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  • 1
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    Inhibition of antigen-induced lymphocyte proliferation by Tat protein from HIV-1 (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-12-22
    Description: The purified human immunodeficiency virus type-l (HIV-l) Tat protein inhibited lymphocyte proliferation induced by tetanus toxoid or Candida antigens by 66 to 97% at nanomolar concentrations of Tat. In contrast, Tat did not cause a significant reduction of lymphocyte proliferation in response to mitogens such as phytohemagglutinin or pokeweed mitogen. Inhibition was blocked by oxidation of the cysteine-rich region of Tat or by incubation with an antibody to Tat before the assay. A synthetic Tat peptide (residues 1 to 58) also inhibited antigen-stimulated proliferation. Experiments with H9 and U937 cell lines showed that Tat can easily enter both lymphocytes and monocytes. The specific inhibition of antigen-induced lymphocyte proliferation by Tat mimics the effect seen with lymphocytes from HIV-infected individuals and suggests that Tat might directly contribute to the immunosuppression associated with HIV infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Viscidi, R P -- Mayur, K -- Lederman, H M -- Frankel, A D -- AI29135/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1989 Dec 22;246(4937):1606-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2556795" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/immunology ; Cells, Cultured ; Concanavalin A ; DNA Replication/drug effects ; Gene Products, tat/immunology/*pharmacology ; HIV-1/genetics/*immunology ; HeLa Cells/metabolism ; Humans ; Immunosuppression ; Lymphocyte Activation/*drug effects ; Lymphocytes/drug effects/immunology ; Pokeweed Mitogens ; Promoter Regions, Genetic ; Recombinant Proteins/immunology/pharmacology ; Staphylococcal Protein A ; Trans-Activators/*pharmacology ; Transcriptional Activation ; tat Gene Products, Human Immunodeficiency Virus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Arginine-mediated RNA recognition: the arginine fork (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-24
    Description: Short peptides that contain the basic region of the HIV-1 Tat protein bind specifically to a bulged region in TAR RNA. A peptide that contained nine arginines (R9) also bound specifically to TAR, and a mutant Tat protein that contained R9 was fully active for transactivation. In contrast, a peptide that contained nine lysines (K9) bound TAR poorly and the corresponding protein gave only marginal activity. By starting with the K9 mutant and replacing lysine residues with arginines, a single arginine was identified that is required for specific binding and transactivation. Ethylation interference experiments suggest that this arginine contacts two adjacent phosphates at the RNA bulge. Model building suggests that the arginine eta nitrogens and the epsilon nitrogen can form specific networks of hydrogen bonds with adjacent pairs of phosphates and that these arrangements are likely to occur near RNA loops and bulges and not within double-stranded A-form RNA. Thus, arginine side chains may be commonly used to recognize specific RNA structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Calnan, B J -- Tidor, B -- Biancalana, S -- Hudson, D -- Frankel, A D -- AI29135/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 May 24;252(5009):1167-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Nine Cambridge Center, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1709522" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Arginine ; Base Sequence ; Cloning, Molecular ; Gene Products, tat/genetics/*metabolism ; Genes, tat ; HIV Long Terminal Repeat/physiology ; HIV-1/genetics/*metabolism ; Hydrogen Bonding ; Membrane Proteins/genetics/metabolism ; Molecular Sequence Data ; Mutagenesis, Insertional ; Nucleic Acid Conformation ; Peptides/metabolism ; Protein Binding ; RNA/genetics/*metabolism ; Transcriptional Activation ; tat Gene Products, Human Immunodeficiency Virus
    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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  • 3
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    Conformation of the TAR RNA-arginine complex by NMR spectroscopy (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-03
