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  • Base Sequence  (130)
  • American Association for the Advancement of Science (AAAS)  (130)
  • American Meteorological Society
  • Cell Press
  • 1995-1999  (130)
  • 1990-1994
  • 1996  (130)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (130)
  • American Meteorological Society
  • Cell Press
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  • 1995-1999  (130)
  • 1990-1994
Year
  • 101
    Publication Date: 1996-07-12
    Description: C2 domains are found in many proteins involved in membrane traffic or signal transduction. Although C2 domains are thought to bind calcium ions, the structural basis for calcium binding is unclear. Analysis of calcium binding to C2 domains of synaptotagmin I and protein kinase C-beta by nuclear magnetic resonance spectroscopy revealed a bipartite calcium-binding motif that involves the coordination of two calcium ions by five aspartate residues located on two separate loops. Sequence comparisons indicated that this may be a widely used calcium-binding motif, designated here as the C2 motif.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shao, X -- Davletov, B A -- Sutton, R B -- Sudhof, T C -- Rizo, J -- R01-MH52804-01/MH/NIMH NIH HHS/ -- R29 NS33731-01A1/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):248-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75235, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662510" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/chemistry ; Base Sequence ; Calcium/*metabolism ; *Calcium-Binding Proteins ; Crystallography, X-Ray ; Hydrogen-Ion Concentration ; Magnetic Resonance Spectroscopy ; Membrane Glycoproteins/*chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Nerve Tissue Proteins/*chemistry/*metabolism ; Phospholipids/metabolism ; Protein Conformation ; Protein Folding ; Protein Kinase C/chemistry/*metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Synaptotagmin I ; Synaptotagmins ; Temperature
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  • 102
    Publication Date: 1996-08-02
    Description: A cytoplasmically inherited genetic element in yeast, [PSI+], was confirmed to be a prionlike aggregate of the cellular protein Sup35 by differential centrifugation analysis and microscopic localization of a Sup35-green fluorescent protein fusion. Aggregation depended on the intracellular concentration and functional state of the chaperone protein Hsp104 in the same manner as did [PSI+] inheritance. The amino-terminal and carboxy-terminal domains of Sup35 contributed to the unusual behavior of [PSI+]. [PSI+] altered the conformational state of newly synthesized prion proteins, inducing them to aggregate as well, thus fulfilling a major tenet of the prion hypothesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Patino, M M -- Liu, J J -- Glover, J R -- Lindquist, S -- GM25874/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 2;273(5275):622-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and the Department of Molecular Genetics and Cell Biology, University of Chicago, 5841 South Maryland Avenue, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662547" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Fungal Proteins/analysis/*chemistry/genetics/physiology ; Green Fluorescent Proteins ; Heat-Shock Proteins/physiology ; Luminescent Proteins/analysis ; Molecular Sequence Data ; Peptide Termination Factors ; Phenotype ; Prions/*chemistry/genetics ; *Protein Conformation ; Recombinant Fusion Proteins/analysis/chemistry ; Saccharomyces cerevisiae/*chemistry/*genetics ; *Saccharomyces cerevisiae Proteins ; Solubility
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  • 103
    Publication Date: 1996-05-24
    Description: Transforming growth factor-beta (TGF-beta) regulates many aspects of cellular function. A member of the mitogen-activated protein kinase kinase kinase (MAPKKK) family, TAK1, was previously identified as a mediator in the signaling pathway of TGF-beta superfamily members. The yeast two-hybrid system has now revealed two human proteins, termed TAB1 and TAB2 (for TAK1 binding protein), that interact with TAK1. TAB1 and TAK1 were co-immunoprecipitated from mammalian cells. Overproduction of TAB1 enhanced activity of the plasminogen activator inhibitor 1 gene promoter, which is regulated by TGF-beta, and increased the kinase activity of TAK1. TAB1 may function as an activator of the TAK1 MAPKKK in TGF-beta signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shibuya, H -- Yamaguchi, K -- Shirakabe, K -- Tonegawa, A -- Gotoh, Y -- Ueno, N -- Irie, K -- Nishida, E -- Matsumoto, K -- New York, N.Y. -- Science. 1996 May 24;272(5265):1179-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638164" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/chemistry/*metabolism ; Cell Line ; Cloning, Molecular ; Enzyme Activation ; Genes, Reporter ; Humans ; *Intracellular Signaling Peptides and Proteins ; *MAP Kinase Kinase Kinases ; Mice ; Molecular Sequence Data ; Plasminogen Activator Inhibitor 1/genetics ; Promoter Regions, Genetic ; Protein-Serine-Threonine Kinases/*metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics/metabolism ; *Signal Transduction ; Transfection ; Transformation, Genetic ; Transforming Growth Factor beta/*metabolism
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  • 104
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-01-26
    Description: The CD44 family of surface receptors regulates adhesion, movement, and activation of normal and neoplastic cells. The cytokine osteopontin (Eta-1), which regulates similar cellular functions, was found to be a protein ligand of CD44. Osteopontin induces cellular chemotaxis but not homotypic aggregation, whereas the inverse is true for the interaction between CD44 and a carbohydrate ligand, hyaluronate. The different responses of cells after CD44 ligation by either osteopontin or hyaluronate may account for the independent effects of CD44 on cell migration and growth. This mechanism may also be exploited by tumor cells to promote metastasis formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weber, G F -- Ashkar, S -- Glimcher, M J -- Cantor, H -- AI12184/AI/NIAID NIH HHS/ -- AI13600/AI/NIAID NIH HHS/ -- P01 AR34078/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):509-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560266" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD44/*metabolism ; Base Sequence ; *Cell Adhesion ; Cell Aggregation ; Cell Line ; *Chemotaxis ; Cytokines/*metabolism/pharmacology ; Hyaluronic Acid/metabolism/pharmacology ; Ligands ; Mice ; Molecular Sequence Data ; Monocytes/metabolism ; Oligopeptides/pharmacology ; Osteopontin ; Sialoglycoproteins/*metabolism/pharmacology ; Transfection ; Tumor Cells, Cultured
