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  • Male  (403)
  • Kinetics  (239)
  • Models, Molecular  (214)
  • American Association for the Advancement of Science (AAAS)  (831)
  • American Chemical Society (ACS)
  • 1990-1994  (831)
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  • American Association for the Advancement of Science (AAAS)  (831)
  • American Chemical Society (ACS)
  • Springer  (26)
  • Wiley-Blackwell  (21)
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Year
  • 101
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    Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-15
    Description: The tailspike protein (TSP) of Salmonella typhimurium phage P22 is a part of the apparatus by which the phage attaches to the bacterial host and hydrolyzes the O antigen. It has served as a model system for genetic and biochemical analysis of protein folding. The x-ray structure of a shortened TSP (residues 109 to 666) was determined to a 2.0 angstrom resolution. Each subunit of the homotrimer contains a large parallel beta helix. The interdigitation of the polypeptide chains at the carboxyl termini is important to protrimer formation in the folding pathway and to thermostability of the mature protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steinbacher, S -- Seckler, R -- Miller, S -- Steipe, B -- Huber, R -- Reinemer, P -- New York, N.Y. -- Science. 1994 Jul 15;265(5170):383-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biochemie, Abteilung Strukturforschung, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023158" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacteriophage P22 ; Computer Graphics ; Crystallization ; Crystallography, X-Ray ; Glycoside Hydrolases/*chemistry/genetics ; Models, Molecular ; Point Mutation ; Protein Conformation ; *Protein Folding ; Protein Structure, Secondary ; *Protein Structure, Tertiary ; Viral Proteins/*chemistry/genetics ; *Viral Tail Proteins
    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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    Reactivation of hippocampal ensemble memories during sleep (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-29
    Description: Simultaneous recordings were made from large ensembles of hippocampal "place cells" in three rats during spatial behavioral tasks and in slow-wave sleep preceding and following these behaviors. Cells that fired together when the animal occupied particular locations in the environment exhibited an increased tendency to fire together during subsequent sleep, in comparison to sleep episodes preceding the behavioral tasks. Cells that were inactive during behavior, or that were active but had non-overlapping spatial firing, did not show this increase. This effect, which declined gradually during each post-behavior sleep session, may result from synaptic modification during waking experience. Information acquired during active behavior is thus re-expressed in hippocampal circuits during sleep, as postulated by some theories of memory consolidation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, M A -- McNaughton, B L -- MH46823/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1994 Jul 29;265(5172):676-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neural Systems, Memory, and Aging, University of Arizona, Tucson 85724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8036517" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/physiology ; Animals ; Hippocampus/*physiology ; Male ; Memory/*physiology ; Models, Neurological ; Motor Activity/physiology ; Nerve Net/physiology ; Neurons/*physiology ; Pyramidal Cells/physiology ; Rats ; Rats, Inbred F344 ; Reaction Time/physiology ; Sleep/*physiology ; Spatial Behavior/physiology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 103
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    Natural vertical transmission of western equine encephalomyelitis virus in mosquitoes (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-04
    Description: The mechanism by which western equine encephalomyelitis (WEE) virus and other mosquito-borne alphaviruses (Togaviridae) survive during periods of vector inactivity is unknown. Recently, three strains of WEE virus were isolated from adult Aedes dorsalis collected as larvae from a salt marsh in a coastal region of California. This provides evidence of vertical transmission of WEE virus in mosquitoes in nature. Vertical transmission in Ae. dorsalis and closely related mosquito species may be an important mechanism for the maintenance of WEE virus in temperate regions in North America where horizontal transmission of the virus is seasonal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fulhorst, C F -- Hardy, J L -- Eldridge, B F -- Presser, S B -- Reeves, W C -- AI-03028/AI/NIAID NIH HHS/ -- AI-26154/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 4;263(5147):676-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Public Health, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303276" target="_blank"〉PubMed〈/a〉
    Keywords: Aedes/*microbiology ; Animals ; California ; Encephalitis Virus, Western Equine/isolation & purification/*physiology ; Encephalomyelitis, Equine/transmission ; Female ; Insect Vectors/*microbiology ; Larva/microbiology ; Male ; Seasons
    Print ISSN: 0036-8075
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  • 104
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    Cystic fibrosis heterozygote resistance to cholera toxin in the cystic fibrosis mouse model (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-07
    Description: The effect of the number of cystic fibrosis (CF) alleles on cholera toxin (CT)-induced intestinal secretion was examined in the CF mouse model. CF mice that expressed no CF transmembrane conductance regulator (CFTR) protein did not secrete fluid in response to CT. Heterozygotes expressed 50 percent of the normal amount of CFTR protein in the intestinal epithelium and secreted 50 percent of the normal fluid and chloride ion in intestinal epithelium and secreted 50 percent of the normal fluid and chloride ion and fluid secretion suggests that CF heterozygotes might possess a selective advantage of resistance to cholera.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabriel, S E -- Brigman, K N -- Koller, B H -- Boucher, R C -- Stutts, M J -- DK46003/DK/NIDDK NIH HHS/ -- HL34322/HL/NHLBI NIH HHS/ -- HL42384/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 7;266(5182):107-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of North Carolina, Chapel Hill 27599.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7524148" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Body Fluids/*secretion ; Chloride Channels/metabolism ; Chlorides/*metabolism ; Cholera Toxin/*toxicity ; Crosses, Genetic ; Cyclic AMP/metabolism ; Cystic Fibrosis/*genetics/physiopathology ; Cystic Fibrosis Transmembrane Conductance Regulator ; Female ; Heterozygote ; Intestinal Mucosa/*secretion ; Intestine, Small/secretion ; Male ; Membrane Proteins/*genetics/metabolism ; Mice
    Print ISSN: 0036-8075
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  • 105
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    DNA repair rates mapped along the human PGK1 gene at nucleotide resolution (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-11
    Description: The repair of cyclobutane pyrimidine dimers (CPDs), DNA lesions induced by ultraviolet light, was studied at nucleotide resolution. Human fibroblasts were irradiated with ultraviolet light and allowed to repair. The DNA was enzymatically cleaved at the CPDs, and the induced breaks along the promoter and exon 1 of the PGK1 gene were mapped by ligation-mediated polymerase chain reaction. Repair rates within the nontranscribed strand varied as much as 15-fold, depending on nucleotide position. Preferential repair of the transcribed strand began just downstream of the transcription start site but was most pronounced beginning at nucleotide +140 in exon 1. The promoter contained two slowly repaired regions that coincided with two transcription factor binding sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gao, S -- Drouin, R -- Holmquist, G P -- CA54773/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Mar 11;263(5152):1438-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Beckman Research Institute of the City of Hope, Department of Biology, Duarte, CA 91010.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128226" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cells, Cultured ; *DNA Repair ; Exons ; *Genes ; HeLa Cells ; Humans ; Kinetics ; Phosphoglycerate Kinase/*genetics ; Promoter Regions, Genetic ; Pyrimidine Dimers/*metabolism ; Skin/metabolism/*radiation effects ; Transcription Factors/metabolism ; Transcription, Genetic ; Ultraviolet Rays
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 106
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    T cell receptor-MHC class I peptide interactions: affinity, kinetics, and specificity (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-12
