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  • Amino Acid Sequence  (50)
  • Mutation  (25)
  • American Association for the Advancement of Science (AAAS)  (72)
  • American Chemical Society
  • 1985-1989  (72)
  • 1980-1984
  • 1965-1969
  • 1985  (72)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (72)
  • American Chemical Society
  • Springer  (3)
Years
  • 1985-1989  (72)
  • 1980-1984
  • 1965-1969
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
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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
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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
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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
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  • 6
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    Evolution of bunyaviruses by genome reassortment in dually infected mosquitoes (Aedes triseriatus) (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-01
    Description: Aedes triseriatus mosquitoes became dually infected after ingesting two mutants of LaCrosse (LAC) virus simultaneously or after ingesting, by interrupted feeding, the two viruses sequentially within a 2-day period. After 2 weeks of incubation, approximately 25 percent of the vectors contained new virus genotypes as the result of RNA segment reassortment. New viruses were transmitted when the mosquitoes fed on mice. Viruses ingested more than 2 days after the initial infecting virus did not cause superinfection of the mosquito vectors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beaty, B J -- Sundin, D R -- Chandler, L J -- Bishop, D H -- AI 15400/AI/NIAID NIH HHS/ -- AI 19688/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 1;230(4725):548-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4048949" target="_blank"〉PubMed〈/a〉
    Keywords: Aedes/*microbiology ; Animals ; Blood ; Bunyaviridae/*genetics ; Genotype ; Insect Vectors ; Mutation ; Phenotype ; RNA, Viral/analysis ; Time Factors
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  • 7
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    The mosaic genome of warm-blooded vertebrates (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-24
    Description: Most of the nuclear genome of warm-blooded vertebrates is a mosaic of very long (much greater than 200 kilobases) DNA segments, the isochores; these isochores are fairly homogeneous in base composition and belong to a small number of major classes distinguished by differences in guanine-cytosine (GC) content. The families of DNA molecules derived from such classes can be separated and used to study the genome distribution of any sequence which can be probed. This approach has revealed (i) that the distribution of genes, integrated viral sequences, and interspersed repeats is highly nonuniform in the genome, and (ii) that the base composition and ratio of CpG to GpC in both coding and noncoding sequences, as well as codon usage, mainly depend on the GC content of the isochores harboring the sequences. The compositional compartmentalization of the genome of warm-blooded vertebrates is discussed with respect to its evolutionary origin, its causes, and its effects on chromosome structure and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bernardi, G -- Olofsson, B -- Filipski, J -- Zerial, M -- Salinas, J -- Cuny, G -- Meunier-Rotival, M -- Rodier, F -- New York, N.Y. -- Science. 1985 May 24;228(4702):953-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4001930" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Base Sequence ; Biological Evolution ; Centrifugation, Density Gradient ; Chickens/*genetics ; Chromosome Banding ; Codon ; Cytosine/analysis ; DNA/analysis/*genetics ; DNA Replication ; DNA, Viral/genetics ; Gene Amplification ; *Genes ; Genes, Viral ; Guanine/analysis ; Humans ; Mammals/*genetics ; Mice/genetics ; Mutation ; Rabbits/genetics ; Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; Xenopus/*genetics
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  • 8
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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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  • 9
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    The "spliceosome": yeast pre-messenger RNA associates with a 40S complex in a splicing-dependent reaction (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-24
    Description: The in vitro splicing reactions of pre-messenger RNA (pre-mRNA) in a yeast extract were analyzed by glycerol gradient centrifugation. Labeled pre-mRNA appears in a 40S peak only if the pre-mRNA undergoes the first of the two partial splicing reactions. RNA analysis after extraction of glycerol gradient fractions shows that lariat-form intermediates, molecules that occur only in mRNA splicing, are found almost exclusively in this 40S complex. Another reaction intermediate, cut 5' exon RNA, can also be found concentrated in this complex. The complex is stable even in 400 mM KCl, although at this salt concentration, it sediments at 35S and is clearly distinguishable from 40S ribosomal subunits. This complex, termed a "spliceosome," is thought to contain components necessary for mRNA splicing; its existence can explain how separated exons on pre-mRNA are brought into contact.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brody, E -- Abelson, J -- New York, N.Y. -- Science. 1985 May 24;228(4702):963-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3890181" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/genetics ; Base Sequence ; Centrifugation, Density Gradient ; Mutation ; Nucleic Acid Conformation ; Nucleic Acid Precursors/*genetics/metabolism ; RNA Precursors ; *RNA Splicing ; RNA, Fungal/*genetics/metabolism ; RNA, Messenger/*genetics/metabolism ; Saccharomyces cerevisiae/*genetics/metabolism
