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  • Amino Acid Sequence  (123)
  • Male  (85)
  • American Association for the Advancement of Science (AAAS)  (199)
  • American Institute of Physics (AIP)
  • Elsevier
  • Oxford University Press
  • 1995-1999  (199)
  • 1970-1974
  • 1997  (199)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (199)
  • American Institute of Physics (AIP)
  • Elsevier
  • Oxford University Press
Years
  • 1995-1999  (199)
  • 1970-1974
Year
  • 1
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    Genetic testing for cancer risk (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-14
    Description: Genetic testing for cancer susceptibility is already part of the clinical management of families with some of the well-defined (but uncommon) inherited cancer syndromes. In cases where the risks associated with a predisposing mutation are less certain, or where there is no clearly effective intervention to offer those with a positive result, its use is more controversial. Careful evaluation of costs and benefits, and of the efficacy of interventions in those found to be at risk, is essential and is only just beginning. An immediate challenge is to ensure that both health professionals and the public understand clearly the issues involved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ponder, B -- New York, N.Y. -- Science. 1997 Nov 7;278(5340):1050-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oncology, University of Cambridge, Addenbrooke's Hospital, Box 238, Level 3 Lab Block, Hills Road, Cambridge CB2 2QQ, UK. bajp@mole.bio.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9353178" target="_blank"〉PubMed〈/a〉
    Keywords: Confidentiality ; Cost-Benefit Analysis ; Female ; Genetic Counseling ; Genetic Predisposition to Disease ; Genetic Services ; *Genetic Testing ; Genetic Variation ; Humans ; Insurance, Health ; Insurance, Life ; Male ; Mutation ; Neoplasms/*diagnosis/*genetics ; Resource Allocation ; Risk Assessment ; Risk Factors ; Uncertainty
    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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    Metal ion chaperone function of the soluble Cu(I) receptor Atx1 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-05
    Description: Reactive and potentially toxic cofactors such as copper ions are imported into eukaryotic cells and incorporated into target proteins by unknown mechanisms. Atx1, a prototypical copper chaperone protein from yeast, has now been shown to act as a soluble cytoplasmic copper(I) receptor that can adopt either a two- or three-coordinate metal center in the active site. Atx1 also associated directly with the Atx1-like cytosolic domains of Ccc2, a vesicular protein defined in genetic studies as a member of the copper-trafficking pathway. The unusual structure and dynamics of Atx1 suggest a copper exchange function for this protein and related domains in the Menkes and Wilson disease proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pufahl, R A -- Singer, C P -- Peariso, K L -- Lin, S J -- Schmidt, P J -- Fahrni, C J -- Culotta, V C -- Penner-Hahn, J E -- O'Halloran, T V -- GM-38047/GM/NIGMS NIH HHS/ -- GM-50016/GM/NIGMS NIH HHS/ -- GM-54111/GM/NIGMS NIH HHS/ -- R01 GM054111/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 Oct 31;278(5339):853-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Northwestern University, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9346482" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Carrier Proteins ; *Cation Transport Proteins ; Copper/*metabolism ; Escherichia coli ; Fungal Proteins/metabolism/*physiology ; Humans ; Molecular Chaperones/*physiology ; Molecular Sequence Data ; Recombinant Proteins ; Saccharomyces cerevisiae/metabolism/*physiology ; *Saccharomyces cerevisiae Proteins ; Sequence Homology, Amino Acid
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  • 3
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    Sexual selection in Asian elephants (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tiedemann, R -- New York, N.Y. -- Science. 1997 Nov 28;278(5343):1550-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9411772" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Elephants/*anatomy & histology/*physiology ; Female ; Incisor/anatomy & histology ; India ; Male ; Models, Biological ; Models, Statistical ; *Sexual Behavior, Animal ; Sri Lanka
    Print ISSN: 0036-8075
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  • 4
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    Mitochondrial and chloroplast phage-type RNA polymerases in Arabidopsis (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-08
    Description: In addition to the RNA polymerases (RNAPs) transcribing the nuclear genes, eukaryotic cells also require RNAPs to transcribe the genes of the mitochondrial genome and, in plants, of the chloroplast genome. The plant Arabidopsis thaliana was found to contain two nuclear genes similar to genes encoding the mitochondrial RNAP from yeast and RNAPs of bacteriophages T7, T3, and SP6. The putative transit peptides of the two polymerases were capable of targeting fusion proteins to mitochondria and chloroplasts, respectively, in vitro. The results indicate that the mitochondrial RNAP in plants is a bacteriophage-type enzyme. A gene duplication event may have generated the second RNAP, which along with the plastid-encoded eubacteria-like RNAP could transcribe the chloroplast genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hedtke, B -- Borner, T -- Weihe, A -- New York, N.Y. -- Science. 1997 Aug 8;277(5327):809-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Humboldt University Berlin, Institute of Biology, Chausseestrasse 117, D-10115 Berlin, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9242608" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/*enzymology/genetics ; Cell Nucleus/genetics ; Chloroplasts/*enzymology ; Cloning, Molecular ; DNA-Directed RNA Polymerases/chemistry/*genetics ; Exons ; *Genes, Plant ; Introns ; Mitochondria/*enzymology ; Molecular Sequence Data ; Phylogeny ; Recombinant Fusion Proteins/metabolism ; Sequence Alignment ; T-Phages/enzymology
    Print ISSN: 0036-8075
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  • 5
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    Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo angiogenesis (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-04
    Description: Angiogenesis is thought to depend on a precise balance of positive and negative regulation. Angiopoietin-1 (Ang1) is an angiogenic factor that signals through the endothelial cell-specific Tie2 receptor tyrosine kinase. Like vascular endothelial growth factor, Ang1 is essential for normal vascular development in the mouse. An Ang1 relative, termed angiopoietin-2 (Ang2), was identified by homology screening and shown to be a naturally occurring antagonist for Ang1 and Tie2. Transgenic overexpression of Ang2 disrupts blood vessel formation in the mouse embryo. In adult mice and humans, Ang2 is expressed only at sites of vascular remodeling. Natural antagonists for vertebrate receptor tyrosine kinases are atypical; thus, the discovery of a negative regulator acting on Tie2 emphasizes the need for exquisite regulation of this angiogenic receptor system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maisonpierre, P C -- Suri, C -- Jones, P F -- Bartunkova, S -- Wiegand, S J -- Radziejewski, C -- Compton, D -- McClain, J -- Aldrich, T H -- Papadopoulos, N -- Daly, T J -- Davis, S -- Sato, T N -- Yancopoulos, G D -- New York, N.Y. -- Science. 1997 Jul 4;277(5322):55-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals Inc., 777 Old Saw Mill River Road, Tarrytown, NY 10591, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9204896" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Angiopoietin-1 ; Angiopoietin-2 ; Animals ; Blood Vessels/embryology/*metabolism ; Cells, Cultured ; Cloning, Molecular ; Embryo, Mammalian/metabolism ; Endothelial Growth Factors/genetics/metabolism ; Endothelium, Vascular/*cytology/metabolism ; Female ; Humans ; Ligands ; Lymphokines/genetics/metabolism ; Membrane Glycoproteins/antagonists & inhibitors/metabolism ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; *Neovascularization, Physiologic ; Phosphorylation ; Proteins/chemistry/*metabolism ; Rats ; Rats, Sprague-Dawley ; Receptor Protein-Tyrosine Kinases/*antagonists & inhibitors/metabolism ; Receptor, TIE-2 ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factors
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  • 6
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    Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-18
    Description: The crystal structure of the adenine nucleotide exchange factor GrpE in complex with the adenosine triphosphatase (ATPase) domain of Escherichia coli DnaK [heat shock protein 70 (Hsp70)] was determined at 2.8 angstrom resolution. A dimer of GrpE binds asymmetrically to a single molecule of DnaK. The structure of the nucleotide-free ATPase domain in complex with GrpE resembles closely that of the nucleotide-bound mammalian Hsp70 homolog, except for an outward rotation of one of the subdomains of the protein. This conformational change is not consistent with tight nucleotide binding. Two long alpha helices extend away from the GrpE dimer and suggest a role for GrpE in peptide release from DnaK.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harrison, C J -- Hayer-Hartl, M -- Di Liberto, M -- Hartl, F -- Kuriyan, J -- New York, N.Y. -- Science. 1997 Apr 18;276(5311):431-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratories of Molecular Biophysics and Howard Hughes Medical Institute, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9103205" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Adenosine Triphosphatases/*chemistry/metabolism ; Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Crystallography, X-Ray ; Dimerization ; *Escherichia coli Proteins ; HSP70 Heat-Shock Proteins/*chemistry/metabolism ; Heat-Shock Proteins/*chemistry/metabolism ; Hydrogen Bonding ; Models, Molecular ; Molecular Chaperones/*chemistry/metabolism ; Molecular Sequence Data ; *Protein Conformation ; Protein Structure, Secondary
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  • 7
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    Pain affect encoded in human anterior cingulate but not somatosensory cortex (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-15
    Description: Recent evidence demonstrating multiple regions of human cerebral cortex activated by pain has prompted speculation about their individual contributions to this complex experience. To differentiate cortical areas involved in pain affect, hypnotic suggestions were used to alter selectively the unpleasantness of noxious stimuli, without changing the perceived intensity. Positron emission tomography revealed significant changes in pain-evoked activity within anterior cingulate cortex, consistent with the encoding of perceived unpleasantness, whereas primary somatosensory cortex activation was unaltered. These findings provide direct experimental evidence in humans linking frontal-lobe limbic activity with pain affect, as originally suggested by early clinical lesion studies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rainville, P -- Duncan, G H -- Price, D D -- Carrier, B -- Bushnell, M C -- New York, N.Y. -- Science. 1997 Aug 15;277(5328):968-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉D-epartement de Psychologie and Centre de Recherche en Sciences Neurologiques, Universite de Montreal, Montreal, Quebec, Canada H3C 3J7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9252330" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Affect/*physiology ; *Brain Mapping ; Female ; Frontal Lobe/blood supply/*physiology/radionuclide imaging ; Gyrus Cinguli/blood supply/*physiology/radionuclide imaging ; Humans ; Hypnosis ; Male ; Middle Aged ; Pain/*physiopathology/*psychology ; Pain Measurement ; Regional Blood Flow ; Regression Analysis ; Somatosensory Cortex/blood supply/*physiology/radionuclide imaging ; Thermosensing ; Tomography, Emission-Computed
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  • 8
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    Control of vertebrate left-right asymmetry by a snail-related zinc finger gene (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-02-28
    Description: A gene encoding a zinc finger protein of the Snail family, cSnR, is expressed in the right-hand lateral mesoderm during normal chick development. Antisense disruption of cSnR function during the hours immediately preceding heart formation randomized the normally reliable direction of heart looping and subsequent embryo torsion. Implanted ectopic sources of intercellular signal proteins that are involved in establishing normal left-right information randomized the handedness of heart development and also altered the asymmetry of cSnR expression. cSnR thus appears to act downstream of these signals, or perhaps in parallel with the latest expressed of them, the Nodal protein, in controlling the anatomical asymmetry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Isaac, A -- Sargent, M G -- Cooke, J -- New York, N.Y. -- Science. 1997 Feb 28;275(5304):1301-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute for Medical Research, Mill Hill, London NW7 1AA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9036854" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors ; Amino Acid Sequence ; Animals ; Body Patterning/*genetics ; Chick Embryo ; Culture Techniques ; DNA-Binding Proteins/chemistry/*genetics/physiology ; Embryonic Induction/genetics/physiology ; *Gene Expression Regulation, Developmental ; Heart/*embryology ; Hedgehog Proteins ; Levocardia/embryology/genetics ; Mesoderm/*metabolism ; Molecular Sequence Data ; Nodal Protein ; Oligonucleotides, Antisense ; Proteins/genetics/physiology ; RNA, Messenger/genetics/metabolism ; Receptors, Growth Factor/genetics/physiology ; Somites/metabolism ; *Trans-Activators ; *Transforming Growth Factor beta ; Up-Regulation ; Zinc Fingers/*genetics
    Print ISSN: 0036-8075
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  • 9
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    Rescue of a Drosophila NF1 mutant phenotype by protein kinase A (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-02
    Description: The neurofibromatosis type 1 (NF1) tumor suppressor protein is thought to restrict cell proliferation by functioning as a Ras-specific guanosine triphosphatase-activating protein. However, Drosophila homozygous for null mutations of an NF1 homolog showed no obvious signs of perturbed Ras1-mediated signaling. Loss of NF1 resulted in a reduction in size of larvae, pupae, and adults. This size defect was not modified by manipulating Ras1 signaling but was restored by expression of activated adenosine 3', 5'-monophosphate-dependent protein kinase (PKA). Thus, NF1 and PKA appear to interact in a pathway that controls the overall growth of Drosophila.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉The, I -- Hannigan, G E -- Cowley, G S -- Reginald, S -- Zhong, Y -- Gusella, J F -- Hariharan, I K -- Bernards, A -- NS22229/NS/NINDS NIH HHS/ -- NS34779/NS/NINDS NIH HHS/ -- NS36084/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 May 2;276(5313):791-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Massachusetts General Hospital Cancer Center and Harvard Medical School Building 149, 13th Street, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9115203" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Count ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinases/genetics/*metabolism ; Drosophila/cytology/*genetics/growth & development/metabolism ; *Drosophila Proteins ; GTP Phosphohydrolases/metabolism ; Genes, Insect ; Insect Proteins/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Mutation ; *Nerve Tissue Proteins ; Neurofibromin 1 ; Phenotype ; Proteins/chemistry/genetics ; Recombinant Fusion Proteins/pharmacology ; Signal Transduction ; *ras GTPase-Activating Proteins ; ras Proteins/metabolism
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  • 10
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    A mouse model with features of familial combined hyperlipidemia (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-17
    Description: Familial combined hyperlipidemia (FCHL) is a common inherited lipid disorder, affecting 1 to 2 percent of the population in Westernized societies. Individuals with FCHL have large quantities of very low density lipoprotein (VLDL) and low density lipoprotein (LDL) and develop premature coronary heart disease. A mouse model displaying some of the features of FCHL was created by crossing mice carrying the human apolipoprotein C-III (APOC3) transgene with mice deficient in the LDL receptor. A synergistic interaction between the apolipoprotein C-III and the LDL receptor defects produced large quantities of VLDL and LDL and enhanced the development of atherosclerosis. This mouse model may provide clues to the origin of human FCHL.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Masucci-Magoulas, L -- Goldberg, I J -- Bisgaier, C L -- Serajuddin, H -- Francone, O L -- Breslow, J L -- Tall, A R -- HL 21006/HL/NHLBI NIH HHS/ -- HL 54591/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1997 Jan 17;275(5298):391-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Columbia University, 630 West 168 Street, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8994037" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apolipoprotein C-III ; Apolipoproteins B/blood ; Apolipoproteins C/*genetics ; Apolipoproteins E/blood ; Arteriosclerosis/etiology ; Carrier Proteins/genetics ; Cholesterol/blood ; Cholesterol Ester Transfer Proteins ; Cholesterol, HDL/blood ; Cholesterol, LDL/blood ; Cholesterol, VLDL/blood ; Diet ; *Disease Models, Animal ; Disease Susceptibility ; Female ; *Glycoproteins ; Humans ; *Hyperlipidemia, Familial Combined/blood/genetics ; Hyperlipoproteinemia Type IV/genetics ; Lipoproteins/blood ; Lipoproteins, VLDL/blood ; Male ; Mice ; Mice, Inbred C57BL ; *Mice, Transgenic ; Receptors, LDL/*genetics/metabolism ; Transgenes ; Triglycerides/blood
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  • 11
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    Proteins from scratch (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeGrado, W F -- New York, N.Y. -- Science. 1997 Oct 3;278(5335):80-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA. wdegrado@mail.med.upenn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9340760" target="_blank"〉PubMed〈/a〉
    Keywords: *Algorithms ; Amino Acid Sequence ; Computer Simulation ; DNA-Binding Proteins/chemical synthesis/*chemistry ; Models, Molecular ; *Protein Conformation ; *Protein Engineering ; Protein Folding ; Protein Structure, Tertiary ; Software ; Thermodynamics ; Transcription Factors/chemical synthesis/*chemistry ; Zinc Fingers
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  • 12
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    A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-14
    Description: Pathogenic Yersinia species have a specialized secretion system (type III) to target cytotoxic Yop proteins during infection. The signals of YopE and YopN sufficient for the secretion of translational reporter fusions were mapped to the first 15 codons. No common amino acid or peptide sequence could be identified among the secretion signals. Systematic mutagenesis of the secretion signal yielded mutants defective in Yop translation; however, no point mutants could be identified that specifically abolished secretion. Frameshift mutations that completely altered the peptide sequences of these signals also failed to prevent secretion. Thus, the signal that leads to the type III secretion of Yop proteins appears to be encoded in their messenger RNA rather than the peptide sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, D M -- Schneewind, O -- AI 07323/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 7;278(5340):1140-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Molecular Biology Institute, University of California, Los Angeles, School of Medicine, 10833 Le Conte Avenue, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9353199" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Outer Membrane Proteins/chemistry/genetics/*secretion ; Bacterial Proteins/chemistry/genetics/*secretion ; Base Sequence ; Codon ; Frameshift Mutation ; *Membrane Proteins ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Point Mutation ; Protein Biosynthesis ; RNA, Bacterial/chemistry/*genetics/metabolism ; RNA, Messenger/chemistry/*genetics/metabolism ; Recombinant Fusion Proteins/biosynthesis/secretion ; Yersinia enterocolitica/*metabolism/pathogenicity
