
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  • 24
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    Enhanced morphine analgesia in mice lacking beta-arrestin 2 (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-05
    Description: The ability of morphine to alleviate pain is mediated through a heterotrimeric guanine nucleotide binding protein (G protein)-coupled heptahelical receptor (GPCR), the mu opioid receptor (muOR). The efficiency of GPCR signaling is tightly regulated and ultimately limited by the coordinated phosphorylation of the receptors by specific GPCR kinases and the subsequent interaction of the phosphorylated receptors with beta-arrestin 1 and beta-arrestin 2. Functional deletion of the beta-arrestin 2 gene in mice resulted in remarkable potentiation and prolongation of the analgesic effect of morphine, suggesting that muOR desensitization was impaired. These results provide evidence in vivo for the physiological importance of beta-arrestin 2 in regulating the function of a specific GPCR, the muOR. Moreover, they suggest that inhibition of beta-arrestin 2 function might lead to enhanced analgesic effectiveness of morphine and provide potential new avenues for the study and treatment of pain, narcotic tolerance, and dependence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bohn, L M -- Lefkowitz, R J -- Gainetdinov, R R -- Peppel, K -- Caron, M G -- Lin, F T -- F32 DA006023/DA/NIDA NIH HHS/ -- HL16037/HL/NHLBI NIH HHS/ -- NS 19576/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1999 Dec 24;286(5449):2495-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute Laboratories, Departments of Cell Biology and Medicine, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10617462" target="_blank"〉PubMed〈/a〉
    Keywords: Analgesia ; Analgesics, Opioid/administration & dosage/metabolism/*pharmacology ; Animals ; Arrestins/genetics/*physiology ; Binding Sites ; Body Temperature/drug effects ; Brain/metabolism ; Enkephalin, Ala(2)-MePhe(4)-Gly(5)-/pharmacology ; GTP-Binding Proteins/metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Morphine/administration & dosage/metabolism/*pharmacology ; Naloxone/metabolism/pharmacology ; Narcotic Antagonists/metabolism/pharmacology ; Pain Measurement ; Pain Threshold ; Phosphorylation ; Receptors, Opioid, mu/*metabolism ; Signal Transduction
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    Structural assets of a tumor suppressor (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tonks, N K -- Myers, M P -- New York, N.Y. -- Science. 1999 Dec 10;286(5447):2096-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA. tonks@cshl.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10617421" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cell Membrane/metabolism ; Crystallography, X-Ray ; *Genes, Tumor Suppressor ; Humans ; Hydrogen Bonding ; Membrane Lipids/metabolism ; Models, Biological ; Mutation ; Neoplasms/*etiology/genetics ; PTEN Phosphohydrolase ; Phosphatidylinositol 3-Kinases/chemistry/metabolism ; Phosphatidylinositol Phosphates/metabolism ; Phosphoric Monoester Hydrolases/*chemistry/genetics/*metabolism ; Phosphorylation ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Signal Transduction ; *Tumor Suppressor Proteins
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    Checkpoint gene linked to human cancer (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hagmann, M -- New York, N.Y. -- Science. 1999 Dec 24;286(5449):2433-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10636795" target="_blank"〉PubMed〈/a〉
    Keywords: *Cell Cycle ; Checkpoint Kinase 2 ; Genes, Tumor Suppressor ; Genes, p53 ; Humans ; Li-Fraumeni Syndrome/enzymology/*genetics/pathology ; Mutation ; Phosphorylation ; *Protein Kinases ; Protein-Serine-Threonine Kinases/*genetics/metabolism ; Signal Transduction ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53/genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Tracking the movements that shape an embryo (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-04-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, G -- New York, N.Y. -- Science. 2000 Apr 7;288(5463):86-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10766642" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cadherins/genetics/physiology ; Cell Adhesion ; *Cell Movement ; Cell Size ; DNA-Binding Proteins/genetics/physiology ; Embryo, Mammalian/cytology/*physiology ; Embryo, Nonmammalian/cytology/*physiology ; Embryonic Development ; Gastrula/cytology/*physiology ; Morphogenesis ; Neural Crest/cytology/physiology ; Organizers, Embryonic/*physiology ; Signal Transduction ; T-Box Domain Proteins/genetics/physiology ; Transcription Factors/genetics/physiology ; *Zebrafish Proteins
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    T-Independent immune response: new aspects of B cell biology (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-06
    Description: Recent results emphasize the roles of T-independent antibody response in humoral defenses, for which B1 cells and marginal zone B cells are mostly responsible. We discuss how these cells are activated, migrate, and differentiate into antibody-producing cells in various lymphoid tissues. Based on recent findings in each of these areas of B cell biology, we propose a possible mechanism for peripheral tolerance of autoreactive B cells at target organs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fagarasan, S -- Honjo, T -- New York, N.Y. -- Science. 2000 Oct 6;290(5489):89-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Chemistry, Faculty of Medicine, Kyoto University, Yoshida, Sakyo-ku, Kyoto 606-8501, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11021805" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antibody Formation ; Autoantibodies/biosynthesis ; B-Cell Activating Factor ; B-Lymphocytes/cytology/*immunology ; Cell Differentiation ; Cell Movement ; DNA-Binding Proteins/physiology ; Humans ; Immune Tolerance ; Immunity, Innate ; Immunity, Mucosal ; *Lymphocyte Activation ; Lymphoid Tissue/cytology/immunology ; *Membrane Proteins ; Models, Immunological ; Signal Transduction ; T-Lymphocytes/*immunology ; Tumor Necrosis Factor-alpha/physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    The genetic program of hematopoietic stem cells (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-06-02
    Description: Blood cell production originates from a rare population of multipotent, self-renewing stem cells. A genome-wide gene expression analysis was performed in order to define regulatory pathways in stem cells as well as their global genetic program. Subtracted complementary DNA libraries from highly purified murine fetal liver stem cells were analyzed with bioinformatic and array hybridization strategies. A large percentage of the several thousand gene products that have been characterized correspond to previously undescribed molecules with properties suggestive of regulatory functions. The complete data, available in a biological process-oriented database, represent the molecular phenotype of the hematopoietic stem cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Phillips, R L -- Ernst, R E -- Brunk, B -- Ivanova, N -- Mahan, M A -- Deanehan, J K -- Moore, K A -- Overton, G C -- Lemischka, I R -- R01-DK42989/DK/NIDDK NIH HHS/ -- R01-RR04026/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2000 Jun 2;288(5471):1635-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10834841" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Computational Biology ; Databases, Factual ; Expressed Sequence Tags ; *Gene Expression Profiling ; Gene Library ; *Genes ; Hematopoietic Stem Cells/chemistry/cytology/*physiology ; Liver/cytology/embryology ; Membrane Proteins/chemistry/genetics/physiology ; Mice ; Molecular Sequence Data ; Polymerase Chain Reaction ; Proteins/chemistry/*genetics/*physiology ; Signal Transduction ; Transcription Factors/chemistry/genetics/physiology
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    Immunology. Lymphocyte survival--ignorance is BLys (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-29
    Description: As if the TNF receptor and ligand superfamily was not big enough, two new receptors and their ligands have now been added to it. As Laabi and Strasser explain in their Perspective, the receptors BCMA and TACI and their ligands BAFF/BLys and APRIL, respectively, are important for B lymphocyte survival, proliferation, and differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Laabi, Y -- Strasser, A -- New York, N.Y. -- Science. 2000 Aug 11;289(5481):883-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Walter and Eliza Hall Institute of Medical Research, Post Office Royal Victoria, Australia. laabi@wehi.edu.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10960320" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; B-Cell Activating Factor ; B-Cell Maturation Antigen ; B-Lymphocytes/*cytology/*immunology/metabolism ; CD40 Ligand ; Cell Differentiation ; Cell Division ; Cell Survival ; Cytokines/metabolism ; Humans ; Ligands ; Lymphocyte Activation ; Membrane Glycoproteins/metabolism ; Membrane Proteins/*metabolism ; Mice ; NF-kappa B/metabolism ; Neoplasms/etiology/pathology ; Receptors, Antigen, B-Cell/metabolism ; Receptors, Tumor Necrosis Factor/*metabolism ; Signal Transduction ; Transcription Factors/metabolism ; Transmembrane Activator and CAML Interactor Protein ; Tumor Necrosis Factor Ligand Superfamily Member 13 ; Tumor Necrosis Factor-alpha/*metabolism
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    Response of Schwann cells to action potentials in development (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-24
    Description: Sensory axons become functional late in development when Schwann cells (SC) stop proliferating and differentiate into distinct phenotypes. We report that impulse activity in premyelinated axons can inhibit proliferation and differentiation of SCs. This neuron-glial signaling is mediated by adenosine triphosphate acting through P2 receptors on SCs and intracellular signaling pathways involving Ca2+, Ca2+/calmodulin kinase, mitogen-activated protein kinase, cyclic adenosine 3',5'-monophosphate response element binding protein, and expression of c-fos and Krox-24. Adenosine triphosphate arrests maturation of SCs in an immature morphological stage and prevents expression of O4, myelin basic protein, and the formation of myelin. Through this mechanism, functional activity in the developing nervous system could delay terminal differentiation of SCs until exposure to appropriate axon-derived signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stevens, B -- Fields, R D -- New York, N.Y. -- Science. 2000 Mar 24;287(5461):2267-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Developmental Neurobiology, National Institutes of Health, National Institute of Child Health and Human Development, Building 49, Room 5A38, 49 Convent Drive, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10731149" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Adenosine Triphosphate/metabolism ; Animals ; Axons/*physiology ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Cell Differentiation ; Cell Division ; Cells, Cultured ; Coculture Techniques ; Cyclic AMP Response Element-Binding Protein/metabolism ; DNA-Binding Proteins/genetics/metabolism ; Early Growth Response Protein 1 ; Electric Stimulation ; Ganglia, Spinal/physiology ; Gene Expression Regulation, Developmental ; Genes, fos ; *Immediate-Early Proteins ; Mice ; Microscopy, Confocal ; Myelin Sheath/metabolism ; Neurons, Afferent/*physiology ; Phosphorylation ; Proto-Oncogene Proteins c-fos/metabolism ; Receptors, Purinergic P2/metabolism ; Schwann Cells/*cytology/*physiology ; Signal Transduction ; Transcription Factors/genetics/metabolism
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    A Drosophila mechanosensory transduction channel (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-04-01
    Description: Mechanosensory transduction underlies a wide range of senses, including proprioception, touch, balance, and hearing. The pivotal element of these senses is a mechanically gated ion channel that transduces sound, pressure, or movement into changes in excitability of specialized sensory cells. Despite the prevalence of mechanosensory systems, little is known about the molecular nature of the transduction channels. To identify such a channel, we analyzed Drosophila melanogaster mechanoreceptive mutants for defects in mechanosensory physiology. Loss-of-function mutations in the no mechanoreceptor potential C (nompC) gene virtually abolished mechanosensory signaling. nompC encodes a new ion channel that is essential for mechanosensory transduction. As expected for a transduction channel, D. melanogaster NOMPC and a Caenorhabditis elegans homolog were selectively expressed in mechanosensory organs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walker, R G -- Willingham, A T -- Zuker, C S -- 5T32GM08107/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Mar 24;287(5461):2229-34.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Howard Hughes Medical Institute, University of California, San Diego,CA 92093-0649, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10744543" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Adaptation, Physiological ; Amino Acid Sequence ; Animals ; Caenorhabditis elegans/genetics/physiology ; Chromosome Mapping ; Cloning, Molecular ; Dendrites/physiology ; *Drosophila Proteins ; Drosophila melanogaster/genetics/*physiology ; Gene Expression Profiling ; Genes, Insect ; Hair Cells, Auditory/physiology ; Insect Proteins/chemistry/genetics/physiology ; Ion Channels/chemistry/*genetics/*physiology ; Mechanoreceptors/*physiology ; Molecular Sequence Data ; Mutation ; Neurons, Afferent/*physiology ; Patch-Clamp Techniques ; Physical Stimulation ; Proprioception ; Sensation/physiology ; Sense Organs/physiology ; Signal Transduction ; Touch ; Transient Receptor Potential Channels
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    Neuronal plasticity: increasing the gain in pain (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-06-10
    Description: We describe those sensations that are unpleasant, intense, or distressing as painful. Pain is not homogeneous, however, and comprises three categories: physiological, inflammatory, and neuropathic pain. Multiple mechanisms contribute, each of which is subject to or an expression of neural plasticity-the capacity of neurons to change their function, chemical profile, or structure. Here, we develop a conceptual framework for the contribution of plasticity in primary sensory and dorsal horn neurons to the pathogenesis of pain, identifying distinct forms of plasticity, which we term activation, modulation, and modification, that by increasing gain, elicit pain hypersensitivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Woolf, C J -- Salter, M W -- New York, N.Y. -- Science. 2000 Jun 9;288(5472):1765-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neural Plasticity Research Group, Department of Anesthesia and Critical Care, Massachusetts General Hospital and Harvard Medical School, MGH-East, Charlestown, MA 02129, USA. woolf.clifford@mgh.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10846153" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Humans ; Inflammation/physiopathology ; Models, Neurological ; *Neuronal Plasticity ; Neurons, Afferent/*physiology ; Nociceptors/physiology ; Pain/*physiopathology ; Peripheral Nerve Injuries ; Posterior Horn Cells/*physiology ; Signal Transduction ; Synaptic Transmission
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    Global analysis of the genetic network controlling a bacterial cell cycle (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-12-16
    Description: This report presents full-genome evidence that bacterial cells use discrete transcription patterns to control cell cycle progression. Global transcription analysis of synchronized Caulobacter crescentus cells was used to identify 553 genes (19% of the genome) whose messenger RNA levels varied as a function of the cell cycle. We conclude that in bacteria, as in yeast, (i) genes involved in a given cell function are activated at the time of execution of that function, (ii) genes encoding proteins that function in complexes are coexpressed, and (iii) temporal cascades of gene expression control multiprotein structure biogenesis. A single regulatory factor, the CtrA member of the two-component signal transduction family, is directly or indirectly involved in the control of 26% of the cell cycle-regulated genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Laub, M T -- McAdams, H H -- Feldblyum, T -- Fraser, C M -- Shapiro, L -- GM32506/GM/NIGMS NIH HHS/ -- GM51426/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Dec 15;290(5499):2144-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology, Beckman Center, Stanford University School of Medicine, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11118148" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/genetics/metabolism ; Binding Sites ; Caulobacter crescentus/*cytology/*genetics/growth & development/physiology ; Cell Cycle/*genetics ; Chemotaxis/genetics ; *DNA-Binding Proteins ; DNA-Directed RNA Polymerases/genetics ; Fimbriae Proteins ; Flagella/metabolism ; Gene Expression Profiling ; *Gene Expression Regulation, Bacterial ; Interphase ; Membrane Proteins/genetics ; Oligonucleotide Array Sequence Analysis ; RNA, Bacterial/genetics/metabolism ; RNA, Messenger/genetics/metabolism ; S Phase ; Signal Transduction ; *Transcription Factors ; Transcription, Genetic