    Description: The messenger RNAs of human immunodeficiency virus-1 (HIV-1) have an RNA hairpin structure, TAR, at their 5' ends that contains a six-nucleotide loop and a three-nucleotide bulge. The conformations of TAR RNA and of TAR with an arginine analog specifically bound at the binding site for the viral protein, Tat, were characterized by nuclear magnetic resonance (NMR) spectroscopy. Upon arginine binding, the bulge changes conformation, and essential nucleotides for binding, U23 and A27.U38, form a base-triple interaction that stabilizes arginine hydrogen bonding to G26 and phosphates. Specificity in the arginine-TAR interaction appears to be derived largely from the structure of the RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Puglisi, J D -- Tan, R -- Calnan, B J -- Frankel, A D -- Williamson, J R -- AI29135/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 3;257(5066):76-80.〈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/1621097" target="_blank"〉PubMed〈/a〉
    Keywords: Arginine/*metabolism ; Base Sequence ; Binding Sites ; Gene Products, tat/metabolism ; HIV-1/*genetics ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy/methods ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA, Messenger/*chemistry/metabolism ; RNA, Viral/*chemistry/metabolism ; RNA-Binding Proteins/*chemistry/metabolism ; tat Gene Products, Human Immunodeficiency Virus
    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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  • 4
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    The 2002 Denali fault earthquake, Alaska: a large magnitude, slip-partitioned event (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-17
    Description: The MW (moment magnitude) 7.9 Denali fault earthquake on 3 November 2002 was associated with 340 kilometers of surface rupture and was the largest strike-slip earthquake in North America in almost 150 years. It illuminates earthquake mechanics and hazards of large strike-slip faults. It began with thrusting on the previously unrecognized Susitna Glacier fault, continued with right-slip on the Denali fault, then took a right step and continued with right-slip on the Totschunda fault. There is good correlation between geologically observed and geophysically inferred moment release. The earthquake produced unusually strong distal effects in the rupture propagation direction, including triggered seismicity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eberhart-Phillips, Donna -- Haeussler, Peter J -- Freymueller, Jeffrey T -- Frankel, Arthur D -- Rubin, Charles M -- Craw, Patricia -- Ratchkovski, Natalia A -- Anderson, Greg -- Carver, Gary A -- Crone, Anthony J -- Dawson, Timothy E -- Fletcher, Hilary -- Hansen, Roger -- Harp, Edwin L -- Harris, Ruth A -- Hill, David P -- Hreinsdottir, Sigrun -- Jibson, Randall W -- Jones, Lucile M -- Kayen, Robert -- Keefer, David K -- Larsen, Christopher F -- Moran, Seth C -- Personius, Stephen F -- Plafker, George -- Sherrod, Brian -- Sieh, Kerry -- Sitar, Nicholas -- Wallace, Wesley K -- New York, N.Y. -- Science. 2003 May 16;300(5622):1113-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉U.S. Geological Survey, 4200 University Drive, Anchorage, AK 99508, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12750512" target="_blank"〉PubMed〈/a〉
    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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  • 5
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    Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: The Tat protein of bovine immunodeficiency virus (BIV) binds to its target RNA, TAR, and activates transcription. A 14-amino acid arginine-rich peptide corresponding to the RNA-binding domain of BIV Tat binds specifically to BIV TAR, and biochemical and in vivo experiments have identified the amino acids and nucleotides required for binding. The solution structure of the RNA-peptide complex has now been determined by nuclear magnetic resonance spectroscopy. TAR forms a virtually continuous A-form helix with two unstacked bulged nucleotides. The peptide adopts a beta-turn conformation and sits in the major groove of the RNA. Specific contacts are apparent between critical amino acids in the peptide and bases and phosphates in the RNA. The structure is consistent with all biochemical data and demonstrates ways in which proteins can recognize the major groove of RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Puglisi, J D -- Chen, L -- Blanchard, S -- Frankel, A D -- AI08591/AI/NIAID NIH HHS/ -- AI29135/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1200-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, Santa Cruz 95064, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502045" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Composition ; Base Sequence ; Gene Products, tat/*chemistry/metabolism ; Hydrogen Bonding ; Immunodeficiency Virus, Bovine/*chemistry ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Conformation ; Protein Structure, Secondary ; RNA, Viral/*chemistry/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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  • 6
