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  • Humans  (544)
  • Amino Acid Sequence  (181)
  • Mutation  (83)
  • American Association for the Advancement of Science (AAAS)  (689)
  • American Association of Petroleum Geologists (AAPG)
  • Elsevier
  • 1995-1999  (689)
  • 1995  (689)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (689)
  • American Association of Petroleum Geologists (AAPG)
  • Elsevier
  • Springer  (5)
  • Wiley-Blackwell  (4)
Years
  • 1995-1999  (689)
Year
  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heymann, S J -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):797-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Harvard Medical School, Kennedy School of Government, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638595" target="_blank"〉PubMed〈/a〉
    Keywords: *Biomedical Research ; Clinical Trials as Topic ; Health Care Costs ; Humans ; *Patient Participation ; *Research ; Research Design ; Research Subjects ; Social Values
    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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-08-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stewart, W W -- Feder, N -- New York, N.Y. -- Science. 1995 Aug 25;269(5227):1030-1; author reply 1034.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7652538" target="_blank"〉PubMed〈/a〉
    Keywords: *Authorship ; Cryptococcus neoformans/*immunology ; *Fungal Vaccines ; Humans ; National Institutes of Health (U.S.) ; Plagiarism ; *Publishing ; United States ; United States Office of Research Integrity ; Vaccines, Conjugate
    Print ISSN: 0036-8075
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  • 3
    Publication Date: 1995-09-08
    Description: Centromeres attach chromosomes to the spindle during mitosis, thereby ensuring the equal distribution of chromosomes into daughter cells. Transcriptionally silent heterochromatin of unknown function is associated with centromeres in many organisms. In the fission yeast Schizosaccharomyces pombe, the silent mating-type loci, centromeres, and telomeres are assembled into silent heterochromatin-like domains. The Swi6 chromodomain protein affects this silencing, and now it is shown that Swi6p localizes with these three chromosomal regions. In cells lacking Swi6p, centromeres lag on the spindle during anaphase and chromosomes are lost at high rates. Thus, Swi6p is located at fission yeast centromeres and is required for their proper function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ekwall, K -- Javerzat, J P -- Lorentz, A -- Schmidt, H -- Cranston, G -- Allshire, R -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1429-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Human Genetics Unit, Western General Hospital, Edinburgh, Scotland, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660126" target="_blank"〉PubMed〈/a〉
    Keywords: Centromere/chemistry/*physiology ; Chromosomes, Fungal ; Fluorescent Antibody Technique ; Fungal Proteins/analysis/genetics/*physiology ; Genes, Fungal ; Genes, Mating Type, Fungal ; Heterochromatin/chemistry ; In Situ Hybridization, Fluorescence ; Interphase ; Mitosis ; Mutation ; *Saccharomyces cerevisiae Proteins ; Schizosaccharomyces/cytology/genetics/*physiology ; Telomere/chemistry ; Transcription Factors/analysis/genetics/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 1995-10-13
    Description: Magnetic source imaging revealed that the cortical representation of the digits of the left hand of string players was larger than that in controls. The effect was smallest for the left thumb, and no such differences were observed for the representations of the right hand digits. The amount of cortical reorganization in the representation of the fingering digits was correlated with the age at which the person had begun to play. These results suggest that the representation of different parts of the body in the primary somatosensory cortex of humans depends on use and changes to conform to the current needs and experiences of the individual.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Elbert, T -- Pantev, C -- Wienbruch, C -- Rockstroh, B -- Taub, E -- New York, N.Y. -- Science. 1995 Oct 13;270(5234):305-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychology, University of Konstanz, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569982" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Afferent Pathways ; Aging ; Brain Mapping ; Fingers/*innervation ; Humans ; Magnetoencephalography ; *Music ; *Neuronal Plasticity ; Neurons, Afferent/*physiology ; Physical Stimulation ; Somatosensory Cortex/anatomy & histology/*physiology ; Thumb/*innervation ; Touch
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  • 5
    Publication Date: 1995-04-28
    Description: DCoH, the dimerization cofactor of hepatocyte nuclear factor-1, stimulates gene expression by associating with specific DNA binding proteins and also catalyzes the dehydration of the biopterin cofactor of phenylalanine hydroxylase. The x-ray crystal structure determined at 3 angstrom resolution reveals that DCoH forms a tetramer containing two saddle-shaped grooves that comprise likely macromolecule binding sites. Two equivalent enzyme active sites flank each saddle, suggesting that there is a spatial connection between the catalytic and binding activities. Structural similarities between the DCoH fold and nucleic acid-binding proteins argue that the saddle motif has evolved to bind diverse ligands or that DCoH unexpectedly may bind nucleic acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Endrizzi, J A -- Cronk, J D -- Wang, W -- Crabtree, G R -- Alber, T -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):556-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720-3206, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725101" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Computer Graphics ; Crystallography, X-Ray ; Gene Expression Regulation ; Hydro-Lyases/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Rats ; Recombinant Fusion Proteins/chemistry/metabolism ; Transcription Factors/*chemistry/metabolism
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  • 6
    Publication Date: 1995-07-07
    Description: Human T cell lymphotropic virus I (HTLV-I) is the etiological agent for adult T cell leukemia and tropical spastic paraparesis (also termed HTLV-I-associated myelopathy). HTLV-I-infected peripheral blood T cells exhibit an initial phase of interleukin-2 (IL-2)-dependent growth; over time, by an unknown mechanism, the cells become IL-2-independent. Whereas the Jak kinases Jak1 and Jak3 and the signal transducer and activator of transcription proteins Stat3 and Stat5 are activated in normal T cells in response to IL-2, this signaling pathway was constitutively activated in HTLV-I-transformed cells. In HTLV-I-infected cord blood lymphocytes, the transition from IL-2-dependent to IL-2-independent growth correlated with the acquisition of a constitutively activated Jak-STAT pathway, which suggests that this pathway participates in HTLV-I-mediated T cell transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Migone, T S -- Lin, J X -- Cereseto, A -- Mulloy, J C -- O'Shea, J J -- Franchini, G -- Leonard, W J -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):79-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Immunology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604283" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Line, Transformed ; *Cell Transformation, Viral ; Cells, Cultured ; DNA-Binding Proteins/*metabolism ; Enzyme Activation ; Fetal Blood/cytology ; Human T-lymphotropic virus 1/*physiology ; Humans ; Interleukin-2/pharmacology ; Janus Kinase 1 ; Janus Kinase 3 ; *Milk Proteins ; Molecular Sequence Data ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; Receptors, Interleukin-2/metabolism ; STAT3 Transcription Factor ; STAT5 Transcription Factor ; Signal Transduction ; T-Lymphocytes/metabolism/*virology ; Trans-Activators/*metabolism
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-09-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erikson, J -- New York, N.Y. -- Science. 1995 Sep 15;269(5230):1508-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7667631" target="_blank"〉PubMed〈/a〉
    Keywords: Advisory Committees ; *Biomedical Research ; *Breast Neoplasms ; *Consumer Advocacy ; Consumer Organizations ; Ethical Review ; Federal Government ; Female ; Humans ; National Institutes of Health (U.S.) ; Peer Review, Research ; *Research ; United States
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-03-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erikson, J -- New York, N.Y. -- Science. 1995 Mar 24;267(5205):1762.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7892594" target="_blank"〉PubMed〈/a〉
    Keywords: Administrative Personnel ; Breast Neoplasms/surgery ; *Clinical Trials as Topic ; History, 20th Century ; Humans ; Intestinal Neoplasms/surgery ; United States
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-07-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, R -- New York, N.Y. -- Science. 1995 Jul 21;269(5222):298.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618097" target="_blank"〉PubMed〈/a〉
    Keywords: 2,4,5-Trichlorophenoxyacetic Acid/*adverse effects/analysis ; 2,4-Dichlorophenoxyacetic Acid/*adverse effects/analysis ; Defoliants, Chemical/*adverse effects ; Dioxins/*adverse effects/analysis ; Humans ; *International Cooperation ; National Institutes of Health (U.S.) ; *Research ; Tetrachlorodibenzodioxin/*adverse effects/analysis ; United States ; Vietnam ; World Health Organization
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  • 10
    Publication Date: 1995-11-03
    Description: A heptadecapeptide was identified and purified from porcine brain tissue as a ligand for an orphan heterotrimeric GTP-binding protein (G protein)-coupled receptor (LC132) that is similar in sequence to opioid receptors. This peptide, orphanin FQ, has a primary structure reminiscent of that of opioid peptides. Nanomolar concentrations of orphanin FQ inhibited forskolin-stimulated adenylyl cyclase activity in cells transfected with LC132. This inhibitory activity was not affected by the addition of opioid ligands, nor did the peptide activate opioid receptors. Orphanin FQ bound to its receptor in a saturable manner and with high affinity. When injected intracerebroventricularly into mice, orphanin FQ caused a decrease in locomotor activity but did not induce analgesia in the hot-plate test. However, the peptide produced hyperalgesia in the tail-flick assay. Thus, orphanin FQ may act as a transmitter in the brain by modulating nociceptive and locomotor behavior.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reinscheid, R K -- Nothacker, H P -- Bourson, A -- Ardati, A -- Henningsen, R A -- Bunzow, J R -- Grandy, D K -- Langen, H -- Monsma, F J Jr -- Civelli, O -- DA 08562/DA/NIDA NIH HHS/ -- DA 09620/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):792-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pharma Division, Hoffmann-La Roche AG, Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481766" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclase Inhibitors ; Amino Acid Sequence ; Analgesics/pharmacology ; Animals ; CHO Cells ; Colforsin/pharmacology ; Cricetinae ; GTP-Binding Proteins/*metabolism ; Hypothalamus/chemistry ; Injections, Intraventricular ; Injections, Spinal ; Ligands ; Mice ; Molecular Sequence Data ; Motor Activity/drug effects ; Opioid Peptides/chemistry/*isolation & purification/*metabolism/pharmacology ; Pain Measurement ; Receptors, Neuropeptide/*metabolism ; Receptors, Opioid/*metabolism ; Swine ; Transfection
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  • 11
    Publication Date: 1995-04-28
    Description: Three archaeological sites at Katanda on the Upper Semliki River in the Western Rift Valley of Zaire have provided evidence for a well-developed bone industry in a Middle Stone Age context. Artifacts include both barbed and unbarbed points as well as a daggerlike object. Dating by both direct and indirect means indicate an age of approximately 90,000 years or older. Together with abundant fish (primarily catfish) remains, the bone technology indicates that a complex subsistence specialization had developed in Africa by this time. The level of behavioral competence required is consistent with that of upper Paleolithic Homo sapiens sapiens. These data support an African origin of behaviorally as well as biologically modern humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yellen, J E -- Brooks, A S -- Cornelissen, E -- Mehlman, M J -- Stewart, K -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):553-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Archaeology Program, National Science Foundation, Arlington, VA 22230, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725100" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Archaeology ; *Behavior ; Democratic Republic of the Congo ; History, Ancient ; *Hominidae ; Humans
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-12-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Farland, W H -- Vaughn-Dellarco, V -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):1907, 1909.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533076" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Carcinogenicity Tests ; Diet ; Humans ; Risk Assessment ; *Toxicity Tests ; United States ; *United States Environmental Protection Agency
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  • 13
    Publication Date: 1995-06-16
