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  • Male  (403)
  • Protein Conformation  (228)
  • American Association for the Advancement of Science (AAAS)  (629)
  • American Association of Petroleum Geologists (AAPG)
  • Elsevier
  • 1990-1994  (629)
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  • American Association for the Advancement of Science (AAAS)  (629)
  • American Association of Petroleum Geologists (AAPG)
  • Elsevier
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  • 101
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-01-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mann, C C -- New York, N.Y. -- Science. 1994 Jan 28;263(5146):470-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8290954" target="_blank"〉PubMed〈/a〉
    Keywords: *Bioethics ; Child ; Disclosure ; Federal Government ; Female ; History, 20th Century ; Human Experimentation/*history ; Humans ; *Informed Consent ; Male ; Parental Consent ; Patient Selection ; Plutonium/toxicity ; Prisoners ; *Radiation Injuries ; Radioisotopes/*administration & dosage ; Research Subjects ; Risk Assessment ; Testis/radiation effects ; United States
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 102
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-11-11
    Description: In primates, the premotor cortex is involved in the sensory guidance of movement. Many neurons in ventral premotor cortex respond to visual stimuli in the space adjacent to the hand or arm. These visual receptive fields were found to move when the arm moved but not when the eye moved; that is, they are in arm-centered, not retinocentric, coordinates. Thus, they provide a representation of space near the body that may be useful for the visual control of reaching.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Graziano, M S -- Yap, G S -- Gross, C G -- MH 19420/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1994 Nov 11;266(5187):1054-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychology, Princeton University, NJ 08544.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973661" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Macaca fascicularis ; Male ; Neurons/*physiology ; Prefrontal Cortex/cytology/*physiology ; Space Perception/*physiology ; Visual Fields/*physiology
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  • 103
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-09-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Katz, S L -- Gellin, B G -- New York, N.Y. -- Science. 1994 Sep 2;265(5177):1391-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8073281" target="_blank"〉PubMed〈/a〉
    Keywords: Disease Outbreaks/prevention & control ; Female ; Humans ; Immunity, Maternally-Acquired ; *Immunization Programs ; Infant ; Male ; Measles/epidemiology/immunology/*prevention & control ; *Measles Vaccine/adverse effects/immunology ; Measles virus/genetics/immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 104
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aldhous, P -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1484-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985014" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoantibodies/biosynthesis ; Chorionic Gonadotropin/*immunology ; Clinical Trials as Topic ; *Contraception, Immunologic ; Contraceptive Agents, Male ; Egg Proteins/immunology ; Female ; Fertilization ; Humans ; L-Lactate Dehydrogenase/immunology ; Male ; Membrane Glycoproteins/immunology ; *Receptors, Cell Surface ; Spermatozoa/immunology ; T-Lymphocytes/immunology ; *Vaccines
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  • 105
    Publication Date: 1994-12-23
    Description: A synthetic combinatorial library containing 52,128,400 D-amino acid hexapeptides was used to identify a ligand for the mu opioid receptor. The peptide, Ac-rfwink-NH2, bears no resemblance to any known opioid peptide. Simulations using molecular dynamics, however, showed that three amino acid moieties have the same spatial orientation as the corresponding pharmacophoric groups of the opioid peptide PLO17. Ac-rfwink-NH2 was shown to be a potent agonist at the mu receptor and induced long-lasting analgesia in mice. Analgesia produced by intraperitoneally administered Ac-rfwink-NH2 was blocked by intracerebroventricular administration of naloxone, demonstrating that this peptide may cross the blood-brain barrier.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dooley, C T -- Chung, N N -- Wilkes, B C -- Schiller, P W -- Bidlack, J M -- Pasternak, G W -- Houghten, R A -- DA-000138/DA/NIDA NIH HHS/ -- DA-02615/DA/NIDA NIH HHS/ -- DA-03742/DA/NIDA NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):2019-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Torrey Pines Institute for Molecular Studies, San Diego, CA 92121.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7801131" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Analgesics/chemistry/metabolism/*pharmacology ; Animals ; Brain/metabolism ; Dose-Response Relationship, Drug ; Endorphins/pharmacology ; Enkephalin, Ala(2)-MePhe(4)-Gly(5)- ; Enkephalin, D-Penicillamine (2,5)- ; Enkephalins/metabolism ; Guinea Pigs ; Injections, Intraventricular ; Male ; Mice ; Models, Molecular ; Molecular Sequence Data ; Naloxone/administration & dosage/pharmacology ; Opioid Peptides/chemistry/metabolism/*pharmacology ; Pain Measurement ; Protein Conformation ; Rats ; Receptors, Opioid, mu/agonists/metabolism ; Stereoisomerism
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  • 106
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-06-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nowak, R -- New York, N.Y. -- Science. 1994 Jun 10;264(5165):1538-41.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8202708" target="_blank"〉PubMed〈/a〉
    Keywords: Biomarkers ; Editorial Policies ; Education, Medical, Continuing ; Federal Government ; Female ; Government Regulation ; Humans ; Male ; Meta-Analysis as Topic ; National Institutes of Health (U.S.) ; Random Allocation ; Randomized Controlled Trials as Topic/*standards/statistics & numerical data ; Scientific Misconduct ; United States ; United States Food and Drug Administration
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  • 107
    Publication Date: 1994-12-09
    Description: The crystal structure of a 27-kilodalton methylcobalamin-containing fragment of methionine synthase from Escherichia coli was determined at 3.0 A resolution. This structure depicts cobalamin-protein interactions and reveals that the corrin macrocycle lies between a helical amino-terminal domain and an alpha/beta carboxyl-terminal domain that is a variant of the Rossmann fold. Methylcobalamin undergoes a conformational change on binding the protein; the dimethylbenzimidazole group, which is coordinated to the cobalt in the free cofactor, moves away from the corrin and is replaced by a histidine contributed by the protein. The sequence Asp-X-His-X-X-Gly, which contains this histidine ligand, is conserved in the adenosylcobalamin-dependent enzymes methylmalonyl-coenzyme A mutase and glutamate mutase, suggesting that displacement of the dimethylbenzimidazole will be a feature common to many cobalamin-binding proteins. Thus the cobalt ligand, His759, and the neighboring residues Asp757 and Ser810, may form a catalytic quartet, Co-His-Asp-Ser, that modulates the reactivity of the B12 prosthetic group in methionine synthase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Drennan, C L -- Huang, S -- Drummond, J T -- Matthews, R G -- Lidwig, M L -- GM08570/GM/NIGMS NIH HHS/ -- GM16429/GM/NIGMS NIH HHS/ -- GM24908/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1669-74.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biophysics Research Division, University of Michigan, Ann Arbor 48109-1055.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7992050" target="_blank"〉PubMed〈/a〉
    Keywords: 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase/*chemistry/metabolism ; Amino Acid Isomerases/chemistry ; Amino Acid Sequence ; Benzimidazoles ; Catalysis ; Computer Graphics ; Crystallography, X-Ray ; Electron Spin Resonance Spectroscopy ; Escherichia coli/*enzymology ; Histidine/metabolism ; *Intramolecular Transferases ; Ligands ; Methylation ; Methylmalonyl-CoA Mutase/chemistry ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Vitamin B 12/*analogs & derivatives/chemistry/metabolism
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  • 108
    Publication Date: 1994-09-09
    Description: The transcription factor PU.1 is a hematopoietic-specific member of the ets family. Mice carrying a mutation in the PU.1 locus were generated by gene targeting. Homozygous mutant embryos died at a late gestational stage. Mutant embryos produced normal numbers of megakaryocytes and erythroid progenitors, but some showed an impairment of erythroblast maturation. An invariant consequence of the mutation was a multilineage defect in the generation of progenitors for B and T lymphocytes, monocytes, and granulocytes. Thus, the developmental programs of lymphoid and myeloid lineages require a common genetic function likely acting at the level of a multipotential progenitor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, E W -- Simon, M C -- Anastasi, J -- Singh, H -- F32 AI08933/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 9;265(5178):1573-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Cell Biology, Howard Hughes Medical Institute, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8079170" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA-Binding Proteins/genetics/*physiology ; Erythropoiesis ; Female ; Gene Rearrangement ; *Hematopoiesis ; Hematopoietic Stem Cells/cytology/*physiology ; Lymphocytes/cytology/physiology ; Macrophages/cytology/physiology ; Male ; Mice ; Mice, Inbred C57BL ; Monocytes/cytology/physiology ; Mutation ; Neutrophils/cytology/physiology ; Retroviridae Proteins, Oncogenic ; Transcription Factors/genetics/*physiology
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  • 109
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-04-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seachrist, L -- New York, N.Y. -- Science. 1994 Apr 15;264(5157):340.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8153611" target="_blank"〉PubMed〈/a〉
    Keywords: Budgets ; Female ; Humans ; Male ; *National Institutes of Health (U.S.) ; *Prejudice ; *Research Support as Topic ; United States ; *Women, Working
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  • 110
    Publication Date: 1994-03-18
    Description: P element-induced chromosome breakage on the X chromosome of Drosophila melanogaster was repaired six times more frequently when a homologous template was located anywhere on the X chromosome rather than on an autosome. Cis-trans comparisons confirmed that recombinational repair was more frequent when the interacting sequences were physically connected. These results suggest that the search for homology between the broken ends and a matching template sequence occurs preferentially in the cis configuration. This cis advantage operates over more than 15 megabases of DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Engels, W R -- Preston, C R -- Johnson-Schlitz, D M -- GM30948/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Mar 18;263(5153):1623-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genetics Department, University of Wisconsin, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128250" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Chromosomes ; DNA/chemistry/*genetics ; *DNA Repair ; DNA Transposable Elements ; Drosophila melanogaster/*genetics ; Female ; *Gene Conversion ; Male ; Molecular Sequence Data ; *Sequence Homology, Nucleic Acid ; Templates, Genetic ; X Chromosome
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  • 111
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, R F -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1489.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985016" target="_blank"〉PubMed〈/a〉
    Keywords: *Contraception ; *Contraceptive Agents ; Drug Industry ; Embryo, Mammalian ; Female ; Fertilization ; Financing, Government ; Humans ; Male ; *Research ; Research Support as Topic ; United States ; World Health Organization
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  • 112
    Publication Date: 1994-02-25
    Description: The hypothesis that oxygen free radicals are causally involved in the aging process was tested by a study of the effects of simultaneous overexpression of copper-zinc superoxide dismutase and catalase. As compared to diploid controls, transgenic flies carrying three copies of each of these genes exhibited as much as a one-third extension of life-span, a longer mortality rate doubling time, a lower amount of protein oxidative damage, and a delayed loss in physical performance. Results provide direct support for the free radical hypothesis of aging.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Orr, W C -- Sohal, R S -- R01AG8459/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 25;263(5150):1128-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Southern Methodist University, Dallas, TX 75275.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8108730" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/genetics/*physiology ; Animals ; Animals, Genetically Modified ; Catalase/genetics/*metabolism ; Drosophila melanogaster/enzymology/genetics/*physiology ; Female ; Gene Expression ; Longevity ; Male ; Oxidation-Reduction ; Oxygen Consumption ; Proteins/metabolism ; Reactive Oxygen Species/metabolism ; Superoxide Dismutase/genetics/*metabolism
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  • 113
    Publication Date: 1994-10-14
    Description: Interval mapping of data from two independent samples of sib pairs, at least one member of whom was reading disabled, revealed evidence for a quantitative trait locus (QTL) on chromosome 6. Results obtained from analyses of reading performance from 114 sib pairs genotyped for DNA markers localized the QTL to 6p21.3. Analyses of corresponding data from an independent sample of 50 dizygotic twin pairs provided evidence for linkage to the same region. In combination, the replicate samples yielded a chi 2 value of 16.73 (P = 0.0002). Examination of twin and kindred siblings with more extreme deficits in reading performance yielded even stronger evidence for a QTL (chi 2 = 27.35, P 〈 0.00001). The position of the QTL was narrowly defined with a 100:1 confidence interval to a 2-centimorgan region within the human leukocyte antigen complex.〈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 -- HD-11681/HD/NICHD NIH HHS/ -- HD-27802/HD/NICHD NIH HHS/ -- HG-00085/HG/NHGRI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Oct 14;266(5183):276-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Health Sciences Program, SRI International, Menlo Park, CA 94025.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939663" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Alleles ; Child ; Chromosome Mapping ; *Chromosomes, Human, Pair 6 ; Diseases in Twins/*genetics ; Dyslexia/*genetics ; Female ; Genetic Linkage ; Genetic Markers ; HLA Antigens/genetics ; Humans ; Major Histocompatibility Complex ; Male ; Nuclear Family ; Regression Analysis ; Twins, Dizygotic
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  • 114
    Publication Date: 1994-06-17
    Description: An approximately 5000-year-old mummified human body was recently found in the Tyrolean Alps. The DNA from tissue samples of this Late Neolithic individual, the so-called "Ice Man," has been extracted and analyzed. The number of DNA molecules surviving in the tissue was on the order of 10 genome equivalents per gram of tissue, which meant the only multi-copy sequences could be analyzed. The degradation of the DNA made the enzymatic amplification of mitochondrial DNA fragments of more than 100 to 200 base pairs difficult. One DNA sequence of a hypervariable segment of the mitochondrial control region was determined independently in two different laboratories from internal samples of the body. This sequence showed that the mitochondrial type of the Ice Man fits into the genetic variation of contemporary Europeans and that it was most closely related to mitochondrial types determined from central and northern European populations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Handt, O -- Richards, M -- Trommsdorff, M -- Kilger, C -- Simanainen, J -- Georgiev, O -- Bauer, K -- Stone, A -- Hedges, R -- Schaffner, W -- New York, N.Y. -- Science. 1994 Jun 17;264(5166):1775-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Zoology, University of Munich, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8209259" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Austria ; Base Sequence ; Biological Evolution ; Bone and Bones/chemistry ; Connective Tissue/chemistry ; DNA, Mitochondrial/chemistry/*genetics ; Europe ; Freezing ; History, Ancient ; Hominidae/*genetics ; Humans ; Male ; Molecular Sequence Data ; *Mummies ; Muscles/chemistry ; Polymerase Chain Reaction ; Sequence Analysis, DNA ; Templates, Genetic