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  • 105
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-08-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1162-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8787118" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Biomedical Research ; Confidentiality ; *Disclosure ; Editorial Policies ; Ethics ; Humans ; Interleukin-1/*genetics ; *Patents as Topic ; Peer Review, Research/*legislation & jurisprudence ; Periodicals as Topic ; Publishing ; Washington
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  • 106
    Publication Date: 1996-01-26
    Description: An RNA virus, designated hepatitis G virus (HGV), was identified from the plasma of a patient with chronic hepatitis. Extension from an immunoreactive complementary DNA clone yielded the entire genome (9392 nucleotides) encoding a polyprotein of 2873 amino acids. The virus is closely related to GB virus C (GBV-C) and distantly related to hepatitis C virus, GBV-A, and GBV-B. HGV was associated with acute and chronic hepatitis. Persistent viremia was detected for up to 9 years in patients with hepatitis. The virus is transfusion-transmissible. It has a global distribution and is present within the volunteer blood donor population in the United States.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Linnen, J -- Wages, J Jr -- Zhang-Keck, Z Y -- Fry, K E -- Krawczynski, K Z -- Alter, H -- Koonin, E -- Gallagher, M -- Alter, M -- Hadziyannis, S -- Karayiannis, P -- Fung, K -- Nakatsuji, Y -- Shih, J W -- Young, L -- Piatak, M Jr -- Hoover, C -- Fernandez, J -- Chen, S -- Zou, J C -- Morris, T -- Hyams, K C -- Ismay, S -- Lifson, J D -- Hess, G -- Foung, S K -- Thomas, H -- Bradley, D -- Margolis, H -- Kim, J P -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):505-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genelabs Technologies, Redwood City, CA 94063, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560265" target="_blank"〉PubMed〈/a〉
    Keywords: Acute Disease ; Amino Acid Sequence ; Base Sequence ; Blood Donors ; Blood Transfusion/*adverse effects ; Blood-Borne Pathogens ; Chronic Disease ; Cloning, Molecular ; Consensus Sequence ; Disease Transmission, Infectious ; Flaviviridae/genetics ; Genome, Viral ; Hepatitis Viruses/chemistry/*genetics/isolation & purification ; Hepatitis, Viral, Human/epidemiology/transmission/*virology ; Humans ; Molecular Sequence Data ; Polymerase Chain Reaction ; RNA Viruses/chemistry/*genetics/isolation & purification ; RNA, Viral/blood/genetics ; Sequence Alignment ; United States/epidemiology ; Viral Proteins/chemistry/genetics ; Viremia/epidemiology/virology
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  • 107
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-07-19
    Description: The degenerin family of proteins in Caenorhabditis elegans is homologous to subunits of the mammalian amiloride-sensitive epithelial sodium channels. Mutations in nematode degenerins cause cell death, probably because of defects in channel function. Genetic evidence was obtained that the unc-105 gene product represents a degenerin homolog affecting C. elegans muscles and that this putative channel interacts with type IV collagen in the extracellular matrix underlying the muscle cell. This interaction may serve as a mechanism of stretch-activated muscle contraction, and this system could provide a molecular model for the activation of mechanosensitive ion channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, J -- Schrank, B -- Waterston, R H -- GM23883/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 19;273(5273):361-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Washington University School of Medicine, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662524" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; Caenorhabditis elegans/chemistry/genetics/*metabolism ; *Caenorhabditis elegans Proteins ; Cloning, Molecular ; Collagen/*metabolism ; Extracellular Matrix/metabolism ; Genes, Helminth ; Genetic Complementation Test ; Helminth Proteins/chemistry/genetics/*metabolism/*physiology ; Ion Channel Gating ; Models, Biological ; Molecular Sequence Data ; Muscle Contraction ; Muscles/physiology ; Mutation ; Sensation ; Signal Transduction ; Sodium Channels/chemistry/genetics/*metabolism/*physiology ; Suppression, Genetic
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  • 108
    Publication Date: 1996-07-12
    Description: Hematopoietic stem cells (HSCs) supply all blood cells throughout life by making use of their self-renewal and multilineage differentiation capabilities. A monoclonal antibody raised to the mouse homolog of CD34 (mCD34) was used to purify mouse HSCs to near homogeneity. Unlike in humans, primitive adult mouse bone marrow HSCs were detected in the mCD34 low to negative fraction. Injection of a single mCD34(lo/-), c-Kit+, Sca-1(+), lineage markers negative (Lin-) cell resulted in long-term reconstitution of the lymphohematopoietic system in 21 percent of recipients. Thus, the purified HSC population should enable analysis of the self-renewal and multilineage differentiation of individual HSCs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Osawa, M -- Hanada, K -- Hamada, H -- Nakauchi, H -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):242-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Institute of Basic Medical Sciences and Center for Tsukuba Advanced Research Alliance, University of Tsukuba, Tsukuba Science-City, Ibaraki 305, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662508" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD34/*analysis ; Base Sequence ; *Bone Marrow Cells ; Cell Differentiation ; Cell Lineage ; Cell Separation ; DNA Primers ; *Hematopoiesis ; Hematopoietic Stem Cell Transplantation ; Hematopoietic Stem Cells/*cytology/immunology ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Time Factors