    Description: The critical discriminatory event in the activation of T lymphocytes bearing alpha beta T cell receptors (TCRs) is their interaction with a molecular complex consisting of a peptide bound to a major histocompatibility complex (MHC)-encoded class I or class II molecule on the surface of an antigen-presenting cell. The kinetics of binding were measured of a purified TCR to molecular complexes of a purified soluble analog of the murine MHC class I molecule H-2Ld (sH-2Ld) and a synthetic octamer peptide p2CL in a direct, real-time assay based on surface plasmon resonance. The kinetic dissociation rate of the MHC-peptide complex from the TCR was rapid (2.6 x 10(-2) second-1, corresponding to a half-time for dissociation of approximately 27 seconds), and the kinetic association rate was 2.1 x 10(5) M-1 second-1. The equilibrium constant for dissociation was approximately 10(-7) M. These values indicate that TCRs must interact with a multivalent array of MHC-peptide complexes to trigger T cell signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corr, M -- Slanetz, A E -- Boyd, L F -- Jelonek, M T -- Khilko, S -- al-Ramadi, B K -- Kim, Y S -- Maher, S E -- Bothwell, A L -- Margulies, D H -- New York, N.Y. -- Science. 1994 Aug 12;265(5174):946-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Section, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8052850" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biosensing Techniques ; H-2 Antigens/*metabolism ; Histocompatibility Antigen H-2D ; Kinetics ; *Major Histocompatibility Complex ; Mice ; Molecular Sequence Data ; Oligopeptides/*metabolism ; Receptors, Antigen, T-Cell, alpha-beta/*metabolism ; Solubility
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  • 107
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    Lung cancer risk for female smokers (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Risch, H A -- Howe, G R -- Jain, M -- Burch, J D -- Holowaty, E J -- Miller, A B -- New York, N.Y. -- Science. 1994 Mar 4;263(5151):1206-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8122096" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; Humans ; Lung Neoplasms/*etiology/mortality ; Male ; Risk Factors ; Sex Factors ; Smoking/*adverse effects
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 108
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    A subset of CD4+ thymocytes selected by MHC class I molecules (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-25
    Description: To complete their maturation, most immature thymocytes depend on the simultaneous engagement of their antigen receptor [alpha beta T cell receptor (TCR)] and their CD4 or CD8 coreceptors with major histocompatibility complex class II or I ligands, respectively. However, a normal subset of mature alpha beta TCR+ thymocytes did not follow these rules. These thymocytes expressed NK1.1 and a restricted set of alpha beta TCRs that are intrinsically class I-reactive because their positive selection was class I-dependent but CD8-independent. These cells were CD4+ and CD4-8- but never CD8+, because the presence of CD8 caused negative selection. Thus, neither CD4 nor CD8 contributes signals that direct their maturation into the CD4+ and CD4-8- lineages.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bendelac, A -- Killeen, N -- Littman, D R -- Schwartz, R H -- New York, N.Y. -- Science. 1994 Mar 25;263(5154):1774-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Immunology, National Institute of Allergy and Infectious 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/7907820" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens/analysis ; Antigens, CD4/analysis ; Antigens, CD8/analysis ; Antigens, Ly ; Antigens, Surface ; CD4-Positive T-Lymphocytes/cytology/*immunology ; Female ; Histocompatibility Antigens Class I/*physiology ; Lectins, C-Type ; Ligands ; Lymphocyte Activation ; Male ; Mice ; Mice, Inbred C57BL ; NK Cell Lectin-Like Receptor Subfamily B ; Phenotype ; Proteins/analysis ; Receptors, Antigen, T-Cell, alpha-beta/analysis/*physiology ; T-Lymphocyte Subsets/cytology/*immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 109
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    Design of a G.C-specific DNA minor groove-binding peptide (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-28
    Description: A four-ring tripeptide containing alternating imidazole and pyrrole carboxamides specifically binds six-base pair 5'-(A,T)GCGC(A,T)-3' sites in the minor groove of DNA. The designed peptide has a specificity completely reversed from that of the tripyrrole distamycin, which binds A,T sequences. Structural studies with nuclear magnetic resonance revealed that two peptides bound side-by-side and in an antiparallel orientation in the minor groove. Each of the four imidazoles in the 2:1 ligand-DNA complex recognized a specific guanine amino group in the GCGC core through a hydrogen bond. Targeting a designated four-base pair G.C tract by this synthetic ligand supports the generality of the 2:1 peptide-DNA motif for sequence-specific minor groove recognition of DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geierstanger, B H -- Mrksich, M -- Dervan, P B -- Wemmer, D E -- GM-27681/GM/NIGMS NIH HHS/ -- GM-43129/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 28;266(5185):646-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Group in Biophysics, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939719" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Computer Graphics ; DNA/chemistry/*metabolism ; Drug Design ; Hydrogen Bonding ; Imidazoles/chemical synthesis/*chemistry/metabolism ; Ligands ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry/metabolism ; Oligopeptides/chemical synthesis/*chemistry/metabolism ; Protein Conformation ; Pyrroles/chemical synthesis/*chemistry/metabolism
    Print ISSN: 0036-8075
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  • 110
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    Environmental estrogens stir debate (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, R -- New York, N.Y. -- Science. 1994 Jul 15;265(5170):308-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023147" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Wild/physiology ; Environmental Pollutants/*adverse effects/metabolism/toxicity ; Estrogens/*adverse effects/metabolism/toxicity ; Female ; Humans ; Male ; Pregnancy ; Prenatal Exposure Delayed Effects ; Reproduction/*drug effects ; Sperm Count/drug effects ; Testicular Neoplasms/epidemiology/etiology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 111
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    Rise and fall of the Y chromosome (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1994 Jan 14;263(5144):171-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8284667" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Drosophila melanogaster/genetics ; Female ; Humans ; Male ; Mutation ; *Recombination, Genetic ; Sex Determination Analysis ; *Y Chromosome
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  • 112
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    Kin selection, social structure, gene flow, and the evolution of chimpanzees (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-26
    Description: Hypotheses about chimpanzee social behavior, phylogeography, and evolution were evaluated by noninvasive genotyping of free-ranging individuals from 20 African sites. Degrees of relatedness among individuals in one community were inferred from allele-sharing at eight nuclear simple sequence repeat (SSR) loci. Males are related on the order of half-siblings, and homozygosity is significantly increased at several SSR loci compared to Hardy-Weinberg expectations. These data support the kin-selection hypothesis for the evolution of cooperation among males. Sequence variation patterns at two mitochondrial loci indicate historically high long-distance gene flow and clarify the relationships among three allopatric subspecies. The unexpectedly large genetic distance between the western subspecies, Pan troglodytes verus, and the other two subspecies suggests a divergence time of about 1.58 million years. This result, if confirmed at nuclear loci and supported by eco-behavioral data, implies that P. t. verus should be elevated to full species rank.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morin, P A -- Moore, J J -- Chakraborty, R -- Jin, L -- Goodall, J -- Woodruff, D S -- 1T32 HG00005-02/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 26;265(5176):1193-201.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093-0116.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7915048" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Alleles ; Animals ; Base Sequence ; *Biological Evolution ; DNA/analysis/genetics ; Female ; *Genetic Variation ; Hair/chemistry ; Male ; Molecular Sequence Data ; Pan troglodytes/classification/*genetics/psychology ; Phylogeny ; Polymerase Chain Reaction ; Polymorphism, Restriction Fragment Length ; Repetitive Sequences, Nucleic Acid ; *Social Behavior ; Tanzania
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  • 113
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    Study implicates second-hand smoke (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, R -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8140415" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta, Abdominal ; Aortic Diseases/*etiology ; Arteriosclerosis/*etiology ; Chickens ; Humans ; Male ; Tobacco Smoke Pollution/*adverse effects
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  • 114
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    Crystal structure of the principal neutralization site of HIV-1 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-01