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  • 115
    Publication Date: 1994-01-21
    Description: The structure of the 52-amino acid DNA-binding domain of the prokaryotic Hin recombinase, complexed with a DNA recombination half-site, has been solved by x-ray crystallography at 2.3 angstrom resolution. The Hin domain consists of a three-alpha-helix bundle, with the carboxyl-terminal helix inserted into the major groove of DNA, and two flanking extended polypeptide chains that contact bases in the minor groove. The overall structure displays features resembling both a prototypical bacterial helix-turn-helix and the eukaryotic homeodomain, and in many respects is an intermediate between these two DNA-binding motifs. In addition, a new structural motif is seen: the six-amino acid carboxyl-terminal peptide of the Hin domain runs along the minor groove at the edge of the recombination site, with the peptide backbone facing the floor of the groove and side chains extending away toward the exterior. The x-ray structure provides an almost complete explanation for DNA mutant binding studies in the Hin system and for DNA specificity observed in the Hin-related family of DNA invertases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, J A -- Johnson, R C -- Dickerson, R E -- GM-31299/GM/NIGMS NIH HHS/ -- GM-38509/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jan 21;263(5145):348-55.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Institute, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8278807" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Composition ; Base Sequence ; Binding Sites ; Computer Graphics ; Crystallography, X-Ray ; DNA/chemistry/*metabolism ; DNA Nucleotidyltransferases/chemistry/*metabolism ; Helix-Loop-Helix Motifs ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; *Recombination, Genetic
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  • 116
    Publication Date: 1994-12-16
    Description: The three-dimensional structure of a Staphylococcus aureus superantigen, toxic shock syndrome toxin-1 (TSST-1), complexed with a human class II major histocompatibility molecule (DR1), was determined by x-ray crystallography. The TSST-1 binding site on DR1 overlaps that of the superantigen S. aureus enterotoxin B (SEB), but the two binding modes differ. Whereas SEB binds primarily off one edge of the peptide binding site of DR1, TSST-1 extends over almost one-half of the binding site and contacts both the flanking alpha helices of the histocompatibility antigen and the bound peptide. This difference suggests that the T cell receptor (TCR) would bind to TSST-1:DR1 very differently than to DR1:peptide or SEB:DR1. It also suggests that TSST-1 binding may be dependent on the peptide, though less so than TCR binding, providing a possible explanation for the inability of TSST-1 to competitively block SEB binding to all DR1 molecules on cells (even though the binding sites of TSST-1 and SEB on DR1 overlap almost completely) and suggesting the possibility that T cell activation by superantigen could be directed by peptide antigen.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, J -- Urban, R G -- Strominger, J L -- Wiley, D C -- New York, N.Y. -- Science. 1994 Dec 16;266(5192):1870-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Children's Hospital, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7997880" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacterial Toxins ; Binding Sites ; Crystallography, X-Ray ; Enterotoxins/*chemistry/metabolism ; HLA-DR1 Antigen/*chemistry/metabolism ; Humans ; Hydrogen Bonding ; Models, Molecular ; Protein Conformation ; Protein Structure, Secondary ; Receptors, Antigen, T-Cell/metabolism ; *Staphylococcus aureus ; Superantigens/*chemistry/metabolism
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  • 117
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-09-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1994 Sep 2;265(5177):1364-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8073268" target="_blank"〉PubMed〈/a〉
    Keywords: Carrier Proteins/*genetics ; *Chromosomes, Human, Pair 9 ; Cyclin-Dependent Kinase Inhibitor p16 ; Female ; Genes, Tumor Suppressor ; Humans ; Male ; Melanoma/*genetics ; Mutation ; Pedigree ; Tumor Cells, Cultured
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  • 118
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-08-12
    Description: Magnetic resonance imaging was used to examine the involvement of the dentate nucleus of the cerebellum in cognitive operations. All seven people examined displayed a large bilateral activation in the dentate during their attempts to solve a pegboard puzzle. The area activated was three to four times greater than that activated during simple movements of the pegs. These results provide support for the concept that the computational power of the cerebellum is applied not only to the control of movement but also to cognitive functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, S G -- Ugurbil, K -- Strick, P L -- NS24328/NS/NINDS NIH HHS/ -- RR08079/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 12;265(5174):949-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Radiology, University of Minnesota Medical School, Minneapolis 55455.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8052851" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Cerebellar Nuclei/anatomy & histology/*physiology ; Cognition/*physiology ; Eye Movements ; Humans ; Magnetic Resonance Imaging ; Male ; Psychomotor Performance
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  • 119
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-07-29
    Description: Human feet and toes provide a mechanism for changing the gear ratio of the ankle extensor muscles during a running step. A variable gear ratio could enhance muscle performance during constant-speed running by applying a more effective prestretch during landing, while maintaining the muscles near the high-efficiency or high-power portion of the force-velocity curve during takeoff. Furthermore, during acceleration, variable gearing may allow muscle contractile properties to remain optimized despite rapid changes in running speed. Forceplate and kinematic analyses of running steps show low gear ratios at touchdown that increase throughout the contact phase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carrier, D R -- Heglund, N C -- Earls, K D -- New York, N.Y. -- Science. 1994 Jul 29;265(5172):651-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolutionary Biology, Brown University, Providence, RI 02912.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8036513" target="_blank"〉PubMed〈/a〉
    Keywords: Acceleration ; Achilles Tendon/physiology ; Ankle Joint/physiology ; Biomechanical Phenomena ; Female ; Foot/physiology ; Humans ; Leg/*physiology ; Locomotion/*physiology ; Male ; Multivariate Analysis ; Muscles/*physiology ; Running/physiology ; Toes/physiology
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  • 120
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-07-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koshland, D E Jr -- New York, N.Y. -- Science. 1994 Jul 22;265(5171):455.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8036485" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; Humans ; Male ; *Spouse Abuse/legislation & jurisprudence/prevention & control ; United States
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  • 121
    Publication Date: 1994-06-03
    Description: Spinal muscular atrophies (SMAs) represent the second most common fatal autosomal recessive disorder after cystic fibrosis. Childhood spinal muscular atrophies are divided into severe (type I) and mild forms (types II and III). By a combination of genetic and physical mapping, a yeast artificial chromosome contig of the 5q13 region spanning the disease locus was constructed that showed the presence of low copy repeats in this region. Allele segregation was analyzed at the closest genetic loci detected by markers C212 and C272 in 201 SMA families. Inherited and de novo deletions were observed in nine unrelated SMA patients. Moreover, deletions were strongly suggested in at least 18 percent of SMA type I patients by the observation of marked heterozygosity deficiency for the loci studied. These results indicate that deletion events are statistically associated with the severe form of spinal muscular atrophy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Melki, J -- Lefebvre, S -- Burglen, L -- Burlet, P -- Clermont, O -- Millasseau, P -- Reboullet, S -- Benichou, B -- Zeviani, M -- Le Paslier, D -- New York, N.Y. -- Science. 1994 Jun 3;264(5164):1474-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite de Recherches sur les Handicaps Genetiques de l'Enfant, INSERM U-393, Hopital des Enfants-Malades, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7910982" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Chromosomes, Artificial, Yeast ; *Chromosomes, Human, Pair 5 ; Female ; *Gene Deletion ; Genetic Markers ; Humans ; Male ; Molecular Sequence Data ; Muscular Atrophy, Spinal/*genetics ; Polymerase Chain Reaction ; Polymorphism, Restriction Fragment Length ; Repetitive Sequences, Nucleic Acid ; Spinal Muscular Atrophies of Childhood/*genetics
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  • 122
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-04-29
    Description: Molecular investigations of evolutionary history are being used to study subjects as diverse as the epidemiology of acquired immune deficiency syndrome and the origin of life. These studies depend on accurate estimates of phylogeny. The performance of methods of phylogenetic analysis can be assessed by numerical simulation studies and by the experimental evolution of organisms in controlled laboratory situations. Both kinds of assessment indicate that existing methods are effective at estimating phylogenies over a wide range of evolutionary conditions, especially if information about substitution bias is used to provide differential weightings for character transformations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hillis, D M -- Huelsenbeck, J P -- Cunningham, C W -- New York, N.Y. -- Science. 1994 Apr 29;264(5159):671-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Texas, Austin 78712.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8171318" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage T7/*genetics ; Biological Evolution ; Computer Simulation ; Dentists ; Female ; *Genome, Viral ; HIV/*genetics ; HIV Envelope Protein gp120/genetics ; HIV Infections/microbiology/transmission ; Humans ; Infectious Disease Transmission, Professional-to-Patient ; Male ; Models, Biological ; *Phylogeny ; Probability
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  • 123
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-04-08
    Description: On the page of illustrations accompanying the review of Ann Shelby Blum's Picturing Nature (10 Dec., p. 1753), the caption for the illustration from Thomas Say's American Conchology (lower left) erroneously included the names of species not represented in the plate reproduced; all four specimens shown represent Paludina decisa.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wallace, M R -- New York, N.Y. -- Science. 1994 Apr 8;264(5156):188.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8146644" target="_blank"〉PubMed〈/a〉
    Keywords: Humans ; Male ; *Neurofibromatosis 1 ; *Proteus Syndrome ; *Terminology as Topic
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  • 124
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1648-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7992047" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*chemically induced/immunology ; Clinical Trials as Topic ; Female ; HIV Infections/drug therapy/mortality ; Humans ; Male ; Street Drugs/*adverse effects ; Zidovudine/*adverse effects/therapeutic use
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  • 125
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-09-30
    Description: Medical genetics was revolutionized during the 1980s by the application of genetic mapping to locate the genes responsible for simple Mendelian diseases. Most diseases and traits, however, do not follow simple inheritance patterns. Genetics have thus begun taking up the even greater challenge of the genetic dissection of complex traits. Four major approaches have been developed: linkage analysis, allele-sharing methods, association studies, and polygenic analysis of experimental crosses. This article synthesizes the current state of the genetic dissection of complex traits--describing the methods, limitations, and recent applications to biological problems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lander, E S -- Schork, N J -- HG00098/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 30;265(5181):2037-48.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8091226" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; *Chromosome Mapping ; Cloning, Molecular ; Crosses, Genetic ; Female ; Genetic Linkage ; Genetic Markers ; *Genetic Predisposition to Disease ; Genetics, Medical/*methods ; Genotype ; Humans ; Male ; Pedigree ; Phenotype ; Research Design
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  • 126
    Publication Date: 1994-10-07
    Description: A strong candidate for the 17q-linked BRCA1 gene, which influences susceptibility to breast and ovarian cancer, has been identified by positional cloning methods. Probable predisposing mutations have been detected in five of eight kindreds presumed to segregate BRCA1 susceptibility alleles. The mutations include an 11-base pair deletion, a 1-base pair insertion, a stop codon, a missense substitution, and an inferred regulatory mutation. The BRCA1 gene is expressed in numerous tissues, including breast and ovary, and encodes a predicted protein of 1863 amino acids. This protein contains a zinc finger domain in its amino-terminal region, but is otherwise unrelated to previously described proteins. Identification of BRCA1 should facilitate early diagnosis of breast and ovarian cancer susceptibility in some individuals as well as a better understanding of breast cancer biology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miki, Y -- Swensen, J -- Shattuck-Eidens, D -- Futreal, P A -- Harshman, K -- Tavtigian, S -- Liu, Q -- Cochran, C -- Bennett, L M -- Ding, W -- CA-48711/CA/NCI NIH HHS/ -- CA-54936/CA/NCI NIH HHS/ -- CA-55914/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Oct 7;266(5182):66-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Informatics, University of Utah Medical Center, Salt Lake City 84132.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7545954" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Alternative Splicing ; Amino Acid Sequence ; Animals ; BRCA1 Protein ; Breast Neoplasms/*genetics ; *Chromosomes, Human, Pair 17 ; Female ; *Genes, Tumor Suppressor ; Genetic Predisposition to Disease ; Germ-Line Mutation ; Haplotypes ; Humans ; Lod Score ; Male ; Molecular Sequence Data ; *Mutation ; Neoplasm Proteins/chemistry/*genetics/physiology ; Ovarian Neoplasms/*genetics ; Pedigree ; Phenotype ; Transcription Factors/chemistry/*genetics/physiology ; Zinc Fingers
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  • 127
    Publication Date: 1994-12-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steitz, T A -- Smerdon, S J -- Jager, J -- Joyce, C M -- GM28550/GM/NIGMS NIH HHS/ -- GM39546/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):2022-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7528445" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA Polymerase I/*chemistry/metabolism ; DNA-Directed RNA Polymerases/*chemistry/metabolism ; HIV Reverse Transcriptase ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; RNA-Directed DNA Polymerase/*chemistry/metabolism ; Viral Proteins
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  • 128
    Publication Date: 1994-02-18