    Description: In the news article "Can risky mergers save hospital-based research?" by Wade Roush (19 May, p. 968), the statement that University Hospitals of Cleveland rose from 20th in the rankings of teaching hospitals funded by the National Institutes of Health (NIH) in 1991 to 12th at present was incorrect. In fact, it was Case Western Reserve University (CWRU), with which University Hospitals of Cleveland is affiliated, that received $69 million in NIH grants in 1993, making it the 20th largest recipient of such grants among medical centers; the university then received $97 million in 1994, raising its rank to 12th. About $15 million of the increase, or 53%, was attributable to CWRU's 1992 affiliation with Henry Ford Hospital in Detroit. Other hospitals affiliated with Case Western include MetroHealth Medical Center, Mount Sinai Medical Center, St. Luke's Medical Center, and Cleveland Veterans' Affairs Medical Center.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cardon, L R -- Smith, S D -- Fulker, D W -- Kimberling, W J -- Pennington, B F -- DeFries, J C -- New York, N.Y. -- Science. 1995 Jun 16;268(5217):1553.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7777847" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Mapping ; *Chromosomes, Human, Pair 6 ; Diseases in Twins/*genetics ; Dyslexia/*genetics ; Genetic Markers ; Humans ; Twins, Dizygotic ; Twins, Monozygotic
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-10-20
    Description: Over the past two decades, the small soil nematode Caenorhabditis elegans has become established as a major model system for the study of a great variety of problems in biology and medicine. One of its most significant advantages is its simplicity, both in anatomy and in genomic organization. The entire haploid genetic content amounts to 100 million base pairs of DNA, about 1/30 the size of the human value. As a result, C. elegans has also provided a pilot system for the construction of physical maps of larger animal and plant genomes, and subsequently for the complete sequencing of those genomes. By mid-1995, approximately one-fifth of the complete DNA sequence of this animal had been determined. Caenorhabditis elegans provides a test bed not only for the development and application of mapping and sequencing technologies, but also for the interpretation and use of complete sequence information. This article reviews the progress so far toward a realizable goal--the total description of the genome of a simple animal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hodgkin, J -- Plasterk, R H -- Waterston, R H -- New York, N.Y. -- Science. 1995 Oct 20;270(5235):410-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569995" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*genetics ; *Chromosome Mapping ; Gene Expression ; *Genes, Helminth ; *Genome ; Mutation ; *Sequence Analysis, DNA
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-05-12
    Description: Mutations in genes required for associative learning and memory in Drosophila exist, but isolation of the genes has been difficult because most are defined by a single, chemically induced allele. Here, a simplified genetic screen was used to identify candidate genes involved in learning and memory. Second site suppressors of the dunce (dnc) female sterility phenotype were isolated with the use of transposon mutagenesis. One suppressor mutation that was recovered mapped in the amnesiac (amn) gene. Cloning of the locus revealed that amn encodes a previously uncharacterized neuropeptide gene. Thus, with the cloning of amn, specific neuropeptides are implicated in the memory process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feany, M B -- Quinn, W G -- New York, N.Y. -- Science. 1995 May 12;268(5212):869-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754370" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; Codon ; DNA Transposable Elements ; DNA, Complementary/genetics ; Drosophila/*genetics/physiology ; *Drosophila Proteins ; Female ; *Genes, Insect ; Growth Hormone-Releasing Hormone/chemistry/genetics ; Male ; Memory/*physiology ; Molecular Sequence Data ; Mutagenesis, Insertional ; Mutation ; Neuropeptides/chemistry/*genetics ; Pituitary Adenylate Cyclase-Activating Polypeptide ; Sequence Homology, Amino Acid ; Suppression, Genetic
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-05-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, R -- New York, N.Y. -- Science. 1995 May 5;268(5211):631.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7732366" target="_blank"〉PubMed〈/a〉
    Keywords: Academies and Institutes/economics ; Biotechnology/*economics ; *Genes ; Humans ; Obesity/genetics ; *Patents as Topic ; United States ; Universities/*economics
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  • 17
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-06-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miyashita, Y -- New York, N.Y. -- Science. 1995 Jun 23;268(5218):1719-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Tokyo School of Medicine, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7792596" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Eidetic Imagery/*physiology ; Haplorhini ; Humans ; Memory/*physiology ; Neuronal Plasticity ; Visual Cortex/*physiology ; *Visual Perception
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  • 18
    Publication Date: 1995-06-02
    Description: Fas (also known as Apo1 and CD95) is a cell surface receptor involved in apoptotic cell death. Fas expression and function were analyzed in three children (including two siblings) with a lymphoproliferative syndrome, two of whom also had autoimmune disorders. A large deletion in the gene encoding Fas and no detectable cell surface expression characterized the most affected patient. Clinical manifestations in the two related patients were less severe: Fas-mediated apoptosis was impaired and a deletion within the intracytoplasmic domain was detected. These findings illustrate the crucial regulatory role of Fas and may provide a molecular basis for some autoimmune diseases in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rieux-Laucat, F -- Le Deist, F -- Hivroz, C -- Roberts, I A -- Debatin, K M -- Fischer, A -- de Villartay, J P -- New York, N.Y. -- Science. 1995 Jun 2;268(5215):1347-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut National de la Sante et de la Recherche Medicale (INSERM) U 429, Hopital Necker-Enfants Malades, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7539157" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, CD95 ; Antigens, Surface/chemistry/*genetics/physiology ; Apoptosis ; Autoimmune Diseases/*genetics/immunology/pathology ; Base Sequence ; Child ; Female ; *Frameshift Mutation ; Humans ; Infant ; Lymphoproliferative Disorders/*genetics/immunology/pathology ; Male ; Molecular Sequence Data ; Sequence Deletion ; Syndrome ; Thrombocytopenia/genetics/immunology/pathology
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  • 19
    Publication Date: 1995-06-23
    Description: Deficiency in monoamine oxidase A (MAOA), an enzyme that degrades serotonin and norepinephrine, has recently been shown to be associated with aggressive behavior in men of a Dutch family. A line of transgenic mice was isolated in which transgene integration caused a deletion in the gene encoding MAOA, providing an animal model of MAOA deficiency. In pup brains, serotonin concentrations were increased up to ninefold, and serotonin-like immunoreactivity was present in catecholaminergic neurons. In pup and adult brains, norepinephrine concentrations were increased up to twofold, and cytoarchitectural changes were observed in the somatosensory cortex. Pup behavioral alterations, including trembling, difficulty in righting, and fearfulness were reversed by the serotonin synthesis inhibitor parachlorophenylalanine. Adults manifested a distinct behavioral syndrome, including enhanced aggression in males.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844866/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844866/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cases, O -- Seif, I -- Grimsby, J -- Gaspar, P -- Chen, K -- Pournin, S -- Muller, U -- Aguet, M -- Babinet, C -- Shih, J C -- K05 MH 00796/MH/NIMH NIH HHS/ -- R01 MH 37020/MH/NIMH NIH HHS/ -- R37 MH 39085/MH/NIMH NIH HHS/ -- R37 MH039085/MH/NIMH NIH HHS/ -- R37 MH039085-23/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1995 Jun 23;268(5218):1763-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre National de la Recherche Scientifique (CNRS), Unite de Recherche Associee (URA), Institut Curie, Orsay, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7792602" target="_blank"〉PubMed〈/a〉
    Keywords: Aggression/*physiology ; Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Southern ; Brain/*metabolism ; Disease Models, Animal ; Dopamine/metabolism ; Female ; Interferon-beta/genetics ; Male ; Mice ; Mice, Inbred C3H ; Mice, Transgenic ; Molecular Sequence Data ; Monoamine Oxidase/*deficiency ; Norepinephrine/*metabolism ; Sequence Deletion ; Serotonin/*metabolism
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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-04-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, R -- New York, N.Y. -- Science. 1995 Apr 21;268(5209):356-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716533" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Carcinogenicity Tests ; Carcinogens/*toxicity ; Chloroform/toxicity ; Dioxins/toxicity ; Dose-Response Relationship, Drug ; Guidelines as Topic ; Humans ; National Institutes of Health (U.S.) ; Neoplasms/*chemically induced ; Risk Assessment ; Structure-Activity Relationship ; United States ; United States Environmental Protection Agency
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  • 21
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-12-08
    Description: Telomeres are the protein-DNA structures at the ends of eukaryotic chromosomes. In yeast, and probably most other eukaryotes, telomeres are essential. They allow the cell to distinguish intact from broken chromosomes, protect chromosomes from degradation, and are substrates for novel replication mechanisms. Telomeres are usually replicated by telomerase, a telomere-specific reverse transcriptase, although telomerase-independent mechanisms of telomere maintenance exist. Telomere replication is both cell cycle- and developmentally regulated, and its control is likely to be complex. Because telomere loss causes the kinds of chromosomal changes associated with cancer and aging, an understanding of telomere biology has medical relevance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zakian, V A -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1601-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502069" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Cycle ; Chromosomes/metabolism/physiology ; DNA/analysis/chemistry/metabolism ; DNA Replication ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation ; Humans ; Molecular Sequence Data ; Telomerase/metabolism ; Telomere/chemistry/*physiology
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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-04-14
    Description: The ability of cells to communicate with and respond to their external environment is critical for their continued existence. A universal feature of this communication is that the external signal must in some way penetrate the lipid bilayer surrounding the cell. In most cases of such signal acquisition, the signaling entity itself does not directly enter the cell but rather transmits its information to specific proteins present on the surface of the cell membrane. These proteins then communicate with additional proteins associated with the intracellular face of the membrane. Membrane localization and function of many of these proteins are dependent on their covalent modification by specific lipids, and it is the processes involved that form the focus of this article.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Casey, P J -- New York, N.Y. -- Science. 1995 Apr 14;268(5208):221-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Cancer Biology, Duke University Medical Center, Durham, NC 27710-3686, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716512" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Amino Acid Sequence ; Animals ; Cell Membrane/*metabolism ; GTP-Binding Proteins/*metabolism ; Glycosylphosphatidylinositols/*metabolism ; *Lipid Metabolism ; Molecular Sequence Data ; Protein-Tyrosine Kinases/*metabolism ; *Signal Transduction
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  • 23
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-03-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, Richard -- New York, N.Y. -- Science. 1995 Mar 31;267(5206):1895.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11644749" target="_blank"〉PubMed〈/a〉
    Keywords: Federal Government ; *Financing, Government ; Genetic Predisposition to Disease ; Genetic Testing ; Government ; Government Regulation ; *Human Genome Project ; Humans ; National Institutes of Health (U.S.) ; Politics ; Prejudice ; Social Control, Formal ; United States
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  • 24
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-06-16
    Description: Analysis of differences between siblings (sib pair analysis) is a standard method of genetic linkage analysis for mapping quantitative trait loci, such as those contributing to hypertension and obesity, in humans. In traditional designs, pairs are selected at random or with one sib having an extreme trait value. The majority of such pairs provide little power to detect linkage; only pairs that are concordant for high values, low values, or extremely discordant pairs (for example, one in the top 10 percent and the other in the bottom 10 percent of the distribution) provide substantial power. Focus on discordant pairs can reduce the amount of genotyping necessary over conventional designs by 10- to 40-fold.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Risch, N -- Zhang, H -- HD30712/HD/NICHD NIH HHS/ -- HG00348/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1995 Jun 16;268(5217):1584-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Epidemiology and Public Health, Yale University School of Medicine, New Haven, CT 06520-8034, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7777857" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Chromosome Mapping/*methods/statistics & numerical data ; *Chromosomes, Human ; *Genetic Linkage ; Genotype ; Humans ; Models, Genetic ; Models, Statistical ; Nuclear Family ; Phenotype ; Probability ; Sample Size