    Description: The crystal structure of a complex between a 24-amino acid peptide from the third variable (V3) loop of human immunodeficiency virus-type 1 (HIV-1) gp 120 and the Fab fragment of a broadly neutralizing antibody (59.1) was determined to 3 angstrom resolution. The tip of the V3 loop containing the Gly-Pro-Gly-Arg-Ala-Phe sequence adopts a double-turn conformation, which may be the basis of its conservation in many HIV-1 isolates. A complete map of the HIV-1 principal neutralizing determinant was constructed by stitching together structures of V3 loop peptides bound to 59.1 and to an isolate-specific (MN) neutralizing antibody (50.1). Structural conservation of the overlapping epitopes suggests that this biologically relevant conformation could be of use in the design of synthetic vaccines and drugs to inhibit HIV-1 entry and virus-related cellular fusion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ghiara, J B -- Stura, E A -- Stanfield, R L -- Profy, A T -- Wilson, I A -- GM-46192/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):82-5.〈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/7511253" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal/chemistry/immunology ; Antigen-Antibody Complex/*chemistry/immunology ; Antigen-Antibody Reactions ; Computer Graphics ; Crystallography, X-Ray ; Epitopes/chemistry/immunology ; HIV Antibodies/*chemistry/immunology ; HIV Envelope Protein gp120/*chemistry/immunology ; HIV-1/*chemistry/immunology ; Hydrogen Bonding ; Immunoglobulin Fab Fragments/*chemistry/immunology ; Models, Molecular ; Molecular Sequence Data ; Neutralization Tests ; Peptide Fragments/*chemistry/immunology ; Protein Conformation ; Protein Structure, Secondary
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  • 115
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    DNA bending by asymmetric phosphate neutralization (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-16
    Description: DNA is often bent when complexed with proteins. Understanding the forces responsible for DNA bending would be of fundamental value in exploring the interplay of these macromolecules. A series of experiments was devised to test the hypothesis that proteins with cationic surfaces can induce substantial DNA bending by neutralizing phosphates on one DNA face. Repulsions between phosphates in the remaining anionic helix are predicted to result in an unbalanced compression force acting to deform the DNA toward the protein. This hypothesis is supported by the results of electrophoretic experiments in which DNA spontaneously bends when one helical face is partially modified by incorporation of neutral phosphate analogs. Phasing with respect to a site of intrinsic DNA curvature (hexadeoxyadenylate tract) permits estimation of the electrostatic bend angle, and demonstrates that such modified DNAs are deformed toward the neutralized surface, as predicted. Similar model systems may be useful in exploring the extent to which phosphate neutralization can account for DNA bending by particular proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strauss, J K -- Maher, L J 3rd -- GM47814/GM/NIGMS NIH HHS/ -- P30 CA36727-08/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 16;266(5192):1829-34.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha 68198-6805.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7997878" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cations/chemistry ; DNA/*chemistry ; DNA-Binding Proteins/chemistry ; Electrochemistry ; Electrophoresis, Polyacrylamide Gel ; Models, Molecular ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Nucleosomes/chemistry ; Oligodeoxyribonucleotides ; Organophosphorus Compounds/chemistry ; Phosphates/*chemistry ; Thermodynamics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Crystal structure of a catalytic antibody with a serine protease active site (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-19
    Description: The three-dimensional structure of an unusually active hydrolytic antibody with a phosphonate transition state analog (hapten) bound to the active site has been solved to 2.5 A resolution. The antibody (17E8) catalyzes the hydrolysis of norleucine and methionine phenyl esters and is selective for amino acid esters that have the natural alpha-carbon L configuration. A plot of the pH-dependence of the antibody-catalyzed reaction is bell-shaped with an activity maximum at pH 9.5; experiments on mechanism lend support to the formation of a covalent acyl-antibody intermediate. The structural and kinetic data are complementary and support a hydrolytic mechanism for the antibody that is remarkably similar to that of the serine proteases. The antibody active site contains a Ser-His dyad structure proximal to the phosphorous atom of the bound hapten that resembles two of the three components of the Ser-His-Asp catalytic triad of serine proteases. The antibody active site also contains a Lys residue to stabilize oxyanion formation, and a hydrophobic binding pocket for specific substrate recognition of norleucine and methionine side chains. The structure identifies active site residues that mediate catalysis and suggests specific mutations that may improve the catalytic efficiency of the antibody. This high resolution structure of a catalytic antibody-hapten complex shows that antibodies can converge on active site structures that have arisen through natural enzyme evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, G W -- Guo, J -- Huang, W -- Fletterick, R J -- Scanlan, T S -- DK39304/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 19;265(5175):1059-64.〈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/8066444" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Catalytic/*chemistry/immunology/metabolism ; Binding Sites ; Computer Graphics ; Crystallization ; Crystallography, X-Ray ; Haptens/metabolism ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Hydrolysis ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Serine Endopeptidases/*chemistry/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    An experimental study of inbreeding depression in a natural habitat (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-14
    Description: Inbreeding is known to lead to decreased survival and reproduction in captive populations of animals. It is also important to know whether inbreeding has deleterious effects in natural habitats. An estimate was made of the effects of inbreeding in white-footed mice, Peromyscus leucopus noveboracensis, derived from a wild population. This study demonstrates that inbreeding had a significant detrimental effect on the survivorship of mice reintroduced into a natural habitat. This effect was more severe than the effect observed in laboratory studies of the population.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jimenez, J A -- Hughes, K A -- Alaks, G -- Graham, L -- Lacy, R C -- New York, N.Y. -- Science. 1994 Oct 14;266(5183):271-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Illinois-Chicago 60680.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939661" target="_blank"〉PubMed〈/a〉
    Keywords: Analysis of Variance ; Animals ; Body Weight ; Female ; *Inbreeding ; Likelihood Functions ; Male ; Peromyscus/genetics/*physiology ; Regression Analysis ; Survival Rate
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    Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-21
    Description: Collagenase is a zinc-dependent endoproteinase and is a member of the matrix metalloproteinase (MMP) family of enzymes. The MMPs participate in connective tissue remodeling events and aberrant regulation has been associated with several pathologies. The 2.4 angstrom resolution structure of the inhibited enzyme revealed that, in addition to the catalytic zinc, there is a second zinc ion and a calcium ion which play a major role in stabilizing the tertiary structure of collagenase. Despite scant sequence homology, collagenase shares structural homology with two other endoproteinases, bacterial thermolysin and crayfish astacin. The detailed description of protein-inhibitor interactions present in the structure will aid in the design of compounds that selectively inhibit individual members of the MMP family. Such inhibitors will be useful in examining the function of MMPs in pathological processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lovejoy, B -- Cleasby, A -- Hassell, A M -- Longley, K -- Luther, M A -- Weigl, D -- McGeehan, G -- McElroy, A B -- Drewry, D -- Lambert, M H -- New York, N.Y. -- Science. 1994 Jan 21;263(5145):375-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Glaxo Research Institute, Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8278810" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Calcium/metabolism ; Collagenases/*chemistry/metabolism ; Computer Graphics ; Crystallography, X-Ray ; Humans ; Hydrogen Bonding ; Matrix Metalloproteinase 8 ; Matrix Metalloproteinase Inhibitors ; Metalloendopeptidases/chemistry ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Thermolysin/chemistry ; Zinc/metabolism
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    The return of Phineas Gage: clues about the brain from the skull of a famous patient (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-20
    Description: When the landmark patient Phineas Gage died in 1861, no autopsy was performed, but his skull was later recovered. The brain lesion that caused the profound personality changes for which his case became famous has been presumed to have involved the left frontal region, but questions have been raised about the involvement of other regions and about the exact placement of the lesion within the vast frontal territory. Measurements from Gage's skull and modern neuroimaging techniques were used to reconstitute the accident and determine the probable location of the lesion. The damage involved both left and right prefrontal cortices in a pattern that, as confirmed by Gage's modern counterparts, causes a defect in rational decision making and the processing of emotion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Damasio, H -- Grabowski, T -- Frank, R -- Galaburda, A M -- Damasio, A R -- P01 NS19632/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1994 May 20;264(5162):1102-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, University of Iowa Hospitals & Clinics, Iowa City 52242.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8178168" target="_blank"〉PubMed〈/a〉