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    Structure and function of a human TAFII250 double bromodomain module (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-05-29
    Description: TFIID is a large multiprotein complex that initiates assembly of the transcription machinery. It is unclear how TFIID recognizes promoters in vivo when templates are nucleosome-bound. Here, it is shown that TAFII250, the largest subunit of TFIID, contains two tandem bromodomain modules that bind selectively to multiply acetylated histone H4 peptides. The 2.1 angstrom crystal structure of the double bromodomain reveals two side-by-side, four-helix bundles with a highly polarized surface charge distribution. Each bundle contains an Nepsilon-acetyllysine binding pocket at its center, which results in a structure ideally suited for recognition of diacetylated histone H4 tails. Thus, TFIID may be targeted to specific chromatin-bound promoters and may play a role in chromatin recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobson, R H -- Ladurner, A G -- King, D S -- Tjian, R -- New York, N.Y. -- Science. 2000 May 26;288(5470):1422-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Molecular and Cell Biology, 401 Barker Hall, University of California, Berkeley, CA 94720-3204, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10827952" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Cloning, Molecular ; Crystallography, X-Ray ; DNA-Binding Proteins/*chemistry/genetics/*metabolism ; Histone Acetyltransferases ; Histones/metabolism ; Humans ; Lysine/analogs & derivatives/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nuclear Proteins/*chemistry/genetics/*metabolism ; Nucleosomes/metabolism ; Promoter Regions, Genetic ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; *TATA-Binding Protein Associated Factors ; *Transcription Factor TFIID ; *Transcription, Genetic
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    Inhibition of eukaryotic DNA replication by geminin binding to Cdt1 (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-12-23
    Description: In all eukaryotic organisms, inappropriate firing of replication origins during the G2 phase of the cell cycle is suppressed by cyclin-dependent kinases. Multicellular eukaryotes contain a second putative inhibitor of re-replication called geminin. Geminin is believed to block binding of the mini-chromosome maintenance (MCM) complex to origins of replication, but the mechanism of this inhibition is unclear. Here we show that geminin interacts tightly with Cdt1, a recently identified replication initiation factor necessary for MCM loading. The inhibition of DNA replication by geminin that is observed in cell-free DNA replication extracts is reversed by the addition of excess Cdt1. In the normal cell cycle, Cdt1 is present only in G1 and S, whereas geminin is present in S and G2 phases of the cell cycle. Together, these results suggest that geminin inhibits inappropriate origin firing by targeting Cdt1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wohlschlegel, J A -- Dwyer, B T -- Dhar, S K -- Cvetic, C -- Walter, J C -- Dutta, A -- CA60499/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2000 Dec 22;290(5500):2309-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Brigham and Women's Hospital, Harvard Medical School, 75 Francis Street, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11125146" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Cycle Proteins/chemistry/*metabolism/pharmacology ; Cell Nucleus/metabolism ; Cell-Free System ; Chromatin/metabolism ; *DNA Replication ; DNA-Binding Proteins/chemistry/*metabolism/pharmacology ; Evolution, Molecular ; G1 Phase ; G2 Phase ; Geminin ; HeLa Cells ; Humans ; *Interphase ; Molecular Sequence Data ; Molecular Weight ; Precipitin Tests ; Recombinant Fusion Proteins/metabolism ; Replication Origin ; *S Phase ; Xenopus ; Xenopus Proteins
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    Regulation of STAT3 by direct binding to the Rac1 GTPase (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-06
    Description: The signal transducers and activators of transcription (STAT) transcription factors become phosphorylated on tyrosine and translocate to the nucleus after stimulation of cells with growth factors or cytokines. We show that the Rac1 guanosine triphosphatase can bind to and regulate STAT3 activity. Dominant negative Rac1 inhibited STAT3 activation by growth factors, whereas activated Rac1 stimulated STAT3 phosphorylation on both tyrosine and serine residues. Moreover, activated Rac1 formed a complex with STAT3 in mammalian cells. Yeast two-hybrid analysis indicated that STAT3 binds directly to active but not inactive Rac1 and that the interaction occurs via the effector domain. Rac1 may serve as an alternate mechanism for targeting STAT3 to tyrosine kinase signaling complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simon, A R -- Vikis, H G -- Stewart, S -- Fanburg, B L -- Cochran, B H -- Guan, K L -- GM-54304/GM/NIGMS NIH HHS/ -- K08-HL-03547/HL/NHLBI NIH HHS/ -- P30-DK34928/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 2000 Oct 6;290(5489):144-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pulmonary and Critical Care Division, Tupper Research Institute, New England Medical Center, Boston, MA 02111, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11021801" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; COS Cells ; Cell Line ; Cercopithecus aethiops ; DNA-Binding Proteins/genetics/*metabolism ; Enzyme Activation ; Epidermal Growth Factor/pharmacology ; Gene Expression Regulation ; Genes, Reporter ; Genetic Vectors ; Guanine Nucleotide Exchange Factors/genetics/metabolism ; Humans ; Janus Kinase 2 ; Mutation ; Neoplasm Proteins ; Phosphorylation ; Phosphoserine/metabolism ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/metabolism ; Proteins/genetics/metabolism ; *Proto-Oncogene Proteins ; Rats ; STAT3 Transcription Factor ; Signal Transduction ; Trans-Activators/genetics/*metabolism ; Transfection ; Two-Hybrid System Techniques ; rac1 GTP-Binding Protein/genetics/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    A H+-gated urea channel: the link between Helicobacter pylori urease and gastric colonization (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-22
    Description: Acidic media trigger cytoplasmic urease activity of the unique human gastric pathogen Helicobacter pylori. Deletion of ureI prevents this activation of cytoplasmic urease that is essential for bacterial acid resistance. UreI is an inner membrane protein with six transmembrane segments as shown by in vitro transcription/translation and membrane separation. Expression of UreI in Xenopus oocytes results in acid-stimulated urea uptake, with a pH profile similar to activation of cytoplasmic urease. Mutation of periplasmic histidine 123 abolishes stimulation. UreI-mediated transport is urea specific, passive, nonsaturable, nonelectrogenic, and temperature independent. UreI functions as a H+-gated urea channel regulating cytoplasmic urease that is essential for gastric survival and colonization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weeks, D L -- Eskandari, S -- Scott, D R -- Sachs, G -- DK41301/DK/NIDDK NIH HHS/ -- DK43462/DK/NIDDK NIH HHS/ -- DK46917/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 2000 Jan 21;287(5452):482-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉VA Greater Los Angeles Healthcare System and Department of Physiology, University of California, Los Angeles, CA 90073, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10642549" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Proteins/chemistry/genetics/*metabolism ; Biological Transport ; Cell Membrane/chemistry ; Cell Membrane Permeability ; Cytoplasm/enzymology/metabolism ; Enzyme Activation ; Gastric Acid ; Glycosylation ; Helicobacter pylori/enzymology/growth & development/*metabolism ; Histidine/metabolism ; Humans ; Hydrogen-Ion Concentration ; *Membrane Transport Proteins ; Molecular Sequence Data ; Oocytes/enzymology ; Recombinant Proteins/metabolism ; Stomach/*microbiology ; Temperature ; Urea/*metabolism ; Urease/*metabolism ; Xenopus
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    Response to RAG-mediated VDJ cleavage by NBS1 and gamma-H2AX (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-12-09
    Description: Genetic disorders affecting cellular responses to DNA damage are characterized by high rates of translocations involving antigen receptor loci and increased susceptibility to lymphoid malignancies. We report that the Nijmegen breakage syndrome protein (NBS1) and histone gamma-H2AX, which associate with irradiation-induced DNA double-strand breaks (DSBs), are also found at sites of VDJ (variable, diversity, joining) recombination-induced DSBs. In developing thymocytes, NBS1 and gamma-H2AX form nuclear foci that colocalize with the T cell receptor alpha locus in response to recombination activating gene (RAG) protein-mediated VDJ cleavage. Our results suggest that surveillance of T cell receptor recombination intermediates by NBS1 and gamma-H2AX may be important for preventing oncogenic translocations.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4721589/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4721589/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, H T -- Bhandoola, A -- Difilippantonio, M J -- Zhu, J -- Brown, M J -- Tai, X -- Rogakou, E P -- Brotz, T M -- Bonner, W M -- Ried, T -- Nussenzweig, A -- Z99 CA999999/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2000 Dec 8;290(5498):1962-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11110662" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Nucleus/metabolism ; DNA Damage ; DNA-Binding Proteins/metabolism ; Fluorescent Antibody Technique ; *Gene Rearrangement, alpha-Chain T-Cell Antigen Receptor ; *Genes, T-Cell Receptor alpha ; Histones/*metabolism ; Homeodomain Proteins/metabolism ; Mice ; Mice, Transgenic ; Microscopy, Confocal ; Molecular Sequence Data ; Nuclear Proteins/*metabolism ; Phosphorylation ; *Recombination, Genetic ; T-Lymphocytes/*metabolism
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    Dual signaling regulated by calcyon, a D1 dopamine receptor interacting protein (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-04
    Description: The synergistic response of cells to the stimulation of multiple receptors has been ascribed to receptor cross talk; however, the specific molecules that mediate the resultant signal amplification have not been defined. Here a 24-kilodalton single transmembrane protein, designated calcyon, we functionally characterize that interacts with the D1 dopamine receptor. Calcyon localizes to dendritic spines of D1 receptor-expressing pyramidal cells in prefrontal cortex. These studies delineate a mechanism of Gq- and Gs-coupled heterotrimeric GTP-binding protein-coupled receptor cross talk by which D1 receptors can shift effector coupling to stimulate robust intracellular calcium (Ca2+i) release as a result of interaction with calcyon. The role of calcyon in potentiating Ca2+-dependent signaling should provide insight into the D1 receptor-modulated cognitive functions of prefrontal cortex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lezcano, N -- Mrzljak, L -- Eubanks, S -- Levenson, R -- Goldman-Rakic, P -- Bergson, C -- MH56608/MH/NIMH NIH HHS/ -- P50 MH068789/MH/NIMH NIH HHS/ -- P50 MH44866/MH/NIMH NIH HHS/ -- R01 MH063271/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2000 Mar 3;287(5458):1660-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology and Toxicology, Medical College of Georgia, Augusta, GA 30912-2300, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10698743" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Benzazepines/pharmacology ; Brain/cytology/metabolism ; Calcium/metabolism ; Calcium Signaling ; Cell Line ; Cyclic AMP/metabolism ; Dendrites/chemistry/metabolism ; Dopamine Agonists/pharmacology ; Female ; Heterotrimeric GTP-Binding Proteins/metabolism ; Humans ; Macaca mulatta ; Membrane Proteins/analysis/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Prefrontal Cortex/cytology/*metabolism ; Pyramidal Cells/chemistry/*metabolism ; Rabbits ; *Receptor Cross-Talk ; Receptors, Dopamine D1/analysis/*metabolism ; Receptors, Neurotransmitter/metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Two-Hybrid System Techniques
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    Role of the guanosine triphosphatase Rac2 in T helper 1 cell differentiation (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-06-24
    Description: T helper 1 (TH1) cells mediate cellular immunity, whereas TH2 cells potentiate antiparasite and humoral immunity. We used a complementary DNA subtraction method, representational display analysis, to show that the small guanosine triphosphatase Rac2 is expressed selectively in murine TH1 cells. Rac induces the interferon-gamma (IFN-gamma) promoter through cooperative activation of the nuclear factor kappa B and p38 mitogen-activated protein kinase pathways. Tetracycline-regulated transgenic mice expressing constitutively active Rac2 in T cells exhibited enhanced IFN-gamma production. Dominant-negative Rac inhibited IFN-gamma production in murine T cells. Moreover, T cells from Rac2-/- mice showed decreased IFN-gamma production under TH1 conditions in vitro. Thus, Rac2 activates TH1-specific signaling and IFN-gamma gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, B -- Yu, H -- Zheng, W -- Voll, R -- Na, S -- Roberts, A W -- Williams, D A -- Davis, R J -- Ghosh, S -- Flavell, R A -- New York, N.Y. -- Science. 2000 Jun 23;288(5474):2219-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Immunobiology and Howard Hughes Medical Institute, Yale University School of Medicine, 310 Cedar Street, New Haven, CT 06520-8011, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10864872" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cells, Cultured ; Cytokines/biosynthesis/genetics ; Gene Expression Regulation ; Humans ; Interferon-gamma/biosynthesis/*genetics ; JNK Mitogen-Activated Protein Kinases ; Jurkat Cells ; Lymphocyte Activation ; Mice ; Mice, Transgenic ; Mitogen-Activated Protein Kinases/metabolism ; NF-kappa B/metabolism ; Promoter Regions, Genetic ; Signal Transduction ; Th1 Cells/cytology/*immunology/*metabolism ; Transfection ; p38 Mitogen-Activated Protein Kinases ; rac GTP-Binding Proteins/genetics/*metabolism
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    Regulation of abscisic acid-induced stomatal closure and anion channels by guard cell AAPK kinase (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-15
    Description: Abscisic acid (ABA) stimulates stomatal closure and thus supports water conservation by plants during drought. Mass spectrometry-generated peptide sequence information was used to clone a Vicia faba complementary DNA, AAPK, encoding a guard cell-specific ABA-activated serine-threonine protein kinase (AAPK). Expression in transformed guard cells of AAPK altered by one amino acid (lysine 43 to alanine 43) renders stomata insensitive to ABA-induced closure by eliminating ABA activation of plasma membrane anion channels. This information should allow cell-specific, targeted biotechnological manipulation of crop water status.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, J -- Wang, X Q -- Watson, M B -- Assmann, S M -- New York, N.Y. -- Science. 2000 Jan 14;287(5451):300-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, The Pennsylvania State University, 208 Mueller Laboratory, University Park, PA 16802, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10634783" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid/*pharmacology ; Amino Acid Sequence ; Anions/*metabolism ; Biolistics ; Cloning, Molecular ; DNA, Complementary ; Enzyme Activation ; Fabaceae/cytology/enzymology/genetics/*physiology ; Genes, Plant ; Ion Channels/*metabolism ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Patch-Clamp Techniques ; Plant Leaves/cytology/enzymology/*physiology ; *Plant Proteins ; *Plants, Medicinal ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Protoplasts/enzymology/metabolism ; Recombinant Fusion Proteins/metabolism ; Transformation, Genetic