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  • 109
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-02-09
    Description: Biological processes involved in the control and regulation of transcription are dependent on protein-induced distortions in DNA structure that enhance the recruitment of proteins to their specific DNA targets. This function is often accomplished by accessory factors that bind sequence specifically and locally bend or kink the DNA. The recent determination of the three-dimensional structures of several protein-DNA complexes, involving proteins that perform such architectural tasks, brings to light a common theme of side chain intercalation as a mechanism capable of driving the deformation of the DNA helix. The protein scaffolds orienting the intercalating side chain (or side chains) are structurally diverse, presently comprising four distinct topologies that can accomplish the same task. The intercalating side chain (or side chains), however, is exclusively hydrophobic. Intercalation can either kink or bend the DNA, unstacking one or more adjacent base pairs and locally unwinding the DNA over as much as a full turn of helix. Despite these distortions, the return to B-DNA helical parameters generally occurs within the adjacent half-turns of DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Werner, M H -- Gronenborn, A M -- Clore, G M -- New York, N.Y. -- Science. 1996 Feb 9;271(5250):778-84.〈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 20892-0520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8628992" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; DNA/*chemistry/metabolism ; DNA Helicases/chemistry/metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Hydrogen Bonding ; Intercalating Agents/chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Transcription Factors/chemistry/*metabolism ; *Transcription, Genetic
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  • 110
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-01-12
    Description: Early stages of T cell development are thought to include a series of coordinated interactions between thymocytes and other cells of the thymus. A monoclonal antibody specific for mouse CD81 was identified that blocked the appearance of alpha beta but not gamma delta T cells in fetal organ cultures initiated with day 14.5 thymus lobes. In reaggregation cultures with CD81-transfected fibroblasts, CD4-CD8- thymocytes differentiated into CD4+CD8+ T cells. Thus, interactions between immature thymocytes and stromal cells expressing CD81 are required and may be sufficient to induce early events associated with T cell development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boismenu, R -- Rhein, M -- Fischer, W H -- Havran, W L -- AI32751/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):198-200.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539618" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Antigens, CD/genetics/immunology/*physiology ; Antigens, CD4/analysis ; Antigens, CD8/analysis ; Antigens, CD81 ; Base Sequence ; CHO Cells ; Cell Differentiation ; Cricetinae ; Membrane Proteins/immunology/*physiology ; Mice ; Molecular Sequence Data ; Organ Culture Techniques ; Receptors, Antigen, T-Cell, alpha-beta/*analysis ; Receptors, Antigen, T-Cell, gamma-delta/analysis ; Stromal Cells/immunology ; T-Lymphocyte Subsets/cytology/*immunology ; Thymus Gland/cytology/*immunology ; Transfection
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  • 111
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-03-15
    Description: DNA-binding E2F complexes have been identified throughout the mammalian cell cycle, including the transcriptionally inactive complexes with pocket proteins, which occur early in the prereplicative G1 phase of the cycle, and the transactivating free E2F, which increases in late G1. Here, a regulatory B-myb promoter site was shown to bind with high affinity to free E2F and to E2F-pocket protein complexes in an indistinguishable way in vitro. In contrast, in vivo footprinting with NIH 3T3 cells demonstrated E2F site occupation specifically in early G1, when the B-myb promoter is inactive. These observations indicate that a novel mechanism governs E2F-DNA interactions during the cell cycle and emphasize the relevance of E2F site-directed transcriptional repression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zwicker, J -- Liu, N -- Engeland, K -- Lucibello, F C -- Muller, R -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1595-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Molekularbiologie und Tumorforschung, Philipps-Universitat Marburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599118" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Base Sequence ; *Carrier Proteins ; *Cell Cycle Proteins ; DNA/*metabolism ; DNA-Binding Proteins/*genetics/metabolism ; E2F Transcription Factors ; *G1 Phase ; Mice ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; *Promoter Regions, Genetic ; Retinoblastoma-Binding Protein 1 ; Retinoblastoma-Like Protein p107 ; *S Phase ; *Trans-Activators ; Transcription Factor DP1 ; Transcription Factors/*genetics/*metabolism ; Transcription, Genetic
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  • 112
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-08-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taubes, G -- New York, N.Y. -- Science. 1996 Aug 2;273(5275):588-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8701312" target="_blank"〉PubMed〈/a〉
    Keywords: *Algorithms ; *Amino Acid Sequence ; Base Sequence ; Computer Communication Networks ; *Databases, Factual ; Evolution, Molecular ; Markov Chains ; Models, Molecular ; Molecular Sequence Data ; Neural Networks (Computer) ; *Protein Conformation ; Sequence Alignment
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  • 113
    Publication Date: 1996-11-29