    Print ISSN: 0036-8075
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  • 10
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    The unusual varl gene of yeast mitochondrial DNA (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-28
    Description: The var1 gene specifies the only mitochondrial ribosomal protein known to be encoded by yeast mitochondrial DNA. The gene is unusual in that its base composition is nearly 90 percent adenine plus thymine. It and its expression product show a strain-dependent variation in size of up to 7 percent; this variation does not detectably interfere with function. Furthermore, var1 is an expandable gene that participates in a novel recombinational event resembling gene conversion whereby shorter alleles are preferentially converted to longer ones. The remarkable features of var1 indicate that it may have evolved by a mechanism analogous to exon shuffling, although no introns are actually present.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Butow, R A -- Perlman, P S -- Grossman, L I -- GM-22525/GM/NIGMS NIH HHS/ -- GM-26546/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 28;228(4707):1496-501.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990030" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Biological Evolution ; DNA Restriction Enzymes/metabolism ; DNA, Mitochondrial/*analysis ; *Genes, Fungal ; Mutation ; Neurospora/*genetics ; Polymorphism, Genetic
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  • 11
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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
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  • 12
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    Activated proto-onc genes: sufficient or necessary for cancer? (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-10
    Description: Proto-onc genes are normal cellular genes that are related to the transforming (onc) genes of retroviruses. Because of this relationship these genes are now widely believed to be potential cancer genes. In some tumors, proto-onc genes are mutated or expressed more than in normal cells. Under these conditions, proto-onc genes are hypothesized to be active cancer genes in one of two possible ways: The one gene-one cancer hypothesis suggests that one activated proto-onc gene is sufficient to cause cancer. The multigene-one cancer hypothesis suggests that an activated proto-onc gene is a necessary but not a sufficient cause of cancer. However, mutated or transcriptionally activated proto-onc genes are not consistently associated with the tumors in which they are occasionally found and do not transform primary cells. Further, no set of an activated proto-onc gene and a complementary cancer gene with transforming function has yet been isolated from a tumor. Thus, there is still no proof that activated proto-onc genes are sufficient or even necessary to cause cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duesberg, P H -- CA 11426/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 10;228(4700):669-77.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3992240" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Transformation, Neoplastic/metabolism ; Chickens ; DNA, Neoplasm/genetics ; Genes, Viral ; Humans ; Kirsten murine sarcoma virus/genetics ; Lymphoma/genetics ; Melanoma/genetics ; Mice ; Mutation ; Neoplasms/etiology/*genetics ; *Oncogenes ; Plasmacytoma/genetics ; Rats ; Retroviridae/genetics ; Sarcoma, Experimental/genetics ; Transduction, Genetic ; Translocation, Genetic ; Tumor Virus Infections/genetics
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  • 13
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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
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  • 14
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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
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  • 15
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    Bidirectional SV40 transcription mediated by tandem Sp1 binding interactions (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-01
    Description: The 21-base pair repeat elements of the SV40 promoter contain six tandem copies of the GGGCGG hexanucleotide (GC-box), each of which can bind, with varying affinity, to the cellular transcription factor, Sp1. In vitro SV40 early RNA synthesis is mediated by interaction of Sp1 with GC-boxes I, II, and III, whereas transcription in the late direction is mediated by binding to GC-boxes III, V, and VI.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gidoni, D -- Kadonaga, J T -- Barrera-Saldana, H -- Takahashi, K -- Chambon, P -- Tjian, R -- New York, N.Y. -- Science. 1985 Nov 1;230(4725):511-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996137" target="_blank"〉PubMed〈/a〉