    Description: L-Glutamate and norepinephrine are examples of a major excitatory neurotransmitter and a neuromodulator in the cerebral cortex, respectively. Little is known of how chemical signaling between the anatomically distinct chemical pathways occurs. Specific activation of the N-methyl-D-aspartate (NMDA) class of glutamate receptor in synaptosomal preparations from guinea pig cerebral cortex caused release of both of these chemicals, and this release was blocked by agents that inhibit nitric oxide (NO) production or remove NO from the extracellular space. Furthermore, neurotransmitter release correlated with cortical NO production after NMDA receptor stimulation. These results suggest that NO production and its extracellular movement may be links in the pathway from NMDA receptor activation to changes in chemical signaling in surrounding synaptic terminals in the cerebral cortex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Montague, P R -- Gancayco, C D -- Winn, M J -- Marchase, R B -- Friedlander, M J -- EY05116/EY/NEI NIH HHS/ -- EY06714/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 18;263(5149):973-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neurobiology Research Center, University of Alabama at Birmingham 35294-0021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7508638" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Oxidoreductases/antagonists & inhibitors ; Animals ; Arginine/analogs & derivatives/pharmacology ; Cerebral Cortex/drug effects/*metabolism ; Glutamates/*metabolism ; Glutamic Acid ; Guinea Pigs ; In Vitro Techniques ; Indazoles/pharmacology ; Male ; N-Methylaspartate/pharmacology ; Nitric Oxide/*metabolism ; Nitric Oxide Synthase ; Nitroarginine ; Norepinephrine/*metabolism ; Potassium Chloride/pharmacology ; Receptors, N-Methyl-D-Aspartate/*metabolism ; Synaptosomes/drug effects/*metabolism ; omega-N-Methylarginine
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  • 129
    Publication Date: 1994-10-07
    Description: Para-hydroxybenzoate hydroxylase inserts oxygen into substrates by means of the labile intermediate, flavin C(4a)-hydroperoxide. This reaction requires transient isolation of the flavin and substrate from the bulk solvent. Previous crystal structures have revealed the position of the substrate para-hydroxybenzoate during oxygenation but not how it enters the active site. In this study, enzyme structures with the flavin ring displaced relative to the protein were determined, and it was established that these or similar flavin conformations also occur in solution. Movement of the flavin appears to be essential for the translocation of substrates and products into the solvent-shielded active site during catalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gatti, D L -- Palfey, B A -- Lah, M S -- Entsch, B -- Massey, V -- Ballou, D P -- Ludwig, M L -- GM 11106/GM/NIGMS NIH HHS/ -- GM 16429/GM/NIGMS NIH HHS/ -- GM 20877/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Oct 7;266(5182):110-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of Michigan, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939628" target="_blank"〉PubMed〈/a〉
    Keywords: Benzoate 4-Monooxygenase ; Binding Sites ; Catalysis ; Computer Graphics ; Flavin-Adenine Dinucleotide/chemistry/metabolism ; Flavins/*chemistry/metabolism ; Hydrogen Bonding ; Mixed Function Oxygenases/*chemistry/metabolism ; Models, Molecular ; Molecular Conformation ; Oxidation-Reduction ; Parabens/metabolism ; Protein Conformation
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  • 130
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-08-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1994 Aug 26;265(5176):1172-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8066456" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA/*analysis/genetics ; DNA, Mitochondrial/analysis/genetics ; Fathers ; Female ; Genes ; Genetic Variation ; Hair/chemistry ; Male ; Pan troglodytes/classification/*genetics/psychology ; Social Behavior
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  • 131
    Publication Date: 1994-03-11
    Description: Crystal structures of seryl-tRNA synthetase from Thermus thermophilus complexed with two different analogs of seryl adenylate have been determined at 2.5 A resolution. The first complex is between the enzyme and seryl-hydroxamate-AMP (adenosine monophosphate), produced enzymatically in the crystal from adenosine triphosphate (ATP) and serine hydroxamate, and the second is with a synthetic analog of seryl adenylate (5'-O-[N-(L-seryl)-sulfamoyl]adenosine), which is a strong inhibitor of the enzyme. Both molecules are bound in a similar fashion by a network of hydrogen bond interactions in a deep hydrophilic cleft formed by the antiparallel beta sheet and surrounding loops of the synthetase catalytic domain. Four regions in the primary sequence are involved in the interactions, including the motif 2 and 3 regions of class 2 synthetases. Apart from the specific recognition of the serine side chain, the interactions are likely to be similar in all class 2 synthetases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Belrhali, H -- Yaremchuk, A -- Tukalo, M -- Larsen, K -- Berthet-Colominas, C -- Leberman, R -- Beijer, B -- Sproat, B -- Als-Nielsen, J -- Grubel, G -- New York, N.Y. -- Science. 1994 Mar 11;263(5152):1432-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉EMBL Grenoble Outstation, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128224" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/*analogs & derivatives/chemical synthesis/metabolism ; Adenosine Monophosphate/*analogs & derivatives/chemical synthesis/metabolism ; Amino Acid Sequence ; Binding Sites ; Computer Graphics ; Crystallography, X-Ray ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; Sequence Alignment ; Serine/*analogs & derivatives/chemical synthesis/metabolism ; Serine-tRNA Ligase/*chemistry/metabolism ; Thermus thermophilus/*enzymology
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  • 132
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-09-16
    Description: Pulse-probe transient Raman spectroscopy, with probe excitation at 230 nanometers, reveals changes in signals arising from tyrosine and tryptophan residues of the hemoglobin molecule as it moves from the relaxed (R) to the tense (T) state after photodeligation. Signals associated with intersubunit contacts in the T state develop in about 10 microseconds but are preceded by quite different signals, which reach maximum amplitude in about 50 nanoseconds. These signals involve the interior tryptophan residues that bridge the A and E helices by means of H bonds between the indole rings and serine or threonine side chains. Alterations of the H bond strengths, as a result of interhelix motions, can account for the signals. A model is proposed here in which loss of the ligand from the heme binding pocket is concerted with inward motion of the adjacent E helix; this motion, along with a complementary motion of the proximal F helix, transmits the energy associated with heme deligation to the subunit interfaces, leading to the T state rearrangement.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rodgers, K R -- Spiro, T G -- GM 25158/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 16;265(5179):1697-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, North Dakota State University, Fargo 58105.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8085153" target="_blank"〉PubMed〈/a〉
    Keywords: Carboxyhemoglobin/chemistry ; Heme/chemistry ; Hemoglobins/*chemistry ; Hydrogen Bonding ; Protein Conformation ; Protein Structure, Secondary ; Spectrum Analysis, Raman
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  • 133
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-02
    Description: Exocytosis in mammalian spermatozoa (the acrosome reaction) is a process essential for fertilization. Both progesterone and zona pellucida induce exocytosis in spermatozoa, which may encounter both during penetration of the oocyte's vestments. When mouse spermatozoa were exposed first to progesterone and then to zona pellucida, exocytosis was enhanced to a greater degree than that seen when the agonists were presented together or in the inverse order, which suggests that the steroid exerts a priming effect. Progesterone similarly primed the generation of intracellular messengers evoked by zona pellucida. The effects triggered by progesterone were mimicked by gamma-aminobutyric acid (GABA) and were blocked by bicuculline, which indicates that the steroid acts on a GABAA receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roldan, E R -- Murase, T -- Shi, Q X -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1578-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Development and Signalling, Babraham Institute, Biotechnology and Biological Sciences Research Council, Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985030" target="_blank"〉PubMed〈/a〉
    Keywords: Acrosome/drug effects/*physiology ; Animals ; Bicuculline/pharmacology ; Calcium/metabolism ; Diglycerides/metabolism ; *Exocytosis/drug effects ; Male ; Mice ; Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositol Phosphates/metabolism ; Phospholipase D/metabolism ; Progesterone/*pharmacology ; Receptors, GABA/physiology ; Spermatozoa/drug effects/*physiology ; Zona Pellucida/*physiology ; gamma-Aminobutyric Acid/pharmacology
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  • 134
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-04-22
    Description: Two distinct physiological mechanisms underlying loudness sensation were inferred from electric stimulation of the human auditory nerve and brainstem. In contrast to a power function relating loudness and stimulus intensity in acoustic hearing, loudness in electric stimulation of the auditory nerve depends on stimulus frequency. Loudness is an exponential function of electric amplitude for high frequencies and is a power function for low frequencies. A frequency-dependent, two-stage model is suggested to explain the loudness function, in which the first stage of processing is performed by a mechanical mechanism in the cochlea for high-frequency stimuli and by a neural mechanism in the cochlear nucleus for low-frequency stimuli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zeng, F G -- Shannon, R V -- R01-DC01526/DC/NIDCD NIH HHS/ -- R03-DC01464/DC/NIDCD NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 22;264(5158):564-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉House Ear Institute, Los Angeles, CA 90057.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8160013" target="_blank"〉PubMed〈/a〉
    Keywords: *Acoustic Stimulation ; Adult ; Brain Stem ; Cochlea/*physiology ; Cochlear Implants ; Cochlear Nucleus/*physiology ; Electric Stimulation ; Female ; Hearing Aids ; Humans ; *Loudness Perception ; Male ; Mathematics ; Models, Neurological ; Prostheses and Implants ; Vestibulocochlear Nerve/*physiology
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  • 135
    Publication Date: 1994-05-27
    Description: A line of transgenic mice was generated that contains an insertional mutation causing a phenotype similar to human autosomal recessive polycystic kidney disease. Homozygotes displayed a complex phenotype that included bilateral polycystic kidneys and an unusual liver lesion. The mutant locus was cloned and characterized through use of the transgene as a molecular marker. Additionally, a candidate polycystic kidney disease (PKD) gene was identified whose structure and expression are directly associated with the mutant locus. A complementary DNA derived from this gene predicted a peptide containing a motif that was originally identified in several genes involved in cell cycle control.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moyer, J H -- Lee-Tischler, M J -- Kwon, H Y -- Schrick, J J -- Avner, E D -- Sweeney, W E -- Godfrey, V L -- Cacheiro, N L -- Wilkinson, J E -- Woychik, R P -- IAG 222Y01-ES-10067/ES/NIEHS NIH HHS/ -- R01 DK45633-01/DK/NIDDK NIH HHS/ -- R01 HD25323/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 May 27;264(5163):1329-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Tennessee Graduate School of Biomedical Sciences, Biology Division, Oak Ridge National Laboratory, TN 37831-8077.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8191288" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Caenorhabditis elegans Proteins ; Crosses, Genetic ; Female ; Homozygote ; Kidney Tubules/pathology ; Liver/pathology ; Male ; Mice ; Mice, Inbred C3H ; Mice, Transgenic ; Molecular Sequence Data ; Mutagenesis, Insertional ; *Nerve Tissue Proteins ; Phenotype ; Polycystic Kidney, Autosomal Recessive/*genetics/pathology ; Proteins/chemistry/*genetics ; *Tumor Suppressor Proteins
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  • 136
    Publication Date: 1994-09-30
    Description: In the last few years there have been rapid advances in developing genetic maps for humans, greatly enhancing our ability to localize and identify genes for inherited disorders. Through the collaborative efforts of three large groups generating microsatellite markers and the efforts of the 110 CEPH collaborators, a comprehensive human linkage map is presented here. It consists of 5840 loci, of which 970 are uniquely ordered, covering 4000 centimorgans on the sex-averaged map. Of these loci, 3617 are polymerase chain reaction-formatted short tandem repeat polymorphisms, and another 427 are genes. The map has markers at an average density of 0.7 centimorgan, providing a resource for ready transference to physical maps and achieving one of the first goals of the Human Genome Project--a comprehensive, high-density genetic map.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murray, J C -- Buetow, K H -- Weber, J L -- Ludwigsen, S -- Scherpbier-Heddema, T -- Manion, F -- Quillen, J -- Sheffield, V C -- Sunden, S -- Duyk, G M -- New York, N.Y. -- Science. 1994 Sep 30;265(5181):2049-54.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, University of Iowa, Iowa City 52245.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8091227" target="_blank"〉PubMed〈/a〉
    Keywords: *Chromosome Mapping ; Chromosomes, Human ; Databases, Factual ; Female ; Genetic Markers ; *Genome, Human ; Genotype ; *Human Genome Project ; Humans ; Male
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  • 137
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-04-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, A -- New York, N.Y. -- Science. 1994 Apr 15;264(5157):350-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8153614" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Animals ; *Anthropology, Physical ; Arm/anatomy & histology ; Behavior, Animal ; Biological Evolution ; Callithrix/physiology ; DNA/*genetics ; Female ; Fossils ; Hominidae/*anatomy & histology ; Humans ; Male ; *Repetitive Sequences, Nucleic Acid
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  • 138
    Publication Date: 1994-03-11
    Description: The crystal structure of Thermus thermophilus seryl-transfer RNA synthetase, a class 2 aminoacyl-tRNA synthetase, complexed with a single tRNA(Ser) molecule was solved at 2.9 A resolution. The structure revealed how insertion of conserved base G20b from the D loop into the core of the tRNA determines the orientation of the long variable arm, which is a characteristic feature of most serine specific tRNAs. On tRNA binding, the antiparallel coiled-coil domain of one subunit of the synthetase makes contacts with the variable arm and T psi C loop of the tRNA and directs the acceptor stem of the tRNA into the active site of the other subunit. Specificity depends principally on recognition of the shape of tRNA(Ser) through backbone contacts and secondarily on sequence specific interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biou, V -- Yaremchuk, A -- Tukalo, M -- Cusack, S -- New York, N.Y. -- Science. 1994 Mar 11;263(5152):1404-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Grenoble Outstation, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128220" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Base Composition ; Base Sequence ; Binding Sites ; Crystallography, X-Ray ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Conformation ; Protein Structure, Secondary ; RNA, Transfer, Amino Acyl/*chemistry/metabolism ; Serine-tRNA Ligase/*chemistry/metabolism ; Substrate Specificity ; Thermus thermophilus/*enzymology
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  • 139
    Publication Date: 1994-03-25