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  • 25
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-07-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aitken, R J -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):39-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Reproductive Biology Unit, Medical Research Council, Edinburgh, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604276" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Egg Proteins/*metabolism ; Female ; Humans ; Lectins/metabolism ; Male ; Membrane Glycoproteins/*metabolism ; Mice ; Phosphorylation ; Proto-Oncogene Proteins ; Receptor Protein-Tyrosine Kinases/*metabolism ; Receptors, Cell Surface/*metabolism ; Sperm-Ovum Interactions/*physiology ; Spermatozoa/metabolism ; Zona Pellucida/*metabolism
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  • 26
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-04-14
    Description: A fundamental question in signal transduction is how stimulation of a specific protein kinase leads to phosphorylation of particular protein substrates throughout the cell. Recent studies indicate that specific anchoring proteins located at various sites in the cell compartmentalize the kinases to their sites of action. Inhibitors of the interactions between kinases and their anchoring proteins inhibit the functions mediated by the kinases. These data indicate that the location of these anchoring proteins provides some of the specificity of the responses mediated by each kinase and suggest that inhibitors of the interaction between the kinases and their anchoring proteins may be useful as therapeutic agents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mochly-Rosen, D -- R01 HL-43380/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 14;268(5208):247-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Pharmacology, School of Medicine, Stanford University, CA 94305-5332, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716516" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Compartmentation ; Cell Membrane/metabolism ; Cytoskeleton/metabolism ; Humans ; Protein Kinases/*metabolism ; Proteins/*metabolism ; *Signal Transduction
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  • 27
    Publication Date: 1995-07-14
    Description: CD1 molecules are distantly related to the major histocompatibility complex (MHC) class I proteins. They are of unknown function. Screening random peptide phage display libraries with soluble empty mouse CD1 (mCD1) identified a peptide binding motif. It consists of three anchor positions occupied by aromatic or bulky hydrophobic amino acids. Equilibrium binding studies demonstrated that mCD1 binds peptides containing the appropriate motif with relatively high affinity. However, in contrast to classical MHC class I molecules, strong binding to mCD1 required relatively long peptides. Peptide-specific, mCD1-restricted T cell responses can be raised, which suggests that the findings are of immunological significance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castano, A R -- Tangri, S -- Miller, J E -- Holcombe, H R -- Jackson, M R -- Huse, W D -- Kronenberg, M -- Peterson, P A -- New York, N.Y. -- Science. 1995 Jul 14;269(5221):223-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7542403" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antigen Presentation ; Antigens, CD/chemistry/*immunology/metabolism ; Antigens, CD1 ; Cell Line ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Peptides/chemistry/*immunology/metabolism ; T-Lymphocytes, Cytotoxic/*immunology ; Transfection
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  • 28
    Publication Date: 1995-09-01
    Description: Eukaryotic chromosomes are capped with repetitive telomere sequences that protect the ends from damage and rearrangements. Telomere repeats are synthesized by telomerase, a ribonucleic acid (RNA)-protein complex. Here, the cloning of the RNA component of human telomerase, termed hTR, is described. The template region of hTR encompasses 11 nucleotides (5'-CUAACCCUAAC) complementary to the human telomere sequence (TTAGGG)n. Germline tissues and tumor cell lines expressed more hTR than normal somatic cells and tissues, which have no detectable telomerase activity. Human cell lines that expressed hTR mutated in the template region generated the predicted mutant telomerase activity. HeLa cells transfected with an antisense hTR lost telomeric DNA and began to die after 23 to 26 doublings. Thus, human telomerase is a critical enzyme for the long-term proliferation of immortal tumor cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, J -- Funk, W D -- Wang, S S -- Weinrich, S L -- Avilion, A A -- Chiu, C P -- Adams, R R -- Chang, E -- Allsopp, R C -- Yu, J -- AG09383/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 1;269(5228):1236-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geron Corporation, Menlo Park, CA 94025, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7544491" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Death ; *Cell Division ; Cell Line ; Cloning, Molecular ; DNA Nucleotidylexotransferase/antagonists & ; inhibitors/chemistry/genetics/*metabolism ; HeLa Cells ; Humans ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacology ; Polymerase Chain Reaction ; RNA/chemistry/genetics/*metabolism ; Templates, Genetic ; Transfection ; Tumor Cells, Cultured
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  • 29
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-02-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Akiyama, M -- Kodama, K -- Mabuchi, K -- Ohara, J L -- Preston, D L -- Satoh, C -- Akahoshi, M -- Honda, T -- Soda, M -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1077.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855582" target="_blank"〉PubMed〈/a〉
    Keywords: Government Agencies ; Humans ; International Cooperation ; Japan ; *Nuclear Warfare ; *Radiation Injuries ; Survivors ; United States
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  • 30
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-01-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holden, Constance -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):451.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11644748" target="_blank"〉PubMed〈/a〉
    Keywords: Brazil ; DNA, Recombinant ; Embryo Research ; *Genetic Engineering ; Genetic Therapy ; Germ Cells ; *Government Regulation ; Humans ; *Legislation as Topic ; Reproductive Techniques, Assisted ; Research ; *Social Control, Formal
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  • 31
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-03-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, R -- New York, N.Y. -- Science. 1995 Mar 24;267(5205):1770-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7892597" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Environmental Pollutants/*adverse effects ; Humans ; Ozone/*adverse effects ; Polychlorinated Biphenyls/*adverse effects ; Respiratory Tract Infections/etiology ; Smoke/*adverse effects ; Thyroid Hormones/metabolism ; Water Purification/methods
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  • 32
    Publication Date: 1995-05-05
    Description: Fragile X syndrome is the result of the unstable expansion of a trinucleotide repeat in the 5'-untranslated region of the FMR1 gene. Fibroblast subclones from a mildly affected patient, each containing stable FMR1 alleles with 57 to 285 CGG repeats, were shown to exhibit normal steady-state levels of FMR1 messenger RNA. However, FMR protein was markedly diminished from transcript with more than 200 repeats. Such transcripts were associated with stalled 40S ribosomal subunits. These results suggest that a structural RNA transition beyond 200 repeats impedes the linear 40S migration along the 5'-untranslated region. This results in translational inhibition by trinucleotide repeat expansion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, Y -- Zhang, F -- Lokey, L K -- Chastain, J L -- Lakkis, L -- Eberhart, D -- Warren, S T -- HD20521/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1995 May 5;268(5211):731-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Emory University School of Medicine, Atlanta, GA 30322.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7732383" target="_blank"〉PubMed〈/a〉
    Keywords: Centrifugation, Density Gradient ; Clone Cells ; Down-Regulation/genetics ; Female ; Fibroblasts/chemistry ; Fragile X Mental Retardation Protein ; Fragile X Syndrome/*genetics ; Humans ; Infant ; Male ; Nerve Tissue Proteins/*genetics ; Polymerase Chain Reaction ; Protein Biosynthesis/*genetics ; RNA, Messenger/analysis ; *RNA-Binding Proteins ; Repetitive Sequences, Nucleic Acid/*genetics
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  • 33
    Publication Date: 1995-05-05
    Description: Lactacystin is a Streptomyces metabolite that inhibits cell cycle progression and induces neurite outgrowth in a murine neuroblastoma cell line. Tritium-labeled lactacystin was used to identify the 20S proteasome as its specific cellular target. Three distinct peptidase activities of this enzyme complex (trypsin-like, chymotrypsin-like, and peptidylglutamyl-peptide hydrolyzing activities) were inhibited by lactacystin, the first two irreversibly and all at different rates. None of five other proteases were inhibited, and the ability of lactacystin analogs to inhibit cell cycle progression and induce neurite outgrowth correlated with their ability to inhibit the proteasome. Lactacystin appears to modify covalently the highly conserved amino-terminal threonine of the mammalian proteasome subunit X (also called MB1), a close homolog of the LMP7 proteasome subunit encoded by the major histocompatibility complex. This threonine residue may therefore have a catalytic role, and subunit X/MB1 may be a core component of an amino-terminal-threonine protease activity of the proteasome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fenteany, G -- Standaert, R F -- Lane, W S -- Choi, S -- Corey, E J -- Schreiber, S L -- New York, N.Y. -- Science. 1995 May 5;268(5211):726-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7732382" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcysteine/*analogs & derivatives/pharmacology ; Amino Acid Sequence ; Animals ; Carrier Proteins/metabolism ; Cattle ; Chromatography, High Pressure Liquid ; Cysteine Endopeptidases/*drug effects/metabolism ; Cysteine Proteinase Inhibitors/*pharmacology ; Electrophoresis, Polyacrylamide Gel ; Mice ; Molecular Sequence Data ; Multienzyme Complexes/*drug effects/metabolism ; Nerve Tissue Proteins/metabolism ; Neurons/*drug effects ; Proteasome Endopeptidase Complex ; Threonine/*drug effects ; Tumor Cells, Cultured
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  • 34
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-11-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holtzman, S -- Hillback, E D Jr -- New York, N.Y. -- Science. 1995 Nov 24;270(5240):1283.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481810" target="_blank"〉PubMed〈/a〉
    Keywords: Biotechnology ; *Genetics, Medical ; Health Care Reform ; Humans ; *Insurance Selection Bias ; Insurance, Health/*legislation & jurisprudence ; United States
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-11-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holtzman, S -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502020" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Humans ; Risk Assessment ; *Toxicity Tests/statistics & numerical data
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  • 36
    Publication Date: 1995-07-14
    Description: Oligosaccharides and glycopeptides are of considerable importance in molecular biology and pharmacology. However, their synthesis is complicated by the large number of different linking sites between each saccharide unit, the need for stereochemical control, the chemical sensitivity of the glycopeptide bonds, and the need to harmonize diverse protecting groups. Here, an efficient solid-phase synthesis of three N-linked glycopeptides based on glycal assembly is presented. The peptide domain can be extended while the ensemble remains bound to the polymer. The glycopeptides synthesized here are among the largest N-linked glycopeptides ever accessed by either solution- or solid-phase synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberge, J Y -- Beebe, X -- Danishefsky, S J -- AI 16943/AI/NIAID NIH HHS/ -- T32 CA62948/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 14;269(5221):202-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Bioorganic Chemistry, Sloan-Kettering Institute for Cancer Research, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618080" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Carbohydrate Conformation ; Carbohydrate Sequence ; Glycopeptides/*chemical synthesis/chemistry/isolation & purification ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Oligosaccharides/chemistry ; Peptides/chemistry
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-09-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mohapatra, S S -- New York, N.Y. -- Science. 1995 Sep 15;269(5230):1499.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7667628" target="_blank"〉PubMed〈/a〉
    Keywords: Humans ; Interferon-gamma/immunology ; Interleukin-12/adverse effects/immunology/*therapeutic use
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  • 38