    Keywords: Autoradiography ; Base Sequence ; Binding Sites ; DNA-Binding Proteins/*metabolism ; Deoxyribonuclease I/metabolism ; Electrophoresis, Polyacrylamide Gel ; Gene Expression Regulation ; Mutation ; Pregnancy Proteins/*metabolism ; RNA, Messenger/analysis ; RNA, Viral/biosynthesis ; Simian virus 40/*genetics ; Sp1 Transcription Factor ; Templates, Genetic ; Transcription Factors/*metabolism ; *Transcription, Genetic
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  • 16
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    Rescue of the Drosophila phototransduction mutation trp by germline transformation (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-29
    Description: Phototransduction is the process by which light-stimulated photoreceptor cells of the visual system send electrical signals to the nervous system. Many of the steps that follow the initial event in phototransduction, absorption of light by rhodopsin, are ill-defined. The fruitfly, Drosophila melanogaster, provides a means to dissect phototransduction genetically. Mutations such as transient receptor potential (trp) affect intermediate steps in phototransduction. In order to facilitate molecular studies of phototransduction, the trp gene was isolated and its identity was confirmed by complementing the mutant trpCM allele of the trp gene by P-element mediated germline transformation of a 7.1-kilobase DNA fragment. Expression of the trp gene begins late in pupal development and appears to be limited to the eyes and ocelli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Montell, C -- Jones, K -- Hafen, E -- Rubin, G -- New York, N.Y. -- Science. 1985 Nov 29;230(4729):1040-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3933112" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA/genetics ; Drosophila melanogaster/*genetics/physiology ; Gene Expression Regulation ; Genes ; Mutation ; Ocular Physiological Phenomena ; RNA, Messenger/genetics ; *Vision, Ocular
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  • 17
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    Measles virus matrix protein synthesized in a subacute sclerosing panencephalitis cell line (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-07
    Description: Measles virus generally produces acute illness. Rarely, however, persistent infection of brain cells occurs, resulting in a chronic and fatal neurological disease, subacute sclerosing panencephalitis (SSPE). Evidence indicates that expression of the measles virus matrix protein is selectively restricted in this persistent infection, but the mechanism underlying this restriction has not been identified. Defective translation of matrix messenger RNA has been described in one SSPE cell line. This report presents evidence that in a different SSPE tissue culture cell line IP-3-Ca, the matrix protein is synthesized but fails to accumulate. A general scheme is proposed to reconcile the different levels at which restriction of matrix protein has been observed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sheppard, R D -- Raine, C S -- Bornstein, M B -- Udem, S A -- CA13330-12/CA/NCI NIH HHS/ -- NS 08952/NS/NINDS NIH HHS/ -- NS 11920/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1219-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4001938" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Gene Expression Regulation ; Humans ; Hydrolysis ; Measles virus/genetics/growth & development/*metabolism ; Molecular Weight ; Mutation ; Protein Processing, Post-Translational ; Subacute Sclerosing Panencephalitis/*microbiology ; Viral Matrix Proteins ; Viral Proteins/*biosynthesis/genetics ; Virus Replication
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  • 18
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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
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  • 19
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    Heterologous protein secretion from yeast (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, R A -- Duncan, M J -- Moir, D T -- New York, N.Y. -- Science. 1985 Sep 20;229(4719):1219-24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3939723" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Chymosin/*secretion ; Cloning, Molecular ; Cytoplasm/enzymology ; Enzyme Activation ; Enzyme Precursors/*secretion ; Fungal Proteins/secretion ; Glycosylation ; Mutation ; Plasmids ; Protein Processing, Post-Translational ; Recombinant Fusion Proteins/secretion ; Saccharomyces cerevisiae/enzymology/*genetics ; Solubility
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  • 20
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    Sequence of the immunodominant epitope for the surface protein on sporozoites of Plasmodium vivax (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-20