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  • 13
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    Polyalanine expansion in synpolydactyly might result from unequal crossing-over of HOXD13 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Warren, S T -- New York, N.Y. -- Science. 1997 Jan 17;275(5298):408-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9005557" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Base Sequence ; *Crossing Over, Genetic ; Homeodomain Proteins/chemistry/*genetics ; Humans ; Molecular Sequence Data ; Mutation ; Peptides/analysis/*genetics ; Polydactyly/*genetics ; Syndactyly/*genetics ; *Transcription Factors ; Trinucleotide Repeats
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  • 14
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    Neurospora wc-1 and wc-2: transcription, photoresponses, and the origins of circadian rhythmicity (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-02
    Description: Circadian rhythmicity is universally associated with the ability to perceive light, and the oscillators ("clocks") giving rise to these rhythms, which are feedback loops based on transcription and translation, are reset by light. Although such loops must contain elements of positive and negative regulation, the clock genes analyzed to date-frq in Neurospora and per and tim in Drosophila-are associated only with negative feedback and their biochemical functions are largely inferred. The white collar-1 and white collar-2 genes, both global regulators of photoresponses in Neurospora, encode DNA binding proteins that contain PAS domains and are believed to act as transcriptional activators. Data shown here suggest that wc-1 is a clock-associated gene and wc-2 is a clock component; both play essential roles in the assembly or operation of the Neurospora circadian oscillator. Thus DNA binding and transcriptional activation can now be associated with a clock gene that may provide a positive element in the feedback loop. In addition, similarities between the PAS-domain regions of molecules involved in light perception and circadian rhythmicity in several organisms suggest an evolutionary link between ancient photoreceptor proteins and more modern proteins required for circadian oscillation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crosthwaite, S K -- Dunlap, J C -- Loros, J J -- GM 34985/GM/NIGMS NIH HHS/ -- MH01186/MH/NIMH NIH HHS/ -- MH44651/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1997 May 2;276(5313):763-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, 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/9115195" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Biological Clocks/physiology ; Biological Evolution ; Circadian Rhythm/*physiology ; DNA, Fungal/metabolism ; DNA-Binding Proteins/chemistry/genetics/*physiology ; Feedback ; Fungal Proteins/genetics ; Gene Expression Regulation, Fungal ; Genes, Fungal ; Light ; Molecular Sequence Data ; Neurospora crassa/genetics/*physiology ; Phytochrome/metabolism ; Signal Transduction ; Temperature ; Transcription Factors/chemistry/genetics/*physiology ; *Transcriptional Activation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 15
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    A euryarchaeal lysyl-tRNA synthetase: resemblance to class I synthetases (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-14
    Description: The sequencing of euryarchaeal genomes has suggested that the essential protein lysyl-transfer RNA (tRNA) synthetase (LysRS) is absent from such organisms. However, a single 62-kilodalton protein with canonical LysRS activity was purified from Methanococcus maripaludis, and the gene that encodes this protein was cloned. The predicted amino acid sequence of M. maripaludis LysRS is similar to open reading frames of unassigned function in both Methanobacterium thermoautotrophicum and Methanococcus jannaschii but is unrelated to canonical LysRS proteins reported in eubacteria, eukaryotes, and the crenarchaeote Sulfolobus solfataricus. The presence of amino acid motifs characteristic of the Rossmann dinucleotide-binding domain identifies M. maripaludis LysRS as a class I aminoacyl-tRNA synthetase, in contrast to the known examples of this enzyme, which are class II synthetases. These data question the concept that the classification of aminoacyl-tRNA synthetases does not vary throughout living systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ibba, M -- Morgan, S -- Curnow, A W -- Pridmore, D R -- Vothknecht, U C -- Gardner, W -- Lin, W -- Woese, C R -- Soll, D -- New York, N.Y. -- Science. 1997 Nov 7;278(5340):1119-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, Post Office Box 208114, 266 Whitney Avenue, New Haven, CT 06520-8114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9353192" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Amino Acid Sequence ; Animals ; Bacteria/enzymology ; Cloning, Molecular ; Electrophoresis, Polyacrylamide Gel ; Euryarchaeota/enzymology/genetics ; Evolution, Molecular ; Genes, Archaeal ; Humans ; Kinetics ; Lysine-tRNA Ligase/*chemistry/*classification/genetics/metabolism ; Methanococcus/*enzymology/genetics ; Molecular Sequence Data ; Phylogeny ; RNA, Transfer, Amino Acyl/biosynthesis ; Sequence Alignment ; Sulfolobus/enzymology
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  • 16
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    De novo protein design: fully automated sequence selection (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-10-06
    Description: The first fully automated design and experimental validation of a novel sequence for an entire protein is described. A computational design algorithm based on physical chemical potential functions and stereochemical constraints was used to screen a combinatorial library of 1.9 x 10(27) possible amino acid sequences for compatibility with the design target, a betabetaalpha protein motif based on the polypeptide backbone structure of a zinc finger domain. A BLAST search shows that the designed sequence, full sequence design 1 (FSD-1), has very low identity to any known protein sequence. The solution structure of FSD-1 was solved by nuclear magnetic resonance spectroscopy and indicates that FSD-1 forms a compact well-ordered structure, which is in excellent agreement with the design target structure. This result demonstrates that computational methods can perform the immense combinatorial search required for protein design, and it suggests that an unbiased and quantitative algorithm can be used in various structural contexts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dahiyat, B I -- Mayo, S L -- GM08346/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 3;278(5335):82-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9311930" target="_blank"〉PubMed〈/a〉
    Keywords: *Algorithms ; Amino Acid Sequence ; Computer Simulation ; Crystallography, X-Ray ; DNA-Binding Proteins/chemical synthesis/*chemistry ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; *Protein Conformation ; *Protein Engineering ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Sequence Alignment ; Solutions ; Transcription Factors/chemical synthesis/*chemistry ; Zinc Fingers
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  • 17
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    Peptide agonist of the thrombopoietin receptor as potent as the natural cytokine (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-13
    Description: Two families of small peptides that bind to the human thrombopoietin receptor and compete with the binding of the natural ligand thrombopoietin (TPO) were identified from recombinant peptide libraries. The sequences of these peptides were not found in the primary sequence of TPO. Screening libraries of variants of one of these families under affinity-selective conditions yielded a 14-amino acid peptide (Ile-Glu-Gly-Pro-Thr-Leu-Arg-Gln-Trp-Leu-Ala-Ala-Arg-Ala) with high affinity (dissociation constant approximately 2 nanomolar) that stimulates the proliferation of a TPO-responsive Ba/F3 cell line with a median effective concentration (EC50) of 400 nanomolar. Dimerization of this peptide by a carboxyl-terminal linkage to a lysine branch produced a compound with an EC50 of 100 picomolar, which was equipotent to the 332-amino acid natural cytokine in cell-based assays. The peptide dimer also stimulated the in vitro proliferation and maturation of megakaryocytes from human bone marrow cells and promoted an increase in platelet count when administered to normal mice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cwirla, S E -- Balasubramanian, P -- Duffin, D J -- Wagstrom, C R -- Gates, C M -- Singer, S C -- Davis, A M -- Tansik, R L -- Mattheakis, L C -- Boytos, C M -- Schatz, P J -- Baccanari, D P -- Wrighton, N C -- Barrett, R W -- Dower, W J -- New York, N.Y. -- Science. 1997 Jun 13;276(5319):1696-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Affymax Research Institute, 4001 Miranda Avenue, Palo Alto, CA 94304, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9180079" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; Blood Platelets/cytology ; Cell Division ; Cell Line ; Cells, Cultured ; Consensus Sequence ; Dimerization ; Erythropoietin/pharmacology ; Hematopoiesis/drug effects ; Humans ; Megakaryocytes/cytology ; Mice ; Molecular Sequence Data ; *Neoplasm Proteins ; Oligopeptides/*metabolism/*pharmacology ; Peptide Library ; Peptides/metabolism/pharmacology ; Platelet Count ; Proto-Oncogene Proteins/*agonists/metabolism ; *Receptors, Cytokine ; Receptors, Thrombopoietin ; Recombinant Proteins/metabolism/pharmacology ; Thrombopoietin/*metabolism/pharmacology ; Transfection
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  • 18
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    Thanks to a parasite, asexual reproduction catches on (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Enserink, M -- New York, N.Y. -- Science. 1997 Mar 21;275(5307):1743.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9122678" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Butterflies/parasitology ; Female ; Male ; Moths/parasitology ; Ovum/parasitology ; *Parthenogenesis ; Rickettsiaceae/*physiology ; Wasps/microbiology/*physiology
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  • 19
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    How much pain for cardiac gain? (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1997 May 30;276(5317):1324-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9190672" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Centers for Disease Control and Prevention (U.S.) ; Exercise/*physiology/psychology ; Female ; Guidelines as Topic ; Heart Diseases/epidemiology/*prevention & control ; Humans ; Male ; Middle Aged ; Risk Factors ; United States
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  • 20
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    Stretching single protein molecules: titin is a weird spring (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erickson, H P -- New York, N.Y. -- Science. 1997 May 16;276(5315):1090-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, UDA. H.Erickson@cellbio.duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9173540" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Connectin ; Elasticity ; Entropy ; Immunoglobulins/chemistry ; Muscle Proteins/*chemistry/physiology ; Muscle Relaxation ; Muscle, Skeletal/chemistry/physiology ; *Protein Folding ; Protein Kinases/*chemistry/physiology ; Sarcomeres/chemistry ; Stress, Mechanical
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  • 21
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    Life and death of neurons in the aging brain (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-10-23
    Description: Neurodegenerative disorders are characterized by extensive neuron death that leads to functional decline, but the neurobiological correlates of functional decline in normal aging are less well defined. For decades, it has been a commonly held notion that widespread neuron death in the neocortex and hippocampus is an inevitable concomitant of brain aging, but recent quantitative studies suggest that neuron death is restricted in normal aging and unlikely to account for age-related impairment of neocortical and hippocampal functions. In this article, the qualitative and quantitative differences between aging and Alzheimer's disease with respect to neuron loss are discussed, and age-related changes in functional and biochemical attributes of hippocampal circuits that might mediate functional decline in the absence of neuron death are explored. When these data are viewed comprehensively, it appears that the primary neurobiological substrates for functional impairment in aging differ in important ways from those in neurodegenerative disorders such as Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morrison, J H -- Hof, P R -- AG05138/AG/NIA NIH HHS/ -- AG06647/AG/NIA NIH HHS/ -- MHDA52145/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 17;278(5337):412-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neurobiology of Aging Laboratories, the Fishberg Research Center for Neurobiology, and the Department of Geriatrics and Adult Development, Mount Sinai School of Medicine, New York, NY 10029, USA. morrison@cortex.neuro.mssm.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9334292" target="_blank"〉PubMed〈/a〉
    Keywords: *Aging ; Alzheimer Disease/pathology ; Animals ; Cell Death ; Cell Survival ; Entorhinal Cortex/pathology ; Estrogens/physiology ; Female ; Hippocampus/cytology/pathology/*physiology ; Humans ; Male ; Memory ; Neocortex/cytology/pathology/*physiology ; *Nerve Degeneration ; Neurofibrillary Tangles/pathology ; Neurofilament Proteins/metabolism ; Neurons/cytology/pathology/*physiology
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  • 22
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    New clues found to circadian clocks--including mammals' (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1997 May 16;276(5315):1030-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9173537" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Clocks/*genetics ; CLOCK Proteins ; Chromosome Mapping ; Circadian Rhythm/*genetics ; Cloning, Molecular ; Gene Expression Regulation ; Mice ; Mutation ; Trans-Activators/chemistry/*genetics/physiology
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  • 23
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    A macrophage invasion mechanism of pathogenic mycobacteria (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-08-22
    Description: Tuberculosis is the leading cause of death due to an infectious organism, killing an estimated 3 million people annually. Mycobacterium tuberculosis, the causative agent of tuberculosis, and other pathogenic mycobacteria require entry into host macrophages to initiate infection. An invasion mechanism was defined that was shared among pathogenic mycobacteria including M. tuberculosis, M. leprae, and M. avium but not by nonpathogenic mycobacteria or nonmycobacterial intramacrophage pathogens. This pathway required the association of the complement cleavage product C2a with mycobacteria resulting in the formation of a C3 convertase. The mycobacteria-associated C2a cleaved C3, resulting in C3b opsonization of the mycobacteria and recognition by macrophages.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schorey, J S -- Carroll, M C -- Brown, E J -- AI33348/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1997 Aug 22;277(5329):1091-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9262476" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Complement C2/*physiology ; Complement C2a ; Complement C3/metabolism ; Complement C3-C5 Convertases/metabolism ; Complement C3b/immunology ; Horses ; Humans ; In Vitro Techniques ; Isoflurophate/pharmacology ; Macrophages/immunology/*microbiology ; Mice ; Molecular Sequence Data ; Mycobacterium/*pathogenicity ; Mycobacterium avium Complex/immunology/*pathogenicity ; Mycobacterium bovis/immunology/pathogenicity ; Mycobacterium leprae/immunology/pathogenicity ; Mycobacterium tuberculosis/immunology/pathogenicity ; Opsonin Proteins ; Virulence
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  • 24
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    Longer tusks are healthy signs (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-06-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bagla, P -- New York, N.Y. -- Science. 1997 Jun 27;276(5321):1972.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9221498" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Commerce ; Elephants/*anatomy & histology/genetics/*parasitology ; Female ; Helminthiasis, Animal/*immunology ; Immunity, Innate ; Incisor/anatomy & histology ; Male ; Parasite Egg Count/veterinary ; Sexual Behavior, Animal
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  • 25
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    Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-27
    Description: Long-term potentiation (LTP), a cellular model of learning and memory, requires calcium-dependent protein kinases. Induction of LTP increased the phosphorus-32 labeling of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptors (AMPA-Rs), which mediate rapid excitatory synaptic transmission. This AMPA-R phosphorylation appeared to be catalyzed by Ca2+- and calmodulin-dependent protein kinase II (CaM-KII): (i) it correlated with the activation and autophosphorylation of CaM-KII, (ii) it was blocked by the CaM-KII inhibitor KN-62, and (iii) its phosphorus-32 peptide map was the same as that of GluR1 coexpressed with activated CaM-KII in HEK-293 cells. This covalent modulation of AMPA-Rs in LTP provides a postsynaptic molecular mechanism for synaptic plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barria, A -- Muller, D -- Derkach, V -- Griffith, L C -- Soderling, T R -- NS27037/NS/NINDS NIH HHS/ -- R01 GM054408/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 27;276(5321):2042-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health Sciences University, Portland, OR 97201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9197267" target="_blank"〉PubMed〈/a〉
    Keywords: 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine/analogs & derivatives/pharmacology ; 2-Amino-5-phosphonovalerate/pharmacology ; Animals ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors/*metabolism ; Cell Line ; Enzyme Inhibitors/pharmacology ; Excitatory Amino Acid Antagonists/pharmacology ; Hippocampus/*metabolism ; Humans ; In Vitro Techniques ; *Long-Term Potentiation/drug effects ; Male ; Peptide Mapping ; Phosphorylation ; Rats ; Rats, Sprague-Dawley ; Receptors, AMPA/*metabolism ; Synaptic Transmission/drug effects
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  • 26
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    Estrogen stakes claim to cognition (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickelgren, I -- New York, N.Y. -- Science. 1997 May 2;276(5313):675-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9157544" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*drug therapy ; Animals ; Antioxidants/pharmacology ; Brain/cytology/metabolism ; Choline O-Acetyltransferase/metabolism ; Cognition/drug effects/*physiology ; Controlled Clinical Trials as Topic ; Estrogens/pharmacology/*physiology/therapeutic use ; Female ; Humans ; Male ; Memory/drug effects/*physiology ; Nerve Growth Factors/metabolism ; Receptors, N-Methyl-D-Aspartate/metabolism ; Synapses/physiology
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  • 27
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    Telomerase catalytic subunit homologs from fission yeast and human (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-15