    Description: The 3' ends of most eukaryotic messenger RNAs are generated by internal cleavage and polyadenylation. In mammals, there is a strict dependence of both reactions on the sequence AAUAAA, which occurs upstream of polyadenylation [poly(A)] sites and which is recognized by CPSF. In contrast, cis-acting signals for yeast 3'-end generation are highly divergent from those of mammals, suggesting that trans-acting factors other than poly(A) polymerase would not be conserved. The essential yeast protein Brr5/Ysh1 shows sequence similarity to subunits of mammalian CPSF and is required for 3'-end processing in vivo and in vitro. These results demonstrate a structural and functional conservation of the yeast and mammalian 3'-end processing machineries despite a lack of conservation of the cis sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chanfreau, G -- Noble, S M -- Guthrie, C -- GM21119/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 29;274(5292):1511-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, UCSF School of Medicine, San Francisco, CA 94143-0448. guthrie@cgl.ucsf.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8929408" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cattle ; *Conserved Sequence ; Crystallography, X-Ray ; Fungal Proteins/*chemistry/genetics/metabolism ; Molecular Sequence Data ; Mutation ; Poly A/metabolism ; RNA Precursors/metabolism ; *RNA Processing, Post-Transcriptional ; RNA, Fungal/metabolism ; RNA, Messenger/metabolism ; RNA-Binding Proteins/*chemistry/genetics/metabolism ; Saccharomyces cerevisiae/*chemistry/genetics ; mRNA Cleavage and Polyadenylation Factors
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  • 114
    Publication Date: 1996-03-15
    Description: Human foamy virus (HFV) is the prototype of the Spumavirus genus of Retroviridae. In all other retroviruses, the pol gene products, including reverse transcriptase, are synthesized as Gag-Pol fusion proteins and are cleaved to functional enzymes during viral budding or release. In contrast, the Pol protein of HFV is translated from a spliced messenger RNA and lacks Gag domains. Infectious HFV particles contain double-stranded DNA similar in size to full-length provirus, suggesting that reverse transcription has taken place in viral particles before new rounds of infection, reminiscent of hepadnaviruses. These data suggest that foamy viruses possess a replication pathway containing features of both retroviruses and hepadnaviruses but distinct from both.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, S F -- Baldwin, D N -- Gwynn, S R -- Yendapalli, S -- Linial, M L -- CA18282/CA/NCI NIH HHS/ -- F32 CA60357/CA/NCI NIH HHS/ -- HL53762/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1579-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599113" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cells, Cultured ; Cricetinae ; Fusion Proteins, gag-pol/biosynthesis/genetics/metabolism ; Gene Products, gag/biosynthesis/genetics ; Gene Products, pol/*biosynthesis/genetics/metabolism ; Genes, gag ; Genes, pol ; Genome, Viral ; Hepatitis B virus/genetics/metabolism/physiology ; Humans ; Molecular Sequence Data ; RNA Splicing ; RNA, Viral/genetics ; RNA-Directed DNA Polymerase/metabolism ; Retroviridae/genetics/metabolism/physiology ; Spumavirus/genetics/metabolism/*physiology ; *Virus Replication
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  • 115
    Publication Date: 1996-10-25
    Description: Rapid access to genetic information is central to the revolution taking place in molecular genetics. The simultaneous analysis of the entire human mitochondrial genome is described here. DNA arrays containing up to 135,000 probes complementary to the 16.6-kilobase human mitochondrial genome were generated by light-directed chemical synthesis. A two-color labeling scheme was developed that allows simultaneous comparison of a polymorphic target to a reference DNA or RNA. Complete hybridization patterns were revealed in a matter of minutes. Sequence polymorphisms were detected with single-base resolution and unprecedented efficiency. The methods described are generic and can be used to address a variety of questions in molecular genetics including gene expression, genetic linkage, and genetic variability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chee, M -- Yang, R -- Hubbell, E -- Berno, A -- Huang, X C -- Stern, D -- Winkler, J -- Lockhart, D J -- Morris, M S -- Fodor, S P -- 5RO1HG00813/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):610-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Affymetrix, 3380 Central Expressway, Santa Clara, CA 95051, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849452" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Base Composition ; Base Sequence ; Cloning, Molecular ; DNA, Mitochondrial/*genetics ; Fluorescein ; Fluoresceins ; Gene Expression ; Genetic Variation ; *Genome ; Humans ; Mitochondria/*genetics ; *Nucleic Acid Hybridization ; *Oligonucleotide Probes ; Phycoerythrin ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Sequence Analysis, DNA
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  • 116
    Publication Date: 1996-03-08
    Description: A number of pathophysiologically relevant genes, including platelet-derived growth factor B-chain (PDGF-B), are induced in the vasculature after acute mechanical injury. In rat aorta, the activated expression of these genes was preceded by a marked increase in the amount of the early-growth-response gene product Egr-1 at the endothelial wound edge. Egr-1 interacts with a novel element in the proximal PDGF-B promoter, as well as with consensus elements in the promoters of other genes induced by endothelial injury. This interaction is crucial for injury-induced PDGF-B promoter-dependent expression. Sp1, whose binding site in the PDGF-B promoter overlaps that of Egr-1, occupies this element in unstimulated cells and is displaced by increasing amounts of Egr-1. These findings implicate Egr-1 in the up-regulated expression of PDGF-B and other potent mediators in mechanically injured arterial endothelial cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khachigian, L M -- Lindner, V -- Williams, A J -- Collins, T -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1427-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vascular Research Division, Department of Pathology, Brigham and Women's Hospital, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596917" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta/injuries/metabolism ; Base Sequence ; Binding Sites ; DNA-Binding Proteins/genetics/*metabolism ; Early Growth Response Protein 1 ; Endothelium, Vascular/injuries/*metabolism ; *Gene Expression Regulation ; Genes, Reporter ; Humans ; *Immediate-Early Proteins ; Male ; Molecular Sequence Data ; Platelet-Derived Growth Factor/biosynthesis/*genetics ; *Promoter Regions, Genetic ; Rats ; Rats, Sprague-Dawley ; Recombinant Proteins/metabolism ; Sp1 Transcription Factor/metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; Transcription Factors/genetics/*metabolism ; *Zinc Fingers
