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  • STRUCTURAL MECHANICS  (10)
  • Amino Acid Sequence  (9)
  • *Genes, Viral  (7)
  • 1
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    Inhibition of HIV-1 infection by the beta-chemokine MDC (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-24
    Description: CD8(+) T lymphocytes from individuals infected with human immunodeficiency virus-type 1 (HIV-1) secrete a soluble activity that suppresses infection by HIV-1. A protein associated with this activity was purified from the culture supernatant of an immortalized CD8(+) T cell clone and identified as the beta-chemokine macrophage-derived chemokine (MDC). MDC suppressed infection of CD8(+) cell-depleted peripheral blood mononuclear cells by primary non-syncytium-inducing and syncytium-inducing isolates of HIV-1 and the T cell line-adapted isolate HIV-1IIIB. MDC was expressed in activated, but not resting, peripheral blood mononuclear cells and binds a receptor on activated primary T cells. These observations indicate that beta-chemokines are responsible for a major proportion of HIV-1-specific suppressor activity produced by primary T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pal, R -- Garzino-Demo, A -- Markham, P D -- Burns, J -- Brown, M -- Gallo, R C -- DeVico, A L -- N01-AI-55279/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 24;278(5338):695-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Advanced BioScience Laboratories, 5510 Nicholson Lane, Kensington, MD 20895, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381181" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antiviral Agents/*immunology ; Blotting, Northern ; CD8-Positive T-Lymphocytes/*immunology ; Calcium/blood ; Cell Line ; Cell Line, Transformed ; Cells, Cultured ; Chemokine CCL22 ; Chemokines, CC/chemistry/*immunology/isolation & purification/metabolism ; HIV Core Protein p24/biosynthesis ; HIV Infections/immunology ; HIV-1/*immunology/physiology ; Humans ; Leukocytes, Mononuclear/immunology/metabolism/*virology ; Lymphocyte Activation ; Receptors, Chemokine/metabolism ; Receptors, HIV/metabolism ; T-Lymphocytes/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Identification of RANTES, MIP-1 alpha, and MIP-1 beta as the major HIV-suppressive factors produced by CD8+ T cells (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-15
    Description: Evidence suggests that CD8+ T lymphocytes are involved in the control of human immunodeficiency virus (HIV) infection in vivo, either by cytolytic mechanisms or by the release of HIV-suppressive factors (HIV-SF). The chemokines RANTES, MIP-1 alpha, and MIP-1 beta were identified as the major HIV-SF produced by CD8+ T cells. Two active proteins purified from the culture supernatant of an immortalized CD8+ T cell clone revealed sequence identity with human RANTES and MIP-1 alpha. RANTES, MIP-1 alpha, and MIP-1 beta were released by both immortalized and primary CD8+ T cells. HIV-SF activity produced by these cells was completely blocked by a combination of neutralizing antibodies against RANTES, MIP-1 alpha, and MIP-1 beta. Recombinant human RANTES, MIP-1 alpha, and MIP-1 beta induced a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). These data may have relevance for the prevention and therapy of AIDS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cocchi, F -- DeVico, A L -- Garzino-Demo, A -- Arya, S K -- Gallo, R C -- Lusso, P -- New York, N.Y. -- Science. 1995 Dec 15;270(5243):1811-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Tumor Cell Biology, National Cancer Institute, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8525373" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Amino Acid Sequence ; Animals ; Antiviral Agents/*physiology ; CD8-Positive T-Lymphocytes/*immunology ; Cell Division/physiology ; Cell Line ; Cells, Cultured ; Chemokine CCL4 ; Chemokine CCL5/antagonists & inhibitors/*immunology ; Culture Media, Conditioned ; Cytokines/antagonists & inhibitors/*immunology ; Dose-Response Relationship, Immunologic ; Escherichia coli ; HIV Infections/immunology ; HIV-1/*immunology ; HIV-2/immunology ; Herpesvirus 6, Human/immunology ; Herpesvirus 7, Human/immunology ; Human T-lymphotropic virus 1/immunology ; Humans ; Immunoglobulin G/immunology ; Lymphocyte Activation ; Macaca nemestrina ; Macrophage Inflammatory Proteins ; Molecular Sequence Data ; Monokines/antagonists & inhibitors/*immunology ; Recombinant Proteins/immunology ; Simian Immunodeficiency Virus/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Identification of a major growth factor for AIDS-Kaposi's sarcoma cells as oncostatin M (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-13