    Keywords: Accidents, Occupational ; Brain Injuries/history/*psychology ; *Decision Making ; *Emotions ; Explosions ; History, 19th Century ; Humans ; Image Processing, Computer-Assisted ; Male ; Prefrontal Cortex/*injuries/physiology ; Skull/*injuries ; Wounds, Penetrating/history/*psychology
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    Induction of an olfactory memory by the activation of a metabotropic glutamate receptor (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-07-08
    Description: Female mice form an olfactory memory of male pheromones at mating; exposure to the pheromones of a strange male after that mating will block pregnancy. The formation of this memory is mediated by the accessory olfactory system, in which an increase in norepinephrine after mating reduces inhibitory transmission of gamma-aminobutyric acid from the granule cells to the mitral cells. This study shows that the activation of mGluR2, a metabotropic glutamate receptor that suppresses the gamma-aminobutyric acid inhibition of the mitral cells, permits the formation of a specific olfactory memory without the occurrence of mating by infusion of mGluR2 agonists into the female's accessory olfactory bulb. This memory faithfully reflects the memory formed at mating.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaba, H -- Hayashi, Y -- Higuchi, T -- Nakanishi, S -- New York, N.Y. -- Science. 1994 Jul 8;265(5169):262-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, Kochi Medical School, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023145" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cycloleucine/analogs & derivatives/pharmacology ; Cyclopropanes/pharmacology ; Estrus ; Female ; Glycine/analogs & derivatives/pharmacology ; Male ; Mice ; Mice, Inbred BALB C ; Mice, Inbred CBA ; Neuronal Plasticity ; Olfactory Bulb/cytology/*physiology ; Phentolamine/pharmacology ; Pheromones/*pharmacology ; Pregnancy ; Pregnancy, Animal/drug effects/*physiology ; Receptors, AMPA/metabolism ; Receptors, Glutamate/*metabolism ; Receptors, Kainic Acid/metabolism ; Sexual Behavior, Animal/drug effects/*physiology ; gamma-Aminobutyric Acid/metabolism
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    Benefit to male sailfin mollies of mating with heterospecific females (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-01-21
    Description: Female gynogens reproduce clonally but rely on sperm from heterospecific males to initiate embryogenesis. It has been assumed that males gain no benefit from such matings; thus, selection should favor males that avoid them. Here it is shown that males gain a benefit by mating with female gynogens in an asexual-sexual complex of fish. The sexual females increase their preference for males whom they observe consorting with female gynogens. Thus, gynogenetic species might persist because selection favors males to be sexually parasitized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schlupp, I -- Marler, C -- Ryan, M J -- F32 MH10204/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1994 Jan 21;263(5145):373-4.〈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/8278809" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; Male ; Poecilia/*physiology ; *Sexual Behavior, Animal
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    Taking the data in hand--literally--with virtual reality (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taubes, G -- New York, N.Y. -- Science. 1994 Aug 12;265(5174):884-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8052844" target="_blank"〉PubMed〈/a〉
    Keywords: Computer Graphics ; *Computer Simulation ; Drug Design ; Models, Molecular ; User-Computer Interface
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    Long-term potentiation: evidence against an increase in transmitter release probability in the CA1 region of the hippocampus (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-23
    Description: It is widely accepted that N-methyl-D-aspartate (NMDA)-receptor-dependent long-term potentiation (LTP) in the CA1 region of the hippocampus is triggered postsynaptically, but there is considerable debate as to the site at which the increase in synaptic strength is expressed. The irreversible open-channel blocking action of the NMDA receptor antagonist MK-801 has been used to test whether the probability of transmitter release (Pr) is increased during LTP. Although the rate of decline of the amplitude of the NMDA receptor-mediated excitatory postsynaptic current (EPSC) in the presence of MK-801 strongly depends on Pr, the rate of decline of the EPSC evoked at synapses expressing LTP is identical to that observed at synapses not expressing LTP. These findings are difficult to reconcile with models in which the expression of LTP is due to an increase in Pr.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Manabe, T -- Nicoll, R A -- New York, N.Y. -- Science. 1994 Sep 23;265(5180):1888-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7916483" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Dizocilpine Maleate/pharmacology ; Guinea Pigs ; Hippocampus/*metabolism ; In Vitro Techniques ; *Long-Term Potentiation ; Male ; Neurotransmitter Agents/*metabolism ; Receptors, AMPA/antagonists & inhibitors/physiology ; Receptors, N-Methyl-D-Aspartate/antagonists & inhibitors/*physiology ; Synapses/physiology
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    Dependence on REM sleep of overnight improvement of a perceptual skill (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-29
    Description: Several paradigms of perceptual learning suggest that practice can trigger long-term, experience-dependent changes in the adult visual system of humans. As shown here, performance of a basic visual discrimination task improved after a normal night's sleep. Selective disruption of rapid eye movement (REM) sleep resulted in no performance gain during a comparable sleep interval, although non-REM slow-wave sleep disruption did not affect improvement. On the other hand, deprivation of REM sleep had no detrimental effects on the performance of a similar, but previously learned, task. These results indicate that a process of human memory consolidation, active during sleep, is strongly dependent on REM sleep.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karni, A -- Tanne, D -- Rubenstein, B S -- Askenasy, J J -- Sagi, D -- New York, N.Y. -- Science. 1994 Jul 29;265(5172):679-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8036518" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Electrodiagnosis ; Female ; Form Perception/*physiology ; Humans ; Learning/*physiology ; Male ; Sleep Deprivation/physiology ; Sleep Stages/physiology ; Sleep, REM/*physiology
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    Radiation: balancing the record (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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
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    Coding of visual space by premotor neurons (1994)
    American Association for the Advancement of Science (AAAS)
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    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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    Measles vaccine: do we need new vaccines or new programs? (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Mortality rates in a genetically heterogeneous population of Caenorhabditis elegans (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-02-04
    Description: Age-specific mortality rates in isogenic populations of the nematode Caenorhabditis elegans increase exponentially throughout life. In genetically heterogeneous populations, age-specific mortality increases exponentially until about 17 days and then remains constant until the last death occurs at about 60 days. This period of constant age-specific mortality results from genetic heterogeneity. Subpopulations differ in mean life-span, but they all exhibit near exponential, albeit different, rates of increase in age-specific mortality. Thus, much of the observed heterogeneity in mortality rates later in life could result from genetic heterogeneity and not from an inherent effect of aging.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brooks, A -- Lithgow, G J -- Johnson, T E -- K04-AG00369/AG/NIA NIH HHS/ -- R01-AG08332/AG/NIA NIH HHS/ -- R01-AG10248/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 4;263(5147):668-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Behavioral Genetics, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303273" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Animals ; Caenorhabditis elegans/genetics/*physiology ; *Genetic Variation ; Kinetics ; Longevity/genetics ; Mortality
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    A booster for contraceptive vaccines (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    An all D-amino acid opioid peptide with central analgesic activity from a combinatorial library (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Problems in clinical trials go far beyond misconduct (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    How a protein binds B12: A 3.0 A X-ray structure of B12-binding domains of methionine synthase (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Requirement of transcription factor PU.1 in the development of multiple hematopoietic lineages (1994)