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    Extended life-span conferred by cotransporter gene mutations in Drosophila (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-12-16
    Description: Aging is genetically determined and environmentally modulated. In a study of longevity in the adult fruit fly, Drosophila melanogaster, we found that five independent P-element insertional mutations in a single gene resulted in a near doubling of the average adult life-span without a decline in fertility or physical activity. Sequence analysis revealed that the product of this gene, named Indy (for I'm not dead yet), is most closely related to a mammalian sodium dicarboxylate cotransporter-a membrane protein that transports Krebs cycle intermediates. Indy was most abundantly expressed in the fat body, midgut, and oenocytes: the principal sites of intermediary metabolism in the fly. Excision of the P element resulted in a reversion to normal life-span. These mutations may create a metabolic state that mimics caloric restriction, which has been shown to extend life-span.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rogina, B -- Reenan, R A -- Nilsen, S P -- Helfand, S L -- AG14532/AG/NIA NIH HHS/ -- AG16667/AG/NIA NIH HHS/ -- R37 AG016667/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2000 Dec 15;290(5499):2137-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics and Developmental Biology, School of Medicine, University of Connecticut Health Center, 263 Farmington Avenue, Farmington CT 06030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11118146" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*genetics ; Amino Acid Sequence ; Animals ; Behavior, Animal ; Biological Transport ; Carrier Proteins/chemistry/*genetics/metabolism ; Crosses, Genetic ; DNA Transposable Elements ; *Dicarboxylic Acid Transporters ; Digestive System/metabolism ; *Drosophila Proteins ; Drosophila melanogaster/*genetics/metabolism/physiology ; Energy Intake ; Energy Metabolism ; Fat Body/metabolism ; Female ; Fertility ; Gene Expression ; *Genes, Insect ; Longevity/*genetics ; Male ; Membrane Proteins/chemistry/metabolism ; Molecular Sequence Data ; Mutagenesis, Insertional ; Mutagenesis, Site-Directed ; *Organic Anion Transporters, Sodium-Dependent ; Sense Organs/cytology/metabolism ; Sequence Homology, Amino Acid ; *Symporters
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    Biomedicine. New insights into type 2 diabetes (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-08-06
    Description: Researchers studying type 2 diabetes are optimistic that they are closing in on the elusive causes of the world's most prevalent metabolic disorder--although no one is willing to bet the bank on it. Using both biochemical and genetic approaches, diabetes researchers have identified multiple intracellular signaling pathways that appear to lie at the heart of this condition, which affects some 250 million people worldwide and is the leading cause of blindness, kidney failure, and amputation among adults. And in the process, they have thrown out much of the dogma of the past 10 years.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alper, J -- New York, N.Y. -- Science. 2000 Jul 7;289(5476):37-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10928926" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Animals ; Diabetes Mellitus, Type 2/*metabolism ; Glucose/metabolism ; Humans ; Insulin/*metabolism ; Insulin Receptor Substrate Proteins ; Insulin Resistance ; Intracellular Signaling Peptides and Proteins ; Islets of Langerhans/metabolism ; Liver/metabolism ; Mice ; Mice, Knockout ; Muscles/metabolism ; Phosphoproteins/genetics/*metabolism ; Receptor, Insulin/metabolism ; Signal Transduction
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    Development. PARallels in axis formation (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-07-06
    Description: There is an intricate network of molecules called cell fate determinants that instruct the cells of the embryo to take on either an anterior or posterior fate. In a lively Perspective, Lehmann and her colleagues discuss new findings in the fruit fly that identify a key protein, PAR-1, which ensures that the cell fate determinants are themselves located in the correct region of the oocyte. In this way, the anterior-posterior axis is set up in the fruit fly egg before fertilization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morris, J -- Lehmann, R -- Navarro, C -- New York, N.Y. -- Science. 2000 Jun 9;288(5472):1759-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Developmental Genetics Program, Skirball Institute, Howard Hughes Medical Institute, Department of Cell Biology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10877696" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/physiology ; Animals ; *Body Patterning ; Caenorhabditis elegans/*embryology/genetics/physiology ; Cell Polarity ; Centrosome/physiology ; Drosophila/*embryology/genetics/physiology ; *Drosophila Proteins ; Homeodomain Proteins/genetics/metabolism ; Insect Proteins/genetics/metabolism ; Microtubules/physiology ; Mutation ; Oocytes/physiology ; Protein-Serine-Threonine Kinases/genetics/*physiology ; RNA, Messenger/genetics/metabolism ; RNA-Binding Proteins/genetics/metabolism ; Signal Transduction ; Trans-Activators/genetics/metabolism
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    A calmodulin-related protein that suppresses posttranscriptional gene silencing in plants (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-06
    Description: Posttranscriptional gene silencing (PTGS) is an ancient eukaryotic regulatory mechanism in which a particular RNA sequence is targeted and destroyed. The helper component-proteinase (HC-Pro) of plant potyviruses suppresses PTGS in plants. Using a yeast two-hybrid system, we identified a calmodulin-related protein (termed rgs-CaM) that interacts with HC-Pro. Here we report that rgs-CaM, like HC-Pro itself, suppresses gene silencing. Our work is the first report identifying a cellular suppressor of PTGS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anandalakshmi, R -- Marathe, R -- Ge, X -- Herr, J M Jr -- Mau, C -- Mallory, A -- Pruss, G -- Bowman, L -- Vance, V B -- New York, N.Y. -- Science. 2000 Oct 6;290(5489):142-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of South Carolina, Columbia, SC 29208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11021800" target="_blank"〉PubMed〈/a〉
    Keywords: Agrobacterium tumefaciens/genetics ; Amino Acid Sequence ; Cysteine Endopeptidases/*metabolism ; *Gene Silencing ; Genes, Plant ; Green Fluorescent Proteins ; Luminescent Proteins/genetics ; Molecular Sequence Data ; Plant Proteins/chemistry/genetics/*metabolism ; Plant Tumors/genetics ; Plants, Genetically Modified ; *Plants, Toxic ; Plasmids ; Potexvirus/genetics ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism ; Tobacco/*genetics/metabolism ; Transcription, Genetic ; Transgenes ; Viral Proteins/*metabolism
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    Cell biology. Bacterial spelunkers (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-08-19
    Description: Bacteria that are engulfed by phagocytic cells of the immune system are usually destroyed once inside the host cell but not always. Why is it that sometimes engulfed bacteria survive and thrive quite happily inside the host cell? As Mulvey and Hultgren explain in their Perspective, the answer may lie in small indentations in the host cell plasma membrane called caveolae that direct certain signal transduction pathways inside the host cell (Shin et al.). If bacteria adhere to regions of the host cell surface that is rich in caveolae, they are better able to survive once inside the cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mulvey, M A -- Hultgren, S J -- New York, N.Y. -- Science. 2000 Aug 4;289(5480):732-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110-1093, USA. mulvey@borcim.wustl.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10950716" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/metabolism ; *Adhesins, Escherichia coli ; Animals ; Antigens, CD/metabolism ; Bacterial Adhesion ; Caveolin 1 ; *Caveolins ; Cell Membrane/chemistry/*metabolism/microbiology/ultrastructure ; *Endocytosis ; Escherichia coli/*metabolism/pathogenicity ; *Fimbriae Proteins ; Glycosylphosphatidylinositols/metabolism ; Macrophages/microbiology ; Mast Cells/metabolism/*microbiology/ultrastructure ; Membrane Proteins/analysis ; Mice ; Signal Transduction
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    Candidate taste receptors in Drosophila (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-03-10
    Description: Little is known about the molecular mechanisms of taste perception in animals, particularly the initial events of taste signaling. A large and diverse family of seven transmembrane domain proteins was identified from the Drosophila genome database with a computer algorithm that identifies proteins on the basis of structure. Eighteen of 19 genes examined were expressed in the Drosophila labellum, a gustatory organ of the proboscis. Expression was not detected in a variety of other tissues. The genes were not expressed in the labellum of a Drosophila mutant, pox-neuro70, in which taste neurons are eliminated. Tissue specificity of expression of these genes, along with their structural similarity, supports the possibility that the family encodes a large and divergent family of taste receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clyne, P J -- Warr, C G -- Carlson, J R -- DC-02174/DC/NIDCD NIH HHS/ -- New York, N.Y. -- Science. 2000 Mar 10;287(5459):1830-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, and Developmental Biology, Yale University, Post Office Box 208103, New Haven, CT 06520-8103, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10710312" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Alternative Splicing ; Amino Acid Sequence ; Animals ; Chemoreceptor Cells/*metabolism ; *Drosophila Proteins ; Drosophila melanogaster/chemistry/*genetics/physiology ; Exons ; Gene Expression ; Genes, Insect ; In Situ Hybridization ; Insect Proteins/chemistry/*genetics/physiology ; Membrane Proteins/chemistry/*genetics/physiology ; Molecular Sequence Data ; Multigene Family ; Neurons, Afferent/*metabolism ; Organ Specificity ; Protein Structure, Tertiary ; Receptors, Cell Surface/chemistry/*genetics/physiology ; Reverse Transcriptase Polymerase Chain Reaction ; Sense Organs/chemistry/physiology ; Sequence Alignment ; Taste/physiology
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    Activating mineralocorticoid receptor mutation in hypertension exacerbated by pregnancy (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-07-07
    Description: Hypertension and pregnancy-related hypertension are major public health problems of largely unknown causes. We describe a mutation in the mineralocorticoid receptor (MR), S810L, that causes early-onset hypertension that is markedly exacerbated in pregnancy. This mutation results in constitutive MR activity and alters receptor specificity, with progesterone and other steroids lacking 21-hydroxyl groups, normally MR antagonists, becoming potent agonists. Structural and biochemical studies indicate that the mutation results in the gain of a van der Waals interaction between helix 5 and helix 3 that substitutes for interaction of the steroid 21-hydroxyl group with helix 3 in the wild-type receptor. This helix 5-helix 3 interaction is highly conserved among diverse nuclear hormone receptors, suggesting its general role in receptor activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geller, D S -- Farhi, A -- Pinkerton, N -- Fradley, M -- Moritz, M -- Spitzer, A -- Meinke, G -- Tsai, F T -- Sigler, P B -- Lifton, R P -- New York, N.Y. -- Science. 2000 Jul 7;289(5476):119-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Genetics, Yale University School of Medicine, Boyer Center for Molecular Medicine, Room 154, 295 Congress Avenue, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10884226" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Aldosterone/*metabolism ; Amino Acid Sequence ; Amino Acid Substitution ; Base Sequence ; Binding, Competitive ; Dimerization ; Female ; Heterozygote ; Humans ; Hypertension/etiology/*genetics/metabolism ; Male ; Models, Molecular ; Molecular Sequence Data ; Pedigree ; Point Mutation ; Pregnancy ; *Pregnancy Complications, Cardiovascular/etiology/metabolism ; Progesterone/*metabolism ; Protein Conformation ; Protein Structure, Secondary ; Receptors, Mineralocorticoid/chemistry/*genetics/*metabolism ; Receptors, Steroid/chemistry/metabolism ; Steroids/metabolism
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    Regulation of JNK by Src during Drosophila development (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-15
    Description: In Drosophila, the Jun amino-terminal kinase (JNK) homolog Basket (Bsk) is required for epidermal closure. Mutants for Src42A, a Drosophila c-src protooncogene homolog, are described. Src42A functions in epidermal closure during both embryogenesis and metamorphosis. The severity of the epidermal closure defect in the Src42A mutant depended on the amount of Bsk activity, and the amount of Bsk activity depended on the amount of Src42A. Thus, activation of the Bsk pathway is required downstream of Src42A in epidermal closure. This work confirms mammalian studies that demonstrated a physiological link between Src and JNK.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tateno, M -- Nishida, Y -- Adachi-Yamada, T -- New York, N.Y. -- Science. 2000 Jan 14;287(5451):324-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10634792" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Animals ; Drosophila/embryology/genetics/*growth & development/metabolism ; *Drosophila Proteins ; Enzyme Activation ; Epidermis/embryology ; Genes, Insect ; Insect Proteins/genetics/metabolism ; JNK Mitogen-Activated Protein Kinases ; Metamorphosis, Biological ; Mitogen-Activated Protein Kinases/*metabolism ; Phenotype ; Phosphoprotein Phosphatases/genetics/metabolism ; Phosphorylation ; Phosphotyrosine/metabolism ; Point Mutation ; Protein-Tyrosine Kinases/genetics/*metabolism ; Proto-Oncogene Proteins/genetics/*metabolism ; Signal Transduction
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    Aureusidin synthase: a polyphenol oxidase homolog responsible for flower coloration (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-11-10
    Description: Aurones are plant flavonoids that provide yellow color to the flowers of some popular ornamental plants, such as snapdragon and cosmos. In this study, we have identified an enzyme responsible for the synthesis of aurone from chalcones in the yellow snapdragon flower. The enzyme (aureusidin synthase) is a 39-kilodalton, copper-containing glycoprotein catalyzing the hydroxylation and/or oxidative cyclization of the precursor chalcones, 2',4',6',4-tetrahydroxychalcone and 2',4',6',3,4-pentahydroxychalcone. The complementary DNA encoding aureusidin synthase is expressed in the petals of aurone-containing varieties. DNA sequence analysis revealed that aureusidin synthase belongs to the plant polyphenol oxidase family, providing an unequivocal example of the function of the polyphenol oxidase homolog in plants, i.e., flower coloration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakayama, T -- Yonekura-Sakakibara, K -- Sato, T -- Kikuchi, S -- Fukui, Y -- Fukuchi-Mizutani, M -- Ueda, T -- Nakao, M -- Tanaka, Y -- Kusumi, T -- Nishino, T -- New York, N.Y. -- Science. 2000 Nov 10;290(5494):1163-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Aoba-yama 07, Sendai 980-8579, Japan. nakayama@seika.che.tohoku.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11073455" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Angiosperms/*enzymology/genetics ; Benzofurans/*metabolism ; Catalysis ; Catechol Oxidase/chemistry/metabolism ; Cyclization ; DNA, Complementary ; Enzyme Precursors/chemistry/genetics/isolation & purification/metabolism ; Genes, Plant ; Hydroxylation ; Mixed Function Oxygenases/chemistry/genetics/isolation & purification/metabolism ; Molecular Sequence Data ; Molecular Weight ; Pigmentation ; Plant Structures/enzymology ; Plants/enzymology ; Sequence Homology, Amino Acid
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    Role of adenine nucleotide translocator 1 in mtDNA maintenance (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-05