    Description: Catalytic protein subunits of telomerase from the ciliate Euplotes aediculatus and the yeast Saccharomyces cerevisiae contain reverse transcriptase motifs. Here the homologous genes from the fission yeast Schizosaccharomyces pombe and human are identified. Disruption of the S. pombe gene resulted in telomere shortening and senescence, and expression of mRNA from the human gene correlated with telomerase activity in cell lines. Sequence comparisons placed the telomerase proteins in the reverse transcriptase family but revealed hallmarks that distinguish them from retroviral and retrotransposon relatives. Thus, the proposed telomerase catalytic subunits are phylogenetically conserved and represent a deep branch in the evolution of reverse transcriptases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakamura, T M -- Morin, G B -- Chapman, K B -- Weinrich, S L -- Andrews, W H -- Lingner, J -- Harley, C B -- Cech, T R -- GM28039/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Aug 15;277(5328):955-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309-0215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9252327" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Catalysis ; Cell Line ; DNA-Binding Proteins ; Evolution, Molecular ; Genes, Fungal ; Humans ; Introns ; Molecular Sequence Data ; Phylogeny ; Proteins/*chemistry/genetics/metabolism ; *Rna ; RNA, Messenger/genetics/metabolism ; RNA-Directed DNA Polymerase/chemistry ; Retroelements ; Schizosaccharomyces/*enzymology/genetics/growth & development ; Schizosaccharomyces pombe Proteins ; Sequence Alignment ; Telomerase/*chemistry/genetics/metabolism ; Telomere/metabolism
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  • 28
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    Subtle, secret female chimpanzees (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wrangham, R W -- New York, N.Y. -- Science. 1997 Aug 8;277(5327):774-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anthropology, Harvard University, Cambridge, MA 02138, USA. wrangham@fas.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9273699" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; Male ; Pan troglodytes/*psychology ; *Reproduction ; *Sexual Behavior, Animal ; *Social Dominance
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Structural and functional conservation of the Caenorhabditis elegans timing gene clk-1 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-02-14
    Description: Mutations in the Caenorhabditis elegans gene clk-1 affect biological timing and extend longevity. The gene clk-1 was identified, and the cloned gene complemented the clk-1 phenotypes and restored normal longevity. The CLK-1 protein was found to be conserved among eukaryotes, including humans, and structurally similar to the yeast metabolic regulator Cat5p (also called Coq7p). These proteins contain a tandem duplication of a core 82-residue domain. clk-1 complemented the phenotype of cat5/coq7 null mutants, demonstrating that clk-1 and CAT5/COQ7 share biochemical function and that clk-1 acts at the level of cellular physiology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ewbank, J J -- Barnes, T M -- Lakowski, B -- Lussier, M -- Bussey, H -- Hekimi, S -- New York, N.Y. -- Science. 1997 Feb 14;275(5302):980-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, McGill University, 1205 Avenue Docteur Penfield, Montreal, Quebec, Canada H3A 1B1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9020081" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Caenorhabditis elegans/*genetics/metabolism/*physiology ; *Caenorhabditis elegans Proteins ; Cell Aging/*genetics ; Chromosome Mapping ; Conserved Sequence ; Exons ; Fungal Proteins/chemistry/genetics/physiology ; *Genes, Helminth ; Genetic Complementation Test ; Glycerol/metabolism ; Helminth Proteins/chemistry/*genetics/physiology ; Humans ; Longevity/genetics ; Mice ; Molecular Sequence Data ; Phenotype ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA Splicing ; *Saccharomyces cerevisiae Proteins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    The many faces of WAS protein (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Featherstone, C -- New York, N.Y. -- Science. 1997 Jan 3;275(5296):27-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8999530" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism/ultrastructure ; Adaptor Proteins, Signal Transducing ; Cell Cycle Proteins/*metabolism ; Cell Division ; Cell Membrane/metabolism/ultrastructure ; Cytoskeleton/metabolism/ultrastructure ; GTP-Binding Proteins/*metabolism ; Humans ; Male ; Oncogene Proteins/metabolism ; Protein-Tyrosine Kinases/metabolism ; Proteins/genetics/*metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-fyn ; *Signal Transduction ; Wiskott-Aldrich Syndrome/genetics/*metabolism ; Wiskott-Aldrich Syndrome Protein ; cdc42 GTP-Binding Protein ; src Homology Domains
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    Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-20
    Description: Bactericidal/permeability-increasing protein (BPI), a potent antimicrobial protein of 456 residues, binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria. At a resolution of 2.4 angstroms, the crystal structure of human BPI shows a boomerang-shaped molecule formed by two similar domains. Two apolar pockets on the concave surface of the boomerang each bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the pockets may also bind the acyl chains of lipopolysaccharide. As a model for the related plasma lipid transfer proteins, BPI illuminates a mechanism of lipid transfer for this protein family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beamer, L J -- Carroll, S F -- Eisenberg, D -- GM31299/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 20;276(5320):1861-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉UCLA-DOE Laboratory of Structural Biology and Molecular Medicine, Molecular Biology Institute, University of California, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9188532" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antimicrobial Cationic Peptides ; Binding Sites ; Blood Bactericidal Activity ; Blood Proteins/*chemistry/metabolism ; Crystallization ; Crystallography, X-Ray ; Humans ; Lipopolysaccharides/metabolism ; *Membrane Proteins ; Models, Molecular ; Molecular Sequence Data ; Phosphatidylcholines/chemistry/*metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary
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    Role for the amino-terminal region of human TBP in U6 snRNA transcription (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-02-21
    Description: Basal transcription from the human RNA polymerase III U6 promoter depends on a TATA box that recruits the TATA box-binding protein (TBP) and a proximal sequence element that recruits the small nuclear RNA (snRNA)-activating protein complex (SNAPc). TBP consists of a conserved carboxyl-terminal domain that performs all known functions of the protein and a nonconserved amino-terminal region of unknown function. Here, the amino-terminal region is shown to down-regulate binding of TBP to the U6 TATA box, mediate cooperative binding with SNAPc to the U6 promoter, and enhance U6 transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mittal, V -- Hernandez, N -- R01GM38810/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Feb 21;275(5303):1136-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9027316" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; DNA Footprinting ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Down-Regulation ; Humans ; Molecular Sequence Data ; *Promoter Regions, Genetic ; Proteins/metabolism ; RNA, Small Nuclear/*genetics ; RNA-Binding Proteins/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; TATA Box ; TATA-Box Binding Protein ; Transcription Factors/chemistry/genetics/*metabolism ; *Transcription, Genetic
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    Exchange of protein molecules through connections between higher plant plastids (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-27
    Description: Individual plastids of vascular plants have generally been considered to be discrete autonomous entities that do not directly communicate with each other. However, in transgenic plants in which the plastid stroma was labeled with green fluorescent protein (GFP), thin tubular projections emanated from individual plastids and sometimes connected to other plastids. Flow of GFP between interconnected plastids could be observed when a single plastid or an interconnecting plastid tubule was photobleached and the loss of green fluorescence by both plastids was seen. These tubules allow the exchange of molecules within an interplastid communication system, which may facilitate the coordination of plastid activities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kohler, R H -- Cao, J -- Zipfel, W R -- Webb, W W -- Hanson, M R -- R07719/PHS HHS/ -- RR04224/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 27;276(5321):2039-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Genetics and Development, Cornell University, Biotechnology Building, Ithaca, NY 14853-2703, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9197266" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chloroplasts/*metabolism/*ultrastructure ; Cytoplasm/metabolism ; Green Fluorescent Proteins ; Luminescent Proteins/*metabolism ; Microscopy/methods ; Microscopy, Fluorescence ; Molecular Sequence Data ; Plant Leaves/*ultrastructure ; Plants, Genetically Modified ; Plants, Toxic ; Recombinant Fusion Proteins/metabolism ; Tobacco
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    A new way to resist AIDS? (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-02-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, J -- New York, N.Y. -- Science. 1997 Feb 28;275(5304):1258.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9064779" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology/virology ; CD4-Positive T-Lymphocytes/immunology/*virology ; Cells, Cultured ; HIV/*physiology ; Humans ; Immunity, Innate ; Male ; Virus Replication
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Large porous particles for pulmonary drug delivery (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-06-20
    Description: A new type of inhalation aerosol, characterized by particles of small mass density and large size, permitted the highly efficient delivery of inhaled therapeutics into the systemic circulation. Particles with mass densities less than 0.4 gram per cubic centimeter and mean diameters exceeding 5 micrometers were inspired deep into the lungs and escaped the lungs' natural clearance mechanisms until the inhaled particles delivered their therapeutic payload. Inhalation of large porous insulin particles resulted in elevated systemic levels of insulin and suppressed systemic glucose levels for 96 hours, whereas small nonporous insulin particles had this effect for only 4 hours. High systemic bioavailability of testosterone was also achieved by inhalation delivery of porous particles with a mean diameter (20 micrometers) approximately 10 times that of conventional inhaled therapeutic particles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Edwards, D A -- Hanes, J -- Caponetti, G -- Hrkach, J -- Ben-Jebria, A -- Eskew, M L -- Mintzes, J -- Deaver, D -- Lotan, N -- Langer, R -- GM26698/GM/NIGMS NIH HHS/ -- HD29125/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 20;276(5320):1868-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering, Pennsylvania State University, 204 Fenske Laboratory, University Park, PA 16802, USA. dxe11@psuv.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9188534" target="_blank"〉PubMed〈/a〉
    Keywords: *Administration, Inhalation ; Aerosols ; Animals ; Biological Availability ; Blood Glucose/analysis ; Bronchoalveolar Lavage ; *Drug Carriers ; Drug Compounding ; Insulin/administration & dosage/blood/pharmacokinetics ; *Lactic Acid ; *Lung ; Male ; Particle Size ; *Polyglycolic Acid ; *Polylysine ; *Polymers ; Rats ; Rats, Sprague-Dawley ; Testosterone/administration & dosage/blood/pharmacokinetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Quantitative trait loci for refractoriness of Anopheles gambiae to Plasmodium cynomolgi B (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-18
    Description: The severity of the malaria pandemic in the tropics is aggravated by the ongoing spread of parasite resistance to antimalarial drugs and mosquito resistance to insecticides. A strain of Anopheles gambiae, normally a major vector for human malaria in Africa, can encapsulate and kill the malaria parasites within a melanin-rich capsule in the mosquito midgut. Genetic mapping revealed one major and two minor quantitative trait loci (QTLs) for this encapsulation reaction. Understanding such antiparasite mechanisms in mosquitoes may lead to new strategies for malaria control.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zheng, L -- Cornel, A J -- Wang, R -- Erfle, H -- Voss, H -- Ansorge, W -- Kafatos, F C -- Collins, F H -- New York, N.Y. -- Science. 1997 Apr 18;276(5311):425-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany. Disease Control and Prevention, 4770 Buford Hi.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9103203" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anopheles/*genetics/immunology/*parasitology ; Chromosome Mapping ; Crosses, Genetic ; Female ; *Genes, Insect ; Genotype ; Insect Vectors/*genetics/immunology/*parasitology ; Lod Score ; Male ; Melanins/physiology ; Microsatellite Repeats ; Phenotype ; Plasmodium cynomolgi/*immunology
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    Rapid colorectal adenoma formation initiated by conditional targeting of the Apc gene (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-06
    Description: Familial adenomatous polyposis coli (FAP) is a disease characterized by the development of multiple colorectal adenomas, and affected individuals carry germline mutations in the APC gene. With the use of a conditional gene targeting system, a mouse model of FAP was created that circumvents the embryonic lethality of Apc deficiency and directs Apc inactivation specifically to the colorectal epithelium. loxP sites were inserted into the introns around Apc exon 14, and the resultant mutant allele (Apc580S) was introduced into the mouse germline. Mice homozygous for Apc580S were normal; however, upon infection of the colorectal region with an adenovirus encoding the Cre recombinase, the mice developed adenomas within 4 weeks. The adenomas showed deletion of Apc exon 14, indicating that the loss of Apc function was caused by Cre-loxP-mediated recombination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shibata, H -- Toyama, K -- Shioya, H -- Ito, M -- Hirota, M -- Hasegawa, S -- Matsumoto, H -- Takano, H -- Akiyama, T -- Toyoshima, K -- Kanamaru, R -- Kanegae, Y -- Saito, I -- Nakamura, Y -- Shiba, K -- Noda, T -- New York, N.Y. -- Science. 1997 Oct 3;278(5335):120-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Cancer Institute, Toshima-ku, Tokyo 170, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9311916" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli/*genetics ; Adenomatous Polyposis Coli Protein ; Adenoviridae/genetics ; Animals ; Colon/metabolism ; Cytoskeletal Proteins/biosynthesis ; Disease Models, Animal ; Exons ; Female ; Frameshift Mutation ; Gene Deletion ; *Gene Targeting ; *Genes, APC ; Genetic Vectors ; Germ-Line Mutation ; Homozygote ; Integrases/genetics/metabolism ; Introns ; Male ; Mice ; Mice, Inbred C57BL ; Recombination, Genetic ; *Viral Proteins
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    Inducible expression and phosphorylation of coactivator BOB.1/OBF.1 in T cells (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-07-11
    Description: BOB.1/OBF.1 is a transcriptional coactivator that is constitutively expressed in B cells and interacts with the Oct1 and Oct2 transcription factors. Upon activation of Jurkat T cells and primary murine thymocytes with phorbol esters and ionomycin, BOB.1/OBF.1 expression and transactivation function were induced. BOB.1/OBF.1 was phosphorylated at Ser184 both in vivo and in vitro, and this modification was required for inducible activation. Mutation of Ser184 also diminished transactivation function in B cells, suggesting that the activating phosphorylation that is inducible in T cells is constitutively present in B cells. Thus, BOB.1/OBF.1 is a transcriptional coactivator that is critically regulated by posttranslational modifications to mediate cell type-specific gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zwilling, S -- Dieckmann, A -- Pfisterer, P -- Angel, P -- Wirth, T -- New York, N.Y. -- Science. 1997 Jul 11;277(5323):221-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MSZ, Institut fur Medizinische Strahlenkunde und Zellforschung, Universitat Wurzburg, Versbacher Strasse 5, 97078 Wurzburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9211847" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/metabolism ; Cells, Cultured ; *DNA-Binding Proteins ; *Gene Expression Regulation ; HeLa Cells ; Homeodomain Proteins/metabolism ; Host Cell Factor C1 ; Humans ; Immunosuppressive Agents/pharmacology ; Ionomycin/pharmacology ; Jurkat Cells ; *Lymphocyte Activation ; Mice ; Molecular Sequence Data ; Octamer Transcription Factor-1 ; Phosphorylation ; Phosphoserine/metabolism ; Recombinant Fusion Proteins/metabolism ; T-Lymphocytes/immunology/*metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; Trans-Activators/genetics/*metabolism ; Transcription Factors/metabolism ; *Transcriptional Activation
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    Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regulation through Cdc25 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-05
    Description: In response to DNA damage, mammalian cells prevent cell cycle progression through the control of critical cell cycle regulators. A human gene was identified that encodes the protein Chk1, a homolog of the Schizosaccharomyces pombe Chk1 protein kinase, which is required for the DNA damage checkpoint. Human Chk1 protein was modified in response to DNA damage. In vitro Chk1 bound to and phosphorylated the dual-specificity protein phosphatases Cdc25A, Cdc25B, and Cdc25C, which control cell cycle transitions by dephosphorylating cyclin-dependent kinases. Chk1 phosphorylates Cdc25C on serine-216. As shown in an accompanying paper by Peng et al. in this issue, serine-216 phosphorylation creates a binding site for 14-3-3 protein and inhibits function of the phosphatase. These results suggest a model whereby in response to DNA damage, Chk1 phosphorylates and inhibits Cdc25C, thus preventing activation of the Cdc2-cyclin B complex and mitotic entry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sanchez, Y -- Wong, C -- Thoma, R S -- Richman, R -- Wu, Z -- Piwnica-Worms, H -- Elledge, S J -- GM17763/GM/NIGMS NIH HHS/ -- GM44664/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 5;277(5331):1497-501.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Verna and Marrs McLean Department of Biochemistry, Howard Hughes Medical Institute, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9278511" target="_blank"〉PubMed〈/a〉
    Keywords: 14-3-3 Proteins ; Amino Acid Sequence ; Animals ; CDC2 Protein Kinase/*metabolism ; Cell Cycle Proteins/antagonists & inhibitors/*metabolism ; Chromosome Mapping ; Chromosomes, Human, Pair 11 ; Cytoskeletal Proteins ; *DNA Damage ; *F-Box Proteins ; G2 Phase ; HeLa Cells ; Humans ; Mice ; *Mitosis ; Molecular Sequence Data ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Protein Kinases/chemistry/genetics/*metabolism ; Protein Tyrosine Phosphatases/metabolism ; Proteins/metabolism ; Recombinant Fusion Proteins/metabolism ; Schizosaccharomyces pombe Proteins ; Signal Transduction ; Transfection ; *Tyrosine 3-Monooxygenase ; *Ubiquitin-Protein Ligases ; *cdc25 Phosphatases
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    Identification of a naturally occurring peroxidase-lipoxygenase fusion protein (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-26
    Description: A distant relative of catalase that is specialized for metabolism of a fatty acid hydroperoxide was identified. This heme peroxidase occurs in coral as part of a fusion protein, the other component of which is a lipoxygenase that forms the hydroperoxide substrate. The end product is an unstable epoxide (an allene oxide) that is a potential precursor of prostaglandin-like molecules. These results extend the known chemistry of catalase-like proteins and reveal a distinct type of enzymatic construct involved in the metabolism of polyunsaturated fatty acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koljak, R -- Boutaud, O -- Shieh, B H -- Samel, N -- Brash, A R -- GM49502/GM/NIGMS NIH HHS/ -- TW00404/TW/FIC NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 26;277(5334):1994-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232-6602, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9302294" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arachidonic Acid/metabolism ; Binding Sites ; Catalase/chemistry ; Catalysis ; Cloning, Molecular ; Cnidaria/*enzymology/genetics ; Hydrogen Peroxide/metabolism ; *Intramolecular Oxidoreductases ; Isomerases/chemistry ; Lipoxygenase/*chemistry/genetics/isolation & purification/metabolism ; Molecular Sequence Data ; Peroxidase/*chemistry/genetics/isolation & purification/metabolism ; Peroxidases/*chemistry/isolation & purification/metabolism ; Recombinant Proteins/metabolism ; Sequence Homology, Amino Acid
