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  • Amino Acid Sequence  (50)
  • Signal Transduction
  • American Association for the Advancement of Science (AAAS)  (50)
  • American Institute of Physics (AIP)
  • Public Library of Science
  • 1985-1989  (50)
  • 1985  (50)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (50)
  • American Institute of Physics (AIP)
  • Public Library of Science
Years
  • 1985-1989  (50)
Year
  • 1
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    A new HTLV-III/LAV encoded antigen detected by antibodies from AIDS patients (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-15
    Description: A newly identified protein from HTLV-III/LAV, the virus implicated as the etiologic agent of the acquired immune deficiency syndrome, was studied. This protein, which has a molecular weight of 27,000 (p27), was shown by amino acid sequencing to have a coding origin 3' to the env gene on the HTLV-III genome. The presence of antibodies to p27 in virus-exposed individuals indicated that this gene is functional in the natural host.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allan, J S -- Coligan, J E -- Lee, T H -- McLane, M F -- Kanki, P J -- Groopman, J E -- Essex, M -- 2T32-CA09031/CA/NCI NIH HHS/ -- CA23885/CA/NCI NIH HHS/ -- CA37466/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 15;230(4727):810-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2997921" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology/microbiology ; Amino Acid Sequence ; Animals ; Antibodies, Viral/*immunology ; Antibody Formation ; Antigens, Viral/*immunology ; Deltaretrovirus/genetics/*immunology ; Electrophoresis, Polyacrylamide Gel ; Haplorhini/microbiology ; Humans ; Male ; Molecular Weight ; Repetitive Sequences, Nucleic Acid
    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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    Major glycoprotein antigens that induce antibodies in AIDS patients are encoded by HTLV-III (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-31
    Description: Antibodies from the serum of patients with the acquired immune deficiency syndrome (AIDS) or with the AIDS-related complex and from the serum of seropositive healthy homosexuals, recognize two major glycoproteins in cells infected with human T-cell lymphotropic virus type III (HTLV III). These glycoproteins, gp160 and gp120, are encoded by the 2.5-kilobase open reading frame located in the 3' end of the HTLV-III genome, as determined by amino terminus sequence analysis of the radiolabeled forms of these proteins. It is hypothesized that gp160 and gp120 represent the major species of virus-encoded envelope gene products for HTLV-III.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allan, J S -- Coligan, J E -- Barin, F -- McLane, M F -- Sodroski, J G -- Rosen, C A -- Haseltine, W A -- Lee, T H -- Essex, M -- 2T32-CA09031/CA/NCI NIH HHS/ -- CA 13885/CA/NCI NIH HHS/ -- CA 37466/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 31;228(4703):1091-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2986290" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology ; Amino Acid Sequence ; Antibodies, Viral/immunology ; Antigens, Viral/genetics/*immunology ; Base Sequence ; Deltaretrovirus/*immunology ; Genes, Viral ; Glycoproteins/genetics/immunology ; Humans ; Molecular Weight ; Tunicamycin/pharmacology ; Viral Envelope Proteins/genetics/*immunology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Circumsporozoite protein of Plasmodium vivax: gene cloning and characterization of the immunodominant epitope (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-15
    Description: The gene encoding the circumsporozoite (CS) protein of the human malaria parasite Plasmodium vivax has been cloned. The deduced sequence of the protein consists of 373 amino acids with a central region of 19 tandem repeats of the nonapeptide Asp-Arg-Ala-Asp/Ala-Gly-Gln-Pro-Ala-Gly. A synthetic 18-amino acid peptide containing two tandem repeats binds to a monoclonal antibody directed to the CS protein of Plasmodium vivax and inhibits the interaction of this antibody with the native protein in sporozoite extracts. The portions of the CS gene that do not contain repeats are closely related to the corresponding regions of the CS genes of two simian malarias, Plasmodium cynomolgi and Plasmodium knowlesi. In contrast, the homology between the CS genes of Plasmodium vivax and Plasmodium falciparum, another malaria parasite of humans, is very limited.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arnot, D E -- Barnwell, J W -- Tam, J P -- Nussenzweig, V -- Nussenzweig, R S -- Enea, V -- New York, N.Y. -- Science. 1985 Nov 15;230(4727):815-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2414847" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Antigens, Surface/*genetics/immunology ; Cloning, Molecular ; Epitopes/*genetics/immunology ; Haplorhini/parasitology ; Humans ; Malaria/parasitology ; Nucleic Acid Hybridization ; Plasmodium/immunology ; Plasmodium vivax/*genetics/immunology ; *Protozoan Proteins ; Repetitive Sequences, Nucleic Acid
    Print ISSN: 0036-8075
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  • 4
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    Trans-activator gene of human T-lymphotropic virus type III (HTLV-III) (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-07-05