    Description: Conditioned medium from human T cell leukemia virus type 2 (HTLV-II)-infected T cells supports the growth and long-term culture of cells derived from acquired immunodeficiency syndrome (AIDS)-associated Kaposi's sarcoma lesions (AIDS-KS cells). A protein of 30 kilodaltons was purified from conditioned medium that supports the growth of AIDS-KS cells. The amino-terminal sequence of this protein was identical to the amino-terminal sequence of Oncostatin M, a glycoprotein that inhibits the growth of a variety of cancer cells. Oncostatin M from conditioned medium stimulated a twofold increase in the growth of AIDS-KS cells at a concentration of less than 1 nanogram of the protein per milliliter of medium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nair, B C -- DeVico, A L -- Nakamura, S -- Copeland, T D -- Chen, Y -- Patel, A -- O'Neil, T -- Oroszlan, S -- Gallo, R C -- Sarngadharan, M G -- N01-CO-74101/CO/NCI NIH HHS/ -- N01-CP-73723/CP/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Mar 13;255(5050):1430-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Advanced BioScience Laboratories, Inc., Kensington, MD.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1542792" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*complications ; Amino Acid Sequence ; Culture Media/chemistry ; Growth Substances/isolation & purification/*physiology ; Humans ; Molecular Sequence Data ; Oncostatin M ; Peptides/isolation & purification/*physiology ; Sarcoma, Kaposi/etiology/*pathology ; Tumor Cells, Cultured
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6 (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-03-03
    Description: Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease that is familial in 10% of cases. We have identified a missense mutation in the gene encoding fused in sarcoma (FUS) in a British kindred, linked to ALS6. In a survey of 197 familial ALS index cases, we identified two further missense mutations in eight families. Postmortem analysis of three cases with FUS mutations showed FUS-immunoreactive cytoplasmic inclusions and predominantly lower motor neuron degeneration. Cellular expression studies revealed aberrant localization of mutant FUS protein. FUS is involved in the regulation of transcription and RNA splicing and transport, and it has functional homology to another ALS gene, TARDBP, which suggests that a common mechanism may underlie motor neuron degeneration.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4516382/" 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/PMC4516382/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vance, Caroline -- Rogelj, Boris -- Hortobagyi, Tibor -- De Vos, Kurt J -- Nishimura, Agnes Lumi -- Sreedharan, Jemeen -- Hu, Xun -- Smith, Bradley -- Ruddy, Deborah -- Wright, Paul -- Ganesalingam, Jeban -- Williams, Kelly L -- Tripathi, Vineeta -- Al-Saraj, Safa -- Al-Chalabi, Ammar -- Leigh, P Nigel -- Blair, Ian P -- Nicholson, Garth -- de Belleroche, Jackie -- Gallo, Jean-Marc -- Miller, Christopher C -- Shaw, Christopher E -- 078662/Wellcome Trust/United Kingdom -- G0300329/Medical Research Council/United Kingdom -- G0500289/Medical Research Council/United Kingdom -- G0501573/Medical Research Council/United Kingdom -- G0600676/Medical Research Council/United Kingdom -- G0600974/Medical Research Council/United Kingdom -- G0900688/Medical Research Council/United Kingdom -- MC_G1000733/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2009 Feb 27;323(5918):1208-11. doi: 10.1126/science.1165942.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Clinical Neuroscience, King's College London, Medical Research Council (MRC) Centre for Neurodegeneration Research, Institute of Psychiatry, London SE5 8AF, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19251628" target="_blank"〉PubMed〈/a〉
    Keywords: Age of Onset ; Amino Acid Sequence ; Amyotrophic Lateral Sclerosis/*genetics/metabolism/pathology ; Animals ; Brain/pathology ; Cell Line ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; DNA-Binding Proteins/analysis/genetics/metabolism ; Female ; Humans ; Inclusion Bodies/chemistry/ultrastructure ; Male ; Molecular Sequence Data ; Motor Neurons/metabolism ; *Mutation, Missense ; Pedigree ; RNA-Binding Protein FUS/analysis/*genetics/*metabolism ; Rats ; Spinal Cord/pathology ; Transfection