    American Association for the Advancement of Science (AAAS)
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    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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    HIV integrase structure catalyzes drug search (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Brien, C -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):1946.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7801119" target="_blank"〉PubMed〈/a〉
    Keywords: Antiviral Agents/pharmacology ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA Nucleotidyltransferases/antagonists & inhibitors/*chemistry/metabolism ; DNA-Binding Proteins/metabolism ; Drug Design ; HIV-1/drug effects/*enzymology ; Integrases ; Models, Molecular ; Virus Integration
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    Women in science. Disparities detailed in NCI division (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Long-range cis preference in DNA homology search over the length of a Drosophila chromosome (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Barriers hold back new contraception strategies (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 138
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    Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Quantitative trait locus for reading disability on chromosome 6 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Molecular genetic analyses of the Tyrolean Ice Man (1994)
    American Association for the Advancement of Science (AAAS)
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    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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    Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-10-21
    Description: The molecular structure of the D-alanine:D-alanine ligase of the ddlB gene of Escherichia coli, co-crystallized with an S,R-methylphosphinate and adenosine triphosphate, was determined by x-ray diffraction to a resolution of 2.3 angstroms. A catalytic mechanism for the ligation of two D-alanine substrates is proposed in which a helix dipole and a hydrogen-bonded triad of tyrosine, serine, and glutamic acid assist binding and deprotonation steps. From sequence comparison, it is proposed that a different triad exists in a recently discovered D-alanine:D-lactate ligase (VanA) present in vancomycin-resistant enterococci. A molecular mechanism for the altered specificity of VanA is suggested.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fan, C -- Moews, P C -- Walsh, C T -- Knox, J R -- 1RO1-AI-34330/AI/NIAID NIH HHS/ -- GM-49338/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 21;266(5184):439-43.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of Connecticut, Storrs 06269-3125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939684" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/chemistry/metabolism ; Amino Acid Sequence ; Bacterial Proteins/chemistry ; Binding Sites ; *Carbon-Oxygen Ligases ; Computer Graphics ; Crystallography, X-Ray ; Dipeptides/biosynthesis ; Drug Resistance, Microbial ; Escherichia coli/drug effects/*enzymology ; Hydrogen Bonding ; Ligases/chemistry ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Peptide Synthases/*chemistry/genetics/metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Substrate Specificity ; Vancomycin/*pharmacology
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    Hin recombinase bound to DNA: the origin of specificity in major and minor groove interactions (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Toxic shock syndrome toxin-1 complexed with a class II major histocompatibility molecule HLA-DR1 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Link to hereditary melanoma brightens mood for p16 gene (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 145
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    Activation of a cerebellar output nucleus during cognitive processing (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 146
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    Variable gearing during locomotion in the human musculoskeletal system (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 147
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    Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-15
    Description: Mutations in the p53 tumor suppressor are the most frequently observed genetic alterations in human cancer. The majority of the mutations occur in the core domain which contains the sequence-specific DNA binding activity of the p53 protein (residues 102-292), and they result in loss of DNA binding. The crystal structure of a complex containing the core domain of human p53 and a DNA binding site has been determined at 2.2 angstroms resolution and refined to a crystallographic R factor of 20.5 percent. The core domain structure consists of a beta sandwich that serves as a scaffold for two large loops and a loop-sheet-helix motif. The two loops, which are held together in part by a tetrahedrally coordinated zinc atom, and the loop-sheet-helix motif form the DNA binding surface of p53. Residues from the loop-sheet-helix motif interact in the major groove of the DNA, while an arginine from one of the two large loops interacts in the minor groove. The loops and the loop-sheet-helix motif consist of the conserved regions of the core domain and contain the majority of the p53 mutations identified in tumors. The structure supports the hypothesis that DNA binding is critical for the biological activity of p53, and provides a framework for understanding how mutations inactivate it.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cho, Y -- Gorina, S -- Jeffrey, P D -- Pavletich, N P -- NCI CA08748-29/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Jul 15;265(5170):346-55.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023157" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Computer Graphics ; Crystallization ; Crystallography, X-Ray ; DNA/*chemistry/metabolism ; Genes, p53 ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; *Mutation ; Nucleic Acid Conformation ; *Protein Conformation ; Protein Structure, Secondary ; Tumor Suppressor Protein p53/*chemistry/genetics/metabolism
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  • 148
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    The spousal abuse problem (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 149
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    De novo and inherited deletions of the 5q13 region in spinal muscular atrophies (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 150
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    Low-barrier hydrogen bonds and enzymic catalysis (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-24
    Description: Formation of a short (less than 2.5 angstroms), very strong, low-barrier hydrogen bond in the transition state, or in an enzyme-intermediate complex, can be an important contribution to enzymic catalysis. Formation of such a bond can supply 10 to 20 kilocalories per mole and thus facilitate difficult reactions such as enolization of carboxylate groups. Because low-barrier hydrogen bonds form only when the pKa's (negative logarithm of the acid constant) of the oxygens or nitrogens sharing the hydrogen are similar, a weak hydrogen bond in the enzyme-substrate complex in which the pKa's do not match can become a strong, low-barrier one if the pKa's become matched in the transition state or enzyme-intermediate complex. Several examples of enzymatic reactions that appear to use this principle are presented.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cleland, W W -- Kreevoy, M M -- GM 18938/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 24;264(5167):1887-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Enzyme Research, University of Wisconsin, Madison 53705.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8009219" target="_blank"〉PubMed〈/a〉
    Keywords: Aconitate Hydratase/chemistry/metabolism ; Binding Sites ; Carboxypeptidases/chemistry/metabolism ; *Catalysis ; Citrate (si)-Synthase/chemistry/metabolism ; Enzymes/*metabolism ; *Hydrogen Bonding ; Isomerases/chemistry/metabolism ; Kinetics ; Orotidine-5'-Phosphate Decarboxylase/chemistry/metabolism ; Racemases and Epimerases/chemistry/metabolism ; Thermolysin/chemistry/metabolism
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  • 151
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    Application and accuracy of molecular phylogenies (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 152
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    Elephant man's disease (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 153
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    Chemical sequence control of beta-sheet assembly in macromolecular crystals of periodic polypeptides (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-02