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    Evidence for a role of CRM1 in signal-mediated nuclear protein export (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-06
    Description: Chromosome maintenance region 1 (CRM1), a protein that shares sequence similarities with the karyopherin beta family of proteins involved in nuclear import pathway, was shown to form a complex with the leucine-rich nuclear export signal (NES). This interaction was inhibited by leptomycin B, a drug that prevents the function of the CRM1 protein in yeast. To analyze the role of the CRM1-NES interaction in nuclear export, a transport assay based on semipermeabilized cells was developed. In this system, which reconstituted NES-, cytosol-, and energy-dependent nuclear export, leptomycin B specifically blocked export of NES-containing proteins. Thus, the CRM1 protein could act as a NES receptor involved in nuclear protein export.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ossareh-Nazari, B -- Bachelerie, F -- Dargemont, C -- New York, N.Y. -- Science. 1997 Oct 3;278(5335):141-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut Curie-CNRS Unite Mixte de Recherche 144, 26 rue d'Ulm, 75248 Paris Cedex 05, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9311922" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Biological Transport/drug effects ; Carrier Proteins/*physiology ; Cell Nucleus/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Fatty Acids, Unsaturated/pharmacology ; Fluorescent Antibody Technique, Indirect ; HeLa Cells ; Humans ; *I-kappa B Proteins ; Immunoblotting ; *Karyopherins ; Nuclear Localization Signals ; Nuclear Proteins/*metabolism ; Protein Sorting Signals/chemistry/*metabolism ; Pyruvate Kinase/metabolism ; *Receptors, Cytoplasmic and Nuclear ; Recombinant Fusion Proteins/metabolism ; Transfection
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    Role of Cue1p in ubiquitination and degradation at the ER surface (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: Endoplasmic reticulum (ER) degradation of aberrant proteins is mediated by the ubiquitin-proteasome pathway. Here, a membrane-bound component of the ubiquitin system, Cue1p, was identified. It was shown to recruit the soluble ubiquitin-conjugating enzyme Ubc7p to the ER membrane. In the absence of Cue1p, unassembled and thus cytosolically mislocalized Ubc7p was unable to participate in ER degradation or in the turnover of soluble non-ER proteins. Moreover, ubiquitination by Cue1p-assembled Ubc7p and Ubc6p was a prerequisite for retrograde transport of lumenal substrates out of the ER, which suggests that ubiquitination is mechanistically integrated into the ER degradation process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biederer, T -- Volkwein, C -- Sommer, T -- New York, N.Y. -- Science. 1997 Dec 5;278(5344):1806-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Delbruck Center for Molecular Medicine, Robert-Rossle-Strasse 10, 13122 Berlin, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9388185" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Biological Transport ; Carboxypeptidases/*metabolism ; Carrier Proteins/chemistry/genetics/*metabolism ; Cathepsin A ; Cysteine Endopeptidases/metabolism ; Cytosol/metabolism ; Endoplasmic Reticulum/*metabolism ; Intracellular Membranes/metabolism ; Ligases/*metabolism ; Membrane Proteins/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Multienzyme Complexes/metabolism ; Proteasome Endopeptidase Complex ; *Saccharomyces cerevisiae Proteins ; *Ubiquitin-Conjugating Enzymes ; Ubiquitins/*metabolism ; Yeasts/metabolism
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    Antagonism of central melanocortin receptors in vitro and in vivo by agouti-related protein (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-06
    Description: Expression of Agouti protein is normally limited to the skin where it affects pigmentation, but ubiquitous expression causes obesity. An expressed sequence tag was identified that encodes Agouti-related protein, whose RNA is normally expressed in the hypothalamus and whose levels were increased eightfold in ob/ob mice. Recombinant Agouti-related protein was a potent, selective antagonist of Mc3r and Mc4r, melanocortin receptor subtypes implicated in weight regulation. Ubiquitous expression of human AGRP complementary DNA in transgenic mice caused obesity without altering pigmentation. Thus, Agouti-related protein is a neuropeptide implicated in the normal control of body weight downstream of leptin signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ollmann, M M -- Wilson, B D -- Yang, Y K -- Kerns, J A -- Chen, Y -- Gantz, I -- Barsh, G S -- EY07106/EY/NEI NIH HHS/ -- GM07365/GM/NIGMS NIH HHS/ -- P30DK-34933/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 Oct 3;278(5335):135-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Howard Hughes Medical Institute, 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/9311920" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Glands/metabolism ; Amino Acid Sequence ; Animals ; Female ; Humans ; Hypothalamus/metabolism ; Male ; Melanocyte-Stimulating Hormones/antagonists & inhibitors/pharmacology ; Melanophores/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Inbred CBA ; Mice, Obese ; Mice, Transgenic ; Molecular Sequence Data ; Obesity/etiology ; Organophosphorus Compounds/pharmacology ; Proteins/chemistry/genetics/pharmacology/*physiology ; RNA/genetics/metabolism ; Receptor, Melanocortin, Type 3 ; Receptor, Melanocortin, Type 4 ; Receptors, Corticotropin/*antagonists & inhibitors/metabolism ; Receptors, Peptide/*antagonists & inhibitors/metabolism ; Recombinant Proteins/metabolism ; Signal Transduction ; Xenopus
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    Constitutive transcriptional activation by a beta-catenin-Tcf complex in APC-/- colon carcinoma (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-21
    Description: The adenomatous polyposis coli (APC) tumor suppressor protein binds to beta-catenin, a protein recently shown to interact with Tcf and Lef transcription factors. The gene encoding hTcf-4, a Tcf family member that is expressed in colonic epithelium, was cloned and characterized. hTcf-4 transactivates transcription only when associated with beta-catenin. Nuclei of APC-/- colon carcinoma cells were found to contain a stable beta-catenin-hTcf-4 complex that was constitutively active, as measured by transcription of a Tcf reporter gene. Reintroduction of APC removed beta-catenin from hTcf-4 and abrogated the transcriptional transactivation. Constitutive transcription of Tcf target genes, caused by loss of APC function, may be a crucial event in the early transformation of colonic epithelium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Korinek, V -- Barker, N -- Morin, P J -- van Wichen, D -- de Weger, R -- Kinzler, K W -- Vogelstein, B -- Clevers, H -- CA57345/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Mar 21;275(5307):1784-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, University Hospital, Post Office Box 85500, 3508 GA Utrecht, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9065401" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli Protein ; Amino Acid Sequence ; Animals ; Cell Line ; Cell Transformation, Neoplastic ; Cloning, Molecular ; Colon/metabolism ; Colonic Neoplasms/*genetics/metabolism ; Cytoskeletal Proteins/genetics/*metabolism ; Gene Expression Regulation, Neoplastic ; *Genes, APC ; Genes, Reporter ; Humans ; Intestinal Mucosa/metabolism ; Mice ; Molecular Sequence Data ; Signal Transduction ; TCF Transcription Factors ; *Trans-Activators ; Transcription Factor 7-Like 2 Protein ; Transcription Factors/chemistry/genetics/*metabolism ; *Transcriptional Activation ; Transfection ; Tumor Cells, Cultured ; beta Catenin
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    When should fatherhood stop? (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gavrilov, L A -- Gavrilova, N S -- New York, N.Y. -- Science. 1997 Jul 4;277(5322):17-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9229762" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; Humans ; *Longevity ; Male ; *Nuclear Family ; *Paternal Age
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    Macromolecular trafficking indicated by localization and turnover of sucrose transporters in enucleate sieve elements (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-02-28
    Description: The leaf sucrose transporter SUT1 is essential for phloem loading and long-distance transport of assimilates. Both SUT1 messenger RNA (mRNA) and protein were shown to be diurnally regulated and to have high turnover rates. SUT1 protein was detected by immunolocalization in plasma membranes of enucleate sieve elements (SEs) in tobacco, potato, and tomato. Analysis by in situ hybridization showed that SUT1 mRNA localizes mainly to the SE and is preferentially associated with plasmodesmata. Antisense inhibition of SUT1 expression under control of a companion cell (CC)-specific promoter indicated synthesis of SUT1 mRNA in the CC. These results provide evidence for targeting of plant endogenous mRNA and potentially SUT1 protein through phloem plasmodesmata and for sucrose loading at the plasma membrane of SE.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuhn, C -- Franceschi, V R -- Schulz, A -- Lemoine, R -- Frommer, W B -- New York, N.Y. -- Science. 1997 Feb 28;275(5304):1298-300.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Botanik, Eberhard-Karls-Universitat, Auf der Morgenstelle 1, D-72076 Tubingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9036853" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Biological Transport, Active ; Carrier Proteins/analysis/genetics/*metabolism ; Cell Membrane/chemistry/metabolism ; Fluorescent Antibody Technique ; Immunohistochemistry ; In Situ Hybridization ; Lycopersicon esculentum/metabolism ; Membrane Proteins/analysis/genetics/*metabolism ; *Membrane Transport Proteins ; Molecular Sequence Data ; Plant Leaves/chemistry/cytology/*metabolism ; Plant Proteins/analysis/genetics/*metabolism ; Plants, Toxic ; RNA, Messenger/analysis/genetics/metabolism ; RNA, Plant/analysis/genetics/metabolism ; Solanum tuberosum ; Sucrose/metabolism ; Tobacco/metabolism ; Transcription, Genetic
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    Positional cloning of the gene for multiple endocrine neoplasia-type 1 (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-04-18
    Description: Multiple endocrine neoplasia-type 1 (MEN1) is an autosomal dominant familial cancer syndrome characterized by tumors in parathyroids, enteropancreatic endocrine tissues, and the anterior pituitary. DNA sequencing from a previously identified minimal interval on chromosome 11q13 identified several candidate genes, one of which contained 12 different frameshift, nonsense, missense, and in-frame deletion mutations in 14 probands from 15 families. The MEN1 gene contains 10 exons and encodes a ubiquitously expressed 2.8-kilobase transcript. The predicted 610-amino acid protein product, termed menin, exhibits no apparent similarities to any previously known proteins. The identification of MEN1 will enable improved understanding of the mechanism of endocrine tumorigenesis and should facilitate early diagnosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chandrasekharappa, S C -- Guru, S C -- Manickam, P -- Olufemi, S E -- Collins, F S -- Emmert-Buck, M R -- Debelenko, L V -- Zhuang, Z -- Lubensky, I A -- Liotta, L A -- Crabtree, J S -- Wang, Y -- Roe, B A -- Weisemann, J -- Boguski, M S -- Agarwal, S K -- Kester, M B -- Kim, Y S -- Heppner, C -- Dong, Q -- Spiegel, A M -- Burns, A L -- Marx, S J -- New York, N.Y. -- Science. 1997 Apr 18;276(5311):404-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Gene Transfer, National Human Genome Research Institute (NHGRI), National Institutes of Health (NIH), Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9103196" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chromosome Mapping ; Chromosomes, Human, Pair 11 ; *Cloning, Molecular ; DNA, Complementary/genetics ; Exons ; Frameshift Mutation ; *Genes, Tumor Suppressor ; Humans ; Molecular Sequence Data ; Multiple Endocrine Neoplasia Type 1/*genetics ; Mutation ; Neoplasm Proteins/chemistry/*genetics ; *Proto-Oncogene Proteins
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    The origin of dogs: running with the wolves (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1997 Jun 13;276(5319):1647-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9206828" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Breeding ; Carnivora/*genetics ; Crosses, Genetic ; DNA, Mitochondrial/*genetics ; Dogs/*genetics ; Female ; Haplotypes ; Male
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    The telomerase picture fills in (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-04-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1997 Apr 25;276(5312):528-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9148410" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Catalysis ; DNA-Binding Proteins ; Euplotes/enzymology ; Fungal Proteins/*chemistry/genetics/isolation & purification/metabolism ; Genes, Fungal ; *Rna ; RNA-Directed DNA Polymerase/*chemistry/genetics/isolation & ; purification/metabolism ; Saccharomyces cerevisiae/enzymology/genetics ; Telomerase/*chemistry/genetics/isolation & purification/metabolism
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    The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-18
    Description: The three-dimensional structure of the complex between human H-Ras bound to guanosine diphosphate and the guanosine triphosphatase (GTPase)-activating domain of the human GTPase-activating protein p120GAP (GAP-334) in the presence of aluminum fluoride was solved at a resolution of 2.5 angstroms. The structure shows the partly hydrophilic and partly hydrophobic nature of the communication between the two molecules, which explains the sensitivity of the interaction toward both salts and lipids. An arginine side chain (arginine-789) of GAP-334 is supplied into the active site of Ras to neutralize developing charges in the transition state. The switch II region of Ras is stabilized by GAP-334, thus allowing glutamine-61 of Ras, mutation of which activates the oncogenic potential, to participate in catalysis. The structural arrangement in the active site is consistent with a mostly associative mechanism of phosphoryl transfer and provides an explanation for the activation of Ras by glycine-12 and glutamine-61 mutations. Glycine-12 in the transition state mimic is within van der Waals distance of both arginine-789 of GAP-334 and glutamine-61 of Ras, and even its mutation to alanine would disturb the arrangements of residues in the transition state.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scheffzek, K -- Ahmadian, M R -- Kabsch, W -- Wiesmuller, L -- Lautwein, A -- Schmitz, F -- Wittinghofer, A -- New York, N.Y. -- Science. 1997 Jul 18;277(5324):333-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur molekulare Physiologie, Abteilung Strukturelle Biologie, Rheinlanddamm 201, 44139 Dortmund, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9219684" target="_blank"〉PubMed〈/a〉
    Keywords: Aluminum Compounds/chemistry/metabolism ; Amino Acid Sequence ; Binding Sites ; Catalysis ; Cell Transformation, Neoplastic ; Crystallography, X-Ray ; Enzyme Activation ; Fluorides/chemistry/metabolism ; GTP Phosphohydrolases/chemistry/*metabolism ; GTP-Binding Proteins/chemistry/metabolism ; GTPase-Activating Proteins ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Models, Molecular ; Molecular Sequence Data ; Mutation ; *Protein Conformation ; Protein Structure, Secondary ; Proteins/*chemistry/*metabolism ; Signal Transduction ; ras GTPase-Activating Proteins ; ras Proteins/chemistry/genetics/*metabolism
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    Requirement for the transcription factor LSIRF/IRF4 for mature B and T lymphocyte function (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-01-24
    Description: Lymphocyte-specific interferon regulatory factor (LSIRF) (now called IRF4) is a transcription factor expressed only in lymphocytes. Mice deficient in IRF4 showed normal distribution of B and T lymphocyes at 4 to 5 weeks of age but developed progressive generalized lymphadenopathy. IRF4-deficient mice exhibited a profound reduction in serum immunoglobulin concentrations and did not mount detectable antibody responses. T lymphocyte function was also impaired in vivo; these mice could not generate cytotoxic or antitumor responses. Thus, IRF4 is essential for the function and homeostasis of both mature B and mature T lymphocytes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mittrucker, H W -- Matsuyama, T -- Grossman, A -- Kundig, T M -- Potter, J -- Shahinian, A -- Wakeham, A -- Patterson, B -- Ohashi, P S -- Mak, T W -- New York, N.Y. -- Science. 1997 Jan 24;275(5299):540-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, University of Toronto, Toronto, Ontario, M5G 2C1, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8999800" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen Presentation ; B-Lymphocytes/*immunology ; Bone Marrow Cells ; Cytotoxicity, Immunologic ; DNA-Binding Proteins/genetics/*physiology ; Female ; Gene Targeting ; Graft vs Host Reaction ; Immunization ; Immunoglobulins/blood ; Interferon Regulatory Factors ; Lymphatic Diseases/etiology ; Lymphocyte Activation ; Lymphocyte Subsets/cytology ; Lymphoid Tissue/cytology ; Male ; Mast-Cell Sarcoma/immunology ; Mice ; Mice, Inbred C57BL ; Mice, SCID ; Neoplasm Transplantation ; T-Lymphocytes/*immunology ; T-Lymphocytes, Cytotoxic/immunology ; Transcription Factors/genetics/*physiology
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    A di-acidic signal required for selective export from the endoplasmic reticulum (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-07-25
    Description: Transport of membrane proteins between intracellular compartments requires specific sequences in the protein cytoplasmic domain to direct packaging into vesicle shuttles. A sequence that mediates export from the endoplasmic reticulum (ER) has proved elusive. A di-acidic signal (Asp-X-Glu, where X represents any amino acid) on the cytoplasmic tail of vesicular stomatitis virus glycoprotein (VSV-G) and other cargo molecules was required for efficient recruitment to vesicles mediating export from the ER in baby hamster kidney cells. The existence of such a signal provides evidence that export from the ER occurs through a selective mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nishimura, N -- Balch, W E -- GM 42336/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jul 25;277(5325):556-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular 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/9228004" target="_blank"〉PubMed〈/a〉
    Keywords: Acid Phosphatase/metabolism ; Amino Acid Sequence ; Animals ; Biological Transport ; Cell Line ; Cricetinae ; Cytoplasm/chemistry ; Endoplasmic Reticulum/*metabolism ; Golgi Apparatus/metabolism ; *Membrane Glycoproteins ; Membrane Proteins/*chemistry/*metabolism ; Molecular Sequence Data ; Mutation ; Protein Folding ; Protein Sorting Signals/chemistry/*metabolism ; Receptors, Antigen, T-Cell, alpha-beta/metabolism ; Recombinant Fusion Proteins/metabolism ; Viral Envelope Proteins/*chemistry/*metabolism
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    Solution structure of 3-oxo-delta5-steroid isomerase (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-04-18