    Description: The three-dimensional structure of a member of the beta subfamily of chemokines, human macrophage inflammatory protein-1 beta (hMIP-1 beta), has been determined with the use of solution multidimensional heteronuclear magnetic resonance spectroscopy. Human MIP-1 beta is a symmetric homodimer with a relative molecular mass of approximately 16 kilodaltons. The structure of the hMIP-1 beta monomer is similar to that of the related alpha chemokine interleukin-8 (IL-8). However, the quaternary structures of the two proteins are entirely distinct, and the dimer interface is formed by a completely different set of residues. Whereas the IL-8 dimer is globular, the hMIP-1 beta dimer is elongated and cylindrical. This provides a rational explanation for the absence of cross-binding and reactivity between the alpha and beta chemokine subfamilies. Calculation of the solvation free energies of dimerization suggests that the formation and stabilization of the two different types of dimers arise from the burial of hydrophobic residues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lodi, P J -- Garrett, D S -- Kuszewski, J -- Tsang, M L -- Weatherbee, J A -- Leonard, W J -- Gronenborn, A M -- Clore, G M -- New York, N.Y. -- Science. 1994 Mar 25;263(5154):1762-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8134838" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chemokine CCL4 ; Computer Graphics ; Cytokines/*chemistry ; Humans ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Interleukin-8/chemistry ; Macrophage Inflammatory Proteins ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Monokines/*chemistry ; Protein Conformation ; Protein Structure, Secondary ; Sequence Alignment
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  • 140
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-11-04
    Description: A simple technique has been devised that allows the direct synthesis of native backbone proteins of moderate size. Chemoselective reaction of two unprotected peptide segments gives an initial thioester-linked species. Spontaneous rearrangement of this transient intermediate yields a full-length product with a native peptide bond at the ligation site. The utility of native chemical ligation was demonstrated by the one-step preparation of a cytokine containing multiple disulfides. The polypeptide ligation product was folded and oxidized to form the native disulfide-containing protein molecule. Native chemical ligation is an important step toward the general application of chemistry to proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dawson, P E -- Muir, T W -- Clark-Lewis, I -- Kent, S B -- GM 50969-01/GM/NIGMS NIH HHS/ -- GM48870-03/GM/NIGMS NIH HHS/ -- GM48897-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):776-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973629" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Humans ; Interleukin-8/*chemical synthesis/chemistry ; Molecular Sequence Data ; Oxidation-Reduction ; Protein Conformation ; *Protein Folding ; Proteins/*chemical synthesis/chemistry
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  • 141
    Publication Date: 1994-07-08
    Description: Human lymphocyte antigen (HLA) class I proteins of the major histocompatibility complex are largely dependent for expression on small peptides supplied to them by transporter associated with antigen processing (TAP) protein. An inherited human deficiency in the TAP transporter was identified in two siblings suffering from recurrent respiratory bacterial infections. The expression on the cell surface of class I proteins was very low, whereas that of CD1a was normal, and the cytotoxicity of natural killer cells was affected. In addition, CD8+ alpha beta T cells were present in low but significant numbers and were cytotoxic in the most severely affected sibling, who also showed an increase in CD4+CD8+ T cells and gamma delta T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de la Salle, H -- Hanau, D -- Fricker, D -- Urlacher, A -- Kelly, A -- Salamero, J -- Powis, S H -- Donato, L -- Bausinger, H -- Laforet, M -- New York, N.Y. -- Science. 1994 Jul 8;265(5169):237-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire d'Histocompatibilite, Centre Regional de Transfusion Sanguine, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7517574" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Adolescent ; Amino Acid Sequence ; Antigens, CD/analysis ; Antigens, CD1 ; Base Sequence ; Carrier Proteins/analysis/*genetics ; Child ; Female ; Histocompatibility Antigens Class I/*analysis/metabolism ; Homozygote ; Humans ; Immunologic Deficiency Syndromes/*genetics/immunology ; Killer Cells, Natural/immunology ; Langerhans Cells/immunology ; Leukocyte Count ; Lymphocytes/*immunology ; Male ; Molecular Sequence Data ; Mutation ; T-Lymphocyte Subsets/immunology ; T-Lymphocytes, Cytotoxic/immunology
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  • 142
    Publication Date: 1994-04-29
    Description: Mice rendered deficient in lymphotoxin (LT) by gene targeting in embryonic stem cells have no morphologically detectable lymph nodes or Peyer's patches, although development of the thymus appears normal. Within the white pulp of the spleen, there is failure of normal segregation of B and T cells. Spleen and peripheral blood contain CD4+CD8- and CD4-CD8+ T cells in a normal ratio, and both T cells subsets have an apparently normal lytic function. Lymphocytes positive for immunoglobulin M are present in increased numbers in both the spleen and peripheral blood. These data suggest an essential role for LT in the normal development of peripheral lymphoid organs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉De Togni, P -- Goellner, J -- Ruddle, N H -- Streeter, P R -- Fick, A -- Mariathasan, S -- Smith, S C -- Carlson, R -- Shornick, L P -- Strauss-Schoenberger, J -- CA 16885/CA/NCI NIH HHS/ -- CA 28533/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 29;264(5159):703-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8171322" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/immunology ; Blastocyst ; Cytotoxicity, Immunologic ; Female ; Leukocyte Count ; Lymph Nodes/cytology/*growth & development/immunology ; Lymphoid Tissue/cytology/*growth & development/immunology ; Lymphotoxin-alpha/genetics/*physiology ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Peyer's Patches/cytology/growth & development/immunology ; Receptors, Tumor Necrosis Factor/physiology ; Spleen/cytology/immunology ; T-Lymphocyte Subsets/immunology ; T-Lymphocytes/immunology ; Thymus Gland/cytology/immunology ; Tumor Necrosis Factor-alpha/genetics/physiology
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  • 143
    Publication Date: 1994-08-26
    Description: Estrogen and progesterone modulate gene expression in rodents by activation of intracellular receptors in the hypothalamus, which regulate neuronal networks that control female sexual behavior. However, the neurotransmitter dopamine has been shown to activate certain steroid receptors in a ligand-independent manner. A dopamine receptor stimulant and a D1 receptor agonist, but not a D2 receptor agonist, mimicked the effects of progesterone in facilitating sexual behavior in female rats. The facilitory effect of the neurotransmitter was blocked by progesterone receptor antagonists, a D1 receptor antagonist, or antisense oligonucleotides to the progesterone receptor. The results suggest that in rodents neurotransmitters may regulate in vivo gene expression and behavior by means of cross-talk with steroid receptors in the brain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mani, S K -- Allen, J M -- Clark, J H -- Blaustein, J D -- O'Malley, B W -- MH-00885/MH/NIMH NIH HHS/ -- NS 19327/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 26;265(5176):1246-9.〈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/7915049" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Glands/drug effects ; Animals ; Base Sequence ; Benzazepines/pharmacology ; Dopamine/*physiology ; Dopamine Agents/administration & dosage/pharmacology ; Estradiol/analogs & derivatives/pharmacology ; Female ; Hypothalamus/drug effects/*physiology ; Injections, Intraventricular ; Male ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacology ; Posture ; Progesterone/pharmacology/*physiology ; Rats ; Rats, Sprague-Dawley ; Receptors, Progesterone/genetics/*physiology ; Sexual Behavior, Animal/drug effects/*physiology
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  • 144
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-09-23
    Description: During tactile learning there is a transformation in the way the primary somatosensory cortex integrates, represents, and distributes information from the skin. To define this transformation, the site of earliest modification has been identified in rat somatosensory cortex after a change in sensory experience. Afferent activity was manipulated by clipping all except two whiskers on one side of the snout ("whisker pairing"), and the receptive fields of neurons at different cortical depths were mapped 24 hours later. Neurons in layer IV, the target of the primary thalamic pathway, were unaltered, whereas neurons located above and below layer IV showed significant changes. These changes were similar to those that occur in layer IV after longer periods of whisker pairing. The findings support the hypothesis that the layers of cortex contribute differently to plasticity. Neurons in the supragranular and infragranular layers respond rapidly to changes in sensory experience and may contribute to subsequent modification in layer IV.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diamond, M E -- Huang, W -- Ebner, F F -- NS-25907/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 23;265(5180):1885-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Sciences and Biomedical Technologies, University of Udine, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8091215" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Afferent Pathways ; Animals ; Male ; *Neuronal Plasticity ; Neurons, Afferent/*physiology ; Rats ; Somatosensory Cortex/*physiology ; Thalamic Nuclei/physiology ; Vibrissae/*innervation
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  • 145
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-09-30
    Description: Adenosine is present in the mammalian brain in large amounts and has potent effects on neuronal activity, but its role in neural signaling is poorly understood. The glutamate receptor agonist N-methyl-D-aspartate (NMDA) caused a presynaptic depression of excitatory synaptic transmission in the CA1 region of guinea pig hippocampal slices. This depression was blocked by an adenosine A1 receptor antagonist, which suggests that activation of the NMDA subtype of glutamate receptor raises the concentration of extracellular adenosine, which acts on presynaptic inhibitory A1 receptors. Strong tetanic stimulation caused a heterosynaptic inhibition that was blocked by both NMDA and A1 receptor antagonists. Enkephalin, which selectively inhibits interneurons, antagonized the heterosynaptic inhibition. These findings suggest that synaptically released glutamate activates NMDA receptors, which in turn releases adenosine, at least in part from interneurons, that acts at a distance to inhibit presynaptically the release of glutamate from excitatory synapses. Thus, interneurons may mediate a widespread purinergic presynaptic inhibition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Manzoni, O J -- Manabe, T -- Nicoll, R A -- New York, N.Y. -- Science. 1994 Sep 30;265(5181):2098-101.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California at San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7916485" target="_blank"〉PubMed〈/a〉
    Keywords: 2-Amino-5-phosphonovalerate/pharmacology ; Adenosine/*metabolism ; Animals ; Electric Stimulation ; Enkephalins/pharmacology ; GABA-B Receptor Antagonists ; Glutamates/metabolism ; Glutamic Acid ; Guinea Pigs ; Hippocampus/drug effects/*metabolism ; In Vitro Techniques ; Interneurons/drug effects/*metabolism ; Male ; N-Methylaspartate/pharmacology ; Neural Inhibition/drug effects ; Organophosphorus Compounds/pharmacology ; Receptors, N-Methyl-D-Aspartate/drug effects/*metabolism ; Synapses/*metabolism ; Synaptic Transmission/drug effects ; Theophylline/analogs & derivatives/pharmacology
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  • 146
    Publication Date: 1994-11-11
    Description: Currently Alzheimer's disease, which affects more than 20 million people worldwide, can only be definitely diagnosed by histological examination of brain tissue obtained at autopsy or biopsy. There is a great need for an early, noninvasive, sensitive, and easily administered diagnostic test of Alzheimer's disease. Here it is reported that patients diagnosed with probable Alzheimer's disease by standard clinical criteria exhibited a marked hypersensitivity in their pupil dilation response to a cholinergic antagonist, tropicamide, placed in their eyes. It was possible to distinguish 18 of 19 individuals (95%) either clinically diagnosed with Alzheimer's disease or classified as suspect Alzheimer's individuals by neuropsychological screening from 30 of 32 normal elderly controls (94%).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scinto, L F -- Daffner, K R -- Dressler, D -- Ransil, B I -- Rentz, D -- Weintraub, S -- Mesulam, M -- Potter, H -- New York, N.Y. -- Science. 1994 Nov 11;266(5187):1051-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Eye Movements and Higher Cortical Functions, Brigham and Women's Hospital, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973660" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Alzheimer Disease/*diagnosis/physiopathology ; Dementia/physiopathology ; Female ; Humans ; Male ; Neuropsychological Tests ; Pupil/*drug effects ; Reproducibility of Results ; Sensitivity and Specificity ; *Tropicamide/pharmacology
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  • 147
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-04-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nowak, R -- New York, N.Y. -- Science. 1994 Apr 22;264(5158):500-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8160008" target="_blank"〉PubMed〈/a〉
    Keywords: Carotenoids/*adverse effects/*therapeutic use ; Finland ; Humans ; Lung Neoplasms/*etiology/prevention & control ; Male ; Randomized Controlled Trials as Topic ; Smoking/adverse effects ; beta Carotene
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  • 148
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-08-05
    Description: During transcription elongation, three flexibly connected parts of RNA polymerase of Escherichia coli advance along the template so that the front-end domain is followed by the catalytic site which in turn is followed by the RNA product binding site. The advancing enzyme was found to maintain the same conformation throughout extended segments of the transcribed region. However, when the polymerase traveled across certain DNA sites that seemed to briefly anchor the front-end domain, cyclic shifting of the three parts, accompanied by buildup and relief of internal strain, was observed. Thus, elongation proceeded in alternating laps of monotonous and inchworm-like movement with the flexible RNA polymerase configuration being subject to direct sequence control.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nudler, E -- Goldfarb, A -- Kashlev, M -- GM49242/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 5;265(5173):793-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Public Health Research Institute, New York, NY 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8047884" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA-Directed RNA Polymerases/*metabolism ; *Escherichia coli Proteins ; *Models, Genetic ; Molecular Sequence Data ; Movement ; Peptide Elongation Factors/metabolism ; Protein Conformation ; RNA, Messenger/metabolism ; RNA-Binding Proteins/metabolism ; Templates, Genetic ; Transcription Factors/metabolism ; Transcription, Genetic/*physiology ; Transcriptional Elongation Factors
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  • 149
    Publication Date: 1994-06-17
    Description: Mutations of human Cu,Zn superoxide dismutase (SOD) are found in about 20 percent of patients with familial amyotrophic lateral sclerosis (ALS). Expression of high levels of human SOD containing a substitution of glycine to alanine at position 93--a change that has little effect on enzyme activity--caused motor neuron disease in transgenic mice. The mice became paralyzed in one or more limbs as a result of motor neuron loss from the spinal cord and died by 5 to 6 months of age. The results show that dominant, gain-of-function mutations in SOD contribute to the pathogenesis of familial ALS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gurney, M E -- Pu, H -- Chiu, A Y -- Dal Canto, M C -- Polchow, C Y -- Alexander, D D -- Caliendo, J -- Hentati, A -- Kwon, Y W -- Deng, H X -- New York, N.Y. -- Science. 1994 Jun 17;264(5166):1772-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, IL 60611.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8209258" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/enzymology/*genetics/pathology ; Animals ; Brain/enzymology ; Disease Models, Animal ; Female ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Motor Endplate/pathology ; Motor Neuron Disease/enzymology/*genetics/pathology ; Motor Neurons/enzymology/pathology ; Muscles/innervation/pathology ; Mutation ; Pedigree ; Spinal Cord/pathology ; Superoxide Dismutase/*genetics/metabolism