    Description: A family of uniform periodic polypeptides has been prepared by bacterial expression of the corresponding artificial genes, with the objective of exploring the potential for control of supramolecular organization in genetically engineered protein-based polymeric materials. The repeating units of the polypeptides consist of oligomeric alanyl-glycine sequences interspersed with glutamic acid residues inserted at intervals of 8 to 14 amino acids. Crystallization of such materials from formic acid produces beta-sheet structures in the solid state, as shown by vibrational spectroscopy, nuclear magnetic resonance spectroscopy, and wide-angle x-ray diffraction. The diffraction results, together with observations from electron microscopy, are consistent with the formation of needle-shaped lamellar crystals whose thickness is controlled by the periodicity of the primary sequence. These results can be used to control solid-state structure in macromolecular materials.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krejchi, M T -- Atkins, E D -- Waddon, A J -- Fournier, M J -- Mason, T L -- Tirrell, D A -- New York, N.Y. -- Science. 1994 Sep 2;265(5177):1427-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Polymer Science and Engineering, University of Massachusetts, Amherst 01003.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8073284" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Computer Simulation ; Crystallization ; Crystallography, X-Ray ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Microscopy, Electron ; Models, Molecular ; Molecular Sequence Data ; Peptides/*chemistry ; *Protein Engineering ; *Protein Structure, Secondary ; Recombinant Proteins/*chemistry/ultrastructure ; Spectrum Analysis, Raman
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  • 154
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    Alpha-helical coiled coils: more facts and better predictions (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, C -- Parry, D A -- AR17346/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jan 28;263(5146):488-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254-9110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8290957" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography, X-Ray ; *DNA-Binding Proteins ; Fungal Proteins/chemistry ; Hemagglutinin Glycoproteins, Influenza Virus ; Hemagglutinins, Viral/chemistry ; Leucine Zippers ; Models, Molecular ; Protein Kinases/chemistry ; *Protein Structure, Secondary ; *Protein Structure, Tertiary ; *Saccharomyces cerevisiae Proteins ; Spectrin/chemistry
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  • 155
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    Could drugs, rather than a virus, be the cause of AIDS? (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 156
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    Genetic dissection of complex traits (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 157
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    Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-21
    Description: Mechanistic information and structure-based design methods have been used to design a series of nonpeptide cyclic ureas that are potent inhibitors of human immunodeficiency virus (HIV) protease and HIV replication. A fundamental feature of these inhibitors is the cyclic urea carbonyl oxygen that mimics the hydrogen-bonding features of a key structural water molecule. The success of the design in both displacing and mimicking the structural water molecule was confirmed by x-ray crystallographic studies. Highly selective, preorganized inhibitors with relatively low molecular weight and high oral bioavailability were synthesized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lam, P Y -- Jadhav, P K -- Eyermann, C J -- Hodge, C N -- Ru, Y -- Bacheler, L T -- Meek, J L -- Otto, M J -- Rayner, M M -- Wong, Y N -- New York, N.Y. -- Science. 1994 Jan 21;263(5145):380-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Virology Research, DuPont Merck Pharmaceutical Company, Wilmington, DE 19880.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8278812" target="_blank"〉PubMed〈/a〉
    Keywords: Administration, Oral ; Animals ; Azepines/*chemistry/metabolism/pharmacokinetics/pharmacology ; Binding Sites ; Biological Availability ; Cell Line ; Crystallography, X-Ray ; Dogs ; *Drug Design ; Drug Evaluation, Preclinical ; HIV Protease/chemistry/metabolism ; HIV Protease Inhibitors/*chemistry/metabolism/pharmacokinetics/pharmacology ; HIV-1/drug effects/physiology ; Hydrogen Bonding ; Models, Molecular ; Molecular Conformation ; Molecular Weight ; Rats ; Recombinant Proteins/chemistry/metabolism ; Urea ; Virus Replication/drug effects
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    A strong candidate for the breast and ovarian cancer susceptibility gene BRCA1 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 159
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    Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-07
    Description: Bacteriorhodopsin was selectively spin labeled at residues 72, 101, or 105 after replacement of the native amino acids by cysteine. Only the electron paramagnetic resonance spectrum of the label at 101 was time-dependent during the photocycle. The spectral change rose with the decay of the M intermediate and fell with recovery of the ground state. The transient signal is interpreted as the result of movement in the C-D or E-F interhelical loop, or in both, coincident with protonation changes at the key aspartate 96 residue. These results link the optically characterized intermediates with localized conformational changes in bacteriorhodopsin during the photocycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steinhoff, H J -- Mollaaghababa, R -- Altenbach, C -- Hideg, K -- Krebs, M -- Khorana, H G -- Hubbell, W L -- EY05216/EY/NEI NIH HHS/ -- GM28289/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 7;266(5182):105-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Biophysik, Ruhr-Universitat Bochum, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939627" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriorhodopsins/*chemistry/genetics ; Electron Spin Resonance Spectroscopy ; Light ; Models, Molecular ; Mutagenesis, Site-Directed ; *Protein Conformation ; Protein Structure, Secondary ; Spin Labels
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    A unified polymerase mechanism for nonhomologous DNA and RNA polymerases (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 161
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    Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-02
    Description: Mechanisms of guanosine triphosphate (GTP) hydrolysis by members of the G protein alpha subunit-p21ras superfamily of guanosine triphosphatases have been studied extensively but have not been well understood. High-resolution x-ray structures of the GTP gamma S and GDP.AlF4- complexes formed by the G protein Gi alpha 1 demonstrate specific roles in transition-state stabilization for two highly conserved residues. Glutamine204 (Gln61 in p21ras) stabilizes and orients the hydrolytic water in the trigonal-bipyramidal transition state. Arginine 178 stabilizes the negative charge at the equatorial oxygen atoms of the pentacoordinate phosphate intermediate. Conserved only in the G alpha family, this residue may account for the higher hydrolytic rate of G alpha proteins relative to those of the p21ras family members. The fold of Gi alpha 1 differs from that of the homologous Gt alpha subunit in the conformation of a helix-loop sequence located in the alpha-helical domain that is characteristic of these proteins; this site may participate in effector binding. The amino-terminal 33 residues are disordered in GTP gamma S-Gi alpha 1, suggesting a mechanism that may promote release of the beta gamma subunit complex when the alpha subunit is activated by GTP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coleman, D E -- Berghuis, A M -- Lee, E -- Linder, M E -- Gilman, A G -- Sprang, S R -- DK 46371/DK/NIDDK NIH HHS/ -- GM34497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 2;265(5177):1405-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Dallas, TX.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8073283" target="_blank"〉PubMed〈/a〉
    Keywords: Aluminum Compounds/metabolism ; Arginine/chemistry ; Binding Sites ; Catalysis ; Computer Graphics ; Crystallography, X-Ray ; Fluorides/metabolism ; GTP-Binding Proteins/*chemistry/metabolism ; Glutamine/chemistry ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/*metabolism ; Helix-Loop-Helix Motifs ; Hydrogen Bonding ; Hydrolysis ; Models, Molecular ; *Protein Conformation ; Protein Structure, Secondary
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  • 162
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    Role of NO production in NMDA receptor-mediated neurotransmitter release in cerebral cortex (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-07