    Description: Human T-lymphotropic virus type III (HTLV-III) encodes a trans-acting factor that activates the expression of genes linked to the HTLV-III long terminal repeat. By functional mapping of complementary DNA transcripts of viral messenger RNA's the major functional domain of the gene encoding this factor was localized to a region immediately before the env gene of the virus, a region previously thought to be noncoding. This newly identified gene consists of three exons, and its transcription into messenger RNA involves two splicing events bringing together sequences from the 5' part (287 base pairs), middle (268 base pairs), and 3'part (1258 base pairs) of the HTLV-III genome. A similar messenger RNA with a truncated second exon (70 base pairs) does not encode a trans-acting function. It is proposed that this second messenger RNA is the transcript of a gene (3'-orf) located after the env gene. Messenger RNA's were also identified for the env and gag-pol genes of HTLV-III.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arya, S K -- Guo, C -- Josephs, S F -- Wong-Staal, F -- New York, N.Y. -- Science. 1985 Jul 5;229(4708):69-73.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990040" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Deltaretrovirus/*genetics ; Gene Expression Regulation ; Genes, Regulator ; *Genes, Viral ; Humans ; RNA Splicing ; RNA, Messenger/genetics ; RNA, Viral/genetics ; Repetitive Sequences, Nucleic Acid ; Transcription Factors/*genetics ; Viral Proteins/genetics
    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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    Immunogenicity of synthetic peptides from circumsporozoite protein of Plasmodium falciparum (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-24
    Description: In a study of recombinant proteins that might be useful in developing a vaccine against malaria, synthetic peptides from the circumsporozoite (CS) protein of Plasmodium falciparum were found to be immunogenic for mice and rabbits. Antibody to peptides from the repeating region of the CS protein recognized native CS protein and blocked sporozoite invasion of human hepatoma cells in vitro. Antibodies to peptides from regions I and II had no biologic activity, although antibody to region I recognized processed CS protein by Western blot analysis. These data support the feasibility of developing a vaccine against the sporozoite stage of the malaria parasite by using synthetic peptides of the repeating region of the CS protein conjugated to a carrier protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ballou, W R -- Rothbard, J -- Wirtz, R A -- Gordon, D M -- Williams, J S -- Gore, R W -- Schneider, I -- Hollingdale, M R -- Beaudoin, R L -- Maloy, W L -- New York, N.Y. -- Science. 1985 May 24;228(4702):996-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2988126" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies/immunology ; Antibody Formation ; Antigens, Surface/*immunology ; Carcinoma, Hepatocellular ; Cell Line ; Cross Reactions ; Fluorescent Antibody Technique ; Humans ; Immune Sera/immunology ; Liver Neoplasms ; Malaria/prevention & control ; Mice ; Peptides/chemical synthesis/*immunology ; Plasmodium/immunology ; Plasmodium falciparum/*immunology/physiology ; Precipitin Tests ; *Protozoan Proteins ; Rabbits ; Vaccines/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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  • 6
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    Biosynthesis and secretion of proatrial natriuretic factor by cultured rat cardiocytes (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-06
    Description: Rat atrial natriuretic factor (ANF) is translated as a 152-amino acid precursor preproANF. PreproANF is converted to the 126-amino acid proANF, the storage form of ANF in the atria. ANF isolated from the blood is approximately 25 amino acids long. It is demonstrated here that rat cardiocytes in culture store and secrete proANF. Incubation of proANF with serum produced a smaller ANF peptide. PreproANF seems to be processed to proANF in the atria, and proANF appears to be released into the blood, where it is converted by a protease to a smaller peptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bloch, K D -- Scott, J A -- Zisfein, J B -- Fallon, J T -- Margolies, M N -- Seidman, C E -- Matsueda, G R -- Homcy, C J -- Graham, R M -- Seidman, J G -- 1R23CA33570/CA/NCI NIH HHS/ -- HL07208/HL/NHLBI NIH HHS/ -- HL26215/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Dec 6;230(4730):1168-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2933808" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Atrial Natriuretic Factor/*biosynthesis/genetics/secretion ; Autoradiography ; Cells, Cultured ; Electrophoresis, Polyacrylamide Gel ; Heart/physiology ; Immune Sera/immunology ; Myocardium/*cytology/metabolism ; Protein Precursors/*biosynthesis/genetics/secretion ; RNA, Messenger/genetics ; Rabbits/immunology ; Rats
    Print ISSN: 0036-8075
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  • 7
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    A new class of endogenous human retroviral genomes (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-07
    Description: Human DNA contains multiple copies of a novel class of endogenous retroviral genomes. Analysis of a human recombinant DNA clone (HLM-2) containing one such proviral genome revealed that it is a mosaic of retroviral-related sequences with the organization and length of known endogenous retroviral genomes. The HLM-2 long terminal repeat hybridized with the long terminal repeat of the squirrel monkey virus, a type D retrovirus. The HLM-2 gag and pol genes share extensive nucleotide sequence homology with those of the M432 retrovirus (a type A-related retrovirus), mouse mammary tumor virus (a type B retrovirus), and the avian Rous sarcoma virus (a type C retrovirus). Nucleotide sequence analysis revealed regions in the HLM-2 pol gene that were as much as 70 percent identical to the mouse mammary tumor virus pol gene. A portion of the putative HLM-2 env gene hybridized with the corresponding region of the M432 viral genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Callahan, R -- Chiu, I M -- Wong, J F -- Tronick, S R -- Roe, B A -- Aaronson, S A -- Schlom, J -- GM30400/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1208-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2408338" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/genetics ; Base Sequence ; Cloning, Molecular ; DNA Restriction Enzymes ; Gene Products, gag ; Genes, Viral ; Humans ; RNA-Directed DNA Polymerase/genetics ; Retroviridae/classification/*genetics ; Viral Proteins/genetics
