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  • Articles  (15,794)
  • American Geophysical Union  (9,634)
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  • Articles  (15,794)
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  • 11
    Publication Date: 1998-03-21
    Description: The T cell receptor (TCR) inherently has dual specificity. T cells must recognize self-antigens in the thymus during maturation and then discriminate between foreign pathogens in the periphery. A molecular basis for this cross-reactivity is elucidated by the crystal structure of the alloreactive 2C TCR bound to self peptide-major histocompatibility complex (pMHC) antigen H-2Kb-dEV8 refined against anisotropic 3.0 angstrom resolution x-ray data. The interface between peptide and TCR exhibits extremely poor shape complementarity, and the TCR beta chain complementarity-determining region 3 (CDR3) has minimal interaction with the dEV8 peptide. Large conformational changes in three of the TCR CDR loops are induced upon binding, providing a mechanism of structural plasticity to accommodate a variety of different peptide antigens. Extensive TCR interaction with the pMHC alpha helices suggests a generalized orientation that is mediated by the Valpha domain of the TCR and rationalizes how TCRs can effectively "scan" different peptides bound within a large, low-affinity MHC structural framework for those that provide the slight additional kinetic stabilization required for signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garcia, K C -- Degano, M -- Pease, L R -- Huang, M -- Peterson, P A -- Teyton, L -- Wilson, I A -- AI42266/AI/NIAID NIH HHS/ -- AI42267/AI/NIAID NIH HHS/ -- R01 CA58896/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1166-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and the Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9469799" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crystallization ; Crystallography, X-Ray ; H-2 Antigens/*chemistry/*immunology/metabolism ; Ligands ; Mice ; Mice, Transgenic ; Models, Molecular ; Mutation ; Oligopeptides/*chemistry/immunology/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Receptors, Antigen, T-Cell, alpha-beta/*chemistry/*immunology/metabolism ; Recombinant 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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  • 12
    Publication Date: 1998-12-16
    Description: A peripheral membrane protein that is interactive with lymphocytic choriomeningitis virus (LCMV) was purified from cells permissive to infection. Tryptic peptides from this protein were determined to be alpha-dystroglycan (alpha-DG). Several strains of LCMV and other arenaviruses, including Lassa fever virus (LFV), Oliveros, and Mobala, bound to purified alpha-DG protein. Soluble alpha-DG blocked both LCMV and LFV infection. Cells bearing a null mutation of the gene encoding DG were resistant to LCMV infection, and reconstitution of DG expression in null mutant cells restored susceptibility to LCMV infection. Thus, alpha-DG is a cellular receptor for both LCMV and LFV.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cao, W -- Henry, M D -- Borrow, P -- Yamada, H -- Elder, J H -- Ravkov, E V -- Nichol, S T -- Compans, R W -- Campbell, K P -- Oldstone, M B -- AG 00080/AG/NIA NIH HHS/ -- AI 09484/AI/NIAID NIH HHS/ -- DK09712/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 Dec 11;282(5396):2079-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Virology, Department of Neuropharmacology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9851928" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arenavirus/metabolism ; Cell Line ; Cytoskeletal Proteins/chemistry/genetics/*metabolism ; Dystroglycans ; Lassa virus/*metabolism/physiology ; Lymphocytic choriomeningitis virus/*metabolism/physiology ; Membrane Glycoproteins/chemistry/genetics/*metabolism ; Mice ; Molecular Sequence Data ; Mutation ; Receptors, Virus/chemistry/*metabolism ; Recombinant Fusion Proteins/metabolism ; Virus Replication
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-10-30
    Description: High-precision mass spectrometric analysis of chromium in sediment samples from the Cretaceous-Tertiary (K-T) boundary coincident with the extinction of numerous organisms on Earth confirms the cosmic origin of the K-T phenomenon. The isotopic composition of chromium in K-T boundary samples from Stevns Klint, Denmark, and Caravaca, Spain, is different from that of Earth and indicates its extraterrestrial source. The chromium isotopic signature is consistent with a carbonaceous chondrite-type impactor. The observed differences in the chromium isotopic composition among various meteorite classes can serve as a diagnostic tool for deciphering the nature of impactors that have collided with Earth during its history.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shukolyukov, A -- Lugmair, G W -- New York, N.Y. -- Science. 1998 Oct 30;282(5390):927-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Scripps Institution of Oceanography, University of California, San Diego, La Jolla, CA 92093-0212, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9794759" target="_blank"〉PubMed〈/a〉