    Description: The structure of a protein triple helix has been determined at 1.9 angstrom resolution by x-ray crystallographic studies of a collagen-like peptide containing a single substitution of the consensus sequence. This peptide adopts a triple-helical structure that confirms the basic features determined from fiber diffraction studies on collagen: supercoiling of polyproline II helices and interchain hydrogen bonding that follows the model II of Rich and Crick. In addition, the structure provides new information concerning the nature of this protein fold. Each triple helix is surrounded by a cylinder of hydration, with an extensive hydrogen bonding network between water molecules and peptide acceptor groups. Hydroxyproline residues have a critical role in this water network. The interaxial spacing of triple helices in the crystal is similar to that in collagen fibrils, and the water networks linking adjacent triple helices in the crystal structure are likely to be present in connective tissues. The breaking of the repeating (X-Y-Gly)n pattern by a Gly--〉Ala substitution results in a subtle alteration of the conformation, with a local untwisting of the triple helix. At the substitution site, direct interchain hydrogen bonds are replaced with interstitial water bridges between the peptide groups. Similar conformational changes may occur in Gly--〉X mutated collagens responsible for the diseases osteogenesis imperfecta, chondrodysplasias, and Ehlers-Danlos syndrome IV.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bella, J -- Eaton, M -- Brodsky, B -- Berman, H M -- AR 19626/AR/NIAMS NIH HHS/ -- GM 21589/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 7;266(5182):75-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Rutgers University, New Brunswick, NJ 08855.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7695699" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine/chemistry ; Amino Acid Sequence ; Collagen/*chemistry ; Computer Graphics ; Crystallography, X-Ray ; Glycine/chemistry ; Hydrogen Bonding ; Hydroxyproline/chemistry ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Peptides/*chemistry ; *Protein Conformation ; Protein Structure, Secondary
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  • 164
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    The mobile flavin of 4-OH benzoate hydroxylase (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 165
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    Decoding chimp genes and lives (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 166
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    Folding pattern diversity of integral membrane proteins (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cowan, S W -- Rosenbusch, J P -- New York, N.Y. -- Science. 1994 May 13;264(5161):914-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biozentrum, University of Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8178151" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Amino Acid Sequence ; Bacteriorhodopsins/chemistry ; Cell Membrane/chemistry ; Hydrogen Bonding ; Membrane Proteins/*chemistry ; Models, Molecular ; Molecular Sequence Data ; Porins/chemistry ; *Protein Folding ; Protein Structure, Secondary
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  • 167
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    Crystal structures at 2.5 angstrom resolution of seryl-tRNA synthetase complexed with two analogs of seryl adenylate (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 168
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    Antibody catalyzed cationic cyclization (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-05-27
    Description: Two major goals for the design of new catalysts are the facilitation of chemical transformations and control of product outcome. An antibody has been induced that efficiently catalyzes a cationic cyclization in which an acyclic olefinic sulfonate ester substrate is converted almost exclusively (98 percent) to a cyclic alcohol. The key to the catalysis of the reaction and the restriction of the product complexity is the use of antibody binding energy to rigidly enforce a concerted mechanism in accord with the design of the hapten. Thus, the ability to direct binding energy allows the experimenter to dictate a reaction mechanism which is an otherwise difficult task in chemistry. New catalysts for cationic cyclization may be of general use in the formation of carbon-carbon and carbon-heteroatom bonds leading to multi-ring molecules including steroids and heterocyclic compounds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, T -- Janda, K D -- Ashley, J A -- Lerner, R A -- GM-43858/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 May 27;264(5163):1289-93.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Scripps Research Institute, Department of Molecular Biology, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8191282" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Catalytic/*chemistry ; Antibodies, Monoclonal/chemistry ; Catalysis ; Cations/*chemistry ; Chromatography, Gas ; Cyclization ; Haptens ; Kinetics ; Mice ; Organosilicon Compounds/*chemistry ; Sulfanilic Acids/*chemistry
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  • 169
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    Selection of guide sequences that direct efficient cleavage of mRNA by human ribonuclease P (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-04
    Description: Any RNA, when in a complex with another oligoribonucleotide known as an external guide sequence (EGS), can become a substrate for ribonuclease P. Simulation of evolution in vitro was used to select EGSs that bind tightly to a target substrate messenger RNA and that increase the efficiency of cleavage of the target by human ribonuclease P to a level equal to that achieved with natural substrates. The most efficient EGSs form transfer RNA precursor-like structures with the target RNA, in which the analog of the anticodon stem has been disrupted, an indication that selection for the optimal substrate for ribonuclease P yields an RNA structure different from that of present-day transfer RNA precursors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yuan, Y -- Altman, S -- AI31876/AI/NIAID NIH HHS/ -- GM19422/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Mar 4;263(5151):1269-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Yale University, New Haven, CT 06520.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8122108" target="_blank"〉PubMed〈/a〉
    Keywords: Anticodon/chemistry/metabolism ; Base Sequence ; Chloramphenicol O-Acetyltransferase/genetics ; Endoribonucleases/*metabolism ; Humans ; Kinetics ; Magnesium/pharmacology ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligoribonucleotides/chemistry/*metabolism ; RNA Precursors/chemistry/metabolism ; RNA, Catalytic/*metabolism ; RNA, Guide/chemistry/*metabolism ; RNA, Messenger/chemistry/*metabolism ; RNA, Transfer/chemistry/metabolism ; Ribonuclease P ; Thermodynamics
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  • 170
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    Exocytosis in spermatozoa in response to progesterone and zona pellucida (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 171
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    Kinetic intermediates in RNA folding (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-12
    Description: The folding pathways of large, highly structured RNA molecules are largely unexplored. Insight into both the kinetics of folding and the presence of intermediates was provided in a study of the Mg(2+)-induced folding of the Tetrahymena ribozyme by hybridization of complementary oligodeoxynucleotide probes. This RNA folds via a complex mechanism involving both Mg(2+)-dependent and Mg(2+)-independent steps. A hierarchical model for the folding pathway is proposed in which formation of one helical domain (P4-P6) precedes that of a second helical domain (P3-P7). The overall rate-limiting step is formation of P3-P7, and takes place with an observed rate constant of 0.72 +/- 0.14 minute-1. The folding mechanism of large RNAs appears similar to that of many multidomain proteins in that formation of independently stable substructures precedes their association into the final conformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zarrinkar, P P -- Williamson, J R -- New York, N.Y. -- Science. 1994 Aug 12;265(5174):918-24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8052848" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Introns ; Kinetics ; Magnesium/metabolism/pharmacology ; Models, Chemical ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; RNA, Catalytic/*chemistry/metabolism ; RNA, Protozoan/*chemistry ; Ribonuclease H/metabolism ; Temperature ; Tetrahymena/*genetics
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  • 172
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    Pf1 virus structure: helical coat protein and DNA with paraxial phosphates (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-29
    Description: The helical path of the DNA in filamentous bacteriophage Pf1 was deduced from different kinds of existing structural information, including results from x-ray fiber diffraction. The DNA has the same pitch, 16 angstroms, as the surrounding helix of protein subunits; the rise and rotation per nucleotides are 6.1 angstroms and 132 degrees, respectively; and the phosphates are 2.5 angstroms from the axis. The DNA in Pf1 is, therefore, the most extended and twisted DNA structure known. On the basis of the DNA structure and extensive additional information about the protein, a model of the virion is proposed. In the model, the DNA bases reach out, into the protein, and the lysine and arginine side chains reach in, between the DNA bases, to stabilize the paraxial phosphate charges; the conformation of the protein subunit is a combination of alpha and 3(10) helices.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, D J -- Day, L A -- GM42286/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jul 29;265(5172):671-4.〈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/8036516" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Capsid/*chemistry ; *Capsid Proteins ; DNA, Viral/*chemistry ; Inovirus/chemistry/genetics/*ultrastructure ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Phosphates/analysis ; Protein Structure, Secondary ; X-Ray Diffraction
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    Loudness-coding mechanisms inferred from electric stimulation of the human auditory system (1994)
    American Association for the Advancement of Science (AAAS)