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  • 150
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, R F -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1480-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985013" target="_blank"〉PubMed〈/a〉
    Keywords: ADAM Proteins ; Animals ; Clinical Trials as Topic ; Contraception/*methods ; Contraceptive Agents, Male ; Contraceptives, Postcoital ; Egg Proteins/metabolism ; Female ; Fertilization ; Humans ; Male ; Membrane Glycoproteins/metabolism/physiology ; *Metalloendopeptidases ; *Receptors, Cell Surface ; Spermatozoa/metabolism ; World Health Organization ; Zona Pellucida/metabolism
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  • 151
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-08-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Brien, C -- New York, N.Y. -- Science. 1994 Aug 26;265(5176):1176-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8066459" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/biosynthesis ; Crystallization ; Crystallography, X-Ray ; Intracellular Membranes/enzymology ; Mitochondria/enzymology ; Models, Molecular ; Protein Conformation ; Proton-Translocating ATPases/*chemistry/metabolism ; Protons
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  • 152
    Publication Date: 1994-04-08
    Description: Although beta-amyloid is the main constituent of neurite plaques and may play a role in the pathophysiology of Alzheimer's disease, mechanisms by which soluble beta-amyloid might produce early symptoms such as memory loss before diffuse plaque deposition have not been implicated. Treatment of fibroblasts with beta-amyloid (10 nM) induced the same potassium channel dysfunction previously shown to occur specifically in fibroblasts from patients with Alzheimer's disease--namely, the absence of a 113-picosiemen potassium channel. A tetraethylammonium-induced increase of intracellular concentrations of calcium, [Ca2+]i, a response that depends on functional 113-picosiemen potassium channels, was also eliminated or markedly reduced by 10 nM beta-amyloid. Increased [Ca2+]i induced by high concentrations of extracellular potassium and 166-picosiemen potassium channels were unaffected by 10 nM beta-amyloid. In Alzheimer's disease, then, beta-amyloid might alter potassium channels and thus impair neuronal function to produce symptoms such as memory loss by a means other than plaque formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Etcheberrigaray, R -- Ito, E -- Kim, C S -- Alkon, D L -- New York, N.Y. -- Science. 1994 Apr 8;264(5156):276-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Adaptive Systems, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8146663" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*metabolism ; Amyloid beta-Peptides/*pharmacology ; Bombesin/pharmacology ; Calcium/metabolism ; Cell Line ; Cells, Cultured ; Dimethyl Sulfoxide/pharmacology ; Female ; Fibroblasts/*drug effects/metabolism ; Humans ; Male ; Phenotype ; Potassium Channel Blockers ; Potassium Channels/*drug effects/metabolism ; Potassium Chloride/pharmacology ; Solubility ; Tetraethylammonium ; Tetraethylammonium Compounds/pharmacology
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  • 153
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-08-12
    Description: Scalable parallel computer architectures provide the computational performance needed for advanced biomedical computing problems. The National Institutes of Health have developed a number of parallel algorithms and techniques useful in determining biological structure and function. These applications include processing electron micrographs to determine the three-dimensional structure of viruses, calculating the solvent-accessible surface area of proteins to help predict the three-dimensional conformation of these molecules from their primary structures, and searching for homologous DNA or amino acid sequences in large biological databases. Timing results demonstrate substantial performance improvements with parallel implementations compared with conventional sequential systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martino, R L -- Johnson, C A -- Suh, E B -- Trus, B L -- Yap, T K -- New York, N.Y. -- Science. 1994 Aug 12;265(5174):902-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Computational Bioscience and Engineering Laboratory, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8052847" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Capsid/ultrastructure ; *Computer Simulation ; *Computers ; Databases, Factual ; Image Processing, Computer-Assisted ; National Institutes of Health (U.S.) ; Protein Conformation ; Protein Folding ; *Research ; Sequence Homology, Nucleic Acid ; Simplexvirus/ultrastructure ; Tomography, Emission-Computed ; United States
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  • 154
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-01-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Caro, T M -- Laurenson, M K -- New York, N.Y. -- Science. 1994 Jan 28;263(5146):485-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8290956" target="_blank"〉PubMed〈/a〉
    Keywords: Acinonyx/*genetics/physiology ; Animals ; *Ecology ; Female ; *Genetic Variation ; *Homozygote ; Male ; Predatory Behavior ; Reproduction ; Tanzania
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  • 155
    Publication Date: 1994-12-23
    Description: Synthesis of DNA at chromosome ends by telomerase may be necessary for indefinite proliferation of human cells. A highly sensitive assay for measuring telomerase activity was developed. In cultured cells representing 18 different human tissues, 98 of 100 immortal and none of 22 mortal populations were positive for telomerase. Similarly, 90 of 101 biopsies representing 12 human tumor types and none of 50 normal somatic tissues were positive. Normal ovaries and testes were positive, but benign tumors such as fibroids were negative. Thus, telomerase appears to be stringently repressed in normal human somatic tissues but reactivated in cancer, where immortal cells are likely required to maintain tumor growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, N W -- Piatyszek, M A -- Prowse, K R -- Harley, C B -- West, M D -- Ho, P L -- Coviello, G M -- Wright, W E -- Weinrich, S L -- Shay, J W -- AG07992/AG/NIA NIH HHS/ -- CA50195/CA/NCI NIH HHS/ -- CA65178/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):2011-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geron Corporation, Menlo Park, CA 94025.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7605428" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Division ; Cell Line ; Cell Line, Transformed/enzymology ; DNA Nucleotidylexotransferase/*metabolism ; Enzyme Activation ; Enzyme Repression ; Female ; Humans ; Male ; Molecular Sequence Data ; Neoplasms/*enzymology ; Ovary/enzymology ; Polymerase Chain Reaction ; Testis/enzymology ; Tumor Cells, Cultured
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  • 156
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-02
    Description: With the fall of fertility in China to near or below replacement levels in the early 1990s, the whole of East Asia may now be said to have completed a demographic transition. Its experience lies between that of the West and the many developing countries in which demographic transition is now under way. The main features and possible underlying causes of the fertility declines in Japan, Taiwan, South Korea, and China during this century are discussed. Fertility decline in East Asia is interesting both in its own right, as a chapter in the history of human reproduction, and for the light it may shed on fertility decline in the rest of the world.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feeney, G -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1518-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program on Population, East-West Center, Honolulu, HI 96848.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985021" target="_blank"〉PubMed〈/a〉
    Keywords: China ; Family Characteristics ; Family Planning Policy ; Female ; *Fertility ; Humans ; Japan ; Korea ; Male ; Mortality ; *Population Growth ; Taiwan
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  • 157
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-03-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1994 Mar 11;263(5152):1373.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128216" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Computer Graphics ; Crystallography, X-Ray ; Humans ; Models, Molecular ; Phosphates/metabolism ; Protein Conformation ; Protein Folding ; Protein Tyrosine Phosphatases/*chemistry/metabolism ; Tungsten Compounds/metabolism
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  • 158
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-02-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, D G -- New York, N.Y. -- Science. 1994 Feb 4;263(5147):595-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303260" target="_blank"〉PubMed〈/a〉
    Keywords: *Gene Expression Regulation ; Genetic Variation ; Humans ; Male ; *Mutagenesis, Site-Directed ; Nervous System Diseases/genetics ; Phenotype ; *Repetitive Sequences, Nucleic Acid
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  • 159
    Publication Date: 1994-11-18
    Description: Solution structures of two Src homology 3 (SH3) domain-ligand complexes have been determined by nuclear magnetic resonance. Each complex consists of the SH3 domain and a nine-residue proline-rich peptide selected from a large library of ligands prepared by combinatorial synthesis. The bound ligands adopt a left-handed polyproline type II (PPII) helix, although the amino to carboxyl directionalities of their helices are opposite. The peptide orientation is determined by a salt bridge formed by the terminal arginine residues of the ligands and the conserved aspartate-99 of the SH3 domain. Residues at positions 3, 4, 6, and 7 of both peptides also intercalate into the ligand-binding site; however, the respective proline and nonproline residues show exchanged binding positions in the two complexes. These structural results led to a model for the interactions of SH3 domains with proline-rich peptides that can be used to predict critical residues in complexes of unknown structure. The model was used to identify correctly both the binding orientation and the contact and noncontact residues of a peptide derived from the nucleotide exchange factor Sos in association with the amino-terminal SH3 domain of the adaptor protein Grb2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, S -- Chen, J K -- Yu, H -- Simon, J A -- Schreiber, S L -- GM44993/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Nov 18;266(5188):1241-7.〈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/7526465" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Alanine/chemistry ; Amino Acid Sequence ; Arginine/chemistry ; Binding Sites ; GRB2 Adaptor Protein ; Glycine/chemistry ; Guanine Nucleotide Exchange Factors ; Ligands ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Oligopeptides/chemistry/*metabolism ; Peptides/chemistry/metabolism ; Proline/chemistry ; Proline-Rich Protein Domains ; Protein Conformation ; Protein Structure, Secondary ; Protein-Tyrosine Kinases/chemistry/*metabolism ; Proteins/chemistry/metabolism ; Proto-Oncogene Proteins pp60(c-src)/chemistry/*metabolism ; src-Family Kinases
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  • 160
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-05-13
    Description: In both Drosophila melanogaster and Caenorhabditis elegans somatic sex determination, germline sex determination, and dosage compensation are controlled by means of a chromosomal signal known as the X:A ratio. A variety of mechanisms are used for establishing and implementing the chromosomal signal, and these do not appear to be similar in the two species. Instead, the study of sex determination and dosage compensation is providing more general lessons about different types of signaling pathways used to control alternative developmental states of cells and organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parkhurst, S M -- Meneely, P M -- New York, N.Y. -- Science. 1994 May 13;264(5161):924-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8178152" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*genetics ; *Dosage Compensation, Genetic ; *Drosophila Proteins ; Drosophila melanogaster/embryology/*genetics ; Female ; Genes, Helminth ; Genes, Insect ; Humans ; Insect Hormones/genetics ; Male ; Mammals/genetics ; *RNA-Binding Proteins ; *Sex Determination Analysis ; Signal Transduction
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  • 161
    Publication Date: 1994-03-04
    Description: The excitability of the human motor cortex during the development of implicit and declarative knowledge of a motor task was examined. During a serial reaction time test, subjects developed implicit knowledge of the test sequence, which was reflected by diminishing response times. Motor cortical mapping with transcranial magnetic stimulation revealed that the cortical output maps to the muscles involved in the task became progressively larger until explicit knowledge was achieved, after which they returned to their baseline topography. These results illustrate the rapid functional plasticity of cortical outputs associated with learning and with the transfer of knowledge from an implicit to explicit state.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pascual-Leone, A -- Grafman, J -- Hallett, M -- New York, N.Y. -- Science. 1994 Mar 4;263(5151):1287-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Motor Control Section, National Institute of Neurological Disorders and Stroke (NINDS), National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8122113" target="_blank"〉PubMed〈/a〉
    Keywords: Brain Mapping ; Electric Stimulation ; Electromyography ; Female ; Humans ; Learning/*physiology ; Male ; Motor Cortex/*physiology ; Reaction Time ; Transfer (Psychology)/*physiology
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  • 162
    Publication Date: 1993-03-05
    Description: Fertilization depends on cell surface recognition proteins that interact and thereby mediate binding and subsequent fusion of the sperm and egg. Overlapping complementary DNA's encoding the egg plasma membrane receptor for sperm from the sea urchin Strongylocentrotus purpuratus were cloned and sequenced. Analysis of the deduced primary structure suggests that the receptor is a transmembrane protein with a short cytoplasmic domain. This domain showed no sequence similarity to known protein sequences. In contrast, the extracellular, sperm binding domain of the receptor did show sequence similarity to the heat shock protein 70 (hsp70) family of proteins. Recombinant protein representing this portion of the receptor bound to the sperm protein, binding, and also inhibited fertilization in a species-specific manner; beads coated with the protein became specifically bound to acrosome-reacted sperm. These data provide a basis for detailed investigations of molecular interactions that occur in gamete recognition and egg activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Foltz, K R -- Partin, J S -- Lennarz, W J -- HD18590/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 5;259(5100):1421-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of California, Santa Barbara 93106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8383878" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; Female ; Fertilization ; Heat-Shock Proteins/*genetics ; Humans ; Male ; Molecular Sequence Data ; Ovum/physiology ; Receptors, Cell Surface/*genetics/metabolism ; Recombinant Proteins/metabolism ; Restriction Mapping ; Sea Urchins ; Sequence Homology, Amino Acid ; Sperm-Ovum Interactions ; Spermatozoa/cytology/physiology
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  • 163