    Keywords: Chromium/analysis ; Chromium Isotopes/*analysis ; Denmark ; *Earth (Planet) ; Geologic Sediments/*chemistry ; Mass Spectrometry ; *Meteoroids ; Spain
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  • 14
    Publication Date: 1998-10-17
    Description: The Trifid nebula is a young (10(5) years) galactic HII region where several protostellar sources have been detected with the infrared space observatory. The sources are massive (17 to 60 solar masses) and are associated with molecular gas condensations at the edges or inside the nebula. They appear to be in an early evolutionary stage and may represent the most recent generation of stars in the Trifid. These sources range from dense, apparently still inactive cores to more evolved sources, undergoing violent mass ejection episodes, including a source that powers an optical jet. These observations suggest that the protostellar sources may have evolved by induced star formation in the Trifid nebula.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cernicharo -- Lefloch -- Cox -- Cesarsky -- Esteban -- Yusef-Zadeh -- Mendez -- Acosta-Pulido -- Garcia Lopez RJ -- Heras -- New York, N.Y. -- Science. 1998 Oct 16;282(5388):462-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉J. Cernicharo, Instituto de Estructura de la Materia, Dpto. Fisica Molecular, Consejo Superior de Investigaciones Cientificas, (CSIC), Serrano 123, 28006 Madrid, Spain. B. Lefloch, Instituto de Estructura de la Materia, Dpto. Fisica Molecu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9774270" target="_blank"〉PubMed〈/a〉
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-05-19
    Description: Data from mid-ocean ridge basalt glasses indicate that the short-lived radionuclide plutonium-244 that was present during an early stage of the development of the solar system is responsible for roughly 30 percent of the fissiogenic xenon excesses in the interior of Earth today. The rest of the fissiogenic xenon can be ascribed to the spontaneous fission of still live uranium-238. This result, in combination with the refined determination of xenon-129 excesses from extinct iodine-129, implies that the accretion of Earth was finished roughly 50 million to 70 million years after solar system formation and that the atmosphere was formed by mantle degassing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kunz -- Staudacher -- Allegre -- New York, N.Y. -- Science. 1998 May 8;280(5365):877-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉J. Kunz, Institut de Physique du Globe de Paris, Laboratoire de Geochimie et Cosmochimie, Centre National de la Recherche Scientifique URA 1758, 4 place Jussieu, F-75252 Paris Cedex 05, France. T. Staudacher, Institut de Physique du.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9572726" target="_blank"〉PubMed〈/a〉
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  • 16
    Publication Date: 1998-04-16
    Description: Although cytotoxic T lymphocytes (CTLs) are thought to be involved in the control of human immunodeficiency virus-type 1 (HIV-1) infection, it has not been possible to demonstrate a direct relation between CTL activity and plasma RNA viral load. Human leukocyte antigen-peptide tetrameric complexes offer a specific means to directly quantitate circulating CTLs ex vivo. With the use of the tetrameric complexes, a significant inverse correlation was observed between HIV-specific CTL frequency and plasma RNA viral load. In contrast, no significant association was detected between the clearance rate of productively infected cells and frequency of HIV-specific CTLs. These data are consistent with a significant role for HIV-specific CTLs in the control of HIV infection and suggest a considerable cytopathic effect of the virus in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ogg, G S -- Jin, X -- Bonhoeffer, S -- Dunbar, P R -- Nowak, M A -- Monard, S -- Segal, J P -- Cao, Y -- Rowland-Jones, S L -- Cerundolo, V -- Hurley, A -- Markowitz, M -- Ho, D D -- Nixon, D F -- McMichael, A J -- MO1-RR00102/RR/NCRR NIH HHS/ -- U01AI41534/AI/NIAID NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1998 Mar 27;279(5359):2103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Medicine, Nuffield Department of Medicine, Oxford OX3 9DS, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9516110" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-HIV Agents/therapeutic use ; CD4 Lymphocyte Count ; Coloring Agents ; Cytopathogenic Effect, Viral ; Cytotoxicity, Immunologic ; Flow Cytometry ; Gene Products, gag ; Gene Products, pol ; HIV Infections/drug therapy/*immunology/*virology ; HIV-1/genetics/*physiology ; HLA-A Antigens ; Humans ; Lymphocyte Count/*methods ; Oligopeptides ; RNA, Viral/*blood ; Sensitivity and Specificity ; T-Lymphocytes, Cytotoxic/*immunology ; Viral Load ; Viremia
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  • 17
    Publication Date: 1998-04-02