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  • 117
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-05-10
    Description: The crystal structure of the yeast TFIIA/TBP/TATA promoter complex was solved to 3 angstrom resolution by double-edge multiple wavelength anomalous diffraction from two different species of anomalous scattering elements in the same crystal. The large and small subunits of TFIIA associate intimately to form both domains of a two-domain folding pattern. TFIIA binds as a heterodimer to the side of the TBP/TATA complex opposite to the side that binds TFIIB and does not alter the TBP/DNA interaction. The six-stranded beta-sandwich domain interacts with the amino-terminal end of TBP through a stereospecific parallel beta-strand interface and with the backbone of the TATA box and the 5'-flanking B-DNA segment. The four-helix-bundle domain projects away from the TBP/TATA complex, thereby presenting a substantial surface for further protein-protein interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geiger, J H -- Hahn, S -- Lee, S -- Sigler, P B -- New York, N.Y. -- Science. 1996 May 10;272(5263):830-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8629014" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Crystallography, X-Ray ; DNA, Fungal/*chemistry/metabolism ; DNA-Binding Proteins/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis ; Nucleic Acid Conformation ; Promoter Regions, Genetic ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Saccharomyces cerevisiae/chemistry/genetics/metabolism ; TATA Box ; TATA-Box Binding Protein ; Transcription Factor TFIIA ; Transcription Factor TFIIB ; Transcription Factors/*chemistry/metabolism ; Transcription, Genetic
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  • 118
    Publication Date: 1996-05-24
    Description: Little is known about the integral membrane proteins that participate in the early secretory pathway of mammalian cells. The complementary DNA encoding a 28-kilodalton protein (p28) of the cis-Golgi was cloned and sequenced. The protein was predicted to contain a central coiled-coil domain with a carboxyl-terminal membrane anchor. An in vitro assay for endoplasmic reticulum-Golgi transport was used to show that p28 participates in the docking and fusion stage of this transport event. Biochemical studies established that p28 is a core component of the Golgi SNAP receptor (SNARE) complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Subramaniam, V N -- Peter, F -- Philp, R -- Wong, S H -- Hong, W -- New York, N.Y. -- Science. 1996 May 24;272(5265):1161-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Membrane Biology Laboratory, Institute of Molecular and Cell Biology, National University of Singapore.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638159" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biological Transport ; Carrier Proteins/analysis ; Cell Line ; Cloning, Molecular ; DNA, Complementary/genetics ; Egtazic Acid/pharmacology ; Endoplasmic Reticulum/*metabolism ; Golgi Apparatus/*chemistry/metabolism ; *Membrane Glycoproteins ; Membrane Proteins/analysis/*chemistry/genetics/isolation & ; purification/*metabolism ; Molecular Sequence Data ; N-Ethylmaleimide-Sensitive Proteins ; SNARE Proteins ; Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins ; *Vesicular Transport Proteins ; Vesicular stomatitis Indiana virus ; Viral Envelope Proteins/metabolism
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  • 119
    Publication Date: 1996-09-06
    Description: Cdc2, the cyclin-dependent kinase that controls mitosis, is negatively regulated by phosphorylation on its threonine-14 and tyrosine-15 residues. Cdc25, the phosphatase that dephosphorylates both of these residues, undergoes activation and phosphorylation by multiple kinases at mitosis. Plx1, a kinase that associates with and phosphorylates the amino-terminal domain of Cdc25, was purified extensively from Xenopus egg extracts. Cloning of its complementary DNA revealed that Plx1 is related to the Polo family of protein kinases. Recombinant Plx1 phosphorylated Cdc25 and stimulated its activity in a purified system. Cdc25 phosphorylated by Plx1 reacted strongly with MPM-2, a monoclonal antibody to mitotic phosphoproteins. These studies indicate that Plx1 may participate in control of mitotic progression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kumagai, A -- Dunphy, W G -- New York, N.Y. -- Science. 1996 Sep 6;273(5280):1377-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, 216-76, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703070" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; CDC2 Protein Kinase/metabolism ; Cell Cycle Proteins/chemistry/*metabolism ; Cloning, Molecular ; Cyclins/metabolism ; Enzyme Activation ; Molecular Sequence Data ; Mutation ; Oocytes/enzymology ; Peptide Mapping ; Phosphoprotein Phosphatases/chemistry/*metabolism ; Phosphorylation ; Phosphoserine/analysis ; Phosphothreonine/analysis ; Protein-Serine-Threonine Kinases/chemistry/genetics/*isolation & ; purification/metabolism ; Recombinant Proteins/metabolism ; Xenopus ; *Xenopus Proteins ; cdc25 Phosphatases
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  • 120
    Publication Date: 1996-06-14