    Description: The three-dimensional structure of the enzyme 3-oxo-delta5-steroid isomerase (E.C. 5.3.3.1), a 28-kilodalton symmetrical dimer, was solved by multidimensional heteronuclear magnetic resonance spectroscopy. The two independently folded monomers pack together by means of extensive hydrophobic and electrostatic interactions. Each monomer comprises three alpha helices and a six-strand mixed beta-pleated sheet arranged to form a deep hydrophobic cavity. Catalytically important residues Tyr14 (general acid) and Asp38 (general base) are located near the bottom of the cavity and positioned as expected from mechanistic hypotheses. An unexpected acid group (Asp99) is also located in the active site adjacent to Tyr14, and kinetic and binding studies of the Asp99 to Ala mutant demonstrate that Asp99 contributes to catalysis by stabilizing the intermediate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, Z R -- Ebrahimian, S -- Zawrotny, M E -- Thornburg, L D -- Perez-Alvarado, G C -- Brothers, P -- Pollack, R M -- Summers, M F -- GM38155/GM/NIGMS NIH HHS/ -- GM49082/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Apr 18;276(5311):415-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of Maryland Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21250.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9103200" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Androstenedione/metabolism ; Binding Sites ; Dimerization ; Estradiol/metabolism ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; *Protein Conformation ; Protein Structure, Secondary ; Solutions ; Steroid Isomerases/*chemistry/genetics/metabolism
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    Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-28
    Description: Signal transmission by many cell surface receptors results in the activation of phosphoinositide (PI) 3-kinases that phosphorylate the 3' position of polyphosphoinositides. From a screen for mouse proteins that bind phosphoinositides, the protein GRP1was identified. GRP1 binds phosphatidylinositol-3,4,5-trisphosphate [PtdIns(3,4, 5)P3] through a pleckstrin homology (PH) domain and displays a region of high sequence similarity to the yeast Sec7 protein. The PH domain of the closely related protein cytohesin-1, which, through its Sec7 homology domain, regulates integrin beta2 and catalyzes guanine nucleotide exchange of the small guanine nucleotide-binding protein ARF1, was also found to specifically bind PtdIns(3,4,5)P3. GRP1 and cytohesin-1 appear to connect receptor-activated PI 3-kinase signaling pathways with proteins that mediate biological responses such as cell adhesion and membrane trafficking.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klarlund, J K -- Guilherme, A -- Holik, J J -- Virbasius, J V -- Chawla, A -- Czech, M P -- DK30648/DK/NIDDK NIH HHS/ -- DK30898/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1997 Mar 28;275(5308):1927-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular Medicine and Department of Biochemistry and Molecular Biology, University of Massachusetts Medical Center, 373 Plantation Street, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9072969" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factor 1 ; ADP-Ribosylation Factors ; Adipocytes/chemistry ; Amino Acid Sequence ; Animals ; Antigens, CD18/metabolism ; Blood Proteins/*chemistry ; Brain Chemistry ; Cell Adhesion Molecules/chemistry/*metabolism ; Cell Membrane/metabolism ; Cells, Cultured ; Cloning, Molecular ; DNA, Complementary ; Fungal Proteins/*chemistry ; GTP-Binding Proteins/metabolism ; *Guanine Nucleotide Exchange Factors ; Humans ; Mice ; Molecular Sequence Data ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositol Phosphates/*metabolism ; *Phosphoproteins ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/*metabolism ; Receptors, Cytoplasmic and Nuclear/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Sequence Homology, Amino Acid ; *Signal Transduction
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    Fyn-kinase as a determinant of ethanol sensitivity: relation to NMDA-receptor function (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-10-24
    Description: Animals vary in their sensitivity to ethanol, a trait at least partly determined by genetic factors. In order to identify possible responsible genes, mice lacking Fyn, a non-receptor type tyrosine kinase, were investigated. These mice were hypersensitive to the hypnotic effect of ethanol. The administration of ethanol enhanced tyrosine phosphorylation of the N-methyl-D-aspartate receptor (NMDAR) in the hippocampus of control mice but not in Fyn-deficient mice. An acute tolerance to ethanol inhibition of NMDAR-mediated excitatory postsynaptic potentials in hippocampal slices developed in control mice but not in Fyn-deficient mice. These results indicate that Fyn affects behavioral, biochemical, and physiological responses to ethanol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miyakawa, T -- Yagi, T -- Kitazawa, H -- Yasuda, M -- Kawai, N -- Tsuboi, K -- Niki, H -- New York, N.Y. -- Science. 1997 Oct 24;278(5338):698-701.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Neurobiology of Emotion, Brain Science Institute, RIKEN, Hirosawa, Wako-shi, Saitama-ken 351-01, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381182" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Central Nervous System Depressants/*pharmacology ; Ethanol/*pharmacology ; Excitatory Postsynaptic Potentials/drug effects ; Flurazepam/pharmacology ; Hippocampus/metabolism ; Hypnotics and Sedatives/pharmacology ; In Vitro Techniques ; Male ; Mice ; Mice, Knockout ; Motor Activity/*drug effects ; N-Methylaspartate/pharmacology ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/deficiency/genetics/*metabolism ; Proto-Oncogene Proteins/deficiency/genetics/*metabolism ; Proto-Oncogene Proteins c-fyn ; Receptors, N-Methyl-D-Aspartate/*metabolism
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    Inhibition of pathogenicity of the rice blast fungus by Saccharomyces cerevisiae alpha-factor (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-05-16
    Description: Magnaporthe grisea is a fungal pathogen with two mating types, MAT1-1 and MAT1-2, that forms a specialized cell necessary for pathogenesis, the appressorium. Saccharomyces cerevisiae alpha-factor pheromone blocked appressorium formation in a mating type-specific manner and protected plants from infection by MAT1-2 strains. Experiments with alpha-factor analogs suggest that the observed activity is due to a specific interaction of alpha-factor with an M. grisea receptor. Culture filtrates of a MAT1-1 strain contained an activity that inhibited appressorium formation of mating type MAT1-2 strains. These findings provide evidence that a pheromone response pathway exists in M. grisea that can be exploited for plant protection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beckerman, J L -- Naider, F -- Ebbole, D J -- GM22086/GM/NIGMS NIH HHS/ -- R29GM47977/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 May 16;276(5315):1116-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Pathology and Microbiology, Texas A&M University, College Station, TX 77843-2132, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9148806" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Ascomycota/cytology/pathogenicity/*physiology ; Crosses, Genetic ; Cyclic AMP/pharmacology ; Hordeum/microbiology ; Molecular Sequence Data ; Oryza/microbiology ; Peptides/metabolism/*pharmacology ; Pheromones/metabolism/*pharmacology ; Plant Diseases/microbiology ; Receptors, Mating Factor ; Receptors, Peptide/metabolism ; Saccharomyces cerevisiae/*chemistry ; *Transcription Factors
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    Control of TRAIL-induced apoptosis by a family of signaling and decoy receptors (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-08-08
    Description: TRAIL (also called Apo2L) belongs to the tumor necrosis factor family, activates rapid apoptosis in tumor cells, and binds to the death-signaling receptor DR4. Two additional TRAIL receptors were identified. The receptor designated death receptor 5 (DR5) contained a cytoplasmic death domain and induced apoptosis much like DR4. The receptor designated decoy receptor 1 (DcR1) displayed properties of a glycophospholipid-anchored cell surface protein. DcR1 acted as a decoy receptor that inhibited TRAIL signaling. Thus, a cell surface mechanism exists for the regulation of cellular responsiveness to pro-apoptotic stimuli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sheridan, J P -- Marsters, S A -- Pitti, R M -- Gurney, A -- Skubatch, M -- Baldwin, D -- Ramakrishnan, L -- Gray, C L -- Baker, K -- Wood, W I -- Goddard, A D -- Godowski, P -- Ashkenazi, A -- New York, N.Y. -- Science. 1997 Aug 8;277(5327):818-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Oncology, Genentech, South San Francisco, CA 94080-4918, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9242611" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Apoptosis ; Apoptosis Regulatory Proteins ; Cell Membrane/metabolism ; Cells, Cultured ; GPI-Linked Proteins ; Glycosylphosphatidylinositols/metabolism ; HeLa Cells ; Humans ; Ligands ; Membrane Glycoproteins/*metabolism ; Molecular Sequence Data ; NF-kappa B/metabolism ; Receptors, TNF-Related Apoptosis-Inducing Ligand ; Receptors, Tumor Necrosis Factor/chemistry/genetics/*metabolism ; Signal Transduction ; TNF-Related Apoptosis-Inducing Ligand ; Transfection ; Tumor Cells, Cultured ; Tumor Necrosis Factor Decoy Receptors ; Tumor Necrosis Factor-alpha/*metabolism
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    Genetic feminization of pheromones and its behavioral consequences in Drosophila males (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-06-06
    Description: Pheromones are intraspecific chemical signals important for mate attraction and discrimination. In the fruit fly Drosophila melanogaster, hydrocarbons on the cuticular surface of the animal are sexually dimorphic in both their occurrence and their effects: Female-specific molecules stimulate male sexual excitation, whereas the predominant male-specific molecule tends to inhibit male excitation. Complete feminization of the pheromone mixture produced by males was induced by targeted expression of the transformer gene in adult oenocytes (subcuticular abdominal cells) or by ubiquitous expression during early imaginal life. The resulting flies generally exhibited male heterosexual orientation but elicited homosexual courtship from other males.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferveur, J F -- Savarit, F -- O'Kane, C J -- Sureau, G -- Greenspan, R J -- Jallon, J M -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1997 Jun 6;276(5318):1555-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mecanismes de communication, Unite de Recherche Associee-CNRS 1491, Batiment 446, Universite Paris-Sud, 91405, Orsay-Cedex, France. ferveur@ext.jussieu.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9171057" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Drosophila melanogaster ; Female ; Gene Expression Regulation, Developmental ; Homosexuality ; Male ; Nuclear Proteins/genetics/physiology ; Recombinant Fusion Proteins ; Sex Attractants/genetics/*physiology ; *Sex Characteristics ; Sex Differentiation ; *Sexual Behavior, Animal/physiology ; Transgenes
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    daf-2, an insulin receptor-like gene that regulates longevity and diapause in Caenorhabditis elegans (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-08-15
    Description: A C. elegans neurosecretory signaling system regulates whether animals enter the reproductive life cycle or arrest development at the long-lived dauer diapause stage. daf-2, a key gene in the genetic pathway that mediates this endocrine signaling, encodes an insulin receptor family member. Decreases in DAF-2 signaling induce metabolic and developmental changes, as in mammalian metabolic control by the insulin receptor. Decreased DAF-2 signaling also causes an increase in life-span. Life-span regulation by insulin-like metabolic control is analogous to mammalian longevity enhancement induced by caloric restriction, suggesting a general link between metabolism, diapause, and longevity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kimura, K D -- Tissenbaum, H A -- Liu, Y -- Ruvkun, G -- R01AG14161/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1997 Aug 15;277(5328):942-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9252323" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Amino Acid Sequence ; Animals ; Caenorhabditis elegans/chemistry/*genetics/growth & development/metabolism ; Caenorhabditis elegans Proteins ; Chromosome Mapping ; Conserved Sequence ; Energy Intake ; *Genes, Helminth ; Glucose/metabolism ; Humans ; Insulin/metabolism ; Larva/genetics/growth & development/metabolism ; Longevity/*genetics ; Molecular Sequence Data ; Mutation ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositol Phosphates/metabolism ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Receptor, IGF Type 1/chemistry/genetics ; Receptor, Insulin/chemistry/*genetics/metabolism ; Signal Transduction
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    Neighborhoods and violent crime: a multilevel study of collective efficacy (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-08-15
    Description: It is hypothesized that collective efficacy, defined as social cohesion among neighbors combined with their willingness to intervene on behalf of the common good, is linked to reduced violence. This hypothesis was tested on a 1995 survey of 8782 residents of 343 neighborhoods in Chicago, Illinois. Multilevel analyses showed that a measure of collective efficacy yields a high between-neighborhood reliability and is negatively associated with variations in violence, when individual-level characteristics, measurement error, and prior violence are controlled. Associations of concentrated disadvantage and residential instability with violence are largely mediated by collective efficacy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sampson, R J -- Raudenbush, S W -- Earls, F -- New York, N.Y. -- Science. 1997 Aug 15;277(5328):918-24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Sociology, University of Chicago, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9252316" target="_blank"〉PubMed〈/a〉
    Keywords: Chicago ; Female ; Humans ; Male ; Models, Statistical ; *Residence Characteristics ; Social Conditions ; *Social Control, Informal ; *Social Environment ; Social Values ; Socioeconomic Factors ; *Violence
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    Neural correlates of motor memory consolidation (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-08-08
    Description: Computational studies suggest that acquisition of a motor skill involves learning an internal model of the dynamics of the task, which enables the brain to predict and compensate for mechanical behavior. During the hours that follow completion of practice, representation of the internal model gradually changes, becoming less fragile with respect to behavioral interference. Here, functional imaging of the brain demonstrates that within 6 hours after completion of practice, while performance remains unchanged, the brain engages new regions to perform the task; there is a shift from prefrontal regions of the cortex to the premotor, posterior parietal, and cerebellar cortex structures. This shift is specific to recall of an established motor skill and suggests that with the passage of time, there is a change in the neural representation of the internal model and that this change may underlie its increased functional stability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shadmehr, R -- Holcomb, H H -- New York, N.Y. -- Science. 1997 Aug 8;277(5327):821-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biomedical Engineering, School of Medicine, Johns Hopkins University, 720 Rutland Avenue, 419 Traylor, Baltimore, MD 21205-2195, USA. reza@bme.jhu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9242612" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Brain Mapping ; Cerebellar Cortex/blood supply/*physiology/radionuclide imaging ; Humans ; Learning ; Male ; *Memory ; Motor Cortex/blood supply/*physiology/radionuclide imaging ; *Motor Skills ; Parietal Lobe/blood supply/*physiology/radionuclide imaging ; Prefrontal Cortex/blood supply/*physiology/radionuclide imaging ; Putamen/blood supply/physiology/radionuclide imaging ; Regional Blood Flow ; Time Factors ; Tomography, Emission-Computed
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    NMDA channel regulation by channel-associated protein tyrosine kinase Src (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-01-31
    Description: The N-methyl-D-aspartate (NMDA) receptor mediates synaptic transmission and plasticity in the central nervous system (CNS) and is regulated by tyrosine phosphorylation. In membrane patches excised from mammalian central neurons, the endogenous tyrosine kinase Src was shown to regulate the activity of NMDA channels. The action of Src required a sequence [Src(40-58)] within the noncatalytic, unique domain of Src. In addition, Src coprecipitated with NMDA receptor proteins. Finally, endogenous Src regulated the function of NMDA receptors at synapses. Thus, NMDA receptor regulation by Src may be important in development, plasticity, and pathology in the CNS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, X M -- Askalan, R -- Keil, G J 2nd -- Salter, M W -- New York, N.Y. -- Science. 1997 Jan 31;275(5300):674-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Hospital for Sick Children, Department of Physiology, University of Toronto, Toronto, Ontario, M5G 1X8 Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9005855" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cells, Cultured ; Ion Channel Gating ; Ion Channels/*metabolism ; Molecular Sequence Data ; N-Methylaspartate/metabolism ; Neurons/*metabolism ; Oligopeptides/pharmacology ; Patch-Clamp Techniques ; Phosphorylation ; Phosphotyrosine/metabolism ; Rats ; Rats, Wistar ; Receptors, N-Methyl-D-Aspartate/*metabolism ; Spinal Cord/cytology ; Synapses/*metabolism ; Synaptic Transmission ; src-Family Kinases/chemistry/*metabolism
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    Separate neural bases of two fundamental memory processes in the human medial temporal lobe (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-04-11
    Description: The participation of medial temporal-lobe structures in memory performance was examined by functional magnetic resonance imaging of local blood oxygenation level-dependent signals. Signals were measured during encoding into memory complex scenes or line drawings and during retrieval from memory of previously studied line drawings or words. Encoding tasks yielded increased signals for unfamiliar information in a posterior medial-temporal region that were focused in the parahippocampal cortex. Retrieval tasks yielded increased signals for successfully remembered information in an anterior medial-temporal region that were focused in the subiculum. These results indicate that separate components of the human medial temporal-lobe memory system are active during distinct memory processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabrieli, J D -- Brewer, J B -- Desmond, J E -- Glover, G H -- New York, N.Y. -- Science. 1997 Apr 11;276(5310):264-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychology and Neuroscience Program, Stanford University, Stanford, CA 94305, USA. gabrieli@psych.stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9092477" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Brain Mapping ; Female ; Hippocampus/physiology ; Humans ; Magnetic Resonance Imaging ; Male ; Memory/*physiology ; Mental Recall/*physiology ; Temporal Lobe/*physiology
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    Independent and additive effects of central POMC and leptin pathways on murine obesity (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-12-31
    Description: The lethal yellow (AY/a) mouse has a defect in proopiomelanocortin (POMC) signaling in the brain that leads to obesity, and is resistant to the anorexigenic effects of the hormone leptin. It has been proposed that the weight-reducing effects of leptin are thus transmitted primarily by way of POMC neurons. However, the central effects of defective POMC signaling, and the absence of leptin, on weight gain in double-mutant lethal yellow (AY/a) leptin-deficient (lepob/lepob) mice were shown to be independent and additive. Furthermore, deletion of the leptin gene restored leptin sensitivity to AY/a mice. This result implies that in the AY/a mouse, obesity is independent of leptin action, and resistance to leptin results from desensitization of leptin signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boston, B A -- Blaydon, K M -- Varnerin, J -- Cone, R D -- DK/AR517330/DK/NIDDK NIH HHS/ -- DK02404/DK/NIDDK NIH HHS/ -- HD33703/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 28;278(5343):1641-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Oregon Health Sciences University, Portland, OR 97201, USA. Laboratories, Rahway, NJ 07065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9374468" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenalectomy ; Agouti Signaling Protein ; Alleles ; Animals ; Arcuate Nucleus of Hypothalamus/*metabolism ; Blood Glucose/analysis ; Corticosterone/blood ; Crosses, Genetic ; Eating/drug effects ; Energy Metabolism ; Female ; Homeostasis ; Insulin/blood ; *Intercellular Signaling Peptides and Proteins ; Leptin ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Obese ; Neurons/metabolism ; Obesity/genetics/*metabolism ; Pro-Opiomelanocortin/*metabolism ; Proteins/genetics/*metabolism/pharmacology ; Signal Transduction ; Weight Gain