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-06-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 1993 Jun 18;260(5115):1712-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8390093" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines/therapeutic use ; *Acquired Immunodeficiency Syndrome/drug therapy/immunology/prevention & control ; Drug Therapy, Combination ; Female ; Humans ; Immunity, Cellular ; Male ; Sexually Transmitted Diseases/prevention & control ; Zalcitabine/therapeutic use ; Zidovudine/therapeutic use
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  • 164
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-10-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barash, D P -- New York, N.Y. -- Science. 1993 Oct 22;262(5133):491.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211168" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Child ; Child Abuse ; Female ; Humans ; Male ; *Sexual Behavior ; Sexual Behavior, Animal ; Sociology ; *Violence
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  • 165
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-05-14
    Description: The perception of shape is independent of the size and position of the shape and also of the visual cue that defines it. The same shape can be recognized whether defined by a difference in luminance, by motion, or by texture. Experiments showed that the shape selectivity of individual cells in the macaque inferior temporal cortex did not vary with the size and position of a shape and also did not vary with the visual cue used to define the shape. This cue invariance was true for static luminance and texture cues as well as for relative motion cues--that is, for cues that are processed in ventral and dorsal visual pathways. The properties of these inferior temporal cells meet the demands of cue-invariant shape coding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sary, G -- Vogels, R -- Orban, G A -- New York, N.Y. -- Science. 1993 May 14;260(5110):995-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratorium voor Neuro- en Psychofysiologie, Faculteit der Geneeskunde, Katholieke Universiteit Leuven, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493538" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Form Perception ; Light ; Macaca mulatta ; Male ; Movement ; Neurons/*physiology ; Temporal Lobe/*physiology
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  • 166
    Publication Date: 1993-10-22
    Description: Glycogen storage disease (GSD) type 1a is caused by the deficiency of D-glucose-6-phosphatase (G6Pase), the key enzyme in glucose homeostasis. Despite both a high incidence and morbidity, the molecular mechanisms underlying this deficiency have eluded characterization. In the present study, the molecular and biochemical characterization of the human G6Pase complementary DNA, its gene, and the expressed protein, which is indistinguishable from human microsomal G6Pase, are reported. Several mutations in the G6Pase gene of affected individuals that completely inactivate the enzyme have been identified. These results establish the molecular basis of this disease and open the way for future gene therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lei, K J -- Shelly, L L -- Pan, C J -- Sidbury, J B -- Chou, J Y -- New York, N.Y. -- Science. 1993 Oct 22;262(5133):580-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Genetics Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211187" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; DNA, Complementary/genetics ; Exons ; Glucose-6-Phosphatase/*genetics/metabolism ; Glycogen Storage Disease Type I/enzymology/*genetics ; Glycosylation ; Humans ; Liver/enzymology ; Mice ; Molecular Sequence Data ; *Mutation ; Protein Conformation ; Transfection
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  • 167
    Publication Date: 1993-08-27
    Description: The gene encoding alpha 6(IV) collagen, COL4A6, was identified on the human X chromosome in a head-to-head arrangement and within 452 base pairs of the alpha 5(IV) collagen gene, COL4A5. In earlier studies, intragenic deletions of COL4A5 were detected in a subset of patients with Alport syndrome (AS), a hereditary defect of basement membranes. In some families, AS cosegregates with diffuse leiomyomatosis (DL), a benign smooth muscle tumor diathesis. Here it is shown that patients with AS-DL harbor deletions that disrupt both COL4A5 and COL4A6. Thus, type IV collagen may regulate smooth muscle differentiation and morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, J -- Mochizuki, T -- Smeets, H -- Antignac, C -- Laurila, P -- de Paepe, A -- Tryggvason, K -- Reeders, S T -- New York, N.Y. -- Science. 1993 Aug 27;261(5125):1167-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06536-0812.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8356449" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Differentiation ; Collagen/chemistry/*genetics ; Exons ; Female ; Fetus/metabolism ; *Gene Deletion ; Genetic Linkage ; Humans ; Leiomyoma/*genetics ; Male ; Molecular Sequence Data ; Morphogenesis ; Muscle, Smooth/cytology ; Mutation ; Nephritis, Hereditary/*genetics ; RNA, Messenger/genetics/metabolism
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  • 168
    Publication Date: 1993-08-06
    Description: The structure of the bifunctional, pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase was determined to 2.1-angstrom resolution. Model building suggests that a single cleavage site catalyzes both decarboxylation and transamination by maximizing stereoelectronic advantages and providing electrostatic and general base catalysis. The enzyme contains two binding sites for alkali metal ions. One is located near the active site and accounts for the dependence of activity on potassium ions. The other is located at the carboxyl terminus of an alpha helix. These sites help show how proteins can specifically bind alkali metals and how these ions can exert functional effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Toney, M D -- Hohenester, E -- Cowan, S W -- Jansonius, J N -- GM13854/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Aug 6;261(5122):756-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, University of Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8342040" target="_blank"〉PubMed〈/a〉
    Keywords: Amination ; Amino Acid Sequence ; Binding Sites ; Carboxy-Lyases/*chemistry/metabolism ; Catalysis ; Computer Graphics ; Decarboxylation ; Metals, Alkali/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; X-Ray Diffraction
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  • 169
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-05-07
    Description: Colorectal tumor DNA was examined for somatic instability at (CA)n repeats on human chromosomes 5q, 15q, 17p, and 18q. Differences between tumor and normal DNA were detected in 25 of the 90 (28 percent) tumors examined. This instability appeared as either a substantial change in repeat length (often heterogeneous in nature) or a minor change (typically two base pairs). Microsatellite instability was significantly correlated with the tumor's location in the proximal colon (P = 0.003), with increased patient survival (P = 0.02), and, inversely, with loss of heterozygosity for chromosomes 5q, 17p, and 18q. These data suggest that some colorectal cancers may arise through a mechanism that does not necessarily involve loss of heterozygosity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thibodeau, S N -- Bren, G -- Schaid, D -- CA-15083-18E8.1/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 May 7;260(5109):816-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Genetics Laboratory, Mayo Clinic, Rochester, MN 55905.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8484122" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Aged, 80 and over ; Chromosomes, Human, Pair 15 ; Chromosomes, Human, Pair 17 ; Chromosomes, Human, Pair 18 ; Chromosomes, Human, Pair 5 ; Colonic Neoplasms/*genetics ; Colorectal Neoplasms/*genetics ; DNA, Neoplasm/*genetics ; DNA, Satellite/*genetics ; Female ; Heterozygote ; Humans ; Male ; Middle Aged ; *Mutation ; Polymerase Chain Reaction ; Repetitive Sequences, Nucleic Acid
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  • 170
    Publication Date: 1993-10-01
    Description: Technological advances have made possible the development of high-resolution genetic linkage maps for the mouse. These maps in turn offer exciting prospects for understanding mammalian genome evolution through comparative mapping, for developing mouse models of human disease, and for identifying the function of all genes in the organism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Copeland, N G -- Jenkins, N A -- Gilbert, D J -- Eppig, J T -- Maltais, L J -- Miller, J C -- Dietrich, W F -- Weaver, A -- Lincoln, S E -- Steen, R G -- HG00198/HG/NHGRI NIH HHS/ -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Oct 1;262(5130):57-66.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ABL-Basic Research Program, National Cancer Institute-Frederick Cancer Research and Development Center, MD 21702.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211130" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; *Chromosome Mapping ; Cloning, Molecular ; Crosses, Genetic ; Female ; Genetic Markers ; *Genome ; Human Genome Project ; Humans ; Male ; Mice/*genetics ; Multigene Family ; Muridae/*genetics ; Mutation ; Neoplasms/genetics
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  • 171
    Publication Date: 1993-07-30
    Description: Anopheles gambiae, the primary vector of human malaria in Africa, is responsible for approximately a million deaths per year, mostly of children. Despite its significance in disease transmission, this mosquito has not been studied extensively by genetic or molecular techniques. To facilitate studies on this vector, a genetic map has been developed that covers the X chromosome at an average resolution of 2 centimorgans. This map has been integrated with the chromosome banding pattern and used to localize a recessive, sex-linked mutation (white eye) to within 1 centimorgan of flanking markers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zheng, L -- Collins, F H -- Kumar, V -- Kafatos, F C -- New York, N.Y. -- Science. 1993 Jul 30;261(5121):605-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Developmental Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8342025" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Anopheles/*genetics ; Base Sequence ; Chromosome Banding ; *Chromosome Mapping ; Crosses, Genetic ; DNA, Satellite/genetics ; Female ; *Genes, Insect ; Genes, Recessive ; Genetic Markers ; Insect Vectors/*genetics ; Malaria/transmission ; Male ; Molecular Sequence Data ; Mutation ; Recombination, Genetic ; *X Chromosome
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  • 172
    Publication Date: 1993-10-15
    Description: In cystic fibrosis (CF), absence or dysfunction of a phosphorylation-regulated chloride channel [CF transmembrane conductance regulator (CFTR)] leads to the loss or reduction of chloride secretion into the airways. Active sodium absorption is also increased in CF, and both of these ion transport changes could alter fluid transport across the airways. Under baseline conditions, cultured human airway epithelia from normal individuals absorbed fluid, and this absorption was increased in epithelia from patients with CF. In normal and CF epithelial cultures fluid absorption was inhibited by amiloride. Adenosine 3',5'-monophosphate stimulated fluid secretion in normal epithelial cultures but not in cultures from individuals with CF. In contrast, fluid secretion induced by nucleotide triphosphates (uridine triphosphate or adenosine triphosphate) was unaltered in cultures of epithelia from patients with CF, suggesting an approach to the treatment of CF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jiang, C -- Finkbeiner, W E -- Widdicombe, J H -- McCray, P B Jr -- Miller, S S -- HL 42368/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Oct 15;262(5132):424-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211164" target="_blank"〉PubMed〈/a〉
    Keywords: Absorption ; Adenosine Triphosphate/pharmacology ; Adolescent ; Adult ; Amiloride/pharmacology ; Body Fluids/*metabolism ; Cells, Cultured ; Cyclic AMP/pharmacology ; Cystic Fibrosis/*metabolism ; Epithelial Cells ; Epithelium/metabolism ; Female ; Humans ; Male ; Middle Aged ; Nasal Mucosa/cytology/*metabolism ; Sodium/metabolism ; Sodium Channels/metabolism ; Trachea/cytology/*metabolism ; Uridine Triphosphate/pharmacology
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  • 173
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-04-16
    Description: Klenow fragment of Escherichia coli DNA polymerase I, which was cocrystallized with duplex DNA, positioned 11 base pairs of DNA in a groove that lies at right angles to the cleft that contains the polymerase active site and is adjacent to the 3' to 5' exonuclease domain. When the fragment bound DNA, a region previously referred to as the "disordered domain" became more ordered and moved along with two helices toward the 3' to 5' exonuclease domain to form the binding groove. A single-stranded, 3' extension of three nucleotides bound to the 3' to 5' exonuclease active site. Although this cocrystal structure appears to be an editing complex, it suggests that the primer strand approaches the catalytic site of the polymerase from the direction of the 3' to 5' exonuclease domain and that the duplex DNA product may bend to enter the cleft that contains the polymerase catalytic site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beese, L S -- Derbyshire, V -- Steitz, T A -- GM28550/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Apr 16;260(5106):352-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8469987" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Crystallization ; DNA/chemistry/*metabolism ; DNA Polymerase I/*chemistry/metabolism ; DNA Replication ; DNA, Single-Stranded/chemistry/metabolism ; Escherichia coli/*enzymology ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Templates, Genetic
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  • 174
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-02-12
    Description: The analysis of the differences between two complex genomes holds promise for the discovery of infectious agents and probes useful for genetic studies. A system was developed in which subtractive and kinetic enrichment was used to purify restriction endonuclease fragments present in one population of DNA fragments but not in another. Application of this method to DNA populations of reduced complexity ("representations") resulted in the isolation of probes to viral genomes present as single copies in human DNA, and probes that detect polymorphisms between two individuals. In principle, this system, called representational difference analysis (RDA), may also be used for isolating probes linked to sites of genomic rearrangements, whether occurring spontaneously and resulting in genetic disorders or cancer, or programmed during differentiation and development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lisitsyn, N -- Wigler, M -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):946-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8438152" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/genetics ; Bacteriophage lambda/genetics ; Base Sequence ; *Cloning, Molecular ; DNA/*chemistry ; DNA Probes ; DNA, Viral ; Female ; Gene Deletion ; Genetic Diseases, Inborn/genetics ; Humans ; Male ; Molecular Sequence Data ; Neoplasms/genetics ; Nucleic Acid Hybridization/methods ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Sequence Homology, Nucleic Acid
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  • 175
    Publication Date: 1993-06-25
    Description: Female spotted hyenas exhibit male-like genitalia and dominance over males. Hyena ovarian tissues incubated in vitro produced large quantities of the steroid hormone precursor androstenedione. The activity of aromatase, which converts androstenedione to estrogen, was one-twentieth as great in hyena versus human placental homogenates. In comparison, the activity of 17 beta-hydroxysteroid dehydrogenase, which converts androstenedione to testosterone, was equal in the two homogenates. The limited aromatase activity may allow the hyena placenta to convert high circulating concentrations of androstenedione to testosterone, which results in virilization of the fetal external genitalia and possibly destruction of fetal ovarian follicles. Androstenedione production by residual ovarian stromal cells during reproductive life accounts for the epigenetic transmission of virilization in female spotted hyenas.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yalcinkaya, T M -- Siiteri, P K -- Vigne, J L -- Licht, P -- Pavgi, S -- Frank, L G -- Glickman, S E -- CA-39825/CA/NCI NIH HHS/ -- MH-39917/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1993 Jun 25;260(5116):1929-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Obstetrics, Gynecology, University of California School of Medicine, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8391165" target="_blank"〉PubMed〈/a〉