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    Alpha helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-13
    Description: The solution structure of a human immunodeficiency virus type-1 (HIV-1) Rev peptide bound to stem-loop IIB of the Rev response element (RRE) RNA was solved by nuclear magnetic resonance spectroscopy. The Rev peptide has an alpha-helical conformation and binds in the major groove of the RNA near a purine-rich internal loop. Several arginine side chains make base-specific contacts, and an asparagine residue contacts a G.A base pair. The phosphate backbone adjacent to a G.G base pair adopts an unusual structure that allows the peptide to access a widened major groove. The structure formed by the two purine-purine base pairs of the RRE creates a distinctive binding pocket that the peptide can use for specific recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Battiste, J L -- Mao, H -- Rao, N S -- Tan, R -- Muhandiram, D R -- Kay, L E -- Frankel, A D -- Williamson, J R -- GM-08344/GM/NIGMS NIH HHS/ -- GM-39589/GM/NIGMS NIH HHS/ -- GM-53320/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Sep 13;273(5281):1547-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703216" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arginine/chemistry ; Asparagine/chemistry ; Base Composition ; Base Sequence ; *DNA-Binding Proteins ; Fungal Proteins/chemistry ; Gene Products, rev/*chemistry/*metabolism ; *Genes, env ; HIV-1/*chemistry ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Protein Kinases/chemistry ; *Protein Structure, Secondary ; RNA, Viral/*chemistry/genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Threonine/chemistry ; rev Gene Products, Human Immunodeficiency Virus
    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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  • 7
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    Nanosecond X-ray diffraction from biological samples with a laser-produced plasma source (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-05-11
    Description: By using 4.45-angstrom radiation generated by Cl+15 ions in a laser plasma and nanosecond exposures, low-angle x-ray diffraction patterns were obtained from dried rat spinal nerves and a powder of cholesterol. Three to four 400-picosecond, 45-joule pulses were required for the exposure. This new technique should have wide application in structural kinetic studies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frankel, R D -- Forsyth, J M -- New York, N.Y. -- Science. 1979 May 11;204(4393):622-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/432665" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cholesterol ; In Vitro Techniques ; *Lasers ; Neurons/*ultrastructure ; Rats ; Time Factors ; X-Ray Diffraction/*methods
    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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  • 8
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    Tat protein from human immunodeficiency virus forms a metal-linked dimer (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-01
    Description: Tat, the transactivating protein from HIV, forms a metal-linked dimer with metal ions bridging cysteine-rich regions from each monomer. This novel arrangement is distinct from the "zinc finger" domain observed in other eukaryotic regulatory proteins. Ultraviolet absorption spectra show that Tat binds two Zn2+ or two Cd2+ ions per monomer, and electrophoresis of the Tat-metal complexes demonstrates that the protein forms metal-linked dimers. Partial proteolysis and circular dichroism spectra suggest that metal binding has its primary effects in the cysteine-rich region and relatively little effect on the folding of other regions. These results suggest new directions for biological studies and new approaches to drug design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frankel, A D -- Bredt, D S -- Pabo, C O -- GM31471/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 1;240(4848):70-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2832944" target="_blank"〉PubMed〈/a〉
    Keywords: Cadmium/*metabolism ; Circular Dichroism ; Cobalt/metabolism ; Cysteine ; Electrophoresis, Polyacrylamide Gel ; Gene Products, tat ; HIV/*analysis ; Macromolecular Substances ; Metals/metabolism ; Oncogene Proteins, Viral ; Oxidation-Reduction ; Peptide Fragments/metabolism ; Peptide Hydrolases/metabolism ; Protein Conformation ; Spectrophotometry ; Sulfhydryl Compounds/metabolism ; Transcription Factors/*metabolism ; Zinc/*metabolism ; tat Gene Products, Human Immunodeficiency Virus
    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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