    Description: Autosomal dominant progressive external ophthalmoplegia is a rare human disease that shows a Mendelian inheritance pattern, but is characterized by large-scale mitochondrial DNA (mtDNA) deletions. We have identified two heterozygous missense mutations in the nuclear gene encoding the heart/skeletal muscle isoform of the adenine nucleotide translocator (ANT1) in five families and one sporadic patient. The familial mutation substitutes a proline for a highly conserved alanine at position 114 in the ANT1 protein. The analogous mutation in yeast caused a respiratory defect. These results indicate that ANT has a role in mtDNA maintenance and that a mitochondrial disease can be caused by a dominant mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaukonen, J -- Juselius, J K -- Tiranti, V -- Kyttala, A -- Zeviani, M -- Comi, G P -- Keranen, S -- Peltonen, L -- Suomalainen, A -- 1180/Telethon/Italy -- New York, N.Y. -- Science. 2000 Aug 4;289(5480):782-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Public Health Institute, Department of Human Molecular Genetics, Mannerheimintie 166, 00300 Helsinki, Finland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10926541" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; DNA, Mitochondrial/*genetics/*metabolism ; Female ; Founder Effect ; Genes, Dominant ; Humans ; Isoenzymes/chemistry/genetics/metabolism ; Italy ; Male ; Mitochondrial ADP, ATP Translocases/chemistry/*genetics/*metabolism ; Molecular Sequence Data ; Mutation, Missense ; Ophthalmoplegia, Chronic Progressive External/enzymology/*genetics ; Oxygen Consumption ; Pedigree ; Point Mutation ; Saccharomyces cerevisiae/enzymology/genetics/metabolism ; Sequence Deletion ; Transformation, Genetic
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    Cell biology. A universal bicarbonate sensor (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-08-12
    Description: The life-span of sperm may be short but it is certainly busy. The three principal molecular events that prepare sperm for fertilization are all controlled by the intracellular nucleotide adenosine 3',5'-monophosphate (cAMP). One of these, capacitation, is also regulated by bicarbonate ions. The elusive connection between cAMP and bicarbonate ions now appears to be solved as Kaupp and Weyand explain in their Perspective. Bicarbonate ions enter sperm through the anion transporter in the sperm plasma membrane and activate the soluble form of adenylyl cyclase, the enzyme that synthesizes cAMP (Chen et al.)〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaupp, U B -- Weyand, I -- New York, N.Y. -- Science. 2000 Jul 28;289(5479):559-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biologische Informationsverarbeitung, Forschungszentrum Jlich, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10939966" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/chemistry/*metabolism ; Animals ; Bicarbonates/*metabolism/pharmacology ; Calcium Channels/metabolism ; Catalytic Domain ; Cyclic AMP/*metabolism ; Cyclic Nucleotide-Gated Cation Channels ; Enzyme Activation ; Humans ; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels ; Ion Channels/metabolism ; Male ; Molecular Weight ; *Muscle Proteins ; Potassium Channels ; Rats ; Signal Transduction ; Solubility ; *Sperm Capacitation ; Sperm Motility ; Sperm Tail/physiology ; Spermatozoa/metabolism/*physiology
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    A metalloprotease disintegrin that controls cell migration in Caenorhabditis elegans (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-06-24
    Description: In Caenorhabditis elegans, the gonad acquires two U-shaped arms by the directed migration of its distal tip cells (DTCs) along the body wall basement membranes. Correct migration of DTCs requires the mig-17 gene, which encodes a member of the metalloprotease-disintegrin protein family. The MIG-17 protein is secreted from muscle cells of the body wall and localizes in the basement membranes of gonad. This localization is dependent on the disintegrin-like domain of MIG-17 and its catalytic activity. These results suggest that the MIG-17 metalloprotease directs migration of DTCs by remodeling the basement membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nishiwaki, K -- Hisamoto, N -- Matsumoto, K -- New York, N.Y. -- Science. 2000 Jun 23;288(5474):2205-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉PRESTO, Japan Science and Technology Corporation and Fundamental Research Laboratories, NEC Corporation, Miyukigaoka, Tsukuba 305-8501, Japan.nishiwak@frl.cl.nec.co.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10864868" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Basement Membrane/enzymology ; Caenorhabditis elegans/cytology/*enzymology/genetics/growth & development ; *Caenorhabditis elegans Proteins ; Cell Movement ; Cloning, Molecular ; Disintegrins/chemistry/genetics/*metabolism ; Extracellular Matrix/*metabolism ; Gene Expression Profiling ; Genes, Helminth ; Glycosylation ; Gonads/cytology/enzymology/growth & development ; Metalloendopeptidases/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Muscles/cytology/enzymology ; Mutation ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism ; Sequence Alignment ; Transgenes
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    Asef, a link between the tumor suppressor APC and G-protein signaling (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-08-19
    Description: The adenomatous polyposis coli gene (APC) is mutated in familial adenomatous polyposis and in sporadic colorectal tumors. Here the APC gene product is shown to bind through its armadillo repeat domain to a Rac-specific guanine nucleotide exchange factor (GEF), termed Asef. Endogenous APC colocalized with Asef in mouse colon epithelial cells and neuronal cells. Furthermore, APC enhanced the GEF activity of Asef and stimulated Asef-mediated cell flattening, membrane ruffling, and lamellipodia formation in MDCK cells. These results suggest that the APC-Asef complex may regulate the actin cytoskeletal network, cell morphology and migration, and neuronal function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawasaki, Y -- Senda, T -- Ishidate, T -- Koyama, R -- Morishita, T -- Iwayama, Y -- Higuchi, O -- Akiyama, T -- New York, N.Y. -- Science. 2000 Aug 18;289(5482):1194-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular and Genetic Information, Institute for Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10947987" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli Protein ; Amino Acid Sequence ; Animals ; Brain/metabolism ; Cell Line ; Cell Membrane/ultrastructure ; Cell Size ; Colon/cytology/metabolism ; Cytoplasm/metabolism ; Cytoskeletal Proteins/*metabolism ; Guanine Nucleotide Exchange Factors/chemistry/genetics/*metabolism ; Guanosine Diphosphate/metabolism ; Humans ; Immunoblotting ; Intestinal Mucosa/cytology/metabolism ; Mice ; Molecular Sequence Data ; Neurons/metabolism ; Precipitin Tests ; Protein Binding ; Protein Structure, Tertiary ; Rats ; Recombinant Fusion Proteins/metabolism ; Rho Guanine Nucleotide Exchange Factors ; Signal Transduction ; *Trans-Activators ; Transfection ; Two-Hybrid System Techniques ; beta Catenin ; rac GTP-Binding Proteins/*metabolism
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    CLAVATA3, a multimeric ligand for the CLAVATA1 receptor-kinase (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-01
    Description: The CLAVATA1 (CLV1) and CLAVATA3 (CLV3) proteins form a potential receptor and ligand pair that regulates the balance between cell proliferation and differentiation at the shoot meristem of Arabidopsis. CLV1 encodes a receptor-kinase, and CLV3 encodes a predicted small, secreted polypeptide. We demonstrate that the CLV3 and CLV1 proteins coimmunoprecipitate in vivo, that yeast cells expressing CLV1 and CLV2 bind to CLV3 from plant extracts, and that binding requires CLV1 kinase activity. CLV3 only associates with the presumed active CLV1 protein complex in vivo. More than 75% of CLV3 in cauliflower extracts is bound with CLV1, consistent with hypotheses of ligand sequestration. Soluble CLV3 was found in an approximately 25-kilodalton multimeric complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trotochaud, A E -- Jeong, S -- Clark, S E -- New York, N.Y. -- Science. 2000 Jul 28;289(5479):613-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Michigan, Ann Arbor, MI 48109-1048, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10915623" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Arabidopsis/genetics/*metabolism ; *Arabidopsis Proteins ; Biopolymers ; Brassica/genetics/metabolism ; Cell Membrane/metabolism ; Genes, Plant ; Immune Sera ; Ligands ; Membrane Proteins/genetics/metabolism ; Meristem/genetics/*metabolism ; Molecular Weight ; Plant Extracts/metabolism ; Plant Proteins/genetics/immunology/*metabolism ; Protein Binding ; Receptor Protein-Tyrosine Kinases/genetics/immunology/*metabolism ; Recombinant Fusion Proteins ; Signal Transduction
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    Designing small-molecule switches for protein-protein interactions (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-06-17
    Description: Mutations introduced into human growth hormone (hGH) (Thr175 --〉 Gly-hGH) and the extracellular domain of the hGH receptor (Trp104 --〉 Gly-hGHbp) created a cavity at the protein-protein interface that resulted in binding affinity being reduced by a factor of 10(6). A small library of indole analogs was screened for small molecules that bind the cavity created by the mutations and restore binding affinity. The ligand 5-chloro-2-trichloromethylimidazole was found to increase the affinity of the mutant hormone for its receptor more than 1000-fold. Cell proliferation and JAK2 phosphorylation assays showed that the mutant hGH activates growth hormone signaling in the presence of added ligand. This approach may allow other protein-protein and protein-nucleic acid interactions to be switched on or off by the addition or depletion of exogenous small molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guo, Z -- Zhou, D -- Schultz, P G -- New York, N.Y. -- Science. 2000 Jun 16;288(5473):2042-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10856217" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Cell Division ; Cell Line ; Human Growth Hormone/chemistry/genetics/*metabolism ; Imidazoles/*chemistry/metabolism ; Janus Kinase 2 ; Ligands ; Mice ; Molecular Sequence Data ; Peptide Library ; Phosphorylation ; Protein Binding ; Protein-Tyrosine Kinases/metabolism ; *Proto-Oncogene Proteins ; Receptors, Somatotropin/chemistry/genetics/*metabolism ; Signal Transduction ; Structure-Activity Relationship ; Transfection
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    New ion channel may yield clues to hearing (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-04-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 2000 Mar 24;287(5461):2132-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10744528" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cilia/physiology ; Cloning, Molecular ; *Drosophila Proteins ; Drosophila melanogaster/genetics/*physiology ; Genes, Insect ; Hair Cells, Auditory/physiology ; Hearing/*physiology ; Humans ; Insect Proteins/genetics/*physiology ; Ion Channels/genetics/*physiology ; Mechanoreceptors/*physiology ; Neurons, Afferent/*physiology ; Sense Organs/physiology ; Signal Transduction ; Touch ; Transient Receptor Potential Channels
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    Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-01-29
    Description: Light generates reducing equivalents in chloroplasts that are used not only for carbon reduction, but also for the regulation of the activity of chloroplast enzymes by reduction of regulatory disulfides via the ferredoxin:thioredoxin reductase (FTR) system. FTR, the key electron/thiol transducer enzyme in this pathway, is unique in that it can reduce disulfides by an iron-sulfur cluster, a property that is explained by the tight contact of its active-site disulfide and the iron-sulfur center. The thin, flat FTR molecule makes the two-electron reduction possible by forming on one side a mixed disulfide with thioredoxin and by providing on the opposite side access to ferredoxin for delivering electrons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dai, S -- Schwendtmayer, C -- Schurmann, P -- Ramaswamy, S -- Eklund, H -- New York, N.Y. -- Science. 2000 Jan 28;287(5453):655-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Swedish University of Agricultural Sciences, Box 590, Biomedical Center, S-751 24 Uppsala, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10649999" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Catalytic Domain ; Chloroplasts/*metabolism ; Crystallography, X-Ray ; Cyanobacteria/*enzymology ; Cysteine/chemistry ; Dimerization ; Disulfides/chemistry/*metabolism ; Electron Transport ; Ferredoxins/metabolism ; Hydrogen Bonding ; Iron/chemistry ; Iron-Sulfur Proteins ; Models, Molecular ; Oxidation-Reduction ; Oxidoreductases/*chemistry/*metabolism ; Protein Structure, Secondary ; Signal Transduction ; Thioredoxins/metabolism
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    Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-05-12
    Description: A critical function of tumor suppressor p53 is the induction of apoptosis in cells exposed to noxious stresses. We report a previously unidentified pro-apoptotic gene, Noxa. Expression of Noxa induction in primary mouse cells exposed to x-ray irradiation was dependent on p53. Noxa encodes a Bcl-2 homology 3 (BH3)-only member of the Bcl-2 family of proteins; this member contains the BH3 region but not other BH domains. When ectopically expressed, Noxa underwent BH3 motif-dependent localization to mitochondria and interacted with anti-apoptotic Bcl-2 family members, resulting in the activation of caspase-9. We also demonstrate that blocking the endogenous Noxa induction results in the suppression of apoptosis. Noxa may thus represent a mediator of p53-dependent apoptosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oda, E -- Ohki, R -- Murasawa, H -- Nemoto, J -- Shibue, T -- Yamashita, T -- Tokino, T -- Taniguchi, T -- Tanaka, N -- New York, N.Y. -- Science. 2000 May 12;288(5468):1053-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Graduate School of Medicine and Faculty of Medicine, University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-0033, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10807576" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; *Apoptosis ; Caspase 9 ; Caspases/metabolism ; Cell Line ; Cells, Cultured ; DNA Damage ; Enzyme Activation ; Gene Expression Profiling ; Gene Expression Regulation ; Humans ; Mice ; Mitochondria/metabolism ; Molecular Sequence Data ; Promoter Regions, Genetic ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-bcl-2/chemistry/*physiology/*secretion ; RNA, Messenger/genetics/metabolism ; T-Lymphocytes/metabolism ; Tumor Suppressor Protein p53/*physiology ; bcl-2-Associated X Protein
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Interdigital regulation of digit identity and homeotic transformation by modulated BMP signaling (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-07-21
    Description: The developmental mechanisms specifying digital identity have attracted 30 years of intense interest, but still remain poorly understood. Here, through experiments on chick foot development, we show digital identity is not a fixed property of digital primordia. Rather, digital identity is specified by the interdigital mesoderm, demonstrating a patterning function for this tissue before its regression. More posterior interdigits specify more posterior digital identities, and each primordium will develop in accordance with the most posterior cues received. Furthermore, inhibition of interdigital bone morphogenetic protein (BMP) signaling can transform digit identity, suggesting a role for BMPs in this process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dahn, R D -- Fallon, J F -- HD32551/HD/NICHD NIH HHS/ -- T32HD07477/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2000 Jul 21;289(5478):438-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy, University of Wisconsin, 1300 University Avenue, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10903202" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Body Patterning ; Bone Morphogenetic Proteins/*physiology ; Chick Embryo ; Foot/*embryology ; Hedgehog Proteins ; Hindlimb/embryology ; Limb Buds/anatomy & histology/embryology ; Mesoderm/*physiology ; Models, Biological ; Proteins/pharmacology/physiology ; Signal Transduction ; *Trans-Activators
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    Developmental biology. Why chicks aren't all thumbs (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-12