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-03-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, R -- New York, N.Y. -- Science. 1995 Mar 24;267(5205):1759.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7892593" target="_blank"〉PubMed〈/a〉
    Keywords: Antiviral Agents/*adverse effects ; Arabinofuranosyluracil/adverse effects/*analogs & derivatives ; Clinical Trials as Topic/*standards ; Drug-Induced Liver Injury ; Humans ; Institute of Medicine (U.S.) ; *National Institutes of Health (U.S.) ; United States ; United States Food and Drug Administration
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  • 39
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-02-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, R -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1089-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855587" target="_blank"〉PubMed〈/a〉
    Keywords: Child ; Cost-Benefit Analysis ; Environmental Exposure/*legislation & jurisprudence ; Government Agencies/legislation & jurisprudence ; Humans ; Lead/*blood ; Risk Assessment ; United States ; United States Environmental Protection Agency/*legislation & jurisprudence
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  • 40
    Publication Date: 1995-11-03
    Description: The human beta-globin locus control region (LCR) controls the transcription, chromatin structure, and replication timing of the entire locus. DNA replication was found to initiate in a transcription-independent manner within a region located 50 kilobases downstream of the LCR in human, mouse, and chicken cells containing the entire human beta-globin locus. However, DNA replication did not initiate within a deletion mutant locus lacking the sequences that encompass the LCR. This mutant locus replicated in the 3' to 5' direction. Thus, interactions between distantly separated sequences can be required for replication initiation, and factors mediating this interaction appear to be conserved in evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aladjem, M I -- Groudine, M -- Brody, L L -- Dieken, E S -- Fournier, R E -- Wahl, G M -- Epner, E M -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):815-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gene Expression Laboratory, Salk Institute, San Diego, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481774" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Evolution ; Cell Line ; Chickens ; *DNA Replication ; Globins/*genetics ; Humans ; Hybrid Cells ; Mice ; Molecular Sequence Data ; *Regulatory Sequences, Nucleic Acid ; Sequence Deletion ; Tumor Cells, Cultured
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-02-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, R -- New York, N.Y. -- Science. 1995 Feb 17;267(5200):957-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7863337" target="_blank"〉PubMed〈/a〉
    Keywords: Communicable Diseases/*epidemiology/transmission ; Developing Countries ; Disease Outbreaks ; *Greenhouse Effect ; Hot Temperature/*adverse effects ; Humans ; Malaria/epidemiology/transmission ; Population Surveillance ; *Tropical Medicine ; Urban Health ; World Health Organization
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉al-Awqati, Q -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):805-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉College of Physicians and Surgeons, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7543697" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*metabolism ; Adenosine Triphosphate/*secretion ; Animals ; Chloride Channels/metabolism ; Cystic Fibrosis/metabolism ; Cystic Fibrosis Transmembrane Conductance Regulator ; Humans ; Ion Channels/*metabolism ; Membrane Proteins/metabolism ; Multidrug Resistance-Associated Proteins ; Potassium Channels/metabolism ; *Potassium Channels, Inwardly Rectifying ; Receptors, Drug/metabolism ; Sodium Channels/metabolism ; Sulfonylurea Compounds/metabolism ; Sulfonylurea Receptors
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  • 43
    Publication Date: 1995-03-10
    Description: The crystal structure of the tungsten-containing aldehyde ferredoxin oxidoreductase (AOR) from Pyrococcus furiosus, a hyperthermophilic archaeon (formerly archaebacterium) that grows optimally at 100 degrees C, has been determined at 2.3 angstrom resolution by means of multiple isomorphous replacement and multiple crystal form averaging. AOR consists of two identical subunits, each containing an Fe4S4 cluster and a molybdopterin-based tungsten cofactor that is analogous to the molybdenum cofactor found in a large class of oxotransferases. Whereas the general features of the tungsten coordination in this cofactor were consistent with a previously proposed structure, each AOR subunit unexpectedly contained two molybdopterin molecules that coordinate a tungsten by a total of four sulfur ligands, and the pterin system was modified by an intramolecular cyclization that generated a three-ringed structure. In comparison to other proteins, the hyperthermophilic enzyme AOR has a relatively small solvent-exposed surface area, and a relatively large number of both ion pairs and buried atoms. These properties may contribute to the extreme thermostability of this enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, M K -- Mukund, S -- Kletzin, A -- Adams, M W -- Rees, D C -- 1F32 GM15006/GM/NIGMS NIH HHS/ -- GM50775/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Mar 10;267(5203):1463-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, Pasadena, CA 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7878465" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehyde Oxidoreductases/*chemistry/metabolism ; Amino Acid Sequence ; Archaea/*enzymology ; Binding Sites ; *Coenzymes ; Computer Graphics ; Crystallography, X-Ray ; Enzyme Stability ; Ferrous Compounds ; Metalloproteins/analysis/chemistry ; Models, Molecular ; Molecular Sequence Data ; Organometallic Compounds/analysis/*chemistry ; Oxidation-Reduction ; Protein Conformation ; Protein Structure, Secondary ; Pteridines/analysis/chemistry ; Pterins/analysis/*chemistry ; Surface Properties ; Temperature ; Tungsten/analysis/*chemistry
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-05-19
    Description: The three-dimensional structure of the complex formed by two plasma proteins, transthyretin and retinol-binding protein, was determined from x-ray diffraction data to a nominal resolution of 3.1 angstroms. One tetramer of transthyretin was bound to two molecules of retinol-binding protein. The two retinol-binding protein molecules established molecular interactions with the same transthyretin dimer, and each also made contacts with one of the other two monomers. Thus, the other two potential binding sites in a transthyretin tetramer were blocked. The amino acid residues of the retinol-binding protein that were involved in the contacts were close to the retinol-binding site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Monaco, H L -- Rizzi, M -- Coda, A -- New York, N.Y. -- Science. 1995 May 19;268(5213):1039-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, University of Pavia, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754382" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biopolymers ; Chickens ; Crystallography, X-Ray ; Humans ; Models, Molecular ; Molecular Sequence Data ; Prealbumin/*chemistry ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Retinol-Binding Proteins/*chemistry ; Retinol-Binding Proteins, Plasma ; Sequence Homology, Amino Acid
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  • 45
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mongella, G -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):789-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fourth World Conference on Women, United Nations, New York, NY 10017, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638591" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/epidemiology/transmission ; Aging ; Biomedical Research ; Female ; *Global Health ; Health Promotion ; Humans ; *Internationality ; Life Expectancy ; Male ; Neoplasms/epidemiology ; Poverty ; Research ; Research Support as Topic ; Resource Allocation ; Sex Characteristics ; Violence ; *Women's Health ; Women's Health Services ; World Health Organization
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  • 46
    Publication Date: 1995-09-15
    Description: The protein tyrosine kinase c-Src is transiently activated at the transition from the G2 phase to mitosis in the cell cycle of mammalian fibroblasts. Fyn and Yes, the other members of the Src family present in fibroblasts, were also found to be activated at mitosis. In cells microinjected with a neutralizing antibody specific for Src, Fyn, and Yes (anti-cst.1) during G2, cell division was inhibited by 75 percent. The block occurred before nuclear envelope breakdown. Antibodies specific for phosphatidylinositol-3 kinase alpha and phospholipase C-gamma 1 had no effect. Microinjection of the Src homology 2 (SH2) domain of Fyn was also inhibitory. Functional redundancy between members of the Src family was observed; a Src-specific antibody had no effect in NIH 3T3 cells but inhibited cell division in fibroblasts in which the only functional Src family kinase was Src itself. Thus, Src family kinases and proteins associating with their SH2 domains are required for entry into mitosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roche, S -- Fumagalli, S -- Courtneidge, S A -- New York, N.Y. -- Science. 1995 Sep 15;269(5230):1567-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut National de la Sante et de la Recherche Medicale (INSERM) faculte de Pharmacie, Montpellier, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7545311" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Enzyme Activation ; *G2 Phase ; Isoenzymes/immunology/metabolism ; Mice ; Microinjections ; *Mitosis ; Molecular Sequence Data ; Nocodazole/pharmacology ; Phospholipase C gamma ; Protein-Tyrosine Kinases/immunology/*metabolism ; Proto-Oncogene Proteins/immunology/*metabolism ; Proto-Oncogene Proteins c-fyn ; Proto-Oncogene Proteins c-yes ; Proto-Oncogene Proteins pp60(c-src)/immunology/metabolism ; Type C Phospholipases/immunology/metabolism ; *src-Family Kinases
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  • 47
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-04-28
    Description: Epstein-Barr virus (EBV) nuclear antigen 2 (EBNA2) is a transcriptional activator that is essential for EBV-driven B cell immortalization. EBNA2 is targeted to responsive promoters through interaction with a cellular DNA binding protein, C promoter binding factor 1 (CBF1). A transcriptional repression domain has been identified within CBF1. This domain also interacts with EBNA2, and repression is masked by EBNA2 binding. Thus, EBNA2 acts by countering transcriptional repression. Mutation at amino acid 233 of CBF1 abolishes repression and correlates with a loss-of-function mutation in the Drosophila homolog Su(H).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hsieh, J J -- Hayward, S D -- CA42245/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):560-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725102" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Viral/chemistry/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Epstein-Barr Virus Nuclear Antigens ; *Gene Expression Regulation ; HeLa Cells ; Humans ; Immunoglobulin J Recombination Signal Sequence-Binding Protein ; Models, Genetic ; Mutation ; *Nuclear Proteins ; Promoter Regions, Genetic ; Trans-Activators/chemistry/*metabolism ; *Transcription, Genetic ; Transfection
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  • 48
    Publication Date: 1995-03-31
    Description: Members of the interleukin-6 family of cytokines bind to and activate receptors that contain a common subunit, gp130. This leads to the activation of Stat3 and Stat1, two cytoplasmic signal transducers and activators of transcription (STATs), by tyrosine phosphorylation. Serine phosphorylation of Stat3 was constitutive and was enhanced by signaling through gp130. In cells of lymphoid and neuronal origins, inhibition of serine phosphorylation prevented the formation of complexes of DNA with Stat3-Stat3 but not with Stat3-Stat1 or Stat1-Stat1 dimers. In vitro serine dephosphorylation of Stat3 also inhibited DNA binding of Stat3-Stat3. The requirement of serine phosphorylation for Stat3-Stat3.DNA complex formation was inversely correlated with the affinity of Stat3-Stat3 for the binding site. Thus, serine phosphorylation appears to enhance or to be required for the formation of stable Stat3-Stat3.DNA complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, X -- Blenis, J -- Li, H C -- Schindler, C -- Chen-Kiang, S -- CA46595/CA/NCI NIH HHS/ -- HL 21006/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Mar 31;267(5206):1990-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Brookdale Center for Molecular Biology, Mount Sinai School of Medicine, New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701321" target="_blank"〉PubMed〈/a〉
    Keywords: 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cell Nucleus/metabolism ; Ciliary Neurotrophic Factor ; Cytoplasm/metabolism ; DNA/metabolism ; DNA-Binding Proteins/*metabolism ; Humans ; Interleukin-6/metabolism/*pharmacology ; Isoquinolines/pharmacology ; Mice ; Molecular Sequence Data ; Nerve Tissue Proteins/pharmacology ; Phosphorylation ; Piperazines/pharmacology ; *Promoter Regions, Genetic ; STAT1 Transcription Factor ; STAT3 Transcription Factor ; Serine/*metabolism ; Signal Transduction ; Threonine/metabolism ; Trans-Activators/*metabolism ; Tumor Cells, Cultured ; Tyrosine/metabolism
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-01-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Montaner, L J -- Gordon, S -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):538-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824955" target="_blank"〉PubMed〈/a〉