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    Environment and cancer: who are susceptible? (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-11-14
    Description: Acting in concert with individual susceptibility, environmental factors such as smoking, diet, and pollutants play a role in most human cancer. However, new molecular evidence indicates that specific groups-characterized by predisposing genetic traits or ethnicity, the very young, and women-may have heightened risk from certain exposures. This is illustrated by molecular epidemiologic studies of environmental carcinogens such as polycyclic aromatic hydrocarbons and aromatic amines. Individual genetic screening for rare high-risk traits or for more common, low-penetrant susceptibility genes is problematic and not routinely recommended. However, knowledge of the full spectrum of both genetic and acquired susceptibility in the population will be instrumental in developing health and regulatory policies that increase protection of the more susceptible groups from risks of environmental carcinogens. This will necessitate revision of current risk assessment methodologies to explicitly account for individual variation in susceptibility to environmental carcinogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perera, F P -- New York, N.Y. -- Science. 1997 Nov 7;278(5340):1068-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Environmental Health Sciences, Columbia University School of Public Health, 60 Haven Avenue, B-1, New York, NY 10032, USA. fpp1@columbia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9353182" target="_blank"〉PubMed〈/a〉
    Keywords: *Aging ; Amines/adverse effects ; Carcinogens, Environmental/*adverse effects ; Continental Population Groups ; Female ; *Genetic Predisposition to Disease ; Humans ; Male ; Neoplasms/chemically induced/ethnology/*etiology/genetics/prevention & control ; Nutritional Physiological Phenomena ; Polycyclic Hydrocarbons, Aromatic/adverse effects ; Risk Factors ; *Sex Characteristics
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    Murine model of Niemann-Pick C disease: mutation in a cholesterol homeostasis gene (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-11
    Description: An integrated human-mouse positional candidate approach was used to identify the gene responsible for the phenotypes observed in a mouse model of Niemann-Pick type C (NP-C) disease. The predicted murine NPC1 protein has sequence homology to the putative transmembrane domains of the Hedgehog signaling molecule Patched, to the cholesterol-sensing regions of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase and SREBP cleavage-activating protein (SCAP), and to the NPC1 orthologs identified in human, the nematode Caenorhabditis elegans, and the yeast Saccharomyces cerevisiae. The mouse model may provide an important resource for studying the role of NPC1 in cholesterol homeostasis and neurodegeneration and for assessing the efficacy of new drugs for NP-C disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Loftus, S K -- Morris, J A -- Carstea, E D -- Gu, J Z -- Cummings, C -- Brown, A -- Ellison, J -- Ohno, K -- Rosenfeld, M A -- Tagle, D A -- Pentchev, P G -- Pavan, W J -- New York, N.Y. -- Science. 1997 Jul 11;277(5323):232-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetic Disease Research, National Human Genome Research Institute, National Institutes of Health (NIH), Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9211850" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cholesterol/*metabolism ; *Disease Models, Animal ; Homeostasis ; Humans ; Hydroxymethylglutaryl CoA Reductases/chemistry ; Intracellular Signaling Peptides and Proteins ; Lysosomes/metabolism ; Membrane Proteins/chemistry ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mice, Mutant Strains ; Molecular Sequence Data ; Mutation ; Niemann-Pick Diseases/*genetics/metabolism ; Phenotype ; Protein Sorting Signals/chemistry ; Proteins/chemistry/*genetics/physiology ; Sequence Homology, Amino Acid
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    Identification of a chemokine receptor encoded by human cytomegalovirus as a cofactor for HIV-1 entry (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-20
    Description: The human cytomegalovirus encodes a beta-chemokine receptor (US28) that is distantly related to the human chemokine receptors CCR5 and CXCR4, which also serve as cofactors for the entry into cells of human immunodeficiency virus-type 1 (HIV-1). Like CCR5, US28 allowed infection of CD4-positive human cell lines by primary isolates of HIV-1 and HIV-2, as well as fusion of these cell lines with cells expressing the viral envelope proteins. In addition, US28 mediated infection by cell line-adapted HIV-1 for which CXCR4 was an entry cofactor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pleskoff, O -- Treboute, C -- Brelot, A -- Heveker, N -- Seman, M -- Alizon, M -- New York, N.Y. -- Science. 1997 Jun 20;276(5320):1874-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Inserm U.332, Institut Cochin de Genetique Moleculaire, 22 rue Mechain, 75014 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9188536" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS-Related Opportunistic Infections/virology ; Amino Acid Sequence ; Cell Fusion ; Chemokines ; Coculture Techniques ; Cytomegalovirus/*genetics/physiology ; Cytomegalovirus Infections/virology ; Giant Cells ; HIV Infections/virology ; HIV-1/*physiology ; HIV-2/*physiology ; HeLa Cells ; Humans ; Membrane Proteins/physiology ; Molecular Sequence Data ; Receptors, CCR2 ; Receptors, CCR5 ; Receptors, CXCR4 ; *Receptors, Chemokine ; Receptors, Cytokine/genetics/*physiology ; Receptors, HIV/genetics/*physiology ; Transfection ; Tumor Cells, Cultured ; Viral Proteins/genetics/*physiology
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    An aquaporin-like gene required for the Brassica self-incompatibility response (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-06
    Description: Self-incompatibility in Brassica refers to the rejection of self-related pollen and is mediated by a receptor protein kinase localized to the plasma membrane of the stigma epidermis in the flower. The recessive mutation mod eliminates self-incompatibility in the stigma. In mod mutants, self-compatibility was shown to be associated with the absence of transcripts encoded by an aquaporin-related gene. This observation suggests that a water channel is required for the self-incompatibility response of Brassica, which is consistent with the concept that regulation of water transfer from the stigma to pollen is a checkpoint in the early events of pollination in the crucifer family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ikeda, S -- Nasrallah, J B -- Dixit, R -- Preiss, S -- Nasrallah, M E -- New York, N.Y. -- Science. 1997 Jun 6;276(5318):1564-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Plant Biology, Division of Biological Sciences, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9171060" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Brassica/genetics/*physiology ; *Genes, Plant ; Ion Channels/genetics/*physiology ; Molecular Sequence Data ; Plant Proteins/genetics/*physiology ; Pollen ; Reproduction ; Water/physiology
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    PTG, a protein phosphatase 1-binding protein with a role in glycogen metabolism (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-07
    Description: Protein dephosphorylation by phosphatase PP1 plays a central role in mediating the effects of insulin on glucose and lipid metabolism. A PP1C-targeting protein expressed in 3T3-L1 adipocytes (called PTG, for protein targeting to glycogen) was cloned and characterized. PTG was expressed predominantly in insulin-sensitive tissues. In addition to binding and localizing PP1C to glycogen, PTG formed complexes with phosphorylase kinase, phosphorylase a, and glycogen synthase, the primary enzymes involved in the hormonal regulation of glycogen metabolism. Overexpression of PTG markedly increased basal and insulin-stimulated glycogen synthesis in Chinese hamster ovary cells overexpressing the insulin receptor, which do not express endogenous PTG. These results suggest that PTG is critical for glycogen metabolism, possibly functioning as a molecular scaffold.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Printen, J A -- Brady, M J -- Saltiel, A R -- New York, N.Y. -- Science. 1997 Mar 7;275(5305):1475-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Michigan School of Medicine, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9045612" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; CHO Cells ; Carrier Proteins/chemistry/genetics/*metabolism ; Cloning, Molecular ; Cricetinae ; DNA, Complementary/genetics ; Glycogen/biosynthesis/*metabolism ; Glycogen Synthase/metabolism ; Insulin/pharmacology ; *Intracellular Signaling Peptides and Proteins ; Mice ; Molecular Sequence Data ; Phosphoprotein Phosphatases/*metabolism ; Phosphorylase Kinase/metabolism ; Phosphorylase a/metabolism ; Phosphorylation ; Protein Binding ; Protein Phosphatase 1 ; Recombinant Fusion Proteins/metabolism ; Substrate Specificity ; Transfection
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    A mammalian telomerase-associated protein (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-02-14
    Description: The telomerase ribonucleoprotein catalyzes the addition of new telomeres onto chromosome ends. A gene encoding a mammalian telomerase homolog called TP1 (telomerase-associated protein 1) was identified and cloned. TP1 exhibited extensive amino acid similarity to the Tetrahymena telomerase protein p80 and was shown to interact specifically with mammalian telomerase RNA. Antiserum to TP1 immunoprecipitated telomerase activity from cell extracts, suggesting that TP1 is associated with telomerase in vivo. The identification of TP1 suggests that telomerase-associated proteins are conserved from ciliates to humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harrington, L -- McPhail, T -- Mar, V -- Zhou, W -- Oulton, R -- Bass, M B -- Arruda, I -- Robinson, M O -- New York, N.Y. -- Science. 1997 Feb 14;275(5302):973-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Arruda, Ontario Cancer Institute-Amgen Institute, Department of Medical Biophysics, University of Toronto, 620 University Avenue, Toronto, Ontario M5G 2C1, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9020079" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blotting, Northern ; Carrier Proteins/*chemistry/genetics/immunology/*metabolism ; Cell Line ; Cloning, Molecular ; DNA, Complementary/genetics ; Humans ; Mice ; Molecular Sequence Data ; Precipitin Tests ; RNA/*metabolism ; RNA, Messenger/genetics/metabolism ; Sequence Homology, Amino Acid ; Telomerase/*chemistry/genetics/metabolism ; Tetrahymena/chemistry/genetics ; Transfection ; Tumor Cells, Cultured
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    NF-AT activation induced by a CAML-interacting member of the tumor necrosis factor receptor superfamily (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-06
    Description: Activation of the nuclear factor of activated T cells transcription factor (NF-AT) is a key event underlying lymphocyte action. The CAML (calcium-modulator and cyclophilin ligand) protein is a coinducer of NF-AT activation when overexpressed in Jurkat T cells. A member of the tumor necrosis factor receptor superfamily was isolated by virtue of its affinity for CAML. Cross-linking of this lymphocyte-specific protein, designated TACI (transmembrane activator and CAML-interactor), on the surface of transfected Jurkat cells with TACI-specific antibodies led to activation of the transcription factors NF-AT, AP-1, and NFkappaB. TACI-induced activation of NF-AT was specifically blocked by a dominant-negative CAML mutant, thus implicating CAML as a signaling intermediate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉von Bulow, G U -- Bram, R J -- CA21765/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 3;278(5335):138-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Experimental Oncology, St. Jude Children's Research Hospital, 332 North Lauderdale, Memphis, TN 38105, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9311921" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Calcineurin ; Calmodulin-Binding Proteins/metabolism ; Carrier Proteins/genetics/*metabolism ; Cell Line ; Cell Membrane/metabolism ; DNA-Binding Proteins/*metabolism ; Humans ; Jurkat Cells ; Lymphocyte Activation ; *Membrane Proteins ; Molecular Sequence Data ; Mutation ; NF-kappa B/metabolism ; NFATC Transcription Factors ; *Nuclear Proteins ; Phosphoprotein Phosphatases/metabolism ; Receptors, Tumor Necrosis Factor/chemistry/genetics/*metabolism ; Sequence Alignment ; Signal Transduction ; T-Lymphocytes/immunology/*metabolism ; Transcription Factor AP-1/metabolism ; Transcription Factors/*metabolism ; Transcription, Genetic ; Transfection ; Transmembrane Activator and CAML Interactor Protein
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    CD4-independent binding of SIV gp120 to rhesus CCR5 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: CCR5 and CD4 are coreceptors for immunodeficiency virus entry into target cells. The gp120 envelope glycoprotein from human immunodeficiency virus strain HIV-1(YU2) bound human CCR5 (CCR5hu) or rhesus macaque CCR5 (CCR5rh) only in the presence of CD4. The gp120 from simian immunodeficiency virus strain SIVmac239 bound CCR5rh without CD4, but CCR5hu remained CD4-dependent. The CD4-independent binding of SIVmac239 gp120 depended on a single amino acid, Asp13, in the CCR5rh amino-terminus. Thus, CCR5-binding moieties on the immunodeficiency virus envelope glycoprotein can be generated by interaction with CD4 or by direct interaction with the CCR5 amino-terminus. These results may have implications for the evolution of receptor use among lentiviruses as well as utility in the development of effective intervention.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martin, K A -- Wyatt, R -- Farzan, M -- Choe, H -- Marcon, L -- Desjardins, E -- Robinson, J -- Sodroski, J -- Gerard, C -- Gerard, N P -- AI41581/AI/NIAID NIH HHS/ -- HL36162/HL/NHLBI NIH HHS/ -- HL51366/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 Nov 21;278(5342):1470-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Perlmutter Laboratory, Children's Hospital, Department of Medicine, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9367961" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Antigens, CD4/*physiology ; Cell Line ; HIV Antibodies/immunology ; HIV Envelope Protein gp120/chemistry/*metabolism ; HIV-2/immunology ; Humans ; Macaca mulatta ; Macrophages/virology ; *Membrane Glycoproteins ; Mutation ; Receptors, CCR5/chemistry/*metabolism ; Simian Immunodeficiency Virus/*metabolism ; Transfection ; *Viral Envelope Proteins
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    Attentional activation of the cerebellum independent of motor involvement (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-03-28
    Description: The cerebellum traditionally has been viewed as a neural device dedicated to motor control. Although recent evidence shows that it is involved in nonmotor operations as well, an important question is whether this involvement is independent of motor control and motor guidance. Functional magnetic resonance imaging was used to demonstrate that attention and motor performance independently activate distinct cerebellar regions. These findings support a broader concept of cerebellar function, in which the cerebellum is involved in diverse cognitive and noncognitive neurobehavioral systems, including the attention and motor systems, in order to anticipate imminent information acquisition, analysis, or action.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allen, G -- Buxton, R B -- Wong, E C -- Courchesne, E -- R01-MH36840/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1997 Mar 28;275(5308):1940-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉San Diego State University-University of California, San Diego Joint Doctoral Program in Clinical Psychology, San Diego, CA 92120, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9072973" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; *Attention ; Brain Mapping ; Cerebellar Cortex/physiology ; Cerebellum/*physiology ; *Cognition ; Female ; Humans ; Magnetic Resonance Imaging ; Male ; *Motor Activity ; *Psychomotor Performance
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    Regulation of protein phosphatase 2A by direct interaction with casein kinase 2alpha (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-09
    Description: Timely deactivation of kinase cascades is crucial to the normal control of cell signaling and is partly accomplished by protein phosphatase 2A (PP2A). The catalytic (alpha) subunit of the serine-threonine kinase casein kinase 2 (CK2) bound to PP2A in vitro and in mitogen-starved cells; binding required the integrity of a sequence motif common to CK2alpha and SV40 small t antigen. Overexpression of CK2alpha resulted in deactivation of mitogen-activated protein kinase kinase (MEK) and suppression of cell growth. Moreover, CK2alpha inhibited the transforming activity of oncogenic Ras, but not that of constitutively activated MEK. Thus, CK2alpha may regulate the deactivation of the mitogen-activated protein kinase pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heriche, J K -- Lebrin, F -- Rabilloud, T -- Leroy, D -- Chambaz, E M -- Goldberg, Y -- New York, N.Y. -- Science. 1997 May 9;276(5314):952-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Commissariat a l'Energie Atomique, Departement de Biologie Moleculaire et Structurale, Laboratoire de Biochimie des Regulations Cellulaires Endocrines, Unite 244, F-38054 Grenoble Cedex 9, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9139659" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; Antigens, Polyomavirus Transforming ; Binding Sites ; Casein Kinase II ; Cell Division ; Cell Transformation, Neoplastic ; MAP Kinase Kinase 1 ; Mice ; *Mitogen-Activated Protein Kinase Kinases ; Mutation ; Okadaic Acid/pharmacology ; Phosphoprotein Phosphatases/*metabolism ; Phosphorylation ; Platelet-Derived Growth Factor/pharmacology ; Protein Phosphatase 2 ; Protein-Serine-Threonine Kinases/*metabolism/pharmacology ; Protein-Tyrosine Kinases/metabolism/pharmacology ; Recombinant Fusion Proteins/metabolism ; Transfection ; ras Proteins/pharmacology
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    The flu pandemic that might have been (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-10-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 1997 Sep 12;277(5332):1600-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9312852" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chickens/virology ; Child, Preschool ; China/epidemiology ; Disease Outbreaks ; Hong Kong/epidemiology ; Humans ; *Influenza A virus/isolation & purification ; Influenza in Birds/virology ; Influenza, Human/epidemiology/*transmission/*virology ; Male
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    Nonsyndromic deafness DFNA1 associated with mutation of a human homolog of the Drosophila gene diaphanous (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-21