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    Electronic ISSN: 1095-9203
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  • 5
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    Homology of genome of AIDS-associated virus with genomes of human T-cell leukemia viruses (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-08-31
    Description: A T lymphotropic virus found in patients with the acquired immune deficiency syndrome (AIDS) or lymphadenopathy syndrome has been postulated to be the cause of AIDS. Immunological analysis of this retrovirus and its biological properties suggest that it is a member of the family of human T-lymphotropic retroviruses known as HTLV. Accordingly, it has been named HTLV-III. In the present report it is shown by nucleic acid hybridization that sequences of the genome of HTLV-III are homologous to the structural genes (gag, pol, and env) of both HTLV-I and HTLV-II and to a potential coding region called pX located between the env gene and the long terminal repeating sequence that is unique to the HTLV family of retroviruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arya, S K -- Gallo, R C -- Hahn, B H -- Shaw, G M -- Popovic, M -- Salahuddin, S Z -- Wong-Staal, F -- New York, N.Y. -- Science. 1984 Aug 31;225(4665):927-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089333" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; Base Sequence ; Cloning, Molecular ; Dna ; DNA, Viral ; Deltaretrovirus/classification/*genetics ; Genes ; *Genes, Viral ; Humans ; *Nucleic Acid Hybridization ; RNA, Viral ; Repetitive Sequences, Nucleic Acid
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  • 6
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    Antigens encoded by the 3'-terminal region of human T-cell leukemia virus: evidence for a functional gene (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-10-05
    Description: Antibodies in sera from patients with adult T-cell leukemia-lymphoma or from healthy carriers of type I human T-cell leukemia virus (HTLV) recognize an antigen of approximately 42 kilodaltons (p42) in cell lines infected with HTLV-I. Radiolabel sequence analysis of cyanogen bromide fragments of p42 led to the conclusion that this antigen is encoded in part by LOR, a conserved portion of the "X" region that is flanked by the envelope gene and the 3' long terminal repeat of HTLV-I. It is possible that this novel product mediates the unique transformation properties of the HTLV family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, T H -- Coligan, J E -- Sodroski, J G -- Haseltine, W A -- Salahuddin, S Z -- Wong-Staal, F -- Gallo, R C -- Essex, M -- 2-T32-CA0903/CA/NCI NIH HHS/ -- CA07094/CA/NCI NIH HHS/ -- CA13885/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1984 Oct 5;226(4670):57-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089350" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/*genetics ; Base Sequence ; Cell Line ; Cyanogen Bromide ; Deltaretrovirus/*genetics/immunology ; *Genes, Viral ; Humans ; Peptide Fragments ; Trans-Activators ; Viral Proteins/*genetics
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  • 7
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    Novel viral sequences related to human T-cell leukemia virus in T cells of a seropositive baboon (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-03-16
    Description: Antibodies reactive with proteins of human T-cell leukemia virus (HTLV) can be found in Old World monkeys. A T-lymphocyte cell line established from a seropositive baboon (Papio cynocephalus) was analyzed for the presence of viral DNA sequences. The provirus found in these cells was related to but distinct from HTLV subgroup I. These results add to recent evidence from human studies that HTLV represents a spectrum of infectious T-lymphotropic retroviruses that includes closely and distantly related members.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guo, H G -- Wong-Stall, F -- Gallo, R C -- New York, N.Y. -- Science. 1984 Mar 16;223(4641):1195-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6322297" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Viral/analysis ; Antigens, Viral/immunology ; Base Sequence ; Cell Line ; DNA Restriction Enzymes ; DNA, Viral/*analysis ; Deltaretrovirus/*genetics/immunology ; *Genes, Viral ; Humans ; Nucleic Acid Hybridization ; Papio/immunology/*microbiology ; Repetitive Sequences, Nucleic Acid ; T-Lymphocytes/*analysis/microbiology
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  • 8