    Keywords: Cells, Cultured ; Down-Regulation ; HIV-1/*physiology ; Humans ; Interleukins/biosynthesis/*immunology ; Macrophages/*virology ; T-Lymphocytes, Helper-Inducer/*immunology/virology ; Virus Replication
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  • 50
    Publication Date: 1995-01-27
    Description: Vascular smooth muscle cell (SMC) proliferation in response to injury is an important etiologic factor in vascular proliferative disorders such as atherosclerosis and restenosis after balloon angioplasty. The retinoblastoma gene product (Rb) is present in the unphosphorylated and active form in quiescent primary arterial SMCs, but is rapidly inactivated by phosphorylation in response to growth factor stimulation in vitro. A replication-defective adenovirus encoding a nonphosphorylatable, constitutively active form of Rb was constructed. Infection of cultured primary rat aortic SMCs with this virus inhibited growth factor-stimulated cell proliferation in vitro. Localized arterial infection with the virus at the time of balloon angioplasty significantly reduced SMC proliferation and neointima formation in both the rat carotid and porcine femoral artery models of restenosis. These results demonstrate the role of Rb in regulating vascular SMC proliferation and suggest a gene therapy approach for vascular proliferative disorders associated with arterial injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, M W -- Barr, E -- Seltzer, J -- Jiang, Y Q -- Nabel, G J -- Nabel, E G -- Parmacek, M S -- Leiden, J M -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):518-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824950" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/genetics/physiology ; Angioplasty, Balloon ; Animals ; Base Sequence ; Blood ; Carotid Arteries/virology ; Cell Division ; Disease Models, Animal ; Femoral Artery/virology ; *Genes, Retinoblastoma ; *Genetic Therapy ; Genetic Vectors ; Humans ; Molecular Sequence Data ; Muscle, Smooth, Vascular/*cytology/pathology/virology ; Rats ; Rats, Sprague-Dawley ; Retinoblastoma Protein/*physiology ; Swine ; Vascular Diseases/pathology/*therapy
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-01-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, R -- New York, N.Y. -- Science. 1995 Jan 6;267(5194):23-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809603" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biotechnology/*legislation & jurisprudence ; Humans ; *Patents as Topic ; United States ; United States Food and Drug Administration
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  • 52
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-10-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, P S -- Chang, Y -- New York, N.Y. -- Science. 1995 Oct 6;270(5233):15.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569942" target="_blank"〉PubMed〈/a〉
    Keywords: DNA, Viral/*analysis ; Herpesviridae/*genetics ; Humans ; Lymphoma, AIDS-Related/pathology/*virology ; Lymphoma, Non-Hodgkin/pathology/*virology ; Sarcoma, Kaposi/pathology/*virology ; Tumor Cells, Cultured
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  • 53
    Publication Date: 1995-12-15
    Description: The crystal structure of the V alpha domain of a T cell antigen receptor (TCR) was determined at a resolution of 2.2 angstroms. This structure represents an immunoglobulin topology set different from those previously described. A switch in a polypeptide strand from one beta sheet to the other enables a pair of V alpha homodimers to pack together to form a tetramer, such that the homodimers are parallel to each other and all hypervariable loops face in one direction. On the basis of the observed mode of V alpha association, a model of an (alpha beta)2 TCR tetramer can be positioned relative to the major histocompatibility complex class II (alpha beta)2 tetramer with the third hypervariable loop of V alpha over the amino-terminal portion of the antigenic peptide and the corresponding loop of V beta over its carboxyl-terminal residues. TCR dimerization that is mediated by the alpha chain may contribute to the coupling of antigen recognition to signal transduction during T cell activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fields, B A -- Ober, B -- Malchiodi, E L -- Lebedeva, M I -- Braden, B C -- Ysern, X -- Kim, J K -- Shao, X -- Ward, E S -- Mariuzza, R A -- AI31592/AI/NIAID NIH HHS/ -- GM52801/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Dec 15;270(5243):1821-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, MD 20850, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8525376" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crystallography, X-Ray ; Humans ; Mice ; Models, Molecular ; Protein Conformation ; Protein Folding ; Receptors, Antigen, T-Cell, alpha-beta/*chemistry/immunology
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  • 54
    Publication Date: 1995-05-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zischler, H -- Hoss, M -- Handt, O -- von Haeseler, A -- van der Kuyl, A C -- Goudsmit, J -- New York, N.Y. -- Science. 1995 May 26;268(5214):1192-3; author reply 1194.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7605504" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cytochrome b Group/*genetics ; DNA, Mitochondrial/*genetics ; *Fossils ; Humans ; Molecular Sequence Data ; Phylogeny
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  • 55
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-09-22
    Description: ERS (ethylene response sensor), a gene in the Arabidopsis thaliana ethylene hormone-response pathway, was uncovered by cross-hybridization with the Arabidopsis ETR1 gene. The deduced ERS protein has sequence similarity with the amino-terminal domain and putative histidine protein kinase domain of ETR1, but it does not have a receiver domain as found in ETR1. A missense mutation identical to the dominant etr1-4 mutation was introduced into the ERS gene. The altered ERS gene conferred dominant ethylene insensitivity to wild-type Arabidopsis. Double-mutant analysis indicates that ERS acts upstream of the CTR1 protein kinase gene in the ethylene-response pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hua, J -- Chang, C -- Sun, Q -- Meyerowitz, E M -- New York, N.Y. -- Science. 1995 Sep 22;269(5231):1712-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569898" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/chemistry/drug effects/*genetics/physiology ; Arabidopsis Proteins ; Base Sequence ; Cloning, Molecular ; Ethylenes/*pharmacology ; *Genes, Plant ; Kanamycin Resistance ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phenotype ; Plant Proteins/chemistry/*genetics/physiology ; Plants, Genetically Modified ; *Receptors, Cell Surface
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  • 56
    Publication Date: 1995-11-17
    Description: The crystal structure of the aldehyde oxido-reductase (Mop) from the sulfate reducing anaerobic Gram-negative bacterium Desulfovibrio gigas has been determined at 2.25 A resolution by multiple isomorphous replacement and refined. The protein, a homodimer of 907 amino acid residues subunits, is a member of the xanthine oxidase family. The protein contains a molybdopterin cofactor (Mo-co) and two different [2Fe-2S] centers. It is folded into four domains of which the first two bind the iron sulfur centers and the last two are involved in Mo-co binding. Mo-co is a molybdenum molybdopterin cytosine dinucleotide. Molybdopterin forms a tricyclic system with the pterin bicycle annealed to a pyran ring. The molybdopterin dinucleotide is deeply buried in the protein. The cis-dithiolene group of the pyran ring binds the molybdenum, which is coordinated by three more (oxygen) ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Romao, M J -- Archer, M -- Moura, I -- Moura, J J -- LeGall, J -- Engh, R -- Schneider, M -- Hof, P -- Huber, R -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1170-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Instituto de Tecnologia Quimica e Biologica, Oeiras, Portugal.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502041" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehyde Oxidoreductases/*chemistry/metabolism ; Amino Acid Sequence ; Animals ; Coenzymes/chemistry/metabolism ; Crystallization ; Crystallography, X-Ray ; Cytosine Nucleotides/chemistry/metabolism ; Desulfovibrio/*enzymology ; Drosophila melanogaster/enzymology ; Electron Transport ; Hydrogen Bonding ; Iron/chemistry ; Ligands ; Metalloproteins/chemistry/metabolism ; Molecular Sequence Data ; Molybdenum/chemistry/metabolism ; Oxidation-Reduction ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Pteridines/chemistry/metabolism ; Pterins/chemistry/metabolism ; Xanthine ; Xanthine Oxidase/*chemistry ; Xanthines/metabolism
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  • 57
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-06-16
    Description: Analysis of data collected on 131 species of primates, bats, and insectivores showed that the sizes of brain components, from medulla to forebrain, are highly predictable from absolute brain size by a nonlinear function. The order of neurogenesis was found to be highly conserved across a wide range of mammals and to correlate with the relative enlargement of structures as brain size increases, with disproportionately large growth occurring in late-generated structures. Because the order of neurogenesis is conserved, the most likely brain alteration resulting from selection for any behavioral ability may be a coordinated enlargement of the entire nonolfactory brain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finlay, B L -- Darlington, R B -- NS19245/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jun 16;268(5217):1578-84.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychology, Uris Hall, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7777856" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Analysis of Variance ; Animals ; *Biological Evolution ; Brain/*anatomy & histology/cytology/growth & development ; Cell Division ; Chiroptera/anatomy & histology ; Databases, Factual ; Humans ; Insectivora/anatomy & histology ; Mammals/*anatomy & histology ; Models, Neurological ; Models, Statistical ; Neurons/*cytology ; Primates/anatomy & histology ; Regression Analysis ; Species Specificity
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  • 58
    Publication Date: 1995-07-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chase, G A -- DeLeon, P A -- Dronamraju, K R -- Erickson, R P -- Glorioso, J C 3rd -- Hirschhorn, R -- Lysaught, M T -- McGraw, K M -- Meyers, A S -- Miller, A D -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):14-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604272" target="_blank"〉PubMed〈/a〉
    Keywords: *Advisory Committees ; Clinical Protocols ; Clinical Trials, Phase I as Topic/legislation & jurisprudence ; Clinical Trials, Phase II as Topic/legislation & jurisprudence ; DNA, Recombinant ; Ethical Review ; Federal Government ; Genetic Therapy/*legislation & jurisprudence ; *Government Regulation ; Humans ; *National Institutes of Health (U.S.) ; United States
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  • 59
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-05-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allard, M W -- Young, D -- Huyen, Y -- New York, N.Y. -- Science. 1995 May 26;268(5214):1192; author reply 1194.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7761840" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone and Bones/chemistry ; Cytochrome b Group/*genetics ; DNA/*genetics ; Humans ; Mammals/genetics ; Sequence Homology, Nucleic Acid
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  • 60
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-11-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1117.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502032" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Animals ; Biological Evolution ; *Fossils ; History, Ancient ; *Hominidae/anatomy & histology ; Humans
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  • 61
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-01-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roop, D -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):474-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7529942" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Membrane/metabolism ; Humans ; Ichthyosis/*genetics/metabolism/pathology ; Ichthyosis, Lamellar/*genetics/metabolism/pathology ; Intermediate Filaments/metabolism/ultrastructure ; Keratinocytes/metabolism/*ultrastructure ; Keratins/genetics ; Lipid Metabolism ; Mutation ; Transglutaminases/genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 62
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-09-15
    Description: The stretch of a frog muscle within the physiological range can more than double the spontaneous and evoked release of neurotransmitter from its motor nerve terminals. Here, stretch enhancement of release was suppressed by peptides containing the sequence arginine-glycine-aspartic acid (RGD), which blocks integrin binding. Integrin antibodies also inhibited the enhancement obtained by stretching. Stretch enhancement depended on intraterminal calcium derived both from external calcium and from internal stores. Muscle stretch thus might enhance the release of neurotransmitters either by elevating internal calcium concentrations or by increasing the sensitivity of transmitter release to calcium in the nerve terminal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, B M -- Grinnell, A D -- NS06232/NS/NINDS NIH HHS/ -- NS30673/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 15;269(5230):1578-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jerry Lewis Neuromuscular Research Center, University of California at Los Angeles School of Medicine, 90024, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7667637" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcium/metabolism ; In Vitro Techniques ; Integrins/*physiology ; Membrane Potentials ; Microelectrodes ; Molecular Sequence Data ; Motor Endplate/physiology ; Motor Neurons/*physiology ; Neuromuscular Junction/*physiology ; Neurotransmitter Agents/*metabolism ; Oligopeptides/pharmacology ; Rana pipiens