    Description: A new study on page 438 offers some surprising insights on when and how digits assume their distinctive shapes. Scientists had thought that even before cartilage cells begin to develop into a finger or toe, they already know what shape digit to make. The new findings, however, suggest that digit identity is programmed much later in development, by chemical messengers from the surrounding tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hagmann, M -- New York, N.Y. -- Science. 2000 Jul 21;289(5478):372-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10939939" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Body Patterning ; Bone Morphogenetic Proteins/*physiology ; Cartilage/cytology/*embryology/physiology ; Chick Embryo ; Extremities/*embryology ; Foot/*embryology ; Hindlimb/embryology ; Signal Transduction ; Toes/embryology
    Print ISSN: 0036-8075
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    Biomedicine. Staying slim with insulin in mind (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-14
    Description: Striking the delicate balance between energy intake in the form of food and energy expenditure in the form of metabolic activity keeps the body extremely busy. As Schwartz explains in his enlightening Perspective, the finding that insulin signals the brain to promote weight loss (Bruning et al.) flies in the face of the notion that insulin is involved solely in glucose storage, its conversion to fat, and weight gain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwartz, M W -- New York, N.Y. -- Science. 2000 Sep 22;289(5487):2066-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Metabolism, Endocrinology and Nutrition, University of Washington, Seattle, WA 98105, USA. mschwart@u.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11032558" target="_blank"〉PubMed〈/a〉
    Keywords: Adipocytes/physiology ; Animals ; Blood Glucose/analysis ; *Body Weight ; Brain/*physiology ; Eating ; Female ; Insulin/*physiology ; Leptin/physiology ; Male ; Mice ; Neurons/physiology ; Obesity/etiology ; Receptor, Insulin/*physiology ; Signal Transduction ; Weight Loss
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    Structure of murine CTLA-4 and its role in modulating T cell responsiveness (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-29
    Description: The effective regulation of T cell responses is dependent on opposing signals transmitted through two related cell-surface receptors, CD28 and cytotoxic T lymphocyte-associated antigen 4 (CTLA-4). Dimerization of CTLA-4 is required for the formation of high-avidity complexes with B7 ligands and for transmission of signals that attenuate T cell activation. We determined the crystal structure of the extracellular portion of CTLA-4 to 2.0 angstrom resolution. CTLA-4 belongs to the immunoglobulin superfamily and displays a strand topology similar to Valpha domains, with an unusual mode of dimerization that places the B7 binding sites distal to the dimerization interface. This organization allows each CTLA-4 dimer to bind two bivalent B7 molecules and suggests that a periodic arrangement of these components within the immunological synapse may contribute to the regulation of T cell responsiveness.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ostrov, D A -- Shi, W -- Schwartz, J C -- Almo, S C -- Nathenson, S G -- AI07289/AI/NIAID NIH HHS/ -- AI42970/AI/NIAID NIH HHS/ -- CA09173/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 2000 Oct 27;290(5492):816-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11052947" target="_blank"〉PubMed〈/a〉
    Keywords: Abatacept ; Amino Acid Sequence ; Animals ; Antigen-Presenting Cells/immunology ; Antigens, CD ; Antigens, CD28/immunology/metabolism ; Antigens, CD80/chemistry/metabolism ; Antigens, Differentiation/*chemistry/*immunology/metabolism ; CTLA-4 Antigen ; Crystallography, X-Ray ; Dimerization ; Hydrogen Bonding ; *Immunoconjugates ; Ligands ; Lymphocyte Activation ; Mice ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction ; T-Lymphocytes/*immunology
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    Regulated cleavage of a contact-mediated axon repellent (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-26
    Description: Contact-mediated axon repulsion by ephrins raises an unresolved question: these cell surface ligands form a high-affinity multivalent complex with their receptors present on axons, yet rather than being bound, axons can be rapidly repelled. We show here that ephrin-A2 forms a stable complex with the metalloprotease Kuzbanian, involving interactions outside the cleavage region and the protease domain. Eph receptor binding triggered ephrin-A2 cleavage in a localized reaction specific to the cognate ligand. A cleavage-inhibiting mutation in ephrin-A2 delayed axon withdrawal. These studies reveal mechanisms for protease recognition and control of cell surface proteins, and, for ephrin-A2, they may provide a means for efficient axon detachment and termination of signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hattori, M -- Osterfield, M -- Flanagan, J G -- EY11559/EY/NEI NIH HHS/ -- HD29417/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2000 Aug 25;289(5483):1360-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Program in Neuroscience, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10958785" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Axons/*physiology ; Cell Adhesion ; Cell Communication ; Cell Membrane/metabolism ; Cells, Cultured ; Disintegrins/genetics/*metabolism ; *Drosophila Proteins ; Ephrin-A2 ; Gene Expression ; Glycosylphosphatidylinositols/metabolism ; Growth Cones/physiology ; Humans ; Ligands ; Metalloendopeptidases/genetics/*metabolism ; Mice ; Molecular Sequence Data ; Mutation ; Nervous System/embryology/enzymology ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptor, EphA3 ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transcription Factors/chemistry/genetics/*metabolism ; Tumor Cells, Cultured
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    Crystal structure of rhodopsin: A G protein-coupled receptor (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-08-05
    Description: Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) respond to a variety of different external stimuli and activate G proteins. GPCRs share many structural features, including a bundle of seven transmembrane alpha helices connected by six loops of varying lengths. We determined the structure of rhodopsin from diffraction data extending to 2.8 angstroms resolution. The highly organized structure in the extracellular region, including a conserved disulfide bridge, forms a basis for the arrangement of the seven-helix transmembrane motif. The ground-state chromophore, 11-cis-retinal, holds the transmembrane region of the protein in the inactive conformation. Interactions of the chromophore with a cluster of key residues determine the wavelength of the maximum absorption. Changes in these interactions among rhodopsins facilitate color discrimination. Identification of a set of residues that mediate interactions between the transmembrane helices and the cytoplasmic surface, where G-protein activation occurs, also suggests a possible structural change upon photoactivation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palczewski, K -- Kumasaka, T -- Hori, T -- Behnke, C A -- Motoshima, H -- Fox, B A -- Le Trong, I -- Teller, D C -- Okada, T -- Stenkamp, R E -- Yamamoto, M -- Miyano, M -- EY09339/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2000 Aug 4;289(5480):739-45.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ophthalmology, University of Washington, Seattle, WA 98195, USA. palczews@u.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10926528" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Cattle ; Cell Membrane/chemistry ; Crystallography, X-Ray ; Heterotrimeric GTP-Binding Proteins/*metabolism ; Hydrogen Bonding ; Light ; Molecular Sequence Data ; Receptors, Cell Surface/*chemistry/metabolism ; Retinaldehyde/chemistry/metabolism ; Rhodopsin/*chemistry/metabolism ; Schiff Bases ; Stereoisomerism ; Vision, Ocular
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    An inherited functional circadian clock in zebrafish embryos (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-07-15
    Description: Circadian clocks are time-keeping systems found in most organisms. In zebrafish, expression of the clock gene Period3 (Per3) oscillates throughout embryogenesis in the central nervous system and the retina. Per3 rhythmic expression was free-running and was reset by light but not by the developmental delays caused by low temperature. The time of fertilization had no effect on Per3 expression. Per3 messenger RNA accumulates rhythmically in oocytes and persists in embryos. Our results establish that the circadian clock functions during early embryogenesis in zebrafish. Inheritance of maternal clock gene products suggests a mechanism of phase inheritance through ovogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Delaunay, F -- Thisse, C -- Marchand, O -- Laudet, V -- Thisse, B -- New York, N.Y. -- Science. 2000 Jul 14;289(5477):297-300.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ecole Normale Superieure, CNRS UMR 5665, 46 allee d'Italie, 69364 Lyon Cedex, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10894777" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Circadian Rhythm/genetics ; *DNA-Binding Proteins ; Embryo, Nonmammalian/metabolism ; Embryonic Development ; Female ; Gene Expression Regulation, Developmental ; Light ; Molecular Sequence Data ; Nuclear Proteins/*genetics/physiology ; Period Circadian Proteins ; Proteins/genetics ; *Receptors, Cytoplasmic and Nuclear ; Transcription Factors ; Zebrafish/embryology/*physiology ; Zebrafish Proteins
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    Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-06-10
    Description: Experiments with vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B (NR2B subunit) show that they are transported along microtubules by KIF17, a neuron-specific molecular motor in neuronal dendrites. Selective transport is accomplished by direct interaction of the KIF17 tail with a PDZ domain of mLin-10 (Mint1/X11), which is a constituent of a large protein complex including mLin-2 (CASK), mLin-7 (MALS/Velis), and the NR2B subunit. This interaction, specific for a neurotransmitter receptor critically important for plasticity in the postsynaptic terminal, may be a regulatory point for synaptic plasticity and neuronal morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Setou, M -- Nakagawa, T -- Seog, D H -- Hirokawa, N -- New York, N.Y. -- Science. 2000 Jun 9;288(5472):1796-802.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Anatomy, Graduate School of Medicine, University of Tokyo, Bunkyo-ku, Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10846156" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Binding Sites ; Biological Transport ; *Caenorhabditis elegans Proteins ; Cloning, Molecular ; Dendrites/*metabolism ; Dimerization ; Kinesin/chemistry/genetics/*metabolism ; Male ; *Membrane Proteins ; Mice ; Microtubules/metabolism ; Models, Biological ; Molecular Motor Proteins/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Molecular Weight ; Organelles/metabolism ; Precipitin Tests ; Protein Binding ; Proteins/chemistry/*metabolism ; Receptors, N-Methyl-D-Aspartate/*metabolism ; Recombinant Proteins/chemistry/metabolism ; Two-Hybrid System Techniques
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    Nota bene: aging. Sensing old age (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, O -- New York, N.Y. -- Science. 2000 Jan 7;287(5450):54.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10644225" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*physiology ; Animals ; Caenorhabditis elegans/*physiology ; *Caenorhabditis elegans Proteins ; GTP-Binding Proteins/metabolism ; Helminth Proteins/metabolism ; Ion Channels/metabolism ; Longevity/*physiology ; Receptor, Insulin/metabolism ; Receptors, Odorant/metabolism ; Reproduction ; Signal Transduction ; Smell/*physiology
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    Identification of synergistic signals initiating inner ear development (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-12-09
    Description: Tissue manipulation experiments in amphibians more than 50 years ago showed that induction of the inner ear requires two signals: a mesodermal signal followed by a neural signal. However, the molecules mediating this process have remained elusive. We present evidence for mesodermal initiation of otic development in higher vertebrates and show that the mesoderm can direct terminal differentiation of the inner ear in rostral ectoderm. Furthermore, we demonstrate the synergistic interactions of the extracellular polypeptide ligands FGF-19 and Wnt-8c as mediators of mesodermal and neural signals, respectively, initiating inner ear development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ladher, R K -- Anakwe, K U -- Gurney, A L -- Schoenwolf, G C -- Francis-West, P H -- New York, N.Y. -- Science. 2000 Dec 8;290(5498):1965-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Craniofacial Development, King's College, London, SE1 9RT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11110663" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Central Nervous System/embryology/metabolism ; Chick Embryo ; Culture Techniques ; Ear, Inner/*embryology/metabolism ; Ectoderm/cytology ; *Embryonic Induction ; Fibroblast Growth Factor 3 ; Fibroblast Growth Factors/genetics/*metabolism/pharmacology ; Gene Expression ; Homeodomain Proteins/genetics/metabolism ; Humans ; In Situ Hybridization ; Mesoderm/*metabolism ; Molecular Sequence Data ; Proto-Oncogene Proteins/genetics/*metabolism/pharmacology ; Quail/embryology ; Rhombencephalon/embryology/metabolism ; Signal Transduction ; Wnt Proteins ; *Zebrafish Proteins
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    Identification of vaccine candidates against serogroup B meningococcus by whole-genome sequencing (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-03-10
    Description: Neisseria meningitidis is a major cause of bacterial septicemia and meningitis. Sequence variation of surface-exposed proteins and cross-reactivity of the serogroup B capsular polysaccharide with human tissues have hampered efforts to develop a successful vaccine. To overcome these obstacles, the entire genome sequence of a virulent serogroup B strain (MC58) was used to identify vaccine candidates. A total of 350 candidate antigens were expressed in Escherichia coli, purified, and used to immunize mice. The sera allowed the identification of proteins that are surface exposed, that are conserved in sequence across a range of strains, and that induce a bactericidal antibody response, a property known to correlate with vaccine efficacy in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pizza, M -- Scarlato, V -- Masignani, V -- Giuliani, M M -- Arico, B -- Comanducci, M -- Jennings, G T -- Baldi, L -- Bartolini, E -- Capecchi, B -- Galeotti, C L -- Luzzi, E -- Manetti, R -- Marchetti, E -- Mora, M -- Nuti, S -- Ratti, G -- Santini, L -- Savino, S -- Scarselli, M -- Storni, E -- Zuo, P -- Broeker, M -- Hundt, E -- Knapp, B -- Blair, E -- Mason, T -- Tettelin, H -- Hood, D W -- Jeffries, A C -- Saunders, N J -- Granoff, D M -- Venter, J C -- Moxon, E R -- Grandi, G -- Rappuoli, R -- New York, N.Y. -- Science. 2000 Mar 10;287(5459):1816-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉IRIS, Chiron S.p.A., Via Fiorentina 1, 53100 Siena, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10710308" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Bacterial/biosynthesis/blood ; Antigens, Bacterial/chemistry/genetics/*immunology ; Antigens, Surface/chemistry/genetics/immunology ; Bacterial Capsules ; Bacterial Proteins/chemistry/genetics/*immunology ; *Bacterial Vaccines/genetics/immunology ; Conserved Sequence ; Escherichia coli/genetics ; *Genome, Bacterial ; Humans ; Immune Sera/immunology ; Mice ; Neisseria meningitidis/classification/*genetics/*immunology/pathogenicity ; Open Reading Frames ; Recombinant Fusion Proteins/chemistry/immunology/isolation & purification ; Recombination, Genetic ; Sequence Analysis, DNA ; Serotyping ; Vaccination ; Virulence
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    Structural evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-09-01