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    5' viral and human cellular sequences corresponding to the transforming gene of simian sarcoma virus (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-02-04
    Description: The 5' nucleotide sequences of the transforming gene of simian sarcoma virus (v-sis) and its human cellular homolog (c-sis) were compared. A short homology was found between helper virus and cellular DNA sequences at the junction of v-sis and c-sis, which may have had a role in the original recombination event leading to the generation of simian sarcoma virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Josephs, S F -- Dalla-Favera, R -- Gelmann, E P -- Gallo, R C -- Wong-Staal, F -- New York, N.Y. -- Science. 1983 Feb 4;219(4584):503-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6297002" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Genes, Viral ; Helper Viruses/genetics ; Humans ; *Oncogenes ; Recombination, Genetic ; Retroviridae/*genetics ; Sarcoma Virus, Woolly Monkey/*genetics
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  • 9
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    Type-restricted neutralization of molecular clones of human immunodeficiency virus (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-15
    Description: In a study of the immunologic significance of the genetic diversity present within single isolates of human immunodeficiency virus type 1 (HIV-1), the neutralization of viruses derived from molecular clones of the HIV-1 strain HTLV-IIIB by an extensive panel of sera was compared. Sera from HIV-1-infected patients and from goats immunized with polyacrylamide gel-purified HIV-1 envelope glycoprotein (gp120), native gp120, or gp120-derived recombinant peptides, showed marked heterogeneity in neutralizing activity against these closely related viruses. The change of a single amino acid residue in gp120 may account for such "clonal restriction" of neutralizing activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Looney, D J -- Fisher, A G -- Putney, S D -- Rusche, J R -- Redfield, R R -- Burke, D S -- Gallo, R C -- Wong-Staal, F -- New York, N.Y. -- Science. 1988 Jul 15;241(4863):357-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Viral Diseases, Walter Reed Army Institute of Research, Washington, DC 20307.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3388046" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Viral/*immunology ; Binding, Competitive ; Cloning, Molecular ; HIV/genetics/*immunology ; HIV Seropositivity/immunology ; Humans ; Molecular Sequence Data ; Neutralization Tests ; Oligopeptides/chemical synthesis/immunology
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  • 10
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    Characterization of long terminal repeat sequences of HTLV-III (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-02-01
    Description: The nucleotide sequence of the long terminal repeat sequence (LTR) of the human T-cell leukemia (lymphotropic) virus type III (HTLV-III) was determined. This virus is associated etiologically with the acquired immune deficiency syndrome. The LTR was found to be 634 base pairs in length with U3, R, and U5 regions of 453, 98, and 83 bp, respectively. The proviral DNA is flanked by a 7-base-pair direct repeat. The promoter and polyadenylation signals are situated 27 and 24 base pairs upstream from the respective transcriptional initiation and polyadenylation sites. The primer binding site is complementary to transfer RNA-lysine. The LTR of HTLV-III, like that of HTLV-I, showed a limited homology to enhancer-like sequences within two genes expressed specifically in T lymphocytes, T-cell growth factor, and gamma-interferon. Structural comparisons revealed that the LTR of HTLV-III is distantly related to those of HTLV-I, HTLV-II, and bovine leukemia virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Starcich, B -- Ratner, L -- Josephs, S F -- Okamoto, T -- Gallo, R C -- Wong-Staal, F -- New York, N.Y. -- Science. 1985 Feb 1;227(4686):538-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2981438" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Evolution ; Dna ; DNA, Viral ; Deltaretrovirus/*genetics ; *Genes, Viral ; Humans ; Interferon-gamma/genetics ; Interleukin-2/genetics ; Leukemia Virus, Bovine/genetics ; Operon ; RNA, Viral ; *Repetitive Sequences, Nucleic Acid ; Retroviridae/genetics ; Transcription, Genetic
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