    Description: Many bacteria, including several pathogens of plants and humans, use a pheromone called an autoinducer to regulate gene expression in a cell density-dependent manner. Agrobacterium autoinducer [AAI, N-(3-oxo-octanoyl)-L-homoserine lactone] of A. tumefaciens is synthesized by the Tral protein, which is encoded by the tumor-inducing plasmid. Purified hexahistidinyl-Tral (H6-Tral) used S-adenosylmethionine to make the homoserine lactone moiety of AAI, but did not use related compounds. H6-Tral used 3-oxo-octanoyl-acyl carrier protein to make the 3-oxo-octanoyl moiety of AAI, but did not use 3-oxo-octanoyl-coenzyme A. These results demonstrate the enzymatic synthesis of an autoinducer through the use of purified substrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉More, M I -- Finger, L D -- Stryker, J L -- Fuqua, C -- Eberhard, A -- Winans, S C -- GM42893/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1655-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Microbiology, Cornell University, Ithaca, New York 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658141" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/antagonists & inhibitors/metabolism ; Acyl Carrier Protein/metabolism ; Agrobacterium tumefaciens/*genetics/metabolism ; Base Sequence ; Cerulenin/pharmacology ; Chromatography, Gel ; Chromatography, High Pressure Liquid ; Cloning, Molecular ; DNA Helicases/*metabolism ; DNA Primers ; Escherichia coli ; Escherichia coli Proteins ; Fatty Acids/metabolism ; *Gene Expression Regulation, Bacterial/drug effects ; Homoserine/*analogs & derivatives/biosynthesis ; Malonyl Coenzyme A/metabolism ; Molecular Sequence Data ; NADP/metabolism ; Plasmids ; S-Adenosylmethionine/metabolism
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  • 121
    Publication Date: 1996-02-16
    Description: Mice harboring mutations in the obese (ob) and diabetes (db) genes display similar phenotypes, and it has been proposed that these genes encode the ligand and receptor, respectively, for a physiologic pathway that regulates body weight. The cloning of ob, and the demonstration that it encodes a secreted protein (leptin) that binds specifically to a receptor (OB-R) in the brain, have validated critical aspects of this hypothesis. Here it is shown by genetic mapping and genomic analysis that mouse db, rat fatty (a homolog of db), and the gene encoding the OB-R are the same gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chua, S C Jr -- Chung, W K -- Wu-Peng, X S -- Zhang, Y -- Liu, S M -- Tartaglia, L -- Leibel, R L -- DK26687/DK/NIDDK NIH HHS/ -- DK47473/DK/NIDDK NIH HHS/ -- HD28047/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 16;271(5251):994-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Human Behavior and Metabolism, Rockefeller University, New York 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8584938" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blotting, Southern ; Carrier Proteins/*genetics ; Chromosome Mapping ; Cloning, Molecular ; DNA Mutational Analysis ; Diabetes Mellitus/*genetics ; Genetic Markers ; Leptin ; Mice ; Mice, Inbred C57BL ; Mice, Inbred Strains ; Molecular Sequence Data ; Obesity/*genetics ; Phenotype ; Polymerase Chain Reaction ; Proteins/genetics ; Rats ; Rats, Inbred Strains ; *Receptors, Cell Surface ; Receptors, Cytokine/*genetics ; Receptors, Leptin
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  • 122
    Publication Date: 1996-05-17
    Description: The retinal cyclic guanosine 3',5'-monophosphate (cGMP) phosphodiesterase (PDE) is a key regulator of phototransduction in the vertebrate visual system. PDE consists of a catalytic core of alpha and beta subunits associated with two inhibitory gamma subunits. A gene-targeting approach was used to disrupt the mouse PDEgamma gene. This mutation resulted in a rapid retinal degeneration resembling human retinitis pigmentosa. In homozygous mutant mice, reduced rather than increased PDE activity was apparent; the PDEalphabeta dimer was formed but lacked hydrolytic activity. Thus, the inhibitory gamma subunit appears to be necessary for integrity of the photoreceptors and expression of PDE activity in vivo.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2757426/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2757426/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsang, S H -- Gouras, P -- Yamashita, C K -- Kjeldbye, H -- Fisher, J -- Farber, D B -- Goff, S P -- EY08285/EY/NEI NIH HHS/ -- K08 EY000408/EY/NEI NIH HHS/ -- K08 EY000408-01/EY/NEI NIH HHS/ -- T32 GM 073667-14/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 May 17;272(5264):1026-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, College of Physicians and Surgeons, New York 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638127" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-GMP Phosphodiesterases/deficiency/genetics/*metabolism ; Animals ; Base Sequence ; Chimera ; Crosses, Genetic ; Cyclic GMP/*metabolism ; Electroretinography ; Enzyme Activation ; Female ; Gene Targeting ; Humans ; Light ; Male ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; Phenotype ; Retina/metabolism/*pathology/physiopathology ; Retinal Degeneration/*enzymology/pathology/physiopathology ; Retinal Rod Photoreceptor Cells/*enzymology/metabolism/pathology ; Retinitis Pigmentosa/pathology
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  • 123
    Publication Date: 1996-07-19
    Description: The gene ENOD40 is expressed during early stages of legume nodule development. A homolog was isolated from tobacco, which, as does ENOD40 from legumes, encodes an oligopeptide of about 10 amino acids. In tobacco protoplasts, these peptides change the response to auxin at concentrations as low as 10(-12) to 10(-16)M. The peptides encoded by ENOD40 appear to act as plant growth regulators.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van de Sande, K -- Pawlowski, K -- Czaja, I -- Wieneke, U -- Schell, J -- Schmidt, J -- Walden, R -- Matvienko, M -- Wellink, J -- van Kammen, A -- Franssen, H -- Bisseling, T -- New York, N.Y. -- Science. 1996 Jul 19;273(5273):370-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Zuchtungsforschung, Koln, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662527" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Division ; Fabaceae/chemistry/*genetics/growth & development ; *Genes, Plant ; Green Fluorescent Proteins ; Indoleacetic Acids/*pharmacology ; Luminescent Proteins/biosynthesis ; Molecular Sequence Data ; Naphthaleneacetic Acids/pharmacology ; Open Reading Frames ; Plant Growth Regulators ; Plant Proteins/biosynthesis/*genetics/*physiology ; Plant Roots/growth & development/metabolism ; *Plants, Medicinal ; *Plants, Toxic ; Protoplasts/cytology ; RNA, Long Noncoding ; RNA, Untranslated/*physiology ; Recombinant Fusion Proteins ; Tobacco/chemistry/*genetics/growth & development ; Transfection
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  • 124
    Publication Date: 1996-03-08