    Description: The atomic structures of two proteins in the histidine biosynthesis pathway consist of beta/alpha barrels with a twofold repeat pattern. It is likely that these proteins evolved by twofold gene duplication and gene fusion from a common half-barrel ancestor. These ancestral domains are not visible as independent domains in the extant proteins but can be inferred from a combination of sequence and structural analysis. The detection of subdomain structures may be useful in efforts to search genome sequences for functionally and structurally related proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lang, D -- Thoma, R -- Henn-Sax, M -- Sterner, R -- Wilmanns, M -- New York, N.Y. -- Science. 2000 Sep 1;289(5484):1546-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory (EMBL) Hamburg Outstation, EMBL c/o Deutsches Elektronen- Synchrotron (DESY), Notkestrasse 85, D-22603 Hamburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10968789" target="_blank"〉PubMed〈/a〉
    Keywords: Aldose-Ketose Isomerases/*chemistry/genetics/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Aminohydrolases/*chemistry/genetics/metabolism ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; *Evolution, Molecular ; *Gene Duplication ; Histidine/biosynthesis ; Models, Molecular ; Molecular Sequence Data ; Protein Folding ; *Protein Structure, Tertiary ; *Recombination, Genetic ; Sequence Alignment ; Thermotoga maritima/enzymology
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    A bacterial toxin that controls cell cycle progression as a deoxyribonuclease I-like protein (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-10-13
    Description: Many bacterial pathogens encode a multisubunit toxin, termed cytolethal distending toxin (CDT), that induces cell cycle arrest, cytoplasm distention, and, eventually, chromatin fragmentation and cell death. In one such pathogen, Campylobacter jejuni, one of the subunits of this toxin, CdtB, was shown to exhibit features of type I deoxyribonucleases. Transient expression of this subunit in cultured cells caused marked chromatin disruption. Microinjection of low amounts of CdtB induced cytoplasmic distention and cell cycle arrest. CdtB mutants with substitutions in residues equivalent to those required for catalysis or magnesium binding in type I deoxyribonucleases did not cause chromatin disruption. CDT holotoxin containing these mutant forms of CdtB did not induce morphological changes or cell cycle arrest.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lara-Tejero, M -- Galan, J E -- New York, N.Y. -- Science. 2000 Oct 13;290(5490):354-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Microbial Pathogenesis, Boyer Center for Molecular Medicine, Yale School of Medicine, New Haven, CT 06536, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11030657" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Toxins/chemistry/genetics/*metabolism/*toxicity ; COS Cells ; *Campylobacter jejuni/genetics/pathogenicity ; Cell Death ; Cell Line ; Cell Nucleus/metabolism ; Chromatin/ultrastructure ; DNA/*metabolism ; *DNA Damage ; Deoxyribonuclease I/chemistry/*metabolism ; *G2 Phase ; Microinjections ; Molecular Sequence Data ; Mutation ; Transfection
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    Oxygen activation and reduction in respiration: involvement of redox-active tyrosine 244 (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-11-25
    Description: Cytochrome oxidase activates and reduces O(2) to water to sustain respiration and uses the energy released to drive proton translocation and adenosine 5'-triphosphate synthesis. A key intermediate in this process, P, lies at the junction of the O(2)-reducing and proton-pumping functions. We used radioactive iodide labeling followed by peptide mapping to gain insight into the structure of P. We show that the cross-linked histidine 240-tyrosine 244 (His240-Tyr244) species is redox active in P formation, which establishes its structure as Fe(IV) = O/Cu(B)2+-H240-Y244. Thus, energy transfer from O2 to the protein moiety is used as a strategy to avoid toxic intermediates and to control energy utilization in subsequent proton-pumping events.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Proshlyakov, D A -- Pressler, M A -- DeMaso, C -- Leykam, J F -- DeWitt, D L -- Babcock, G T -- GM25480/GM/NIGMS NIH HHS/ -- GM57323/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Nov 24;290(5496):1588-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Department of Biochemistry, Michigan State University, East Lansing, MI 48824, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11090359" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cattle ; Dimerization ; Electron Transport Complex IV/*chemistry/*metabolism ; Histidine/chemistry/metabolism ; Iodine Radioisotopes ; Molecular Sequence Data ; Oxidation-Reduction ; Oxygen/*metabolism ; *Oxygen Consumption ; Peptide Fragments/chemistry/*metabolism ; Peptide Mapping ; Proton Pumps ; Tyrosine/chemistry/*metabolism
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    Interconnected feedback loops in the Neurospora circadian system (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-07-07
    Description: In Neurospora crassa, white collar 1 (WC-1), a transcriptional activator and positive clock element, is rhythmically expressed from a nonrhythmic steady-state pool of wc-1 transcript, consistent with posttranscriptional regulation of rhythmicity. Mutations in frq influence both the level and periodicity of WC-1 expression, and driven FRQ expression not only depresses its own endogenous levels, but positively regulates WC-1 synthesis with a lag of about 8 hours, a delay similar to that seen in the wild-type clock. FRQ thus plays dual roles in the Neurospora clock and thereby, with WC-1, forms a second feedback loop that would promote robustness and stability in this circadian system. The existence also of interlocked loops in Drosophila melanogaster and mouse clocks suggests that such interlocked loops may be a conserved aspect of circadian timing systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, K -- Loros, J J -- Dunlap, J C -- MH44651/MH/NIMH NIH HHS/ -- R37-GM 34985/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Jul 7;289(5476):107-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Dartmouth Medical School, Hanover, NH 03755-3844, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10884222" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Circadian Rhythm ; DNA-Binding Proteins/biosynthesis/chemistry/genetics/*metabolism ; Darkness ; Feedback ; Fungal Proteins/genetics/*metabolism ; Gene Expression Regulation, Fungal ; Humans ; Kinetics ; Light ; Molecular Sequence Data ; Mutation ; Neurospora crassa/genetics/metabolism/*physiology ; Phosphorylation ; RNA, Fungal/genetics/metabolism ; RNA, Messenger/genetics/metabolism ; Sequence Alignment ; Signal Transduction ; Transcription Factors/biosynthesis/chemistry/genetics/*metabolism
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    Hepatitis C virus, the E2 envelope protein, and alpha-interferon resistance (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abid, K -- Quadri, R -- Negro, F -- New York, N.Y. -- Science. 2000 Mar 3;287(5458):1555.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Gastroenterology and Hepatology, University of Geneva Medical School, Geneva, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10733410" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Drug Resistance, Microbial ; Eukaryotic Initiation Factor-2/chemistry/metabolism ; Genotype ; Hepacivirus/*drug effects/genetics ; Hepatitis C/virology ; Humans ; Interferon-alpha/*pharmacology ; Phosphorylation ; Viral Envelope Proteins/*chemistry/*physiology ; eIF-2 Kinase/*antagonists & inhibitors/metabolism
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    A mutation in PRKAG3 associated with excess glycogen content in pig skeletal muscle (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-05-20
    Description: A high proportion of purebred Hampshire pigs carries the dominant RN- mutation, which causes high glycogen content in skeletal muscle. The mutation has beneficial effects on meat content but detrimental effects on processing yield. Here, it is shown that the mutation is a nonconservative substitution (R200Q) in the PRKAG3 gene, which encodes a muscle-specific isoform of the regulatory gamma subunit of adenosine monophosphate-activated protein kinase (AMPK). Loss-of-function mutations in the homologous gene in yeast (SNF4) cause defects in glucose metabolism, including glycogen storage. Further analysis of the PRKAG3 signaling pathway may provide insights into muscle physiology as well as the pathogenesis of noninsulin-dependent diabetes mellitus in humans, a metabolic disorder associated with impaired glycogen synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milan, D -- Jeon, J T -- Looft, C -- Amarger, V -- Robic, A -- Thelander, M -- Rogel-Gaillard, C -- Paul, S -- Iannuccelli, N -- Rask, L -- Ronne, H -- Lundstrom, K -- Reinsch, N -- Gellin, J -- Kalm, E -- Roy, P L -- Chardon, P -- Andersson, L -- New York, N.Y. -- Science. 2000 May 19;288(5469):1248-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Genetique Cellulaire, Institut National de la Recherche Agronomique (INRA), 31326 Castanet-Tolosan, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10818001" target="_blank"〉PubMed〈/a〉
    Keywords: AMP-Activated Protein Kinases ; Alleles ; Amino Acid Sequence ; Amino Acid Substitution/genetics ; Animals ; Blotting, Northern ; Cloning, Molecular ; DNA, Complementary/isolation & purification ; Gene Expression Regulation, Enzymologic ; Glycogen/*metabolism ; Homozygote ; Humans ; Isoenzymes/biosynthesis/genetics/isolation & purification ; Molecular Sequence Data ; Muscle, Skeletal/*enzymology/metabolism ; Organ Specificity/genetics ; Phenotype ; *Point Mutation ; Protein Kinases/biosynthesis/*genetics/isolation & purification ; Sequence Homology, Amino Acid ; Swine
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  • 78
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    Soluble adenylyl cyclase as an evolutionarily conserved bicarbonate sensor (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-01
    Description: Spermatozoa undergo a poorly understood activation process induced by bicarbonate and mediated by cyclic adenosine 3',5'-monophosphate (cAMP). It has been assumed that bicarbonate mediates its effects through changes in intracellular pH or membrane potential; however, we demonstrate here that bicarbonate directly stimulates mammalian soluble adenylyl cyclase (sAC) activity in vivo and in vitro in a pH-independent manner. sAC is most similar to adenylyl cyclases from cyanobacteria, and bicarbonate regulation of cyclase activity is conserved in these early forms of life. sAC is also expressed in other bicarbonate-responsive tissues, which suggests that bicarbonate regulation of cAMP signaling plays a fundamental role in many biological systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Y -- Cann, M J -- Litvin, T N -- Iourgenko, V -- Sinclair, M L -- Levin, L R -- Buck, J -- New York, N.Y. -- Science. 2000 Jul 28;289(5479):625-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Joan and Sanford I. Weill Medical College of Cornell University, 1300 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10915626" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/chemistry/genetics/isolation & purification/*metabolism ; Animals ; Bicarbonates/*metabolism/pharmacology ; Catalytic Domain ; Cell Line ; Cyanobacteria/enzymology ; Cyclic AMP/metabolism ; Enzyme Activation ; Evolution, Molecular ; Humans ; Hydrogen-Ion Concentration ; Male ; Phylogeny ; Rats ; Recombinant Proteins/isolation & purification/metabolism ; Second Messenger Systems ; Signal Transduction ; Solubility ; Sperm Capacitation ; Spermatozoa/enzymology/*metabolism/physiology ; Testis/metabolism
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    Cloning of the Arabidopsis clock gene TOC1, an autoregulatory response regulator homolog (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-05
    Description: The toc1 mutation causes shortened circadian rhythms in light-grown Arabidopsis plants. Here, we report the same toc1 effect in the absence of light input to the clock. We also show that TOC1 controls photoperiodic flowering response through clock function. The TOC1 gene was isolated and found to encode a nuclear protein containing an atypical response regulator receiver domain and two motifs that suggest a role in transcriptional regulation: a basic motif conserved within the CONSTANS family of transcription factors and an acidic domain. TOC1 is itself circadianly regulated and participates in a feedback loop to control its own expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strayer, C -- Oyama, T -- Schultz, T F -- Raman, R -- Somers, D E -- Mas, P -- Panda, S -- Kreps, J A -- Kay, S A -- GM 56006/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Aug 4;289(5480):768-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell 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/10926537" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Arabidopsis/*genetics/physiology ; *Arabidopsis Proteins ; Biological Clocks/*genetics ; Circadian Rhythm/*genetics ; Cloning, Molecular ; DNA-Binding Proteins/chemistry/genetics/physiology ; Feedback ; Gene Expression Regulation, Plant ; Genes, Plant ; Molecular Sequence Data ; Mutation, Missense ; Phenotype ; Photoperiod ; Plant Proteins/chemistry/*genetics/physiology ; Plants, Genetically Modified ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism ; Repetitive Sequences, Amino Acid ; Transcription Factors/chemistry/genetics/physiology ; Transcription, Genetic
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  • 80
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    Requirement of Mis6 centromere connector for localizing a CENP-A-like protein in fission yeast (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-06-24
    Description: Mammalian kinetochores contain the centromere-specific histone H3 variant CENP-A, whose incorporation into limited chromosomal regions may be important for centromere function and chromosome segregation during mitosis. However, regulation of CENP-A localization and its role have not been clear. Here we report that the fission yeast homolog SpCENP-A is essential for establishing centromere chromatin associated with equal chromosome segregation. SpCENP-A binding to the nonrepetitious inner centromeres depended on Mis6, an essential centromere connector protein acting during G1-S phase of the cell cycle. Mis6 is likely required for recruiting SpCENP-A to form proper connection of sister centromeres.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takahashi, K -- Chen, E S -- Yanagida, M -- New York, N.Y. -- Science. 2000 Jun 23;288(5474):2215-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CREST Research Project, Japan Science and Technology Corporation, Kyoto, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10864871" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Cell Cycle ; Cell Cycle Proteins/metabolism ; Centromere/*metabolism ; Chromatin/metabolism ; Chromosomal Proteins, Non-Histone/chemistry/genetics/*metabolism ; *Chromosome Segregation ; DNA Replication ; DNA, Fungal/metabolism ; Fungal Proteins/chemistry/genetics/*metabolism ; G1 Phase ; Histones/chemistry/genetics/metabolism ; Mitosis ; Molecular Sequence Data ; Mutation ; Recombinant Fusion Proteins/metabolism ; S Phase ; Schizosaccharomyces/cytology/genetics/*metabolism ; *Schizosaccharomyces pombe Proteins ; Temperature
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  • 81
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    gridlock, an HLH gene required for assembly of the aorta in zebrafish (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-10
    Description: The first artery and vein of the vertebrate embryo assemble in the trunk by migration and coalescence of angioblasts to form endothelial tubes. The gridlock (grl) mutation in zebrafish selectively perturbs assembly of the artery (the aorta). Here it is shown that grl encodes a basic helix-loop-helix (bHLH) protein belonging to the Hairy/Enhancer of the split family of bHLH proteins. The grl gene is expressed in lateral plate mesoderm before vessel formation, and thereafter in the aorta and not in the vein. These results suggest that the arterial endothelial identity is established even before the onset of blood flow and implicate the grl gene in assignment of vessel-specific cell fate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhong, T P -- Rosenberg, M -- Mohideen, M A -- Weinstein, B -- Fishman, M C -- R01DK55383/DK/NIDDK NIH HHS/ -- R01RR0888/RR/NCRR NIH HHS/ -- T32HL07208/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 2000 Mar 10;287(5459):1820-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cardiovascular Research Center, Massachusetts General Hospital-Harvard Medical School, 149 13th Street, 4th floor, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10710309" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aorta/*embryology/metabolism ; Basic Helix-Loop-Helix Transcription Factors ; Cloning, Molecular ; Embryo, Nonmammalian/metabolism ; Embryonic Development ; Endothelium, Vascular/embryology/metabolism ; Gene Expression ; Genotype ; *Helix-Loop-Helix Motifs ; Humans ; Mesoderm/metabolism ; Molecular Sequence Data ; Morphogenesis/genetics ; Mutation ; Phenotype ; Physical Chromosome Mapping ; Proteins/chemistry/*genetics/*physiology ; Sequence Alignment ; Stem Cells/cytology/metabolism ; Zebrafish/embryology/*genetics ; *Zebrafish Proteins