    Description: Nucleophilic displacement reactions (the SN2 reaction) of ions in the gas phase are a prototypical reaction system that allows a study of dynamics, mechanisms, and structure-energy relations. This article reviews aspects of the kinetics (especially the applicability of statistical reaction rate theory), the relation of structure and reactivity, and the effects of small numbers of solvent molecules on the reaction and compares the behavior of the ionic reaction in the gas phase with that in solution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chabinyc -- Craig -- Regan -- Brauman -- New York, N.Y. -- Science. 1998 Mar 20;279(5358):1882-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉M. L. Chabinyc, C. K. Regan, and J. I. Brauman are in the Department of Chemistry, Stanford University, Stanford, CA 94305-5080, USA. S. L. Craig is in the Central Research and Development Department, E. I. DuPont de Nemours and Company, Incorporated〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9506930" target="_blank"〉PubMed〈/a〉
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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-09-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, A -- New York, N.Y. -- Science. 1998 Sep 4;281(5382):1432-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9750111" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; *Chromosomes, Human ; Gene Expression ; *Genome ; *Genome, Human ; Hominidae/*genetics ; *Human Characteristics ; Humans ; Mutation ; Pan troglodytes/genetics ; *Sequence Analysis, DNA ; Sialic Acids/chemistry/physiology ; Species Specificity
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-04-29
    Description: After the vertebrate lens is induced from head ectoderm, lens-specific genes are expressed. Transcriptional regulation of the lens-specific alphaA-crystallin gene is controlled by an enhancer element, alphaCE2. A gene encoding an alphaCE2-binding protein, L-maf(lens-specific maf), was isolated. L-maf expression is initiated in the lens placode and is restricted to lens cells. The gene product L-Maf regulates the expression of multiple genes expressed in the lens, and ectopic expression of this transcription factor converts chick embryonic ectodermal cells and cultured cells into lens fibers. Thus, vertebrate lens induction and differentiation can be triggered by the activation of L-Maf.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ogino, H -- Yasuda, K -- New York, N.Y. -- Science. 1998 Apr 3;280(5360):115-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-0101, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9525857" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Basic-Leucine Zipper Transcription Factors ; Cell Differentiation ; Cells, Cultured ; Chick Embryo ; Crystallins/genetics ; DNA, Complementary ; DNA-Binding Proteins/chemistry/genetics ; Ectoderm ; Enhancer Elements, Genetic ; Eye Proteins/genetics ; G-Box Binding Factors ; *Gene Expression Regulation, Developmental ; Genes, Reporter ; Intermediate Filament Proteins/genetics ; Lens, Crystalline/*cytology/*embryology/metabolism ; Maf Transcription Factors ; Molecular Sequence Data ; Promoter Regions, Genetic ; Recombinant Fusion Proteins/metabolism ; Transcription Factors/chemistry/genetics/*metabolism ; *Transcription, Genetic ; Transcriptional Activation ; Transfection
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  • 20
    Publication Date: 1998-08-07
    Description: The small guanosine triphosphatases (GTPases) Cdc42 and Rac1 regulate E-cadherin-mediated cell-cell adhesion. IQGAP1, a target of Cdc42 and Rac1, was localized with E-cadherin and beta-catenin at sites of cell-cell contact in mouse L fibroblasts expressing E-cadherin (EL cells), and interacted with E-cadherin and beta-catenin both in vivo and in vitro. IQGAP1 induced the dissociation of alpha-catenin from a cadherin-catenin complex in vitro and in vivo. Overexpression of IQGAP1 in EL cells, but not in L cells expressing an E-cadherin-alpha-catenin chimeric protein, resulted in a decrease in E-cadherin-mediated cell-cell adhesive activity. Thus, IQGAP1, acting downstream of Cdc42 and Rac1, appears to regulate cell-cell adhesion through the cadherin-catenin pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuroda, S -- Fukata, M -- Nakagawa, M -- Fujii, K -- Nakamura, T -- Ookubo, T -- Izawa, I -- Nagase, T -- Nomura, N -- Tani, H -- Shoji, I -- Matsuura, Y -- Yonehara, S -- Kaibuchi, K -- New York, N.Y. -- Science. 1998 Aug 7;281(5378):832-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Signal Transduction, Nara Institute of Science and Technology, Ikoma 630-0101, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9694656" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cadherins/*metabolism ; *Cell Adhesion ; Cell Cycle Proteins/*metabolism ; Cell Membrane/metabolism ; Cytoskeletal Proteins/metabolism ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/*metabolism ; GTPase-Activating Proteins ; L Cells (Cell Line) ; Mice ; Mutation ; Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism ; *Trans-Activators ; alpha Catenin ; beta Catenin ; cdc42 GTP-Binding Protein ; rac GTP-Binding Proteins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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