    Description: The gene responsible for autosomal dominant, fully penetrant, nonsyndromic sensorineural progressive hearing loss in a large Costa Rican kindred was previously localized to chromosome 5q31 and named DFNA1. Deafness in the family is associated with a protein-truncating mutation in a human homolog of the Drosophila gene diaphanous. The truncation is caused by a single nucleotide substitution in a splice donor, leading to a four-base pair insertion in messenger RNA and a frameshift. The diaphanous protein is a profilin ligand and target of Rho that regulates polymerization of actin, the major component of the cytoskeleton of hair cells of the inner ear.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lynch, E D -- Lee, M K -- Morrow, J E -- Welcsh, P L -- Leon, P E -- King, M C -- R01-DC01076/DC/NIDCD NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 14;278(5341):1315-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Washington, Seattle, WA 98195, USA. eric@lynch.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9360932" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/chemistry/*genetics/physiology ; Chromosome Mapping ; Chromosomes, Human, Pair 5 ; Cochlea/metabolism ; *Contractile Proteins ; Deafness/*genetics/metabolism/pathology ; Drosophila/genetics ; *Drosophila Proteins ; Female ; Frameshift Mutation ; GTP-Binding Proteins/metabolism ; Gene Expression ; Hair Cells, Auditory/*metabolism/ultrastructure ; Humans ; Male ; Microfilament Proteins/metabolism ; Molecular Sequence Data ; Pedigree ; Profilins ; RNA Splicing ; RNA, Messenger/genetics/metabolism ; X Chromosome
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    Epidermal cell differentiation in Arabidopsis determined by a Myb homolog, CPC (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-22
    Description: The roots of plants normally carry small hairs arranged in a regular pattern. Transfer DNA-tagged lines of Arabidopsis thaliana included a mutant with few, randomly distributed root hairs. The mutated gene CAPRICE (CPC) encoded a protein with a Myb-like DNA binding domain typical of transcription factors involved in animal and plant development. Analysis in combination with other root hair mutations showed that CPC may work together with the TTG gene and upstream of the GL2 gene. Transgenic plants overexpressing CPC had more root hairs and fewer trichomes than normal. Thus, the CPC gene determines the fate of epidermal cell differentiation in Arabidopsis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wada, T -- Tachibana, T -- Shimura, Y -- Okada, K -- New York, N.Y. -- Science. 1997 Aug 22;277(5329):1113-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division I of Gene Expression and Regulation, National Institute for Basic Biology, Okazaki, 444, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9262483" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/*cytology/*genetics ; *Arabidopsis Proteins ; Cell Differentiation ; Crosses, Genetic ; DNA-Binding Proteins/chemistry/*genetics/physiology ; Genes, Plant ; Homeodomain Proteins/genetics ; Molecular Sequence Data ; Mutation ; Oncogenes ; Phenotype ; Plant Proteins/genetics ; Plant Roots/*cytology/genetics ; Plants, Genetically Modified ; Proto-Oncogene Proteins/chemistry/genetics ; Proto-Oncogene Proteins c-myb ; Trans-Activators/chemistry/genetics ; Transcription Factors/chemistry/*genetics/physiology
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    Mutation of the Stargardt disease gene (ABCR) in age-related macular degeneration (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-09-20
    Description: Age-related macular degeneration (AMD) is the leading cause of severe central visual impairment among the elderly and is associated both with environmental factors such as smoking and with genetic factors. Here, 167 unrelated AMD patients were screened for alterations in ABCR, a gene that encodes a retinal rod photoreceptor protein and is defective in Stargardt disease, a common hereditary form of macular dystrophy. Thirteen different AMD-associated alterations, both deletions and amino acid substitutions, were found in one allele of ABCR in 26 patients (16%). Identification of ABCR alterations will permit presymptomatic testing of high-risk individuals and may lead to earlier diagnosis of AMD and to new strategies for prevention and therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allikmets, R -- Shroyer, N F -- Singh, N -- Seddon, J M -- Lewis, R A -- Bernstein, P S -- Peiffer, A -- Zabriskie, N A -- Li, Y -- Hutchinson, A -- Dean, M -- Lupski, J R -- Leppert, M -- New York, N.Y. -- Science. 1997 Sep 19;277(5333):1805-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Intramural Research Support Program, SAIC-Frederick, NCI-Frederick Cancer Research and Development Center, Frederick, MD 21702, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9295268" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*genetics/metabolism ; Adult ; Aged ; Aged, 80 and over ; Female ; Frameshift Mutation ; Heterozygote ; Humans ; Macula Lutea/pathology ; Macular Degeneration/*genetics/metabolism/pathology ; Male ; Middle Aged ; *Mutation ; Pedigree ; Pigment Epithelium of Eye/pathology ; Retinal Drusen/pathology ; Sequence Deletion
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    Hyaluronan synthase of chlorella virus PBCV-1 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: Sequence analysis of the 330-kilobase genome of the virus PBCV-1 that infects a chlorella-like green algae revealed an open reading frame, A98R, with similarity to several hyaluronan synthases. Hyaluronan is an essential polysaccharide found in higher animals as well as in a few pathogenic bacteria. Expression of the A98R gene product in Escherichia coli indicated that the recombinant protein is an authentic hyaluronan synthase. A98R is expressed early in PBCV-1 infection and hyaluronan is produced in infected algae. These results demonstrate that a virus can encode an enzyme capable of synthesizing a carbohydrate polymer and that hyaluronan exists outside of animals and their pathogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeAngelis, P L -- Jing, W -- Graves, M V -- Burbank, D E -- Van Etten, J L -- R01-GM32441/GM/NIGMS NIH HHS/ -- R01-GM56497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Dec 5;278(5344):1800-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, 940 Stanton L. Young Boulevard, Oklahoma City, OK 73104, USA. paul-deangelis@OUHSC.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9388183" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chlorella/*virology ; Genes, Viral ; Glucuronosyltransferase/chemistry/*genetics/*metabolism ; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)/genetics/metabolism ; *Glycosyltransferases ; Hyaluronic Acid/*biosynthesis ; *Membrane Proteins ; Molecular Sequence Data ; Phycodnaviridae/chemistry/*enzymology/genetics/physiology ; Recombinant Proteins/metabolism ; Sequence Alignment ; Substrate Specificity ; *Transferases ; Uridine Diphosphate Glucose Dehydrogenase/genetics/metabolism ; *Xenopus Proteins
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    Microtubule architecture specified by a beta-tubulin isoform (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-03
    Description: In Drosophila melanogaster, a testis-specific beta-tubulin (beta2) is required for spermatogenesis. A sequence motif was identified in carboxyl termini of axonemal beta-tubulins in diverse taxa. As a test of whether orthologous beta-tubulins from different species are functionally equivalent, the moth Heliothis virescens beta2 homolog was expressed in Drosophila testes. When coexpressed with beta2, the moth isoform imposed the 16-protofilament structure characteristic of that found in the moth on the corresponding subset of Drosophila microtubules, which normally contain only 13-protofilament microtubules. Thus, the architecture of the microtubule cytoskeleton can be directed by a component beta-tubulin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raff, E C -- Fackenthal, J D -- Hutchens, J A -- Hoyle, H D -- Turner, F R -- New York, N.Y. -- Science. 1997 Jan 3;275(5296):70-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Indiana Molecular Biology Institute, Indiana University, Bloomington, IN 47405, USA. eraff@bio.indiana.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8974394" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Drosophila melanogaster/genetics ; Humans ; Male ; Microtubules/chemistry/*ultrastructure ; Molecular Sequence Data ; Moths/genetics ; Spermatids/chemistry/physiology/*ultrastructure ; Spermatogenesis ; Tubulin/chemistry/genetics/*physiology
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  • 81
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    Modulating irrelevant motion perception by varying attentional load in an unrelated task (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: Lavie's theory of attention proposes that the processing load in a relevant task determines the extent to which irrelevant distractors are processed. This theory was tested by asking participants in a study to perform linguistic tasks of low or high load while ignoring irrelevant visual motion in the periphery of the display. Although task and distractor were unrelated, both functional imaging of motion-related activity in cortical area V5 and psychophysical measures of the motion aftereffect showed reduced motion processing during high load in the linguistic task. These findings fulfill the prediction that perception of irrelevant distractors depends on the relevant processing load.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rees, G -- Frith, C D -- Lavie, N -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1997 Nov 28;278(5343):1616-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Department of Cognitive Neurology, Institute of Neurology, 12 Queen Square, London WC1N 3BG, UK. g.rees@fil.ion.ucl.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9374459" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Attention/*physiology ; Cerebral Cortex/*physiology ; Female ; Humans ; Magnetic Resonance Imaging ; Male ; *Motion Perception ; Psychomotor Performance ; Superior Colliculi/physiology
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    Evolutionary psychologists look for roots of cognition (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-01-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, N -- New York, N.Y. -- Science. 1997 Jan 3;275(5296):29-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8999531" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Behavior, Animal ; *Biological Evolution ; Birds ; *Cognition ; Female ; Humans ; Macaca mulatta/psychology ; Male ; Memory ; Reward ; *Social Sciences
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  • 83
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    Folding-unfolding transitions in single titin molecules characterized with laser tweezers (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-16
    Description: Titin, a giant filamentous polypeptide, is believed to play a fundamental role in maintaining sarcomeric structural integrity and developing what is known as passive force in muscle. Measurements of the force required to stretch a single molecule revealed that titin behaves as a highly nonlinear entropic spring. The molecule unfolds in a high-force transition beginning at 20 to 30 piconewtons and refolds in a low-force transition at approximately 2.5 piconewtons. A fraction of the molecule (5 to 40 percent) remains permanently unfolded, behaving as a wormlike chain with a persistence length (a measure of the chain's bending rigidity) of 20 angstroms. Force hysteresis arises from a difference between the unfolding and refolding kinetics of the molecule relative to the stretch and release rates in the experiments, respectively. Scaling the molecular data up to sarcomeric dimensions reproduced many features of the passive force versus extension curve of muscle fibers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kellermayer, M S -- Smith, S B -- Granzier, H L -- Bustamante, C -- AR-42652/AR/NIAMS NIH HHS/ -- GM-32543/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 May 16;276(5315):1112-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Veterinary Comparative Anatomy, Pharmacology, and Physiology, Washington State University, Pullman, WA 99164-6520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9148805" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Connectin ; Elasticity ; Entropy ; Immunoglobulins/chemistry ; Lasers ; Models, Chemical ; Muscle Contraction ; Muscle Proteins/*chemistry ; Muscle Relaxation ; Muscle, Skeletal/chemistry/physiology ; Protein Denaturation ; *Protein Folding ; Protein Kinases/*chemistry ; Stress, Mechanical
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  • 84
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    Positive selection of T cells induced by viral delivery of neopeptides to the thymus (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-31
    Description: The relation between an antigenic peptide that can stimulate a mature T cell and the natural peptide that promoted selection of this cell in the thymus is still unknown. An experimental system was devised to address this issue in vivo-mice expressing neopeptides in thymic stromal cells after adenovirus-mediated delivery of invariant chain-peptide fusion proteins. In this system, selection of T cells capable of responding to a given antigenic peptide could be promoted by the peptide itself, by closely related analogs lacking agonist and antagonist activity, or by ostensibly unrelated peptides. However, the precise repertoire of T cells selected was dictated by the particular neopeptide expressed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakano, N -- Rooke, R -- Benoist, C -- Mathis, D -- New York, N.Y. -- Science. 1997 Jan 31;275(5300):678-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Genetique et de Biologie Moleculaire et Cellulaire (INSERM, CNRS, Universite Louis Pasteur), 1 rue Laurent Fries, 67404 Illkirch, C.U. de Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9005856" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/genetics ; Amino Acid Sequence ; Animals ; Antigen-Presenting Cells/immunology ; Antigens, Differentiation, B-Lymphocyte/genetics ; Cells, Cultured ; Cloning, Molecular ; Cross Reactions ; Cytochrome c Group/immunology ; DNA, Complementary/genetics ; Genetic Vectors ; Histocompatibility Antigens Class II/genetics ; Hybridomas ; Interleukin-2/biosynthesis ; *Lymphocyte Activation ; Mice ; Molecular Sequence Data ; Peptides/chemistry/*immunology ; Receptors, Antigen, T-Cell/*immunology ; Recombinant Fusion Proteins ; T-Lymphocytes/*immunology ; Thymus Gland/cytology/*immunology
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  • 85
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    Getting the brain's attention (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickelgren, I -- New York, N.Y. -- Science. 1997 Oct 3;278(5335):35-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9340756" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Attention/*physiology ; Brain/*physiology ; Dopamine/*physiology ; Emotions/*physiology ; Female ; Humans ; Learning/*physiology ; Male ; Memory/physiology ; Neurons/physiology ; Nucleus Accumbens/physiology ; Prefrontal Cortex/physiology ; *Reward ; Ventral Tegmental Area/physiology
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  • 86
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    Nuclear export of NF-ATc enhanced by glycogen synthase kinase-3 (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-03-28
    Description: The transcription factor NF-AT responds to Ca2+-calcineurin signals by translocating to the nucleus, where it participates in the activation of early immune response genes. Calcineurin dephosphorylates conserved serine residues in the amino terminus of NF-AT, resulting in nuclear import. Purification of the NF-AT kinase revealed that it is composed of a priming kinase activity and glycogen synthase kinase-3 (GSK-3). GSK-3 phosphorylates conserved serines necessary for nuclear export, promotes nuclear exit, and thereby opposes Ca2+-calcineurin signaling. Because GSK-3 responds to signals initiated by Wnt and other ligands, NF-AT family members could be effectors of these pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beals, C R -- Sheridan, C M -- Turck, C W -- Gardner, P -- Crabtree, G R -- New York, N.Y. -- Science. 1997 Mar 28;275(5308):1930-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Developmental Biology, Stanford University, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9072970" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Transport ; Brain/enzymology ; COS Cells ; Calcineurin ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Calmodulin-Binding Proteins/metabolism ; Cell Nucleus/*metabolism ; Cloning, Molecular ; Cyclic AMP-Dependent Protein Kinases/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Glycogen Synthase Kinase 3 ; Glycogen Synthase Kinases ; Humans ; Molecular Sequence Data ; NFATC Transcription Factors ; *Nuclear Proteins ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Rats ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transcription Factors/genetics/*metabolism ; Transfection
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  • 87
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    Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-12
    Description: An essential step in retrovirus infection is the binding of the virus to its receptor on a target cell. The structure of the receptor-binding domain of the envelope glycoprotein from Friend murine leukemia virus was determined to 2.0 angstrom resolution by x-ray crystallography. The core of the domain is an antiparallel beta sandwich, with two interstrand loops forming a helical subdomain atop the sandwich. The residues in the helical region, but not in the beta sandwich, are highly variable among mammalian C-type retroviruses with distinct tropisms, indicating that the helical subdomain determines the receptor specificity of the virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fass, D -- Davey, R A -- Hamson, C A -- Kim, P S -- Cunningham, J M -- Berger, J M -- New York, N.Y. -- Science. 1997 Sep 12;277(5332):1662-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9287219" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Carrier Proteins/metabolism ; Crystallography, X-Ray ; Friend murine leukemia virus/*chemistry ; Glycoproteins/*chemistry ; *Membrane Glycoproteins ; Membrane Proteins/metabolism ; Models, Molecular ; Molecular Sequence Data ; *Protein Conformation ; Protein Folding ; *Protein Structure, Secondary ; Receptors, Virus/metabolism ; Viral Envelope Proteins/*chemistry/metabolism
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  • 88
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    Deciding advantageously before knowing the advantageous strategy (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-02-28
    Description: Deciding advantageously in a complex situation is thought to require overt reasoning on declarative knowledge, namely, on facts pertaining to premises, options for action, and outcomes of actions that embody the pertinent previous experience. An alternative possibility was investigated: that overt reasoning is preceded by a nonconscious biasing step that uses neural systems other than those that support declarative knowledge. Normal participants and patients with prefrontal damage and decision-making defects performed a gambling task in which behavioral, psychophysiological, and self-account measures were obtained in parallel. Normals began to choose advantageously before they realized which strategy worked best, whereas prefrontal patients continued to choose disadvantageously even after they knew the correct strategy. Moreover, normals began to generate anticipatory skin conductance responses (SCRs) whenever they pondered a choice that turned out to be risky, before they knew explicitly that it was a risky choice, whereas patients never developed anticipatory SCRs, although some eventually realized which choices were risky. The results suggest that, in normal individuals, nonconscious biases guide behavior before conscious knowledge does. Without the help of such biases, overt knowledge may be insufficient to ensure advantageous behavior.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bechara, A -- Damasio, H -- Tranel, D -- Damasio, A R -- P01 NS19632/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1997 Feb 28;275(5304):1293-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Division of Behavioral Neurology and Cognitive Neuroscience, University of Iowa College of Medicine, Iowa City, IA 52242, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9036851" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Brain Damage, Chronic/physiopathology/psychology ; *Decision Making ; Female ; Galvanic Skin Response ; Gambling/psychology ; Humans ; *Intuition ; Male ; Middle Aged ; Prefrontal Cortex/*physiology/physiopathology ; *Unconscious (Psychology)
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  • 89
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    A cyanobacterial phytochrome two-component light sensory system (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-09-05