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    Patterning of the zebrafish retina by a wave of sonic hedgehog activity (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-09-23
    Description: The Drosophila retina is patterned by a morphogenetic wave driven by the Hedgehog signaling protein. Hedgehog, secreted by the first neurons, induces neuronal differentiation and hedgehog expression in nearby uncommitted cells, thereby propagating the wave. Evidence is presented here that the zebrafish Hedgehog homolog, Sonic Hedgehog, is also expressed in the first retinal neurons, and that Sonic Hedgehog drives a wave of neurogenesis across the retina, strikingly similar to the wave in Drosophila. The conservation of this patterning mechanism is unexpected, given the highly divergent structures of vertebrate and invertebrate eyes, and supports a common evolutionary origin of the animal visual system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neumann, C J -- Nuesslein-Volhard, C -- New York, N.Y. -- Science. 2000 Sep 22;289(5487):2137-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck Institut fuer Entwicklungsbiologie, Spemannstrasse 35/III, D-72076 Tuebingen, Germany. carl.neumann@tuebingen.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11000118" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; *Body Patterning ; Cell Differentiation ; Embryonic Induction ; Gene Expression Regulation, Developmental ; Hedgehog Proteins ; Mitogen-Activated Protein Kinases/metabolism ; Proteins/genetics/*metabolism ; Retina/cytology/*embryology ; Retinal Ganglion Cells/cytology/*metabolism ; Signal Transduction ; *Trans-Activators ; Zebrafish/*embryology/genetics/metabolism
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    Positional syntenic cloning and functional characterization of the mammalian circadian mutation tau (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-04-25
    Description: The tau mutation is a semidominant autosomal allele that dramatically shortens period length of circadian rhythms in Syrian hamsters. We report the molecular identification of the tau locus using genetically directed representational difference analysis to define a region of conserved synteny in hamsters with both the mouse and human genomes. The tau locus is encoded by casein kinase I epsilon (CKIepsilon), a homolog of the Drosophila circadian gene double-time. In vitro expression and functional studies of wild-type and tau mutant CKIepsilon enzyme reveal that the mutant enzyme has a markedly reduced maximal velocity and autophosphorylation state. In addition, in vitro CKIepsilon can interact with mammalian PERIOD proteins, and the mutant enzyme is deficient in its ability to phosphorylate PERIOD. We conclude that tau is an allele of hamster CKIepsilon and propose a mechanism by which the mutation leads to the observed aberrant circadian phenotype in mutant animals.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3869379/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3869379/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lowrey, P L -- Shimomura, K -- Antoch, M P -- Yamazaki, S -- Zemenides, P D -- Ralph, M R -- Menaker, M -- Takahashi, J S -- R01MH56647/MH/NIMH NIH HHS/ -- R37MH39592/MH/NIMH NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2000 Apr 21;288(5465):483-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology and Physiology, Howard Hughes Medical Institute, Northwestern University, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10775102" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Casein Kinases ; Cell Cycle Proteins ; Chromosome Mapping ; *Circadian Rhythm/genetics ; Cloning, Molecular ; Cricetinae ; Female ; Heterozygote ; Humans ; Male ; Mesocricetus ; Mice ; Microsatellite Repeats ; Molecular Sequence Data ; Nuclear Proteins/genetics/metabolism ; Period Circadian Proteins ; Phenotype ; Phosphorylation ; *Point Mutation ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Protein Kinases/chemistry/*genetics/*metabolism ; RNA, Messenger/genetics/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Suprachiasmatic Nucleus/metabolism
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    Identification of HE1 as the second gene of Niemann-Pick C disease (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-12-23
    Description: Niemann-Pick type C2 disease (NP-C2) is a fatal hereditary disorder of unknown etiology characterized by defective egress of cholesterol from lysosomes. Here we show that the disease is caused by a deficiency in HE1, a ubiquitously expressed lysosomal protein identified previously as a cholesterol-binding protein. HE1 was undetectable in fibroblasts from NP-C2 patients but present in fibroblasts from unaffected controls and NP-C1 patients. Mutations in the HE1 gene, which maps to chromosome 14q24.3, were found in NP-C2 patients but not in controls. Treatment of NP-C2 fibroblasts with exogenous recombinant HE1 protein ameliorated lysosomal accumulation of low density lipoprotein-derived cholesterol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Naureckiene, S -- Sleat, D E -- Lackland, H -- Fensom, A -- Vanier, M T -- Wattiaux, R -- Jadot, M -- Lobel, P -- DK45992/DK/NIDDK NIH HHS/ -- DK54317/DK/NIDDK NIH HHS/ -- NS37918/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2000 Dec 22;290(5500):2298-301.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Advanced Biotechnology and Medicine, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway, NJ, 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11125141" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Transport ; CHO Cells ; *Carrier Proteins ; Cell Membrane/metabolism ; Cells, Cultured ; Cholesterol/*metabolism ; Cricetinae ; Culture Media, Conditioned ; Fibroblasts/metabolism ; Glycoproteins/chemistry/*genetics/*metabolism/pharmacology ; Humans ; Lysosomes/*metabolism ; Molecular Sequence Data ; Mutation ; Niemann-Pick Diseases/*genetics/metabolism ; Rats ; Receptor, IGF Type 2/metabolism ; Recombinant Proteins/metabolism/pharmacology ; Transfection
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    A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-17
    Description: Phospholipase C and two inositol polyphosphate (IP) kinases constitute a signaling pathway that regulates nuclear messenger RNA export through production of inositol hexakisphosphate (IP6). The inositol 1,4,5-trisphosphate kinase of this pathway in Saccharomyces cerevisiae, designated Ipk2, was found to be identical to Arg82, a regulator of the transcriptional complex ArgR-Mcm1. Synthesis of inositol 1,4,5,6-tetrakisphosphate, but not IP6, was required for gene regulation through ArgR-Mcm1. Thus, the phospholipase C pathway produces multiple IP messengers that modulate distinct nuclear processes. The results reveal a direct mechanism by which activation of IP signaling may control gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Odom, A R -- Stahlberg, A -- Wente, S R -- York, J D -- New York, N.Y. -- Science. 2000 Mar 17;287(5460):2026-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Pharmacology and Cancer Biology and of Biochemistry, Duke University Medical Center, DUMC 3813, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10720331" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arginine/metabolism ; Cell Nucleus/enzymology/*metabolism ; DNA-Binding Proteins/metabolism ; *Gene Expression Regulation, Fungal ; Inositol 1,4,5-Trisphosphate/metabolism ; Inositol Phosphates/*metabolism ; Minichromosome Maintenance 1 Protein ; Molecular Sequence Data ; Phosphoric Monoester Hydrolases/metabolism ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/chemistry/*metabolism ; Phytic Acid/metabolism ; Saccharomyces cerevisiae/enzymology/*genetics ; Signal Transduction ; Transcription Factors/metabolism ; *Transcription, Genetic ; Type C Phospholipases/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 86
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    Long-term survival but impaired homeostatic proliferation of Naive T cells in the absence of p56lck (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-06
    Description: Interactions between the T cell receptor (TCR) and major histocompatibility complex antigens are essential for the survival and homeostasis of peripheral T lymphocytes. However, little is known about the TCR signaling events that result from these interactions. The peripheral T cell pool of p56lck (lck)-deficient mice was reconstituted by the expression of an inducible lck transgene. Continued survival of peripheral naive T cells was observed for long periods after switching off the transgene. Adoptive transfer of T cells from these mice into T lymphopoienic hosts confirmed that T cell survival was independent of lck but revealed its essential role in TCR-driven homeostatic proliferation of naive T cells in response to the T cell-deficient host environment. These data suggest that survival and homeostatic expansion depend on different signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seddon, B -- Legname, G -- Tomlinson, P -- Zamoyska, R -- New York, N.Y. -- Science. 2000 Oct 6;290(5489):127-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Immunology, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11021796" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD3/metabolism ; CD4-Positive T-Lymphocytes/immunology/physiology ; CD8-Positive T-Lymphocytes/immunology/physiology ; Cell Division ; Cell Survival ; Doxycycline/pharmacology ; Gene Expression ; Homeostasis ; Lymphocyte Activation ; Lymphocyte Count ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck)/genetics/*physiology ; Lymphocyte Transfusion ; Lymphoid Tissue/cytology/immunology ; Mice ; Mice, Knockout ; Mice, Transgenic ; Phosphorylation ; Proto-Oncogene Proteins c-bcl-2/genetics/metabolism ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction ; T-Lymphocyte Subsets/immunology/physiology ; T-Lymphocytes/immunology/*physiology/transplantation ; Thymus Gland/cytology/immunology ; Transgenes
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Disruption of signaling by Yersinia effector YopJ, a ubiquitin-like protein protease (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-11-25
    Description: Homologs of the Yersinia virulence effector YopJ are found in both plant and animal bacterial pathogens, as well as plant symbionts. These YopJ family members were shown to act as cysteine proteases. The catalytic triad of the protease was required for inhibition of the mitogen-activated protein kinase (MAPK) and nuclear factor kappaB (NF-kappaB) signaling in animal cells and for induction of localized cell death in plants. The substrates for YopJ were shown to be highly conserved ubiquitin-like molecules, which are covalently added to numerous regulatory proteins. YopJ family members exert their pathogenic effect on cells by disrupting this posttranslational modification.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Orth, K -- Xu, Z -- Mudgett, M B -- Bao, Z Q -- Palmer, L E -- Bliska, J B -- Mangel, W F -- Staskawicz, B -- Dixon, J E -- 18024/PHS HHS/ -- AI41599/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Nov 24;290(5496):1594-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11090361" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Proteins/*chemistry/genetics/*metabolism ; Catalysis ; Catalytic Domain ; Cell Line ; Cysteine Endopeptidases/chemistry/genetics/*metabolism ; Humans ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinases/metabolism ; Molecular Sequence Data ; NF-kappa B/*metabolism ; Plant Leaves/cytology/virology ; SUMO-1 Protein ; Sequence Alignment ; Signal Transduction ; Transfection ; Ubiquitins/metabolism ; Virulence ; Xanthomonas campestris/enzymology/pathogenicity ; Yersinia pseudotuberculosis/enzymology/metabolism/*pathogenicity
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  • 88
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    Docosahexaenoic acid, a ligand for the retinoid X receptor in mouse brain (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-12-16
    Description: The retinoid X receptor (RXR) is a nuclear receptor that functions as a ligand-activated transcription factor. Little is known about the ligands that activate RXR in vivo. Here, we identified a factor in brain tissue from adult mice that activates RXR in cell-based assays. Purification and analysis of the factor by mass spectrometry revealed that it is docosahexaenoic acid (DHA), a long-chain polyunsaturated fatty acid that is highly enriched in the adult mammalian brain. Previous work has shown that DHA is essential for brain maturation, and deficiency of DHA in both rodents and humans leads to impaired spatial learning and other abnormalities. These data suggest that DHA may influence neural function through activation of an RXR signaling pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Urquiza, A M -- Liu, S -- Sjoberg, M -- Zetterstrom, R H -- Griffiths, W -- Sjovall, J -- Perlmann, T -- New York, N.Y. -- Science. 2000 Dec 15;290(5499):2140-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ludwig Institute for Cancer Research, Stockholm Branch, Box 240, S-171 77 Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11118147" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Assay ; Brain/growth & development/metabolism ; *Brain Chemistry ; Cell Line ; Chromatography, High Pressure Liquid ; Culture Media, Conditioned ; Dimerization ; Docosahexaenoic Acids/*isolation & purification/*metabolism/pharmacology ; Fatty Acids, Unsaturated/pharmacology ; Histone Acetyltransferases ; Humans ; Ligands ; Male ; Mice ; Nuclear Receptor Coactivator 1 ; Receptors, Retinoic Acid/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Retinoid X Receptors ; Signal Transduction ; Spectrometry, Mass, Electrospray Ionization ; Transcription Factors/genetics/*metabolism ; Transfection ; Tumor Cells, Cultured
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  • 89
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    Transmembrane molecular pump activity of Niemann-Pick C1 protein (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-12-23
    Description: Niemann-Pick C1 (NPC1) disease is characterized by cholesterol accumulation in lysosomes and aberrant feedback regulation of cellular cholesterol homeostasis. We provide evidence that the NPC1 protein has homology with the resistance-nodulation-division (RND) family of prokaryotic permeases and may normally function as a transmembrane efflux pump. Studies of acriflavine loading in normal and NPC1 fibroblasts indicated that NPC1 uses a proton motive force to remove accumulated acriflavine from the endosomal/lysosomal system. Expression of NPC1 in Escherichia coli (i) facilitated the transport of acriflavine across the plasma membrane, causing cytosolic accumulation, and (ii) resulted in transport of oleic acid but not cholesterol or cholesterol-oleate across the plasma membrane. These studies establish NPC1 as a eukaryotic member of the RND permease family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davies, J P -- Chen, F W -- Ioannou, Y A -- R01 DK54736/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2000 Dec 22;290(5500):2295-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics, Box 1498, The Mount Sinai School of Medicine, One 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/11125140" target="_blank"〉PubMed〈/a〉
    Keywords: Acriflavine/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Biological Transport ; *Carrier Proteins ; Cell Membrane/metabolism ; Cells, Cultured ; Cholesterol/metabolism ; Cholesterol Esters/metabolism ; Endosomes/metabolism ; Escherichia coli/genetics/metabolism ; Fibroblasts ; Fluorescence ; Fluorescent Dyes/metabolism ; Humans ; Lysosomes/metabolism ; *Membrane Glycoproteins ; Membrane Proteins/chemistry ; Membrane Transport Proteins/chemistry/*metabolism ; Molecular Sequence Data ; Niemann-Pick Diseases/genetics/*metabolism ; Oleic Acid/metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/chemistry/*metabolism ; Proton-Motive Force ; Recombinant Proteins/metabolism ; Sequence Alignment
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  • 90
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    A PEST-like sequence in listeriolysin O essential for Listeria monocytogenes pathogenicity (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-11-04