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    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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    Candidate gene associated with a mutation causing recessive polycystic kidney disease in mice (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    A comprehensive human linkage map with centimorgan density. Cooperative Human Linkage Center (CHLC) (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Anthropologists take the measure of humanity (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    The 2.9 A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser) (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR (1994)
    American Association for the Advancement of Science (AAAS)
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    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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  • 179
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    Homozygous human TAP peptide transporter mutation in HLA class I deficiency (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Abnormal development of peripheral lymphoid organs in mice deficient in lymphotoxin (1994)
    American Association for the Advancement of Science (AAAS)
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    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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    Mutational isolation of a sieve for editing in a transfer RNA synthetase (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-04-08
    Description: Editing reactions are essential for the high fidelity of information transfer in processes such as replication, RNA splicing, and protein synthesis. The accuracy of interpretation of the genetic code is enhanced by the editing reactions of aminoacyl transfer RNA (tRNA) synthetases, whereby amino acids are prevented from being attached to the wrong tRNAs. Amino acid discrimination is achieved through sieves that may overlap with or coincide with the amino acid binding site. With the class I Escherichia coli isoleucine tRNA synthetase, which activates isoleucine and occasionally misactivates valine, as an example, a rationally chosen mutant enzyme was constructed that lacks entirely its normal strong ability to distinguish valine from isoleucine by the initial amino acid recognition sieve. The misactivated valine, however, is still eliminated by hydrolytic editing reactions. These data suggest that there is a distinct sieve for editing that is functionally independent of the amino acid binding site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schmidt, E -- Schimmel, P -- GM 15539/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 8;264(5156):265-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8146659" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Binding Sites ; Escherichia coli/enzymology ; Isoleucine/*metabolism ; Isoleucine-tRNA Ligase/chemistry/genetics/*metabolism ; Kinetics ; Mutation ; Protein Structure, Secondary ; *RNA Editing ; RNA, Transfer, Ile/metabolism ; Valine/*metabolism
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    Convergent pathways for steroid hormone- and neurotransmitter-induced rat sexual behavior (1994)
    American Association for the Advancement of Science (AAAS)
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    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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    Laminar comparison of somatosensory cortical plasticity (1994)
    American Association for the Advancement of Science (AAAS)
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    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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  • 184
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    Release of adenosine by activation of NMDA receptors in the hippocampus (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 185
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    Experimental support for the "hydrophobic zipper" hypothesis (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gronenborn, A M -- Clore, G M -- New York, N.Y. -- Science. 1994 Jan 28;263(5146):536.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8290964" target="_blank"〉PubMed〈/a〉
    Keywords: Hydrogen Bonding ; Interleukin-1/*chemistry ; Models, Molecular ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 186
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    A potential noninvasive neurobiological test for Alzheimer's disease (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 187
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    Cancer prevention. Beta-carotene: helpful or harmful? (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 188
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    Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 189
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    Contraceptive methods go back to the basics (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 190
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    Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-25
    Description: Intracellular vesicles destined to fuse with the plasma membrane and secrete their contents must have a mechanism for specifically interacting with the appropriate target membrane. Such a mechanism is now suggested by the demonstration of specific interaction between vesicular proteins and plasma membrane proteins. The vesicle-associated membrane proteins (VAMPs) 1 and 2 specifically bind the acceptor membrane proteins syntaxin 1A and 4 but not syntaxin 2 or 3. The binding site is within amino acids 194 to 267 of syntaxin 1A, and the approximate equilibrium dissociation constants is 4.7 x 10(-6) molar. These data suggest a physical basis for the specificity of intracellular vesicular transport.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Calakos, N -- Bennett, M K -- Peterson, K E -- Scheller, R H -- New York, N.Y. -- Science. 1994 Feb 25;263(5150):1146-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Stanford University Medical Center, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8108733" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Surface/*metabolism ; Binding Sites ; Cell Line ; Cell Membrane/metabolism ; Cytoplasm/metabolism ; Haplorhini ; Kinetics ; Membrane Proteins/*metabolism ; Molecular Sequence Data ; Nerve Tissue Proteins/*metabolism ; R-SNARE Proteins ; Recombinant Fusion Proteins/metabolism ; Synaptic Vesicles/*metabolism ; Syntaxin 1
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 191
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    New enzyme structure reveals cell's rotary engine (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 192
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    Soluble beta-amyloid induction of Alzheimer's phenotype for human fibroblast K+ channels (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 193
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    Ecological and genetic factors in conservation: a cautionary tale (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 194
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    Specific association of human telomerase activity with immortal cells and cancer (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 195
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    Fertility decline in East Asia (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 196
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    Taking a first look at a tyrosine phosphatase (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 197
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    Triple repeat DNA as a highly mutable regulatory mechanism (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 198
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    Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 199
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    Magnetic field effects on B12 ethanolamine ammonia lyase: evidence for a radical mechanism (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-18
    Description: A change in radical pair recombination rates is one of the few mechanisms by which a magnetic field can interact with a biological system. The kinetic parameter Vmax/Km (where Km is the Michaelis constant) for the coenzyme B12-dependent enzyme ethanolamine ammonia lyase was decreased 25 percent by a static magnetic field near 0.1 tesla (1000 gauss) with unlabeled ethanolamine and decreased 60 percent near 0.15 tesla with perdeuterated ethanolamine. This effect is likely caused by a magnetic field-induced change in intersystem crossing rates between the singlet and triplet spin states in the [cob(II)alamin:5'-deoxyadenosyl radical] spin-correlated radical pair.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harkins, T T -- Grissom, C B -- ES05728/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 18;263(5149):958-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Utah, Salt Lake City 84112.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8310292" target="_blank"〉PubMed〈/a〉
    Keywords: Deuterium ; Ethanolamine ; Ethanolamine Ammonia-Lyase/*metabolism ; Ethanolamines/metabolism ; Kinetics ; *Magnetics ; Photolysis ; Vitamin B 12/pharmacology
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  • 200
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    Sex determination and dosage compensation: lessons from flies and worms (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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