    Description: Transcriptional regulatory elements have been shown to be necessary but not sufficient for the developmental regulation of immunoglobulin gene rearrangement in mouse precursor B cells. In the chicken lambda light chain locus, additional elements in the V-J intervening sequence are involved in negative and positive regulation of rearrangement. Here, mutation of the mouse homolog of a chicken element, located in the V(K)-J(K) intervening sequence upstream of the J(K) cluster, was shown to significantly decrease rearrangement. This cis-acting recombination-enhancing element affects the rearrangement process without being involved in regulating transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferradini, L -- Gu, H -- De Smet, A -- Rajewsky, K -- Reynaud, C A -- Weill, J C -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1416-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INSERM U373, Institut Necker, Faculte de Medecine, Universite Paris V, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596914" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; B-Lymphocytes/cytology/immunology ; Base Sequence ; Chimera ; Enhancer Elements, Genetic ; *Gene Rearrangement, B-Lymphocyte ; Gene Rearrangement, T-Lymphocyte ; Gene Targeting ; *Genes, Immunoglobulin ; Immunoglobulin J-Chains/*genetics ; Immunoglobulin Variable Region/genetics ; Immunoglobulin kappa-Chains/*genetics ; Introns ; Mice ; Mice, Inbred C57BL ; Mice, SCID ; Molecular Sequence Data ; Mutation ; Recombination, Genetic ; *Regulatory Sequences, Nucleic Acid ; Stem Cells
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  • 125
    Publication Date: 1996-02-23
    Description: The germline genes used by the mouse to generate the esterolytic antibody 48G7 were cloned and expressed in an effort to increase our understanding of the detailed molecular mechanisms by which the immune system evolves catalytic function. The nine replacement mutations that were fixed during affinity maturation increased affinity for the transition state analogue by a factor of 10(4), primarily the result of a decrease in the dissociation rate of the hapten-antibody complex. There was a corresponding increase in the rate of reaction of antibody with substrate, k(cat)/k(m), from 1.7 x 10(2)M(-1) min(-1) to 1.4 x 10(4)M(-1) min(-1). The three-dimensional crystal structure of the 48G7-transition state analogue complex at 2.0 angstroms resolution indicates that one of the nine residues in which somatic mutations have been fixed directly contact the hapten. Thus, in the case of 48G7, affinity maturation appears to play a conformational role, either in reorganizing the active site geometry of limiting side-chain and backbone flexibility of the germline antibody. The crystal structure and analysis of somatic and directed active site mutants underscore the role of transition state stabilization in the evolution of this catalytic antibody.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Patten, P A -- Gray, N S -- Yang, P L -- Marks, C B -- Wedemayer, G J -- Boniface, J J -- Stevens, R C -- Schultz, P G -- R01 AL24695/PHS HHS/ -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1086-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599084" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Catalytic/chemistry/genetics/*immunology/metabolism ; Antibody Affinity ; Antigen-Antibody Complex ; Antigen-Antibody Reactions ; Base Sequence ; Binding Sites ; Catalysis ; Cloning, Molecular ; Crystallization ; Crystallography, X-Ray ; *Evolution, Molecular ; Genes, Immunoglobulin ; Haptens/immunology ; Immunoglobulin Fab Fragments/genetics/immunology ; Immunoglobulin Heavy Chains/genetics/immunology ; Immunoglobulin Light Chains/genetics/immunology ; Mice ; Molecular Sequence Data ; Mutation ; Protein Conformation
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  • 126
    Publication Date: 1996-02-23
    Description: The human Dubin-Johnson syndrome and its animal model, the TR(-) rat, are characterized by a chronic conjugated hyperbilirubinemia. TR(-) rats are defective in the canalicular multispecific organic anion transporter (cMOAT), which mediates hepatobiliary excretion of numerous organic anions. The complementary DNA for rat cmoat, a homolog of the human multidrug resistance gene (hMRP1), was isolated and shown to be expressed in the canalicular membrane of hepatocytes. In the TR(-) rat, a single-nucleotide deletion in this gene resulted in a reduced messenger RNA level and absence of the protein. It is likely that this mutation accounts for the TR(-) phenotype.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paulusma, C C -- Bosma, P J -- Zaman, G J -- Bakker, C T -- Otter, M -- Scheffer, G L -- Scheper, R J -- Borst, P -- Oude Elferink, R P -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1126-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Gastrointestinal and Liver Diseases, Center for Liver and Intestinal Research, Academic Medical Center, Amsterdam, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599091" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/analysis/chemistry/*genetics ; Amino Acid Sequence ; Animals ; Anion Transport Proteins ; Base Sequence ; Carrier Proteins/analysis/chemistry/*genetics ; Cell Membrane/chemistry ; DNA, Complementary/genetics ; Frameshift Mutation ; Humans ; Hyperbilirubinemia, Hereditary/*genetics ; Liver/*chemistry/cytology ; Molecular Sequence Data ; Molecular Weight ; Multidrug Resistance-Associated Proteins ; Phenotype ; Rats ; Rats, Wistar ; Sequence Alignment ; Sequence Deletion
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  • 127
    Publication Date: 1996-07-26
    Description: The POU transcription factor Oct-6, also known as SCIP or Tst-1, has been implicated as a major transcriptional regulator in Schwann cell differentiation. Microscopic and immunochemical analysis of sciatic nerves of Oct-6(-/-) mice at different stages of postnatal development reveals a delay in Schwann cell differentiation, with a transient arrest at the promyelination stage. Thus, Oct-6 appears to be required for the transition of promyelin cells to myelinating cells. Once these cells progress past this point, Oct-6 is no longer required, and myelination occurs normally.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jaegle, M -- Mandemakers, W -- Broos, L -- Zwart, R -- Karis, A -- Visser, P -- Grosveld, F -- Meijer, D -- New York, N.Y. -- Science. 1996 Jul 26;273(5274):507-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Genetics Center, Department of Cell Biology and Genetics, Erasmus University, Post Office Box 1738, 3000 DR Rotterdam, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662541" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Axons/ultrastructure ; Base Sequence ; Cell Differentiation ; Gene Expression ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Myelin P0 Protein/genetics/metabolism ; Myelin Proteins/genetics/metabolism ; Myelin Sheath/physiology ; Octamer Transcription Factor-6 ; Recombination, Genetic ; Schwann Cells/*cytology/physiology ; Sciatic Nerve/cytology/growth & development ; Stem Cells ; Transcription Factors/*genetics/*physiology