    Print ISSN: 0036-8075
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  • 8
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    Inhibition of lymphocyte proliferation by a synthetic peptide homologous to retroviral envelope proteins (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-25
    Description: The retroviral transmembrane envelope protein p15E is immunosuppressive in that it inhibits immune responses of lymphocytes, monocytes, and macrophages. A region of p15E has been conserved among murine and feline retroviruses; a homologous region is also found in the transmembrane envelope proteins of the human retroviruses HTLV-I and HTLV-II and in a putative envelope protein encoded by an endogenous C-type human retroviral DNA. A peptide (CKS-17) was synthesized to correspond to this region of homology and was examined for its effects on lymphocyte proliferation. CKS-17 inhibited the proliferation of an interleukin-2-dependent murine cytotoxic T-cell line as well as alloantigen-stimulated proliferation of murine and human lymphocytes. Four other peptides, representing different regions of virus proteins, were inactive. These results suggest that the immunosuppressive portion of retroviral transmembrane envelope proteins may reside, at least in part, in a-conserved sequence represented by the CKS-17 peptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cianciolo, G J -- Copeland, T D -- Oroszlan, S -- Snyderman, R -- P01-CA29589-02/CA/NCI NIH HHS/ -- R23-CA34671-02/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Oct 25;230(4724):453-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996136" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Deltaretrovirus/genetics ; Humans ; Leukemia Virus, Feline/genetics ; Leukemia Virus, Murine/genetics ; Lymphocyte Activation/*drug effects ; Lymphocyte Culture Test, Mixed ; Lymphocytes/drug effects ; Mice ; Mice, Inbred BALB C ; Peptides/*pharmacology ; Retroviridae/*genetics ; Spleen/cytology ; Viral Envelope Proteins/genetics/*pharmacology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Amino acid homology between the encephalitogenic site of myelin basic protein and virus: mechanism for autoimmunity (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-29
    Description: Amino acid sequence homology was found between viral and host encephalitogenic protein. Immune responses were then generated in rabbits by using the viral peptide that cross-reacts with the self protein. Mononuclear cell infiltration was observed in the central nervous systems of animals immunized with the viral peptide. Myelin basic protein (MBP) is a host protein whose encephalitogenic site of ten amino acids induces experimental allergic encephalomyelitis. By computer analysis, hepatitis B virus polymerase (HBVP) was found to share six consecutive amino acids with the encephalitogenic site of rabbit MBP. Rabbits given injections of a selected eight- or ten-amino acid peptide from HBVP made antibody that reacted with the predetermined sequences of HBVP and also with native MBP. Peripheral blood mononuclear cells from the immunized rabbits proliferated when incubated with either MBP or HBVP. Central nervous system tissue taken from these rabbits had a histologic picture reminiscent of experimental allergic encephalomyelitis. Thus, viral infection may trigger the production of antibodies and mononuclear cells that cross-react with self proteins by a mechanism termed molecular mimicry. Tissue injury from the resultant autoallergic event can take place in the absence of the infectious virus that initiated the immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fujinami, R S -- Oldstone, M B -- AG-04342/AG/NIA NIH HHS/ -- AI-07007/AI/NIAID NIH HHS/ -- NS-12428/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 29;230(4729):1043-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2414848" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Autoimmune Diseases/immunology ; Cross Reactions ; *DNA-Directed RNA Polymerases/immunology ; Encephalomyelitis, Autoimmune, Experimental/immunology/*microbiology ; Hepatitis B virus/analysis/*immunology ; *Myelin Basic Protein/immunology ; *Viral Proteins/immunology
    Print ISSN: 0036-8075
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  • 10
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    Diversity of circumsporozoite antigen genes from two strains of the malarial parasite Plasmodium knowlesi (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-08-23
    Description: The complete nucleotide sequence of the coding region of the circumsporozoite antigen gene (CS gene) of the Nuri strain of the malarial parasite Plasmodium knowlesi is presented. The gene from the Nuri strain exhibits a novel form of sequence diversity when compared to the CS gene from the H strain. Instead of the 12 tandem repeating 36-base pair units of the H strain, the Nuri strain contains 16 tandem repeating 27-base pair units of a different nucleotide sequence that encodes a different repeating peptide. In contrast, the 5' and 3' coding and noncoding sequences flanking the repeats are 98 percent conserved in both strains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharma, S -- Svec, P -- Mitchell, G H -- Godson, G N -- 1 R01 AI21496-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 23;229(4715):779-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4023712" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Protozoan/*genetics ; Antigens, Surface/genetics ; Base Sequence ; Genes ; Molecular Sequence Data ; Plasmodium/*genetics/immunology ; Protozoan Proteins/*genetics ; Repetitive Sequences, Nucleic Acid
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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