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  • 63
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):775-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638588" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Chlamydia Infections/complications/immunology ; Endometriosis/*complications/genetics ; Female ; Genetic Predisposition to Disease ; Humans ; Infertility, Female/*etiology/genetics ; Infertility, Male/etiology ; Leiomyoma/*complications/genetics ; Male ; Sexually Transmitted Diseases/*complications/epidemiology/immunology ; Uterine Neoplasms/*complications/genetics
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  • 64
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-02-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lawler, A -- New York, N.Y. -- Science. 1995 Feb 17;267(5200):956.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7695774" target="_blank"〉PubMed〈/a〉
    Keywords: *Boron Neutron Capture Therapy ; Brain Neoplasms/*radiotherapy ; *Clinical Trials as Topic ; Humans
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  • 65
    Publication Date: 1995-12-15
    Description: Ubiquitin is a highly conserved polypeptide found in all eukaryotes. The major function of ubiquitin is to target proteins for complete or partial degradation by a multisubunit protein complex called the proteasome. Here, the Drosophila fat facets gene, which is required for the appropriate determination of particular cells in the fly eye, was shown to encode a ubiquitin-specific protease (Ubp), an enzyme that cleaves ubiquitin from ubiquitin-protein conjugates. The Fat facets protein (FAF) acts as a regulatory Ubp that prevents degradation of its substrate by the proteasome. Flies bearing fat facets gene mutations were used to show that a Ubp is cell type--and substrate-specific and a regulator of cell fate decisions in a multicellular organism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Y -- Baker, R T -- Fischer-Vize, J A -- New York, N.Y. -- Science. 1995 Dec 15;270(5243):1828-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Texas, Austin 78712, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8525378" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; *Cell Differentiation/genetics ; Cysteine/metabolism ; Drosophila/embryology/enzymology/genetics ; Endopeptidases/genetics/*metabolism ; Escherichia coli ; Eye/embryology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligodeoxyribonucleotides ; Recombinant Fusion Proteins/genetics/metabolism ; Ubiquitins/*metabolism ; beta-Galactosidase/genetics
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  • 66
    Publication Date: 1995-02-24
    Description: The periods of circadian clocks are relatively temperature-insensitive. Indeed, the perL mutation in the Drosophila melanogaster period gene, a central component of the clock, affects temperature compensation as well as period length. The per protein (PER) contains a dimerization domain (PAS) within which the perL mutation is located. Amino acid substitutions at the perL position rendered PER dimerization temperature-sensitive. In addition, another region of PER interacted with PAS, and the perL mutation enhanced this putative intramolecular interaction, which may compete with PAS-PAS intermolecular interactions. Therefore, temperature compensation of circadian period in Drosophila may be due in part to temperature-independent PER activity, which is based on competition between inter- and intramolecular interactions with similar temperature coefficients.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Z J -- Curtin, K D -- Rosbash, M -- GM-33205/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1169-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Brandeis University, Department of Biology, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855598" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Biological Clocks ; *Circadian Rhythm ; Drosophila Proteins ; Drosophila melanogaster/genetics/*physiology ; Gene Expression Regulation ; Genes, Insect ; Molecular Sequence Data ; Nuclear Proteins/chemistry/genetics/*metabolism ; Period Circadian Proteins ; Point Mutation ; Temperature
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  • 67
    Publication Date: 1995-08-04
    Description: Phosphoinositide-3 kinase activity is implicated in diverse cellular responses triggered by mammalian cell surface receptors and in the regulation of protein sorting in yeast. Receptors with intrinsic and associated tyrosine kinase activity recruit heterodimeric phosphoinositide-3 kinases that consist of p110 catalytic subunits and p85 adaptor molecules containing Src homology 2 (SH2) domains. A phosphoinositide-3 kinase isotype, p110 gamma, was cloned and characterized. The p110 gamma enzyme was activated in vitro by both the alpha and beta gamma subunits of heterotrimeric guanosine triphosphate (GTP)-binding proteins (G proteins) and did not interact with p85. A potential pleckstrin homology domain is located near its amino terminus. The p110 gamma isotype may link signaling through G protein-coupled receptors to the generation of phosphoinositide second messengers phosphorylated in the D-3 position.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stoyanov, B -- Volinia, S -- Hanck, T -- Rubio, I -- Loubtchenkov, M -- Malek, D -- Stoyanova, S -- Vanhaesebroeck, B -- Dhand, R -- Nurnberg, B -- New York, N.Y. -- Science. 1995 Aug 4;269(5224):690-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Research Unit in Growth Factor Signal Transduction, Medical Faculty, University of Jena, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624799" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Cloning, Molecular ; Enzyme Activation ; GTP-Binding Proteins/*physiology ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Humans ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositols/metabolism ; Phosphotransferases (Alcohol Group Acceptor)/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Substrate Specificity ; Tumor Cells, Cultured
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  • 68
    Publication Date: 1995-01-27
    Description: Lamellar ichthyosis is a severe congenital skin disorder characterized by generalized large scales and variable redness. Affected individuals in three families exhibited drastically reduced keratinocyte transglutaminase (TGK) activity. In two of these families, expression of TGK transcripts was diminished or abnormal and no TGK protein was detected. Homozygous or compound heterozygous mutations of the TGK gene were identified in all families. These data suggest that defects in TGK cause lamellar ichthyosis and that intact cross-linkage of cornified cell envelopes is required for epidermal tissue homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huber, M -- Rettler, I -- Bernasconi, K -- Frenk, E -- Lavrijsen, S P -- Ponec, M -- Bon, A -- Lautenschlager, S -- Schorderet, D F -- Hohl, D -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):525-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Dermatology, Centre Hospitalier Universitaire Vandois (CHUV), Hopital de Beaumont, Lausanne, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824952" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Membrane/metabolism ; Cells, Cultured ; Codon ; Female ; Gene Deletion ; Genetic Linkage ; Heterozygote ; Homozygote ; Humans ; Ichthyosis, Lamellar/enzymology/*genetics ; Introns ; Keratinocytes/*enzymology/ultrastructure ; Male ; Membrane Proteins/metabolism ; Molecular Sequence Data ; Mutation ; Pedigree ; Point Mutation ; Protein Precursors/metabolism ; Transglutaminases/*genetics/metabolism
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  • 69
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):773-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638587" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoimmune Diseases/etiology ; Clinical Trials as Topic ; Estrogens/*physiology ; Female ; Genetic Predisposition to Disease ; Genitalia, Female/physiology ; Gonadal Steroid Hormones/*physiology ; Humans ; Immune System/*physiology ; Infection/immunology ; Male ; Menopause ; *Menstrual Cycle
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  • 70
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-06-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1995 Jun 9;268(5216):1424-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7770766" target="_blank"〉PubMed〈/a〉
    Keywords: Anthropology, Physical/*legislation & jurisprudence ; Archaeology/*legislation & jurisprudence ; *Culture ; Humans ; Indians, North American ; Israel ; Oceanic Ancestry Group ; Tasmania ; United States
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  • 71
    Publication Date: 1995-12-22
    Description: Reliable germline transformation is required for molecular studies and ultimately for genetic control of economically important insects, such as the Mediterranean fruit fly (medfly) Ceratitis capitata. A prerequisite for the establishment and maintenance of transformant lines is selectable or phenotypically dominant markers. To this end, a complementary DNA clone derived from the medfly white gene was isolated, which showed substantial similarity to white genes in Drosophila melanogaster and other Diptera. It is correlated with a spontaneous mutation causing white eyes in the medfly and can be used to restore partial eye color in transgenic Drosophila carrying a null mutation in the endogenous white gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zwiebel, L J -- Saccone, G -- Zacharopoulou, A -- Besansky, N J -- Favia, G -- Collins, F H -- Louis, C -- Kafatos, F C -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):2005-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533095" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Base Sequence ; Cloning, Molecular ; Diptera/chemistry/*genetics ; *Drosophila Proteins ; Drosophila melanogaster/genetics ; Eye Color/genetics ; Eye Proteins/chemistry/*genetics ; *Genes, Insect ; Genetic Markers ; Insect Hormones/chemistry/genetics ; Molecular Sequence Data ; Mutation ; Phenotype ; Sequence Alignment ; *Transformation, Genetic
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  • 72
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-01-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Root-Bernstein, R S -- New York, N.Y. -- Science. 1995 Jan 13;267(5195):159-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809617" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*etiology/virology ; HIV/*pathogenicity ; HIV Infections/*virology ; Humans ; T-Lymphocytopenia, Idiopathic CD4-Positive/etiology
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  • 73
    Publication Date: 1995-10-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hudson, K L -- Rothenberg, K H -- Andrews, L B -- Kahn, M J -- Collins, F S -- New York, N.Y. -- Science. 1995 Oct 20;270(5235):391-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569991" target="_blank"〉PubMed〈/a〉
    Keywords: Federal Government ; Genetic Diseases, Inborn ; *Genetics, Medical ; Government Regulation ; Guidelines as Topic ; *Health Care Reform ; Health Services Accessibility ; Human Genome Project ; Humans ; *Insurance Selection Bias ; *Insurance, Health/legislation & jurisprudence ; *Medically Uninsured ; United States
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  • 74
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-11-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allison, J P -- Krummel, M F -- New York, N.Y. -- Science. 1995 Nov 10;270(5238):932-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481795" target="_blank"〉PubMed〈/a〉
    Keywords: Abatacept ; Animals ; Antigens, CD ; Antigens, CD28/*immunology ; Antigens, CD80/immunology ; Antigens, Differentiation/*immunology ; CTLA-4 Antigen ; Down-Regulation ; Humans ; *Immunoconjugates ; *Lymphocyte Activation ; Mice ; Mice, Knockout ; Receptors, Antigen, T-Cell/immunology ; T-Lymphocytes/*immunology
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  • 75
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-10-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rose, S P -- New York, N.Y. -- Science. 1995 Oct 20;270(5235):362-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569986" target="_blank"〉PubMed〈/a〉
    Keywords: *Aggression ; Animals ; *Behavior, Animal ; Humans ; Male ; Mice ; Mice, Transgenic ; Monoamine Oxidase/*deficiency/genetics
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  • 76
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-05-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1995 May 19;268(5213):974-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754392" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ape Diseases/epidemiology/transmission/*virology ; Cote d'Ivoire/epidemiology ; Disease Outbreaks/*veterinary ; Disease Reservoirs ; *Ebolavirus ; Hemorrhagic Fevers, Viral/epidemiology/transmission/*veterinary ; Humans ; Pan troglodytes/*virology ; Seasons ; Zoonoses
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  • 77
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-01-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strohman, R C -- New York, N.Y. -- Science. 1995 Jan 13;267(5195):157-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809615" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*etiology/virology ; HIV/*pathogenicity ; Humans
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  • 78