    Keywords: 17-Hydroxysteroid Dehydrogenases/metabolism ; Animals ; Aromatase/*metabolism ; Carnivora/embryology/*metabolism ; Corpus Luteum/metabolism ; Estradiol/biosynthesis ; Female ; Humans ; In Vitro Techniques ; Luteinizing Hormone/pharmacology ; Male ; Ovary/*metabolism ; Placenta/enzymology/*metabolism ; Pregnancy ; Progesterone/biosynthesis ; *Sex Differentiation ; Testosterone/*biosynthesis
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  • 176
    Publication Date: 1993-12-24
    Description: The elongated proteins of the spectrin family (dystrophin, alpha-actinin, and spectrin) contain tandemly repeated segments and form resilient cellular meshworks by cross-linking actin filaments. The structure of one of the repetitive segments of alpha-spectrin was determined at a 1.8 angstrom resolution. A segment consists of a three-helix bundle. A model of the interface between two tandem segments suggests that hydrophobic interactions between segments may constrain intersegment flexibility. The helix side chain interactions explain how mutations that are known to produce hemolytic anemias disrupt spectrin associations that sustain the integrity of the erythrocyte membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yan, Y -- Winograd, E -- Viel, A -- Cronin, T -- Harrison, S C -- Branton, D -- CA 13202/CA/NCI NIH HHS/ -- HL 17411/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 24;262(5142):2027-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266097" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Crystallization ; Drosophila ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Spectrin/*chemistry
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  • 177
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-08-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1993 Aug 6;261(5122):683-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8342036" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Australia ; Contraception, Immunologic/*veterinary ; Ecology ; Female ; *Foxes/microbiology ; *Genetic Engineering ; Male ; Myxoma virus/genetics ; Pest Control, Biological/*methods ; *Rabbits/microbiology ; Viruses/*genetics
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  • 178
    Publication Date: 1993-05-21
    Description: The three-dimensional solution structure of the DNA binding domain (DBD) of the retinoid X receptor alpha (RXR alpha) was determined by nuclear magnetic resonance spectroscopy. The two zinc fingers of the RXR DBD fold to form a single structural domain that consists of two perpendicularly oriented helices and that resembles the corresponding regions of the glucocorticoid and estrogen receptors (GR and ER, respectively). However, in contrast to the DBDs of the GR and ER, the RXR DBD contains an additional helix immediately after the second zinc finger. This third helix mediates both protein-protein and protein-DNA interactions required for cooperative, dimeric binding of the RXR DBD to DNA. Identification of the third helix in the RXR DBD thus defines a structural feature required for selective dimerization of the RXR on hormone response elements composed of half-sites (5'-AGGTCA-3') arranged as tandem repeats.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, M S -- Kliewer, S A -- Provencal, J -- Wright, P E -- Evans, R M -- New York, N.Y. -- Science. 1993 May 21;260(5111):1117-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8388124" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA/*metabolism ; DNA-Binding Proteins/*chemistry/metabolism ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Nuclear Proteins/*chemistry/metabolism ; Oligodeoxyribonucleotides ; Protein Conformation ; Protein Structure, Secondary ; Receptors, Cell Surface/*chemistry/metabolism ; *Receptors, Retinoic Acid ; Repetitive Sequences, Nucleic Acid ; Retinoid X Receptors ; *Transcription Factors ; Zinc Fingers
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  • 179
    Publication Date: 1993-01-15
    Description: Endotoxin [lipopolysaccharide (LPS)], the major antigen of the outer membrane of Gram-negative bacteria, consists of a variable-size carbohydrate chain that is covalently linked to N,O-acylated beta-1,6-D-glucosamine disaccharide 1,4'-bisphosphate (lipid A). The toxic activity of LPS resides in the lipid A structure. The structural features of synthetic peptides that bind to lipid A with high affinity, detoxify LPS in vitro, and prevent LPS-induced cytokine release and lethality in vivo were defined. The binding thermodynamics were comparable to that of an antigen-antibody reaction. Such synthetic peptides may provide a strategy for prophylaxis and treatment of LPS-mediated diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rustici, A -- Velucchi, M -- Faggioni, R -- Sironi, M -- Ghezzi, P -- Quataert, S -- Green, B -- Porro, M -- New York, N.Y. -- Science. 1993 Jan 15;259(5093):361-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biosynth Research Laboratories, Siena, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8420003" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; Bordetella pertussis/chemistry ; Escherichia coli/chemistry ; Hydrogen-Ion Concentration ; Limulus Test ; Lipid A/chemistry/*metabolism/toxicity ; Lipopolysaccharides/chemistry/*metabolism/toxicity ; Mice ; Mice, Inbred BALB C ; Micelles ; Microscopy, Electron ; Molecular Sequence Data ; Peptides/chemical synthesis/chemistry/*metabolism ; Polymyxin B/chemistry/*metabolism ; Protein Conformation ; Temperature
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  • 180
    Publication Date: 1993-04-30
    Description: A recessive mutation was identified in a family of transgenic mice that resulted in a reversal of left-right polarity (situs inversus) in 100 percent of the homozygous transgenic mice tested. Sequences that flanked the transgenic integration site were cloned and mapped to mouse chromosome 4, between the Tsha and Hxb loci. During early embryonic development, the direction of postimplantation turning, one of the earliest manifestations of left-right asymmetry, was reversed in homozygous transgenic embryos. This insertional mutation identifies a gene that controls embryonic turning and visceral left-right polarity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yokoyama, T -- Copeland, N G -- Jenkins, N A -- Montgomery, C A -- Elder, F F -- Overbeek, P A -- HD25340/HD/NICHD NIH HHS/ -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Apr 30;260(5108):679-82.〈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/8480178" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Chromosome Mapping ; Cloning, Molecular ; Embryonic and Fetal Development/*genetics ; Female ; *Genes, Recessive ; Homozygote ; Male ; Mice ; Mice, Transgenic ; Mutagenesis, Insertional ; Situs Inversus/*genetics
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  • 181
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-06-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1993 Jun 18;260(5115):1722-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8511575" target="_blank"〉PubMed〈/a〉
    Keywords: *Aggression ; Female ; *Genes, Recessive ; Genetic Diseases, Inborn ; Humans ; Male ; Monoamine Oxidase/deficiency/*genetics ; Mutation ; Pedigree ; *X Chromosome
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  • 182
    Publication Date: 1993-09-10
    Description: Activated autoreactive T cells are potentially pathogenic and regulated by clonotypic networks. Experimental autoimmune diseases can be treated by inoculation with autoreactive T cells (T cell vaccination). In the present study, patients with multiple sclerosis were inoculated with irradiated myelin basic protein (MBP)-reactive T cells. T cell responses to the inoculates were induced to deplete circulating MBP-reactive T cells in the recipients. Regulatory T cell lines isolated from the recipients inhibited T cells used for vaccination. The cytotoxicity of the CD8+ T cell lines was restricted by major histocompatibility antigens. Thus, clonotypic interactions regulating autoreactive T cells in humans can be induced by T cell vaccination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, J -- Medaer, R -- Stinissen, P -- Hafler, D -- Raus, J -- New York, N.Y. -- Science. 1993 Sep 10;261(5127):1451-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Multiple Sclerosis Research Unit, Dr. L. Willems Instituut, Diepenbeek, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7690157" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Antigens, CD4/analysis ; Antigens, CD8/analysis ; Cell Line ; Epitopes/immunology ; Female ; Humans ; *Immunotherapy, Adoptive ; Lymphocyte Activation ; Male ; Middle Aged ; Multiple Sclerosis/immunology/*therapy ; Myelin Basic Protein/*immunology ; Receptors, Antigen, T-Cell, alpha-beta/immunology ; T-Lymphocytes/*immunology ; Vaccination
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  • 183
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-06-11
    Description: Hippocampal long-term potentiation (LTP) is thought to serve as an elementary mechanism for the establishment of certain forms of explicit memory in the mammalian brain. As is the case with behavioral memory, LTP in the CA1 region has stages: a short-term early potentiation lasting 1 to 3 hours, which is independent of protein synthesis, precedes a later, longer lasting stage (L-LTP), which requires protein synthesis. Inhibitors of cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) blocked L-LTP, and analogs of cAMP induced a potentiation that blocked naturally induced L-LTP. The action of the cAMP analog was blocked by inhibitors of protein synthesis. Thus, activation of PKA may be a component of the mechanism that generates L-LTP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frey, U -- Huang, Y Y -- Kandel, E R -- GM32099/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jun 11;260(5114):1661-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Neurobiology and Behavior, Howard Hughes Medical Institute, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8389057" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/drug effects/physiology ; Animals ; Cyclic AMP/*physiology ; Hippocampus/cytology/drug effects/*physiology ; In Vitro Techniques ; Male ; Memory/physiology ; Neurons/drug effects/*physiology ; Protein Kinases/physiology ; Rats ; Rats, Sprague-Dawley ; Receptors, N-Methyl-D-Aspartate/physiology ; Second Messenger Systems/physiology ; Time Factors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 184
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-02-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Friend, S H -- New York, N.Y. -- Science. 1993 Feb 5;259(5096):774-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Genetics, Massachusetts General Hospital Cancer Center, Charlestown 02129.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430329" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crosses, Genetic ; Cyprinodontiformes/*genetics ; Female ; Fish Diseases/*genetics ; Genes, Tumor Suppressor ; *Genetic Predisposition to Disease ; Male ; Melanoma/genetics/*veterinary ; Models, Genetic ; Neoplasms/*genetics ; Proto-Oncogenes
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  • 185
    Publication Date: 1993-08-27
    Description: Better characterization of human immunodeficiency virus-type 1 (HIV-1) in patients with primary infection has important implications for the development of an acquired immunodeficiency syndrome (AIDS) vaccine because vaccine strategies should target viral isolates with the properties of transmitted viruses. In five HIV-1 seroconverters, the viral phenotype was found to be uniformly macrophage-tropic and non-syncytium-inducing. Furthermore, the viruses were genotypically homogeneous within each patient, but a common signature sequence was not discernible among transmitted viruses. In the two cases where the sexual partners were also studied, the sequences of the transmitted viruses matched best with minor variants in the blood of the transmitters. There was also a stronger pressure to conserve sequences in gp120 than in gp41, nef, and p17, suggesting that a selective mechanism is involved in transmission.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhu, T -- Mo, H -- Wang, N -- Nam, D S -- Cao, Y -- Koup, R A -- Ho, D D -- AI24030/AI/NIAID NIH HHS/ -- AI25541/AI/NIAID NIH HHS/ -- AI27742/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1993 Aug 27;261(5125):1179-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Aaron Diamond AIDS Research Center, New York University School of Medicine, NY 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8356453" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; Female ; Gene Products, gag/chemistry/genetics ; Genes, Viral ; Genotype ; Giant Cells/physiology ; HIV Antigens/chemistry/genetics ; HIV Envelope Protein gp120/chemistry/*genetics ; HIV Envelope Protein gp41/chemistry/genetics ; HIV Infections/*microbiology/transmission ; HIV Seropositivity/microbiology ; HIV-1/chemistry/*genetics/*physiology ; Humans ; Macrophages ; Male ; Molecular Sequence Data ; Phenotype ; Sequence Alignment ; Sexual Partners ; *Viral Proteins ; Virus Replication ; gag Gene Products, Human Immunodeficiency Virus
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  • 186
    Publication Date: 1993-05-07
    Description: A predisposition to colorectal cancer is shown to be linked to markers on chromosome 2 in some families. Molecular features of "familial" cancers were compared with those of sporadic colon cancers. Neither the familial nor sporadic cancers showed loss of heterozygosity for chromosome 2 markers, and the incidence of mutations in KRAS, P53, and APC was similar in the two groups of tumors. Most of the familial cancers, however, had widespread alterations in short repeated DNA sequences, suggesting that numerous replication errors had occurred during tumor development. Thirteen percent of sporadic cancers had identical abnormalities and these cancers shared biologic properties with the familial cases. These data suggest a mechanism for familial tumorigenesis different from that mediated by classic tumor suppressor genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aaltonen, L A -- Peltomaki, P -- Leach, F S -- Sistonen, P -- Pylkkanen, L -- Mecklin, J P -- Jarvinen, H -- Powell, S M -- Jen, J -- Hamilton, S R -- CA 35494/CA/NCI NIH HHS/ -- CA 47527/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 May 7;260(5109):812-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Genetics, University of Helsinki, Finland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8484121" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Mapping ; *Chromosomes, Human, Pair 2 ; Colonic Neoplasms/*genetics ; Colorectal Neoplasms/*genetics ; DNA, Satellite/genetics ; Female ; Genetic Markers ; Humans ; Lod Score ; Male ; Mutation ; Pedigree ; Polymorphism, Genetic ; Rectal Neoplasms/genetics ; Repetitive Sequences, Nucleic Acid
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  • 187
    Publication Date: 1993-10-29
    Description: A 24-amino acid peptide designed to solubilize integral membrane proteins has been synthesized. The design was for an amphipathic alpha helix with a "flat" hydrophobic surface that would interact with a transmembrane protein as a detergent. When mixed with peptide, 85 percent of bacteriorhodopsin and 60 percent of rhodopsin remained in solution over a period of 2 days in their native forms. The crystal structure of peptide alone showed it to form an antiparallel four-helix bundle in which monomers interact, flat surface to flat surface, as predicted.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schafmeister, C E -- Miercke, L J -- Stroud, R M -- GM24485/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Oct 29;262(5134):734-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235592" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteriorhodopsins/chemistry ; Crystallography, X-Ray ; Detergents/chemical synthesis/*chemistry ; Drug Design ; Membrane Proteins/*chemistry ; Models, Molecular ; Molecular Sequence Data ; Peptides/chemical synthesis/*chemistry ; Protein Conformation ; Protein Structure, Secondary ; Rhodopsin/chemistry
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  • 188