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  • 128
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-09-06
    Description: The maintenance and significance of the complex populations of microbes present in the mammalian intestine are poorly understood. Comparison of conventionally housed and germ-free NMRI mice revealed that production of fucosylated glycoconjugates and an alpha1, 2-fucosyltransferase messenger RNA in the small-intestinal epithelium requires the normal microflora. Colonization of germ-free mice with Bacteroides thetaiotaomicron, a component of this flora, restored the fucosylation program, whereas an isogenic strain carrying a transposon insertion that disrupts its ability to use L-fucose as a carbon source did not. Simplified models such as this should aid the study of open microbial ecosystems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bry, L -- Falk, P G -- Midtvedt, T -- Gordon, J I -- DK30292/DK/NIDDK NIH HHS/ -- DK37960/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 Sep 6;273(5280):1380-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Pharmacology, Washington University School of Medicine, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703071" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacteroides/growth & development/metabolism/*physiology ; Base Sequence ; Cell Differentiation ; Cell Lineage ; Colony Count, Microbial ; Ecosystem ; Fucose/*metabolism ; Fucosyltransferases/genetics/metabolism ; Germ-Free Life ; Glycoconjugates/*metabolism ; Intestinal Mucosa/cytology/*microbiology ; Intestine, Small/cytology/metabolism/*microbiology ; Male ; Mice ; Mice, Inbred Strains ; Molecular Sequence Data ; Polymerase Chain Reaction ; RNA, Messenger/metabolism
    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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  • 129
    Publication Date: 1996-04-26
    Description: The rate of progression to disease varies considerably among individuals infected with human immunodeficiency virus-type 1 (HIV-1). Analyses of semiannual blood samples obtained from six infected men showed that a rapid rate of CD4 T cell loss was associated with relative evolutionary stasis of the HIV-1 quasispecies virus population. More moderate rates of CD4 T cell loss correlated with genetic evolution within three of four subjects. Consistent with selection by the immune constraints of these subjects, amino acid changes were apparent within the appropriate epitopes of human leukocyte antigen class I-restricted cytotoxic T lymphocytes. Thus, the evolutionary dynamics exhibited by the HIV-1 quasispecies virus populations under natural selection are compatible with adaptive evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolinsky, S M -- Korber, B T -- Neumann, A U -- Daniels, M -- Kunstman, K J -- Whetsell, A J -- Furtado, M R -- Cao, Y -- Ho, D D -- Safrit, J T -- AI32535/AI/NIAID NIH HHS/ -- AI35522/AI/NIAID NIH HHS/ -- AI45218/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Apr 26;272(5261):537-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Northwestern University Medical School, Chicago, IL 60611, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614801" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/immunology/virology ; Amino Acid Sequence ; Animals ; *Antigenic Variation ; Base Sequence ; Biological Evolution ; CD4 Lymphocyte Count ; Cohort Studies ; Disease Progression ; HIV Antibodies/immunology ; HIV Antigens/immunology ; HIV Infections/*immunology/*virology ; HIV-1/*genetics/immunology/pathogenicity/physiology ; Histocompatibility Antigens Class I/immunology ; Humans ; Male ; Mice ; Mice, SCID ; Molecular Sequence Data ; Mutation ; Phenotype ; RNA, Viral/blood ; T-Lymphocytes, Cytotoxic/*immunology ; Virulence ; Virus Replication
    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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  • 130
    Publication Date: 1996-06-14
    Description: The basal cell nevus syndrome (BCNS) is characterized by developmental abnormalities and by the postnatal occurrence of cancers, especially basal cell carcinomas (BCCs), the most common human cancer. Heritable mutations in BCNS patients and a somatic mutation in a sporadic BCC were identified in a human homolog of the Drosophila patched (ptc) gene. The ptc gene encodes a transmembrane protein that in Drosophila acts in opposition to the Hedgehog signaling protein, controlling cell fates, patterning, and growth in numerous tissues. The human PTC gene appears to be crucial for proper embryonic development and for tumor suppression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, R L -- Rothman, A L -- Xie, J -- Goodrich, L V -- Bare, J W -- Bonifas, J M -- Quinn, A G -- Myers, R M -- Cox, D R -- Epstein, E H Jr -- Scott, M P -- AR3995/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1668-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology, Howard Hughes Medical Institute, Stanford University School of Medicine, California 94305-5427, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658145" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Amino Acid Sequence ; Animals ; Basal Cell Nevus Syndrome/*genetics ; Base Sequence ; Cloning, Molecular ; DNA, Neoplasm ; Drosophila ; *Drosophila Proteins ; Female ; Frameshift Mutation ; *Genes, Tumor Suppressor ; Humans ; Insect Hormones/genetics ; Male ; Membrane Proteins/*genetics ; Middle Aged ; Molecular Sequence Data ; Polymerase Chain Reaction ; Polymorphism, Single-Stranded Conformational ; Protein Conformation ; Receptors, Cell Surface
    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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