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-06-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, J -- Heerdt, B -- Augenlicht, L -- New York, N.Y. -- Science. 1995 Jun 16;268(5217):1552.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7777846" target="_blank"〉PubMed〈/a〉
    Keywords: *Alleles ; Chimera ; Colorectal Neoplasms, Hereditary Nonpolyposis/*genetics ; DNA Repair ; Humans ; *Mutation ; *Stem Cells
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  • 79
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-02-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huete-Perez, J A -- New York, N.Y. -- Science. 1995 Feb 10;267(5199):774-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7846517" target="_blank"〉PubMed〈/a〉
    Keywords: Humans ; International Cooperation ; Nicaragua ; *Research Support as Topic ; Technology Transfer
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  • 80
    Publication Date: 1995-12-22
    Description: A physical map has been constructed of the human genome containing 15,086 sequence-tagged sites (STSs), with an average spacing of 199 kilobases. The project involved assembly of a radiation hybrid map of the human genome containing 6193 loci and incorporated a genetic linkage map of the human genome containing 5264 loci. This information was combined with the results of STS-content screening of 10,850 loci against a yeast artificial chromosome library to produce an integrated map, anchored by the radiation hybrid and genetic maps. The map provides radiation hybrid coverage of 99 percent and physical coverage of 94 percent of the human genome. The map also represents an early step in an international project to generate a transcript map of the human genome, with more than 3235 expressed sequences localized. The STSs in the map provide a scaffold for initiating large-scale sequencing of the human genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hudson, T J -- Stein, L D -- Gerety, S S -- Ma, J -- Castle, A B -- Silva, J -- Slonim, D K -- Baptista, R -- Kruglyak, L -- Xu, S H -- Hu, X -- Colbert, A M -- Rosenberg, C -- Reeve-Daly, M P -- Rozen, S -- Hui, L -- Wu, X -- Vestergaard, C -- Wilson, K M -- Bae, J S -- Maitra, S -- Ganiatsas, S -- Evans, C A -- DeAngelis, M M -- Ingalls, K A -- Nahf, R W -- Horton, L T Jr -- Anderson, M O -- Collymore, A J -- Ye, W -- Kouyoumjian, V -- Zemsteva, I S -- Tam, J -- Devine, R -- Courtney, D F -- Renaud, M T -- Nguyen, H -- O'Connor, T J -- Fizames, C -- Faure, S -- Gyapay, G -- Dib, C -- Morissette, J -- Orlin, J B -- Birren, B W -- Goodman, N -- Weissenbach, J -- Hawkins, T L -- Foote, S -- Page, D C -- Lander, E S -- HG00017/HG/NHGRI NIH HHS/ -- HG00098/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):1945-54.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead-MIT Center for Genome Research, Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533086" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; *Chromosome Mapping ; Chromosomes, Artificial, Yeast ; Databases, Factual ; Gene Expression ; Genetic Markers ; *Genome, Human ; *Human Genome Project ; Humans ; Hybrid Cells ; Polymerase Chain Reaction ; *Sequence Analysis, DNA ; *Sequence Tagged Sites
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  • 81
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-01-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lawler, A -- New York, N.Y. -- Science. 1995 Jan 20;267(5196):323.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824926" target="_blank"〉PubMed〈/a〉
    Keywords: *Astronauts ; Humans ; International Cooperation ; Male ; Russia ; *Space Flight ; *Spacecraft ; United States
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  • 82
    Publication Date: 1995-05-26
    Description: Receptor-mediated activation of heterotrimeric guanine nucleotide-binding proteins (G proteins) results in the dissociation of alpha from beta gamma subunits, thereby allowing both to regulate effectors. Little is known about the regions of effectors required for recognition of G beta gamma. A peptide encoding residues 956 to 982 of adenylyl cyclase 2 specifically blocked G beta gamma stimulation of adenylyl cyclase 2, phospholipase C-beta 3, potassium channels, and beta-adrenergic receptor kinase as well as inhibition of calmodulin-stimulated adenylyl cyclases, but had no effect on interactions between G beta gamma and G alpha o. Substitutions in this peptide identified a functionally important motif, Gln-X-X-Glu-Arg, that is also conserved in regions of potassium channels and beta-adrenergic receptor kinases that participate in G beta gamma interactions. Thus, the region defined by residues 956 to 982 of adenylyl cyclase 2 may contain determinants important for receiving signals from G beta gamma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, J -- DeVivo, M -- Dingus, J -- Harry, A -- Li, J -- Sui, J -- Carty, D J -- Blank, J L -- Exton, J H -- Stoffel, R H -- CA-44998/CA/NCI NIH HHS/ -- DK-37219/DK/NIDDK NIH HHS/ -- DK-38761/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 May 26;268(5214):1166-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Mount Sinai School of Medicine, City University of New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7761832" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclase Inhibitors ; Adenylyl Cyclases/*chemistry/metabolism ; Amino Acid Sequence ; Animals ; Cell Line ; Enzyme Activation/physiology ; GTP-Binding Proteins/chemistry/*physiology ; Guanosine Triphosphate/physiology ; In Vitro Techniques ; Molecular Sequence Data ; Peptide Fragments/chemical synthesis/chemistry/physiology ; Potassium Channels/physiology ; Rats ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptors, Adrenergic, beta/metabolism ; Signal Transduction/physiology ; Structure-Activity Relationship ; Type C Phospholipases/metabolism
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  • 83
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-11-24
    Description: Two-dimensional deconvolution techniques are used here to reconstruct age-specific human immunodeficiency virus (HIV) infection rates in the United States from surveillance data on acquired immunodeficiency syndrome (AIDS). This approach suggests that 630,000 to 897,000 adults and adolescents in the United States were living with HIV infection as of January 1993, including 107,000 to 150,000 women. The estimated incidence of HIV infection declined markedly over time among white males, especially those older than 30 years. In contrast, HIV incidence appears to have remained relatively constant among women and minorities. As of January 1993, prevalence was highest among young adults in their late twenties and thirties and among minorities. An estimated 3 percent of black men and 1 percent of black women in their thirties were living with HIV infection as of that date. If infection rates remain at these levels, HIV must be considered as endemic in the United States.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosenberg, P S -- New York, N.Y. -- Science. 1995 Nov 24;270(5240):1372-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Cancer Institute, Rockville, MD 20852-4910, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481828" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*epidemiology ; Adolescent ; Adult ; African Americans/statistics & numerical data ; Age Distribution ; *Disease Outbreaks ; European Continental Ancestry Group/statistics & numerical data ; Female ; HIV Infections/*epidemiology ; Hispanic Americans/statistics & numerical data ; Humans ; Incidence ; Male ; Middle Aged ; Models, Statistical ; Prevalence ; Sex Distribution ; United States/epidemiology
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  • 84
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-04-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fischman, J -- Gibbons, A -- Culotta, E -- New York, N.Y. -- Science. 1995 Apr 21;268(5209):364-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716536" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthropology ; Behavior ; Female ; Fossils ; Genetic Variation ; Haplorhini/physiology ; Hominidae/anatomy & histology ; Humans ; Humerus/anatomy & histology ; Labor, Obstetric ; Male ; Melanesia ; Pregnancy
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  • 85
    Publication Date: 1995-07-28
    Description: Human papillomaviruses (HPVs) are associated with the majority of cervical cancers and encode a transforming protein, E6, that interacts with the tumor suppressor protein p53. Because E6 has p53-independent transforming activity, the yeast two-hybrid system was used to search for other E6-binding proteins. One such protein, E6BP, interacted with cancer-associated HPV E6 and with bovine papillomavirus type 1 (BPV-1) E6. The transforming activity of BPV-1 E6 mutants correlated with their E6BP-binding ability. E6BP is identical to a putative calcium-binding protein, ERC-55, that appears to be localized in the endoplasmic reticulum.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, J J -- Reid, C E -- Band, V -- Androphy, E J -- R01CA44174/CA/NCI NIH HHS/ -- R29CA56803/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 28;269(5223):529-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Dermatology, New England Medical Center, Boston, MA, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624774" target="_blank"〉PubMed〈/a〉
    Keywords: Bovine papillomavirus 1/physiology ; Calcium-Binding Proteins/analysis/*metabolism ; Cell Transformation, Viral ; Cells, Cultured ; Endoplasmic Reticulum/chemistry ; HeLa Cells ; Humans ; Oncogene Proteins, Viral/analysis/*metabolism ; *Papillomaviridae ; Recombinant Fusion Proteins/metabolism ; *Repressor Proteins ; Ubiquitin-Protein Ligases ; Viral Proteins/metabolism
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  • 86
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-09-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altschuler, E L -- Lades, M -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1451-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660132" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallography, X-Ray ; Glycine/*chemistry ; Molecular Sequence Data ; Protein Folding ; *Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/*chemistry
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  • 87
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-06-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1995 Jun 2;268(5215):1281.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7761849" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology ; CD4 Lymphocyte Count/economics/*methods ; Costs and Cost Analysis ; Humans
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  • 88
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-06-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fitzgerald, D J -- New York, N.Y. -- Science. 1995 Jun 30;268(5219):1920; author reply 1921-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604268" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*metabolism ; Amyloid beta-Peptides/*metabolism ; Copper/cerebrospinal fluid/metabolism ; Humans ; Iron/cerebrospinal fluid/metabolism ; Protein Binding ; Silicon/cerebrospinal fluid/metabolism ; Zinc/cerebrospinal fluid/*metabolism/pharmacology
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  • 89
    Publication Date: 1995-04-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ambroziak, J A -- Blackbourn, D J -- Herndier, B G -- Glogau, R G -- Gullett, J H -- McDonald, A R -- Lennette, E T -- Levy, J A -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):582-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725108" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocyte Subsets/virology ; DNA, Viral/*analysis ; HIV Infections/*complications ; Herpesviridae/*genetics ; Humans ; Leukocytes, Mononuclear/virology ; Male ; Saliva/virology ; Sarcoma, Kaposi/etiology/*virology ; Semen/virology ; Tumor Cells, Cultured
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  • 90
    Publication Date: 1995-11-17
    Description: In the yeast Saccharomyces cerevisiae, Ras regulates adenylate cyclase, which is essential for progression through the G1 phase of the cell cycle. However, even when the adenosine 3',5'-monophosphate (cAMP) pathway was bypassed, the double disruption of RAS1 and RAS2 resulted in defects in growth at both low and high temperatures. Furthermore, the simultaneous disruption of RAS1, RAS2, and the RAS-related gene RSR1 was lethal at any temperature. The triple-disrupted cells were arrested late in the mitotic (M) phase, which was accompanied by an accumulation of cells with divided chromosomes and sustained histone H1 kinase activity. The lethality of the triple disruption was suppressed by the multicopies of CDC5, CDC15, DBF2, SPO12, and TEM1, all of which function in the completion of the M phase. Mammalian ras also suppressed the lethality, which suggests that a similar signaling pathway exists in higher eukaryotes. These results demonstrate that S. cerevisiae Ras functions in the completion of the M phase in a manner independent of the Ras-cAMP pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morishita, T -- Mitsuzawa, H -- Nakafuku, M -- Nakamura, S -- Hattori, S -- Anraku, Y -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1213-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biochemistry and Cellular Biology, National Institute of Neuroscience, Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502049" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/genetics/metabolism ; Fungal Proteins/*genetics/physiology ; GTP Phosphohydrolases/genetics/physiology ; Genes, Fungal ; Genes, Suppressor ; *Genes, ras ; *Mitosis ; Mutation ; Phenotype ; Saccharomyces cerevisiae/*cytology/genetics/growth & development ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Temperature ; *rab GTP-Binding Proteins ; ras Proteins/*genetics/physiology