    Description: Establishment and maintenance of an intracellular niche are critical to the success of an intracellular pathogen. Here, the pore-forming protein listeriolysin O (LLO), secreted by Listeria monocytogenes, was shown to contain a PEST-like sequence (P, Pro; E, Glu; S, Ser; T, Thr) that is essential for the virulence and intracellular compartmentalization of this pathogen. Mutants lacking the PEST-like sequence entered the host cytosol but subsequently permeabilized and killed the host cell. LLO lacking the PEST-like sequence accumulated in the host-cell cytosol, suggesting that this sequence targets LLO for degradation. Transfer of the sequence to perfringolysin O transformed this toxic cytolysin into a nontoxic derivative that facilitated intracellular growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Decatur, A L -- Portnoy, D A -- AI10283/AI/NIAID NIH HHS/ -- AI27655/AI/NIAID NIH HHS/ -- R01 AI027655/AI/NIAID NIH HHS/ -- R37 AI029619/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Nov 3;290(5493):992-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, Division of Infectious Diseases, School of Public Health, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11062133" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Bacterial Toxins/chemistry ; Cell Line ; Cytosol/metabolism ; Heat-Shock Proteins/*chemistry/genetics/*metabolism/toxicity ; Hemolysin Proteins ; L-Lactate Dehydrogenase/metabolism ; Listeria monocytogenes/genetics/metabolism/*pathogenicity ; Listeriosis/microbiology ; Macrophages/microbiology ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Mutation ; Phagosomes/microbiology ; Phosphorylation ; Sequence Deletion ; Virulence
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    Reading the worm genome (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, S K -- New York, N.Y. -- Science. 2000 Jan 7;287(5450):52-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology and Genetics, Stanford University Medical Center, Stanford, CA 94305-5329, USA. kim@cmgm.stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10644223" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*genetics/growth & development/*metabolism ; *Caenorhabditis elegans Proteins ; Female ; Genes, Helminth ; *Genome ; Helminth Proteins/genetics/*metabolism ; Protein Binding ; Repressor Proteins/genetics/metabolism ; Retinoblastoma Protein/metabolism ; Signal Transduction ; *Two-Hybrid System Techniques ; Vulva/growth & development ; Yeasts/genetics
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  • 92
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    Genomics. Structural biology gets a $150 million boost (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, R F -- New York, N.Y. -- Science. 2000 Sep 29;289(5488):2254-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11041783" target="_blank"〉PubMed〈/a〉
    Keywords: Academies and Institutes/economics ; Amino Acid Sequence ; Computer Simulation ; Genome ; Laboratories ; National Institutes of Health (U.S.)/economics ; *Protein Conformation ; Protein Folding ; Proteins/*chemistry/genetics ; *Research Support as Topic ; United States ; Universities/economics
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  • 93
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    Accumulation of dietary cholesterol in sitosterolemia caused by mutations in adjacent ABC transporters (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-12-02
    Description: In healthy individuals, acute changes in cholesterol intake produce modest changes in plasma cholesterol levels. A striking exception occurs in sitosterolemia, an autosomal recessive disorder characterized by increased intestinal absorption and decreased biliary excretion of dietary sterols, hypercholesterolemia, and premature coronary atherosclerosis. We identified seven different mutations in two adjacent, oppositely oriented genes that encode new members of the adenosine triphosphate (ATP)-binding cassette (ABC) transporter family (six mutations in ABCG8 and one in ABCG5) in nine patients with sitosterolemia. The two genes are expressed at highest levels in liver and intestine and, in mice, cholesterol feeding up-regulates expressions of both genes. These data suggest that ABCG5 and ABCG8 normally cooperate to limit intestinal absorption and to promote biliary excretion of sterols, and that mutated forms of these transporters predispose to sterol accumulation and atherosclerosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berge, K E -- Tian, H -- Graf, G A -- Yu, L -- Grishin, N V -- Schultz, J -- Kwiterovich, P -- Shan, B -- Barnes, R -- Hobbs, H H -- HL07360/HL/NHLBI NIH HHS/ -- HL20948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2000 Dec 1;290(5497):1771-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and McDermott Center for Human Growth and Development and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, TX 75390-9046, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11099417" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/chemistry/*genetics/metabolism ; Amino Acid Sequence ; Animals ; Bile/metabolism ; Cholesterol/blood ; Cholesterol, Dietary/administration & dosage/*metabolism ; Chromosome Mapping ; Chromosomes, Human, Pair 2 ; Codon ; DNA-Binding Proteins ; Expressed Sequence Tags ; Gene Expression Regulation ; Humans ; *Intestinal Absorption ; Intestines/metabolism ; Lipid Metabolism, Inborn Errors/*genetics/metabolism ; Lipoproteins/chemistry/*genetics/metabolism ; Liver/metabolism ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; Orphan Nuclear Receptors ; RNA, Messenger/genetics/metabolism ; Receptors, Cytoplasmic and Nuclear/metabolism ; Sitosterols/*blood/metabolism
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  • 94
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    Neurobiology. Turning attraction into repulsion (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-09-09
    Description: A series of molecular cues guide axons as they extend in the embryonic environment. In her Perspective, Pasquale discusses new findings that reveal how signals originating from adhesive contacts between axons and the cells they encounter can repel the axon, causing it to break the adhesive contacts and move away (Hattori et al. and Galko and Tessier-Lavigne).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pasquale, E -- New York, N.Y. -- Science. 2000 Aug 25;289(5483):1308-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA. elenap@burnham.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10979856" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/*physiology ; Cell Adhesion ; Cell Adhesion Molecules/metabolism ; Cell Membrane/metabolism ; Disintegrins/antagonists & inhibitors/*metabolism ; *Drosophila Proteins ; Ephrin-A2 ; Glycosylphosphatidylinositols/metabolism ; Growth Cones/physiology ; Ligands ; Membrane Proteins/*metabolism ; Metalloendopeptidases/antagonists & inhibitors/*metabolism ; Mice ; Nerve Growth Factors/*metabolism ; Protease Inhibitors/pharmacology ; Receptors, Cell Surface/metabolism ; Signal Transduction ; Transcription Factors/*metabolism ; *Tumor Suppressor Proteins
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  • 95
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    Flower arranging in Arabidopsis (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-06-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Devlin, P F -- Kay, S A -- New York, N.Y. -- Science. 2000 Jun 2;288(5471):1600-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and National Science Foundation for Biological Timing, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. pdevlin@scripps.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10858139" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*physiology ; *Arabidopsis Proteins ; DNA-Binding Proteins/*genetics/physiology ; *Gene Expression Regulation, Plant ; Genes, Plant ; MADS Domain Proteins ; Mutation ; Photoperiod ; Plant Proteins/genetics/physiology ; Plant Shoots/genetics/physiology ; Promoter Regions, Genetic ; RNA-Binding Proteins/genetics/physiology ; Seasons ; Signal Transduction ; Temperature ; Transcription Factors/*genetics/physiology
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  • 96
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    Biochemistry. All in the ubiquitin family (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-12
    Description: The job of a protein can be altered by addition of molecules such as ubiquitin or the related ubiquitin-like modifiers, which bring about changes in the protein's localization, conformation, or its interactions with other proteins. In a comprehensive Perspective, Hochstrasser brings us up to date with the many new members of the ubiquitin modifier family and their multitudinous and diverse protein targets.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hochstrasser, M -- New York, N.Y. -- Science. 2000 Jul 28;289(5479):563-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Yale University, Department of Molecular Biophysics and Biochemistry, 266 Whitney Avenue, New Haven, CT 06520, USA. mark.hochstrasser@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10939967" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Autophagy ; Binding Sites ; Cell Nucleus/metabolism ; Evolution, Molecular ; Fungal Proteins/chemistry/*metabolism ; Ligases/metabolism ; Models, Chemical ; Protein Binding ; Proteins/chemistry/*metabolism ; SUMO-1 Protein ; *Saccharomyces cerevisiae Proteins ; Ubiquitin-Protein Ligases ; Ubiquitins/chemistry/genetics/*metabolism ; Yeasts/metabolism
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    Gatekeepers of the nucleus (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-05-29
    Description: Nuclear pore complexes (NPCs) form the site for entry and exit from the nucleus. A convergence of studies have defined the physical framework for the nuclear transport mechanism. This includes definition of the soluble transport machinery required for protein and RNA movement, x-ray structure analysis of transport factors, definitive compositional analysis of yeast NPCs, and documentation of the relative steady state arrangement of NPC components within the portal. With this information, researchers are now in the exciting position to examine the dynamic interplay between shuttling transport factors and the static pore complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wente, S R -- New York, N.Y. -- Science. 2000 May 26;288(5470):1374-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Physiology, Box 8228, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA. swente@cellbio.wustl.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10827939" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Biological Transport, Active ; Carrier Proteins/chemistry/metabolism ; Cell Nucleus/chemistry/*metabolism/ultrastructure ; Cytoplasm/metabolism ; Membrane Proteins/chemistry/metabolism ; Models, Biological ; Nuclear Envelope/*chemistry/*metabolism/ultrastructure ; Nuclear Localization Signals ; Nuclear Proteins/chemistry/metabolism ; Proteins/metabolism ; RNA/metabolism ; Saccharomyces cerevisiae/chemistry/metabolism
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  • 98
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    Dependence of stem cell fate in Arabidopsis on a feedback loop regulated by CLV3 activity (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-01
    Description: The fate of stem cells in plant meristems is governed by directional signaling systems that are regulated by negative feedback. In Arabidopsis thaliana, the CLAVATA (CLV) genes encode the essential components of a negative, stem cell-restricting pathway. We used transgenic plants overexpressing CLV3 to show that meristem cell accumulation and fate depends directly on the level of CLV3 activity and that CLV3 signaling occurs exclusively through a CLV1/CLV2 receptor kinase complex. We also demonstrate that the CLV pathway acts by repressing the activity of the transcription factor WUSCHEL, an element of the positive, stem cell-promoting pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brand, U -- Fletcher, J C -- Hobe, M -- Meyerowitz, E M -- Simon, R -- New York, N.Y. -- Science. 2000 Jul 28;289(5479):617-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Entwicklungsbiologie, Universitat zu Koln, Gyrhofstrabetae 17, D-50923 Koln, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10915624" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*cytology/genetics/growth & development/metabolism ; *Arabidopsis Proteins ; Cell Differentiation ; Cell Division ; Down-Regulation ; Feedback ; Gene Expression Regulation, Plant ; Genes, Plant ; Homeodomain Proteins/genetics/metabolism ; In Situ Hybridization ; Membrane Proteins/metabolism ; Meristem/*cytology/metabolism ; Mutation ; Phenotype ; Plant Proteins/genetics/*metabolism ; Plants, Genetically Modified ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism ; Receptor Protein-Tyrosine Kinases/metabolism ; Signal Transduction ; Stem Cells/*cytology/metabolism ; *Transcription Factors ; Transgenes
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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    Apoptosis. Mitochondria--the death signal integrators (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-09-02
    Description: Many of the intricate pathways of apoptosis that instruct a cell to kill itself involve the convergence of key proteins on the membranes of mitochondria. Such proteins induce the permeabilization of mitochondrial membranes and the release of caspase enzymes and nuclease activators that set in motion the final stages of programmed cell death. Now, as Brenner and Kroemer discuss in their Perspective, a proapoptotic transcription factor called TR3 has been found to move from its normal location in the nucleus to the mitochondria and to promote release of cytochrome c, a key event in apoptosis (Li et al.)〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brenner, C -- Kroemer, G -- New York, N.Y. -- Science. 2000 Aug 18;289(5482):1150-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Apoptosis, Cancer and Immunity Laboratory, National League Against Cancer, CNRS-UMR1599, Institut Gustave Roussy, F-94805 Villejuif, France. catherine.brenner@utc.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10970229" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Cell Nucleus/metabolism ; Cytochrome c Group/metabolism ; DNA/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Gene Expression Regulation ; Humans ; Intracellular Membranes/*metabolism/physiology ; Mice ; Mice, Transgenic ; Mitochondria/*metabolism ; Nerve Growth Factor/pharmacology ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Permeability ; Protein Structure, Tertiary ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid ; Response Elements ; Signal Transduction ; T-Lymphocytes/cytology/immunology ; Transcription Factors/chemistry/genetics/*metabolism ; Zinc Fingers
    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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    A myosin I isoform in the nucleus (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-13
    Description: A nuclear isoform of myosin I beta that contains a unique 16-amino acid amino-terminal extension has been identified. An affinity-purified antibody to the 16-amino acid peptide demonstrated nuclear staining. Confocal and electron microscopy revealed that nuclear myosin I beta colocalized with RNA polymerase II in an alpha-amanitin- and actinomycin D-sensitive manner. The antibody coimmunoprecipitated RNA polymerase II and blocked in vitro RNA synthesis. This isoform of myosin I beta appears to be in a complex with RNA polymerase II and may affect transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pestic-Dragovich, L -- Stojiljkovic, L -- Philimonenko, A A -- Nowak, G -- Ke, Y -- Settlage, R E -- Shabanowitz, J -- Hunt, D F -- Hozak, P -- de Lanerolle, P -- GM 37537/GM/NIGMS NIH HHS/ -- GM 56489/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Oct 13;290(5490):337-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Illinois at Chicago, Chicago, IL 60612, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11030652" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Actins/metabolism ; Amanitins/pharmacology ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Nucleus/*metabolism ; Cloning, Molecular ; Dactinomycin/pharmacology ; Exons ; HeLa Cells ; Humans ; Mice ; Microscopy, Confocal ; Microscopy, Electron ; *Molecular Motor Proteins ; Molecular Sequence Data ; Myosins/chemistry/genetics/immunology/*metabolism ; Nucleic Acid Synthesis Inhibitors/pharmacology ; Precipitin Tests ; Protein Isoforms/chemistry/genetics/immunology/metabolism ; RNA/*biosynthesis ; RNA Polymerase II/*metabolism ; *Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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