    Description: The biliprotein phytochrome regulates plant growth and developmental responses to the ambient light environment through an unknown mechanism. Biochemical analyses demonstrate that phytochrome is an ancient molecule that evolved from a more compact light sensor in cyanobacteria. The cyanobacterial phytochrome Cph1 is a light-regulated histidine kinase that mediates red, far-red reversible phosphorylation of a small response regulator, Rcp1 (response regulator for cyanobacterial phytochrome), encoded by the adjacent gene, thus implicating protein phosphorylation-dephosphorylation in the initial step of light signal transduction by phytochrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yeh, K C -- Wu, S H -- Murphy, J T -- Lagarias, J C -- 1 P41 RR06009/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 5;277(5331):1505-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Molecular and Cellular Biology, University of California, Davis, CA 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9278513" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Bacterial Proteins ; Cloning, Molecular ; Cyanobacteria/chemistry/genetics/*metabolism ; Genes, Bacterial ; *Light ; Molecular Sequence Data ; Operon ; Phosphorylation ; Protein Kinases/chemistry/genetics/*metabolism ; Proteins ; Recombinant Fusion Proteins/chemistry/metabolism ; Sequence Deletion ; Signal Transduction
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  • 90
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    Morphologists learn to live with molecular upstarts (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-05-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, M -- New York, N.Y. -- Science. 1997 May 16;276(5315):1032-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9173539" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amphibians/*classification/genetics ; Animals ; Base Sequence ; Biological Evolution ; DNA, Mitochondrial/genetics ; Humans ; Mammals/*classification/genetics ; *Phylogeny
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  • 91
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    Synaptic vesicle endocytosis impaired by disruption of dynamin-SH3 domain interactions (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-04-11
    Description: The proline-rich COOH-terminal region of dynamin binds various Src homology 3 (SH3) domain-containing proteins, but the physiological role of these interactions is unknown. In living nerve terminals, the function of the interaction with SH3 domains was examined. Amphiphysin contains an SH3 domain and is a major dynamin binding partner at the synapse. Microinjection of amphiphysin's SH3 domain or of a dynamin peptide containing the SH3 binding site inhibited synaptic vesicle endocytosis at the stage of invaginated clathrin-coated pits, which resulted in an activity-dependent distortion of the synaptic architecture and a depression of transmitter release. These findings demonstrate that SH3-mediated interactions are required for dynamin function and support an essential role of clathrin-mediated endocytosis in synaptic vesicle recycling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shupliakov, O -- Low, P -- Grabs, D -- Gad, H -- Chen, H -- David, C -- Takei, K -- De Camilli, P -- Brodin, L -- CA46128/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Apr 11;276(5310):259-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Nobel Institute for Neurophysiology, Department of Neuroscience, Karolinska Institutet, S-171 77 Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9092476" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Cell Membrane/ultrastructure ; Coated Pits, Cell-Membrane/ultrastructure ; Dynamins ; *Endocytosis ; GTP Phosphohydrolases/*metabolism ; Humans ; Lampreys ; Microscopy, Electron ; Molecular Sequence Data ; Nerve Tissue Proteins/chemistry/*metabolism ; Proline/chemistry ; Recombinant Fusion Proteins/metabolism ; Synapses/metabolism/ultrastructure ; Synaptic Transmission ; Synaptic Vesicles/*metabolism/ultrastructure ; *src Homology Domains
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  • 92
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    Evidence for a family of archaeal ATPases (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koonin, E V -- New York, N.Y. -- Science. 1997 Mar 7;275(5305):1489-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9045616" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/*chemistry/metabolism ; Amino Acid Sequence ; Archaea/*enzymology ; Bacterial Proteins/*chemistry/metabolism ; Conserved Sequence ; Databases, Factual ; Methanococcus/*enzymology ; Molecular Sequence Data ; Sequence Alignment
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 93
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    Macrophages as a source of HIV during opportunistic infections (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-20
    Description: The source of increasing viremia that characterizes the latter stages of human immunodeficiency virus (HIV) disease has remained a paradox because it occurs at a time when lymphoid tissue is quantitatively and qualitatively impaired, and the patients' CD4 T lymphocytes are steadily declining. Here, macrophages, both infected and uninfected with common opportunistic pathogens of HIV disease such as Mycobacterium avium complex and Pneumocystis carinii, were identified as highly productive sources of HIV in coinfected lymph nodes. These observations indicate that tissue macrophages are not only infected with HIV, but that common pathogens of HIV disease can dramatically increase their production of virus. Thus, prevention or successful treatment of opportunistic coinfections, or both, potentially benefits the patient twofold by limiting the pathology caused by opportunistic infection and by controlling induction of HIV replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Orenstein, J M -- Fox, C -- Wahl, S M -- DE12585/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 20;276(5320):1857-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, George Washington University, Washington, DC 20037, USA. jmo@gwis2.circ.gwu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9188531" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS-Related Opportunistic Infections/*virology ; Adult ; Dendritic Cells/virology ; HIV Infections/*virology ; HIV-1/isolation & purification/*physiology ; Humans ; In Situ Hybridization ; Lymph Nodes/virology ; Macrophages/*virology ; Male ; Microscopy, Electron ; Mycobacterium avium-intracellulare Infection/virology ; Pneumonia, Pneumocystis/virology ; RNA, Viral/analysis ; Virus Replication
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 94
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    Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-05
    Description: The carboxyl-terminal domain, residues 146 to 231, of the human immunodeficiency virus-1 (HIV-1) capsid protein [CA(146-231)] is required for capsid dimerization and viral assembly. This domain contains a stretch of 20 residues, called the major homology region (MHR), which is conserved across retroviruses and is essential for viral assembly, maturation, and infectivity. The crystal structures of CA(146-231) and CA(151-231) reveal that the globular domain is composed of four helices and an extended amino-terminal strand. CA(146-231) dimerizes through parallel packing of helix 2 across a dyad. The MHR is distinct from the dimer interface and instead forms an intricate hydrogen-bonding network that interconnects strand 1 and helices 1 and 2. Alignment of the CA(146-231) dimer with the crystal structure of the capsid amino-terminal domain provides a model for the intact protein and extends models for assembly of the central conical core of HIV-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gamble, T R -- Yoo, S -- Vajdos, F F -- von Schwedler, U K -- Worthylake, D K -- Wang, H -- McCutcheon, J P -- Sundquist, W I -- Hill, C P -- R01 AI40333/AI/NIAID NIH HHS/ -- R01 AI43036/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 31;278(5339):849-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Utah, Salt Lake City, UT 84132, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9346481" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Capsid/*chemistry/genetics ; Cell Line ; Cloning, Molecular ; Cloning, Organism ; Crystallography, X-Ray ; Dimerization ; HIV-1/*chemistry/genetics/physiology ; Humans ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Peptidylprolyl Isomerase/chemistry ; *Protein Conformation ; Virus Replication
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 95
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    The inverse association between tuberculin responses and atopic disorder (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-03
    Description: Human immune responses are heterogeneous and may involve antagonism between T helper (TH) lymphocyte subsets and their cytokines. Atopy is characterized by immediate immunoglobulin E (IgE)-mediated hypersensitivity to agents such as dust mites and pollen, and it underlies the increasingly prevalent disorder asthma. Among Japanese schoolchildren, there was a strong inverse association between delayed hypersensitivity to Mycobacterium tuberculosis and atopy. Positive tuberculin responses predicted a lower incidence of asthma, lower serum IgE levels, and cytokine profiles biased toward TH1 type. Exposure and response to M. tuberculosis may, by modification of immune profiles, inhibit atopic disorder.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shirakawa, T -- Enomoto, T -- Shimazu, S -- Hopkin, J M -- New York, N.Y. -- Science. 1997 Jan 3;275(5296):77-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lung Research Laboratory, Osler Chest Unit, Churchill Hospital, Oxford OX3 7LJ, UK. jhopkin@immsvr.jr2.ox.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8974396" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Asthma/epidemiology/etiology/immunology ; BCG Vaccine/immunology ; Child ; Confounding Factors (Epidemiology) ; Cytokines/blood ; Female ; Humans ; Hypersensitivity, Delayed/*immunology ; Hypersensitivity, Immediate/epidemiology/*etiology/immunology ; Immunoglobulin E/blood ; Interferon-gamma/blood ; Japan/epidemiology ; Male ; Th1 Cells/immunology ; Th2 Cells/immunology ; Tuberculin/*immunology ; Tuberculin Test ; Tuberculosis/*epidemiology/immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 96
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    Bcl-2: prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-25
    Description: Mutations in the gene encoding copper/zinc superoxide dismutase enzyme produce an animal model of familial amyotrophic lateral sclerosis (FALS), a fatal disorder characterized by paralysis. Overexpression of the proto-oncogene bcl-2 delayed onset of motor neuron disease and prolonged survival in transgenic mice expressing the FALS-linked mutation in which glycine is substituted by alanine at position 93. It did not, however, alter the duration of the disease. Overexpression of bcl-2 also attenuated the magnitude of spinal cord motor neuron degeneration in the FALS-transgenic mice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kostic, V -- Jackson-Lewis, V -- de Bilbao, F -- Dubois-Dauphin, M -- Przedborski, S -- NS01724/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jul 25;277(5325):559-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Columbia University, 650 West 168 Street, BB-307, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9228005" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/genetics/mortality/pathology/*therapy ; Animals ; Disease Models, Animal ; Female ; *Gene Expression ; *Genes, bcl-2 ; *Genetic Therapy ; Humans ; Male ; Mice ; Mice, Transgenic ; Motor Neurons/pathology ; Nerve Degeneration ; Proto-Oncogene Proteins c-bcl-2/*physiology ; Proto-Oncogene Proteins c-jun/analysis ; Spinal Cord/pathology ; Superoxide Dismutase/genetics/metabolism ; Survival Rate ; Ubiquitins/analysis
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 97
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    A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-29
    Description: Newly assembled major histocompatibility complex (MHC) class I molecules, together with the endoplasmic reticulum chaperone calreticulin, interact with the transporter associated with antigen processing (TAP) through a molecule called tapasin. The molecular cloning of tapasin revealed it to be a transmembrane glycoprotein encoded by an MHC-linked gene. It is a member of the immunoglobulin superfamily with a probable cytoplasmic endoplasmic reticulum retention signal. Up to four MHC class I-tapasin complexes were found to bind to each TAP molecule. Expression of tapasin in a negative mutant human cell line (220) restored class I-TAP association and normal class I cell surface expression. Tapasin expression also corrected the defective recognition of virus-infected 220 cells by class I-restricted cytotoxic T cells, establishing a critical functional role for tapasin in MHC class I-restricted antigen processing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ortmann, B -- Copeman, J -- Lehner, P J -- Sadasivan, B -- Herberg, J A -- Grandea, A G -- Riddell, S R -- Tampe, R -- Spies, T -- Trowsdale, J -- Cresswell, P -- AI30581/AI/NIAID NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1997 Aug 29;277(5330):1306-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Section of Immunobiology, Yale University School of Medicine, 310 Cedar Street, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9271576" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*metabolism ; Amino Acid Sequence ; Antigen Presentation ; Antiporters/chemistry/genetics/*metabolism ; Calcium-Binding Proteins/metabolism ; Calreticulin ; Cell Line ; Cell Line, Transformed ; Chromosome Mapping ; Chromosomes, Human, Pair 6 ; Cloning, Molecular ; Dimerization ; Endoplasmic Reticulum/metabolism ; Genetic Linkage ; HLA Antigens/*metabolism ; Histocompatibility Antigens Class I/*metabolism ; Humans ; Immunoglobulin G/chemistry ; Immunoglobulins/chemistry/genetics/*metabolism ; Major Histocompatibility Complex/genetics ; Membrane Transport Proteins ; Molecular Sequence Data ; Ribonucleoproteins/metabolism ; Sequence Homology, Amino Acid ; T-Lymphocytes, Cytotoxic ; Tumor Cells, Cultured
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
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    Inhibition of HIV-1 infection by the beta-chemokine MDC (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-24
    Description: CD8(+) T lymphocytes from individuals infected with human immunodeficiency virus-type 1 (HIV-1) secrete a soluble activity that suppresses infection by HIV-1. A protein associated with this activity was purified from the culture supernatant of an immortalized CD8(+) T cell clone and identified as the beta-chemokine macrophage-derived chemokine (MDC). MDC suppressed infection of CD8(+) cell-depleted peripheral blood mononuclear cells by primary non-syncytium-inducing and syncytium-inducing isolates of HIV-1 and the T cell line-adapted isolate HIV-1IIIB. MDC was expressed in activated, but not resting, peripheral blood mononuclear cells and binds a receptor on activated primary T cells. These observations indicate that beta-chemokines are responsible for a major proportion of HIV-1-specific suppressor activity produced by primary T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pal, R -- Garzino-Demo, A -- Markham, P D -- Burns, J -- Brown, M -- Gallo, R C -- DeVico, A L -- N01-AI-55279/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 24;278(5338):695-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Advanced BioScience Laboratories, 5510 Nicholson Lane, Kensington, MD 20895, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381181" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antiviral Agents/*immunology ; Blotting, Northern ; CD8-Positive T-Lymphocytes/*immunology ; Calcium/blood ; Cell Line ; Cell Line, Transformed ; Cells, Cultured ; Chemokine CCL22 ; Chemokines, CC/chemistry/*immunology/isolation & purification/metabolism ; HIV Core Protein p24/biosynthesis ; HIV Infections/immunology ; HIV-1/*immunology/physiology ; Humans ; Leukocytes, Mononuclear/immunology/metabolism/*virology ; Lymphocyte Activation ; Receptors, Chemokine/metabolism ; Receptors, HIV/metabolism ; T-Lymphocytes/immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
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    An antagonist decoy receptor and a death domain-containing receptor for TRAIL (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-08
    Description: TRAIL, also called Apo2L, is a cytotoxic protein that induces apoptosis of many transformed cell lines but not of normal tissues, even though its death domain-containing receptor, DR4, is expressed on both cell types. An antagonist decoy receptor (designated as TRID for TRAIL receptor without an intracellular domain) that may explain the resistant phenotype of normal tissues was identified. TRID is a distinct gene product with an extracellular TRAIL-binding domain and a transmembrane domain but no intracellular signaling domain. TRID transcripts were detected in many normal human tissues but not in most cancer cell lines examined. Ectopic expression of TRID protected mammalian cells from TRAIL-induced apoptosis, which is consistent with a protective role. Another death domain-containing receptor for TRAIL (designated as death receptor-5), which preferentially engaged a FLICE (caspase-8)-related death protease, was also identified.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pan, G -- Ni, J -- Wei, Y F -- Yu, G -- Gentz, R -- Dixit, V M -- ES08111/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1997 Aug 8;277(5327):815-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Michigan Medical School, Ann Arbor, MI, 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9242610" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Apoptosis ; Apoptosis Regulatory Proteins ; Caspase 10 ; Caspase 8 ; Caspase 9 ; *Caspases ; Cell Line, Transformed ; Cysteine Endopeptidases/metabolism ; GPI-Linked Proteins ; HeLa Cells ; Humans ; Ligands ; Membrane Glycoproteins/*metabolism ; Molecular Sequence Data ; Protein Sorting Signals ; Receptors, TNF-Related Apoptosis-Inducing Ligand ; Receptors, Tumor Necrosis Factor/chemistry/genetics/*metabolism ; Sequence Alignment ; Signal Transduction ; TNF-Related Apoptosis-Inducing Ligand ; Transfection ; Tumor Cells, Cultured ; Tumor Necrosis Factor Decoy Receptors ; Tumor Necrosis Factor-alpha/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
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    Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-20
    Description: Classical late-infantile neuronal ceroid lipofuscinosis (LINCL) is a fatal neurodegenerative disease whose defective gene has remained elusive. A molecular basis for LINCL was determined with an approach applicable to other lysosomal storage diseases. When the mannose 6-phosphate modification of newly synthesized lysosomal enzymes was used as an affinity marker, a single protein was identified that is absent in LINCL. Sequence comparisons suggest that this protein is a pepstatin-insensitive lysosomal peptidase, and a corresponding enzymatic activity was deficient in LINCL autopsy specimens. Mutations in the gene encoding this protein were identified in LINCL patients but not in normal controls.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sleat, D E -- Donnelly, R J -- Lackland, H -- Liu, C G -- Sohar, I -- Pullarkat, R K -- Lobel, P -- DK45992/DK/NIDDK NIH HHS/ -- NS30147/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 19;277(5333):1802-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Advanced Biotechnology and Medicine, Piscataway, NJ 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9295267" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aminopeptidases ; Chromosome Mapping ; Chromosomes, Human, Pair 11 ; Codon ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases ; Endopeptidases ; Female ; Glycosylation ; Humans ; Isoelectric Point ; Lysosomes/*enzymology ; Male ; Mannosephosphates/analysis ; Molecular Sequence Data ; Molecular Weight ; *Mutation ; Neuronal Ceroid-Lipofuscinoses/enzymology/*genetics ; Pepstatins/pharmacology ; Peptide Hydrolases/*chemistry/deficiency/*genetics ; Polymerase Chain Reaction ; Serine Proteases
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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