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  • 91
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-12-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moriwaki, K -- Iida, S -- Kinoshita, M -- New York, N.Y. -- Science. 1995 Dec 15;270(5243):1744-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8525358" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Desiccation ; Fetal Blood ; *Genome, Human ; Humans ; Infant ; Infant, Newborn ; Japan ; Preservation, Biological ; *Umbilical Cord
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  • 92
    Publication Date: 1995-03-10
    Description: CD40 is a receptor on the surface of B lymphocytes, the activation of which leads to B cell survival, growth, and differentiation. A yeast two-hybrid screen identified a gene, CRAF1, encoding a protein that interacts directly with the CD40 cytoplasmic tail through a region of similarity to the tumor necrosis factor-alpha (TNF-alpha) receptor-associated factors. Overexpression of a truncated CRAF1 gene inhibited CD40-mediated up-regulation of CD23. A region of CRAF1 was similar to the TNF-alpha receptor-associated factors TRAF1 and TRAF2 and so defined a shared TRAF-C domain that was necessary and sufficient for CD40 binding and homodimerization. The CRAF1 sequence also predicted a long amphipathic helix, a pattern of five zinc fingers, and a zinc ring finger. It is likely that other members of the TNF receptor superfamily use CRAF-related proteins in their signal transduction processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheng, G -- Cleary, A M -- Ye, Z S -- Hong, D I -- Lederman, S -- Baltimore, D -- 5-T32-GM07367/GM/NIGMS NIH HHS/ -- A122346/PHS HHS/ -- R01-CA55713/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Mar 10;267(5203):1494-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7533327" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD/*metabolism ; Antigens, CD40 ; Antigens, Differentiation, B-Lymphocyte/*metabolism ; Humans ; Mice ; Molecular Sequence Data ; Protein Structure, Secondary ; Proteins/chemistry/genetics/*physiology ; Receptors, IgE/metabolism ; Sequence Homology, Amino Acid ; *Signal Transduction ; TNF Receptor-Associated Factor 1 ; TNF Receptor-Associated Factor 2 ; TNF Receptor-Associated Factor 3 ; Up-Regulation ; Zinc Fingers
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  • 93
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-08-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lawler, A -- Stone, R -- New York, N.Y. -- Science. 1995 Aug 25;269(5227):1038, 1040-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7652549" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biotechnology ; Clinical Trials as Topic ; *Drug Approval/legislation & jurisprudence/organization & administration ; Humans ; Investigational New Drug Application ; United States ; United States Food and Drug Administration/*legislation & ; jurisprudence/organization & administration
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 94
    Publication Date: 1995-08-11
    Description: In the molecular scheme of living organisms, adenosine 3',5'-monophosphate (cyclic AMP or cAMP) has been a universal second messenger. In eukaryotic cells, the primary receptors for cAMP are the regulatory subunits of cAMP-dependent protein kinase. The crystal structure of a 1-91 deletion mutant of the type I alpha regulatory subunit was refined to 2.8 A resolution. Each of the two tandem cAMP binding domains provides an extensive network of hydrogen bonds that buries the cyclic phosphate and the ribose between two beta strands that are linked by a short alpha helix. Each adenine base stacks against an aromatic ring that lies outside the beta barrel. This structure provides a molecular basis for understanding how cAMP binds cooperatively to its receptor protein, thus mediating activation of the kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Su, Y -- Dostmann, W R -- Herberg, F W -- Durick, K -- Xuong, N H -- Ten Eyck, L -- Taylor, S S -- Varughese, K I -- GM07313/GM/NIGMS NIH HHS/ -- GM34921/GM/NIGMS NIH HHS/ -- RR01644/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):807-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla 92093-0654, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638597" target="_blank"〉PubMed〈/a〉
    Keywords: Affinity Labels ; Amino Acid Sequence ; Binding Sites ; Carrier Proteins/*chemistry/genetics/metabolism ; Computer Graphics ; Crystallization ; Crystallography, X-Ray ; Cyclic AMP/analogs & derivatives/*metabolism ; Cyclic AMP-Dependent Protein Kinases/*chemistry ; Enzyme Activation ; Hydrogen Bonding ; *Intracellular Signaling Peptides and Proteins ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 95
    Publication Date: 1995-11-03
    Description: The BRCA1 gene product was identified as a 220-kilodalton nuclear phosphoprotein in normal cells, including breast ductal epithelial cells, and in 18 of 20 tumor cell lines derived from tissues other than breast and ovary. In 16 of 17 breast and ovarian cancer lines and 17 of 17 samples of cells obtained from malignant effusions, however, BRCA1 localized mainly in cytoplasm. Absence of BRCA1 or aberrant subcellular location was also observed to a variable extent in histological sections of many breast cancer biopsies. These findings suggest that BRCA1 abnormalities may be involved in the pathogenesis of many breast cancers, sporadic as well as familial.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Y -- Chen, C F -- Riley, D J -- Allred, D C -- Chen, P L -- Von Hoff, D -- Osborne, C K -- Lee, W H -- CA58318/CA/NCI NIH HHS/ -- EY05758/EY/NEI NIH HHS/ -- P50CA58183/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):789-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Medicine/Institute of Biotechnology, University of Texas Health Science Center at San Antonio 78245, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481765" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; BRCA1 Protein ; Base Sequence ; Breast/*chemistry ; Breast Neoplasms/*chemistry/ultrastructure ; Cell Fractionation ; Cell Line ; Cell Nucleus/chemistry ; Cytoplasm/*chemistry ; Female ; Humans ; Male ; Molecular Sequence Data ; Mutation ; Neoplasm Proteins/*analysis/genetics/metabolism ; Neoplasms/chemistry/ultrastructure ; Ovarian Neoplasms/chemistry/ultrastructure ; Pleural Effusion, Malignant/chemistry/pathology ; Transcription Factors/*analysis/genetics/metabolism ; Tumor Cells, Cultured
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  • 96
    Publication Date: 1995-08-11
    Description: Cystic fibrosis transmembrane regulator (CFTR), the gene product that is mutated in cystic fibrosis (CF) patients, has a well-recognized function as a cyclic adenosine 3',5'-monophosphate (cAMP)-regulated chloride channel, but this property does not account for the abnormally high basal rate and cAMP sensitivity of sodium ion absorption in CF airway epithelia. Expression of complementary DNAs for rat epithelial Na+ channel (rENaC) alone in Madin Darby canine kidney (MDCK) epithelial cells generated large amiloride-sensitive sodium currents that were stimulated by cAMP, whereas coexpression of human CFTR with rENaC generated smaller basal sodium currents that were inhibited by cAMP. Parallel studies that measured regulation of sodium permeability in fibroblasts showed similar results. In CF airway epithelia, the absence of this second function of CFTR as a cAMP-dependent regulator likely accounts for abnormal sodium transport.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stutts, M J -- Canessa, C M -- Olsen, J C -- Hamrick, M -- Cohn, J A -- Rossier, B C -- Boucher, R C -- CFF R026/PHS HHS/ -- HL 34322/HL/NHLBI NIH HHS/ -- HL 42384/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):847-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cystic Fibrosis/Pulmonary Research and Treatment Center, University of North Carolina at Chapel Hill 27599-7020, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7543698" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Absorption ; Amiloride/pharmacology ; Animals ; Cell Line ; Cell Membrane Permeability ; Chloride Channels/metabolism ; Cyclic AMP/*metabolism ; Cystic Fibrosis/*metabolism ; Cystic Fibrosis Transmembrane Conductance Regulator ; DNA, Complementary ; Dogs ; Humans ; Membrane Proteins/*metabolism ; Mice ; Patch-Clamp Techniques ; Rats ; Sodium/metabolism ; Sodium Channels/*metabolism ; Transfection
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  • 97
    Publication Date: 1995-06-23
    Description: The rate-limiting step in cholesterol biosynthesis in mammals is catalyzed by 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase, a four-electron oxidoreductase that converts HMG-CoA to mevalonate. The crystal structure of HMG-CoA reductase from Pseudomonas mevalonii was determined at 3.0 angstrom resolution by multiple isomorphous replacement. The structure reveals a tightly bound dimer that brings together at the subunit interface the conserved residues implicated in substrate binding and catalysis. These dimers are packed about a threefold crystallographic axis, forming a hexamer with 23 point group symmetry. Difference Fourier studies reveal the binding sites for the substrates HMG-CoA and reduced or oxidized nicotinamide adenine dinucleotide [NAD(H)] and demonstrate that the active sites are at the dimer interfaces. The HMG-CoA is bound by a domain with an unusual fold, consisting of a central alpha helix surrounded by a triangular set of walls of beta sheets and alpha helices. The NAD(H) is bound by a domain characterized by an antiparallel beta structure that defines a class of dinucleotide-binding domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lawrence, C M -- Rodwell, V W -- Stauffacher, C V -- AI 127713/AI/NIAID NIH HHS/ -- HL 47113/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Jun 23;268(5218):1758-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7792601" target="_blank"〉PubMed〈/a〉
    Keywords: Acyl Coenzyme A/metabolism ; Amino Acid Sequence ; Binding Sites ; Computer Graphics ; Crystallography, X-Ray ; Fourier Analysis ; Hydroxymethylglutaryl CoA Reductases/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; NAD/metabolism ; Protein Folding ; Protein Structure, Secondary ; Pseudomonas/*enzymology
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  • 98
    Publication Date: 1995-05-05
    Description: After germinal center B cells undergo somatic mutation and antigen selection, they become either memory B cells or plasma cells, but the signal requirements that control entry into either pathway have been unclear. When purified human germinal center cells were cultured with interleukin-2, interleukin-10, and cells expressing CD40 ligand, cells with characteristics of memory B cells were generated. Removal of CD40 ligand from the system resulted in terminal differentiation of germinal center B cells into cells with the characteristics of plasma cells. These results indicate that CD40 ligand directs the differentiation of germinal center B cells toward memory B cells rather than toward plasma cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arpin, C -- Dechanet, J -- Van Kooten, C -- Merville, P -- Grouard, G -- Briere, F -- Banchereau, J -- Liu, Y J -- New York, N.Y. -- Science. 1995 May 5;268(5211):720-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Schering-Plough, Laboratory for Immunological Research, Dardilly, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7537388" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-ribosyl Cyclase ; Antigens, CD/analysis ; Antigens, CD20 ; Antigens, CD38 ; Antigens, Differentiation/analysis ; Antigens, Differentiation, B-Lymphocyte/analysis ; B-Lymphocyte Subsets/*immunology ; CD40 Ligand ; Cell Differentiation/*immunology ; Cell Division/immunology ; Cells, Cultured ; Humans ; Immunoglobulin Isotypes/analysis ; Immunologic Memory/immunology ; Immunophenotyping ; Lymph Nodes/cytology ; Membrane Glycoproteins/immunology ; Plasma Cells/*immunology
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  • 99
    Publication Date: 1995-05-12
    Description: The yeast non-Mendelian factor [psi+] has been suggested to be a self-modified protein analogous to mammalian prions. Here it is reported that an intermediate amount of the chaperone protein Hsp104 was required for the propagation of the [psi+] factor. Over-production or inactivation of Hsp104 caused the loss of [psi+]. These results suggest that chaperone proteins play a role in prion-like phenomena, and that a certain level of chaperone expression can cure cells of prions without affecting viability. This may lead to antiprion treatments that involve the alteration of chaperone amounts or activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chernoff, Y O -- Lindquist, S L -- Ono, B -- Inge-Vechtomov, S G -- Liebman, S W -- New York, N.Y. -- Science. 1995 May 12;268(5212):880-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Illinois, Chicago 60607-7020, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754373" target="_blank"〉PubMed〈/a〉
    Keywords: Fungal Proteins/*biosynthesis/genetics/physiology ; Gene Expression ; Heat-Shock Proteins/genetics/*physiology ; Mutation ; Prions/*biosynthesis ; Saccharomyces cerevisiae/genetics/*physiology ; *Saccharomyces cerevisiae Proteins ; Suppression, Genetic
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  • 100
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-09-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1995 Sep 29;269(5232):1808-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569909" target="_blank"〉PubMed〈/a〉
    Keywords: Antisocial Personality Disorder/*genetics ; *Crime ; Eugenics ; *Genetic Research ; *Genetics, Behavioral ; Humans ; Prejudice ; Social Environment ; *Violence
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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