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Myers, R M -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):942-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California, San Francisco 94143-0444.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8094900" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/*chemistry ; DNA Probes ; Female ; Gene Deletion ; Humans ; Male ; Nucleic Acid Hybridization/*methods ; Polymerase Chain Reaction ; Polymorphism, Restriction Fragment Length
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  • 189
    Publication Date: 1993-02-19
    Description: The T cell receptor (TCR) requirements in the pathogenesis of insulin-dependent diabetes were examined with transgenic NOD mice bearing nondisease-related TCR alpha and beta chains. In both TCR beta and TCR alpha beta transgenic NOD mice the beta chain transgene was expressed by 〉 98% of peripheral T cells. The alpha chain transgene was also highly expressed. Insulitis developed in both sets of transgenic animals with most of the lymphocytes in the lesion expressing the transgenic beta chain and with depletion of the endogenous TCR V beta genes. Nonetheless, NOD animals transgenic for TCR beta and TCR alpha beta developed diabetes similar to controls. Thus, skewing the TCR repertoire did not diminish autoimmune susceptibility in NOD mice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lipes, M A -- Rosenzweig, A -- Tan, K N -- Tanigawa, G -- Ladd, D -- Seidman, J G -- Eisenbarth, G S -- New York, N.Y. -- Science. 1993 Feb 19;259(5098):1165-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Joslin Diabetes Center, Harvard Medical School, Brigham and Women's Hospital, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8267690" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/physiology ; Animals ; Base Sequence ; Crosses, Genetic ; Diabetes Mellitus, Type 2/genetics/immunology/*physiopathology ; Female ; Gene Rearrangement, T-Lymphocyte ; Islets of Langerhans/immunology/pathology ; Male ; Mice ; Mice, Inbred NOD/*physiology ; Mice, Transgenic ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Pancreatic Diseases/genetics/immunology/pathology ; Polymerase Chain Reaction/methods ; Receptors, Antigen, T-Cell, alpha-beta/genetics/*physiology ; T-Lymphocytes/*immunology/pathology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 190
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-01-01
    Description: In humans temporal lobe epilepsy (TLE) is characterized by recurrent seizures, neuronal hyperexcitability, and selective loss of certain neuronal populations in the hippocampus. Animal models of the condition indicate that a diminution of inhibition mediated by gamma-aminobutyric acid (GABA) accounts for the altered function, and it has been hypothesized that the diminution arises because GABAergic basket interneurons are "dormant" as a result of their being disconnected from excitatory inputs. In hippocampal slices, inhibitory postsynaptic potentials (IPSPs) were elicited in CA1 pyramidal cells by activation of basket cells; responses from an animal model of TLE were compared to those from control tissue. IPSPs evoked indirectly by activation of terminals that then excited basket cells were reduced in the epileptic tissue, whereas IPSPs evoked by direct activation of basket cells, when excitatory neurotransmission was blocked, were not different from controls. These results provide support for the "dormant basket cell" hypothesis and have implications for the pathophysiology and treatment of human TLE.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bekenstein, J W -- Lothman, E W -- New York, N.Y. -- Science. 1993 Jan 1;259(5091):97-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, University of Virginia Health Sciences Center, Charlottesville 22908.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8093417" target="_blank"〉PubMed〈/a〉
    Keywords: 6-Cyano-7-nitroquinoxaline-2,3-dione ; Action Potentials ; Animals ; Baclofen/analogs & derivatives/pharmacology ; Electric Stimulation ; Epilepsy, Temporal Lobe/*physiopathology ; Evoked Potentials ; Hippocampus/*physiology/*physiopathology ; In Vitro Techniques ; Interneurons/drug effects/*physiology ; Male ; Membrane Potentials ; Picrotoxin/pharmacology ; Pyramidal Tracts/drug effects/*physiology ; Quinoxalines/pharmacology ; Rats ; Rats, Sprague-Dawley ; Receptors, GABA-A/physiology ; Receptors, N-Methyl-D-Aspartate/physiology ; Status Epilepticus/*physiopathology
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  • 191
    Publication Date: 1993-08-13
    Description: The apolipoprotein E type 4 allele (APOE-epsilon 4) is genetically associated with the common late onset familial and sporadic forms of Alzheimer's disease (AD). Risk for AD increased from 20% to 90% and mean age at onset decreased from 84 to 68 years with increasing number of APOE-epsilon 4 alleles in 42 families with late onset AD. Thus APOE-epsilon 4 gene dose is a major risk factor for late onset AD and, in these families, homozygosity for APOE-epsilon 4 was virtually sufficient to cause AD by age 80.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corder, E H -- Saunders, A M -- Strittmatter, W J -- Schmechel, D E -- Gaskell, P C -- Small, G W -- Roses, A D -- Haines, J L -- Pericak-Vance, M A -- New York, N.Y. -- Science. 1993 Aug 13;261(5123):921-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Joseph and Kathleen Bryan Alzheimer's Disease Research Center, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8346443" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Aged, 80 and over ; Aging ; *Alleles ; Alzheimer Disease/*genetics/metabolism/mortality ; Amyloid beta-Peptides/metabolism ; Apolipoprotein E4 ; Apolipoproteins E/*genetics/physiology ; Female ; *Gene Frequency ; Genotype ; Homozygote ; Humans ; Linkage Disequilibrium ; Male ; Risk Factors ; Survival Rate
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  • 192
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-04-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barlow, D P -- New York, N.Y. -- Science. 1993 Apr 16;260(5106):309-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Institute of Molecular Pathology, Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8469984" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA/genetics/*metabolism ; *Dosage Compensation, Genetic ; Embryo, Mammalian/metabolism ; Fathers ; Female ; *Gene Expression Regulation ; Insulin-Like Growth Factor II/genetics ; Male ; Methylation ; Mice ; Models, Genetic ; Mothers ; Oocytes/metabolism ; Receptor, IGF Type 2/genetics ; Spermatozoa/metabolism
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  • 193
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-08-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leccese, A P -- New York, N.Y. -- Science. 1993 Aug 6;261(5122):665.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8204122" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*prevention & control ; Adolescent ; Adult ; Female ; Humans ; Male ; Risk-Taking ; *Sexual Behavior ; *Street Drugs ; *Substance-Related Disorders
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  • 194
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-01-22
    Description: Neurotransmitters acting on presynaptic terminals regulate synaptic transmission and plasticity. Because of the difficulty of direct electrophysiological recording from small presynaptic terminals, little is known about the ion channels that mediate these actions or about the mechanisms by which transmitter secretion is altered. The patch-clamp technique is used to show that the predominant inhibitory presynaptic neurotransmitter, gamma-aminobutyric acid (GABA), activates a GABAA receptor and gates a chloride channel in the membranes of peptidergic nerve terminals of the posterior pituitary. The opening of a chloride channel by GABA weakly depolarizes the nerve terminal membrane and blocks action potentials. In this way, GABA limits secretion by retarding the spread of excitation into the terminal arborization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, S J -- Jackson, M B -- NS30016/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 22;259(5094):531-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Wisconsin Medical School, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8380942" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bicuculline/pharmacology ; Chlordiazepoxide/pharmacology ; Chloride Channels ; Chlorides/*metabolism ; GABA-A Receptor Antagonists ; Male ; Membrane Potentials/drug effects ; Membrane Proteins/drug effects/*physiology ; Muscimol/pharmacology ; Nerve Endings/drug effects/*physiology ; Picrotoxin/pharmacology ; Pituitary Gland, Posterior/drug effects/*physiology ; Rats ; Receptors, GABA-A/*physiology ; gamma-Aminobutyric Acid/*pharmacology
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  • 195
    Publication Date: 1993-02-26
    Description: Attempts to correlate behavioral learning with cellular changes, such as increased synaptic efficacy, have often relied on increased extracellular potentials as an index of enhanced synaptic strength. A recent example is the enlarged excitatory field potentials in the dentate gyrus of rats that are learning spatial relations by exploration. The altered hippocampal field potentials do not reflect learning-specific cellular changes but result from a concomitant rise in brain temperature that is caused by the associated muscular effort. Enhanced dentate field excitatory potentials followed both passive and active heating and were linearly related to the brain temperature. These temperature-related effects may mask any learning-induced changes in field potential.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moser, E -- Mathiesen, I -- Andersen, P -- New York, N.Y. -- Science. 1993 Feb 26;259(5099):1324-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurophysiology, University of Oslo, Norway.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8446900" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior, Animal/physiology ; Body Temperature ; Cerebellar Nuclei/*physiology ; Hippocampus/*physiology ; Male ; Membrane Potentials ; Physical Exertion ; Rats ; Swimming/physiology
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  • 196
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-11-26
    Description: Protein phosphatases play important roles in the regulation of cell growth and metabolism, yet little is known about their enzymatic mechanism. By extrapolation from data on inhibitors of other types of hydrolases, an inhibitor of prostatic acid phosphatase was designed that is likely to function as a mechanism-based phosphotyrosine phosphatase inactivator. This molecule, 4-(fluoromethyl)phenyl phosphate, represents a useful paradigm for the design of potent and specific phosphatase inhibitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Myers, J K -- Widlanski, T S -- R01 GM47918-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 26;262(5138):1451-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Indiana University, Bloomington 47405.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8248785" target="_blank"〉PubMed〈/a〉
    Keywords: Acid Phosphatase/*antagonists & inhibitors/metabolism ; Alkylation ; Binding Sites ; Drug Design ; Humans ; Hydrolysis ; Kinetics ; Male ; Organophosphorus Compounds/metabolism/*pharmacology ; Prostate/*enzymology
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  • 197
    Publication Date: 1993-09-03
    Description: Annexins are a family of calcium- and phospholipid-binding proteins implicated in mediating membrane-related processes such as secretion, signal transduction, and ion channel activity. The crystal structure of rat annexin V was solved to 1.9 angstrom resolution by multiple isomorphous replacement. Unlike previously solved annexin V structures, all four domains bound calcium in this structure. Calcium binding in the third domain induced a large relocation of the calcium-binding loop regions, exposing the single tryptophan residue to the solvent. These alterations in annexin V suggest a role for domain 3 in calcium-triggered interaction with phospholipid membranes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Concha, N O -- Head, J F -- Kaetzel, M A -- Dedman, J R -- Seaton, B A -- R01-DK-41740/DK/NIDDK NIH HHS/ -- R01-NS-20357/NS/NINDS NIH HHS/ -- R29-GM-44554/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 3;261(5126):1321-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, Boston University School of Medicine, MA 02118.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8362244" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Annexin A5/*chemistry/metabolism ; Binding Sites ; Calcium/*metabolism ; Computer Graphics ; Crystallization ; Humans ; Hydrogen Bonding ; Molecular Sequence Data ; Protein Conformation ; Rats ; Sequence Alignment ; Tryptophan/chemistry ; X-Ray Diffraction
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  • 198
    Publication Date: 1993-06-25
    Description: Nitric oxide (NO) and carbon monoxide (CO) may act as retrograde messages for long-term potentiation (LTP) in the hippocampus. Zinc protoporphyrin IX, an inhibitor of the enzyme that produces CO, blocked induction of LTP in the CA1 region of hippocampal slices. Application of either NO or CO to slices produced a rapid and long-lasting increase in the size of evoked synaptic potentials if, and only if, the application occurred at the same time as weak tetanic stimulation. This long-term enhancement was spatially restricted to synapses from active presynaptic fibers and appeared to involve mechanisms utilized by LTP, occluding the subsequent induction of LTP by strong tetanic stimulation. The enhancement by NO and CO was not blocked by an N-methyl-D-aspartate (NMDA) receptor blocker, suggesting that NO and CO act downstream from the NMDA receptor. Also, CO produced long-term enhancement when paired with low-frequency stimulation. These results are consistent with the hypothesis that NO and CO, either alone or in combination, serve as retrograde messages that produce activity-dependent presynaptic enhancement during LTP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhuo, M -- Small, S A -- Kandel, E R -- Hawkins, R D -- AG08702/AG/NIA NIH HHS/ -- MH45923/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1993 Jun 25;260(5116):1946-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Neurobiology and Behavior, College of Physicians and Surgeons, Columbia University, New York, NY.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8100368" target="_blank"〉PubMed〈/a〉
    Keywords: 6-Cyano-7-nitroquinoxaline-2,3-dione ; Animals ; Carbon Monoxide/*pharmacology ; Electric Stimulation ; Guinea Pigs ; Hippocampus/drug effects/*physiology ; In Vitro Techniques ; Male ; Membrane Potentials/drug effects ; Nitric Oxide/*pharmacology ; Protoporphyrins/pharmacology ; Quinoxalines/pharmacology ; Signal Transduction/drug effects ; Synapses/drug effects/*physiology
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  • 199
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-10-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Newman, L S -- ES00173/ES/NIEHS NIH HHS/ -- ES06538/ES/NIEHS NIH HHS/ -- HL273353/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Oct 8;262(5131):197-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Occupational and Environmental Medicine Division, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8105535" target="_blank"〉PubMed〈/a〉
    Keywords: Antigen-Presenting Cells/immunology ; Berylliosis/*etiology/genetics/immunology/prevention & control ; Beryllium/*adverse effects/immunology ; Female ; Genes, MHC Class II ; Genetic Markers ; Glutamates ; Glutamic Acid ; HLA-DP Antigens/chemistry/*genetics/immunology ; Humans ; Male ; *Occupational Exposure ; Risk Factors ; T-Lymphocytes, Helper-Inducer/immunology
    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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  • 200
    Publication Date: 1993-06-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benhorin, J -- Kalman, Y M -- Medina, A -- Towbin, J -- Rave-Harel, N -- Dyer, T D -- Blangero, J -- MacCluer, J W -- Kerem, B S -- 5R01-HL-33843/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jun 25;260(5116):1960-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8316839" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Alleles ; Child ; Female ; Genetic Linkage ; Humans ; Long QT Syndrome/*genetics ; Male ; Pedigree ; Phenotype
    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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