    Description: Plasmodium vivax is one of the four malaria parasites that cause disease in humans. The structure of the immunodominant repeating peptide of the circumsporozoite (CS) protein of P. vivax was determined. A fragment of P. vivax DNA that encodes this tandemly repeating epitope was isolated by use of an oligonucleotide probe whose sequence is thought to be conserved in CS protein genes. DNA sequence analysis of the P. vivax clone indicates that the CS repeat is nine amino acids in length (Gly-Asp-Arg-Ala-Asp-Gly-Gln-Pro-Ala). The structure of the repeating region was confirmed with synthetic peptides and monoclonal antibodies directed against P. vivax sporozoites. This information should allow synthesis of a vaccine for P. vivax that is similar to the one being tested for P. falciparum.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCutchan, T F -- Lal, A A -- de la Cruz, V F -- Miller, L H -- Maloy, W L -- Charoenvit, Y -- Beaudoin, R L -- Guerry, P -- Wistar, R Jr -- Hoffman, S L -- New York, N.Y. -- Science. 1985 Dec 20;230(4732):1381-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2416057" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Surface/*genetics ; Base Sequence ; DNA Restriction Enzymes ; Epitopes/*genetics ; *Genes ; Plasmodium vivax/*immunology ; Species Specificity
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  • 21
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    Cassette of eight exons shared by genes for LDL receptor and EGF precursor (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-17
    Description: The amino acid sequences of the human low-density lipoprotein (LDL) receptor and the human precursor for epidermal growth factor (EGF) show 33 percent identity over a stretch of 400 residues. This region of homologous is encoded by eight contiguous exons in each respective gene. Of the nine introns that separate these exons, five are located in identical positions in the two protein sequences. This finding suggests that the homologous region may have resulted from a duplication of an ancestral gene and that the two genes evolved further by recruitment of exons from other genes, which provided the specific functional domains of the LDL receptor and the EGF precursor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sudhof, T C -- Russell, D W -- Goldstein, J L -- Brown, M S -- Sanchez-Pescador, R -- Bell, G I -- HL 01287/HL/NHLBI NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- HL 31346/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 17;228(4701):893-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3873704" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Base Sequence ; Biological Evolution ; Cloning, Molecular ; Epidermal Growth Factor/*genetics ; Genes ; Humans ; Protein Precursors/genetics ; Receptors, LDL/*genetics ; Repetitive Sequences, Nucleic Acid
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  • 22
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    The LDL receptor gene: a mosaic of exons shared with different proteins (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-17
    Description: The multifunctional nature of coated pit receptors predicts that these proteins will contain multiple domains. To establish the genetic basis for these domains (LDL) receptor. This gene is more than 45 kilobases in length and contains 18 exons, most of which correlate with functional domains previously defined at the protein level. Thirteen of the 18 exons encode protein sequences that are homologous to sequences in other proteins: five of these exons encode a sequence similar to one in the C9 component of complement; three exons encode a sequence similar to a repeat sequence in the precursor for epidermal growth factor (EGF) and in three proteins of the blood clotting system (factor IX, factor X, and protein C); and five other exons encode nonrepeated sequences that are shared only with the EGF precursor. The LDL receptor appears to be a mosaic protein built up of exons shared with different proteins, and it therefore belongs to several supergene families.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4450672/" 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/PMC4450672/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sudhof, T C -- Goldstein, J L -- Brown, M S -- Russell, D W -- HL 01287/HL/NHLBI NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- HL 31346/HL/NHLBI NIH HHS/ -- P01 HL020948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 17;228(4701):815-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2988123" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Base Sequence ; Cloning, Molecular ; Complement C9/genetics ; Dna ; Endonucleases ; Epidermal Growth Factor/genetics ; Factor IX/genetics ; Factor X/genetics ; *Genes ; Glycoproteins/genetics ; Humans ; Hyperlipoproteinemia Type II/genetics ; Molecular Weight ; Protein C ; Protein Precursors ; Protein Processing, Post-Translational ; Receptors, LDL/*genetics ; Repetitive Sequences, Nucleic Acid ; Single-Strand Specific DNA and RNA Endonucleases ; Transcription, Genetic
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  • 23
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    HTLV x-gene product: requirement for the env methionine initiation codon (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-28
    Description: The human T-cell leukemia viruses (HTLV) are replication-competent retroviruses whose genomes contain gag, pol, and env genes as well as a fourth gene, termed x, which is believed to be the transforming gene of HTLV. The product of the x gene is now shown to be encoded by a 2.1-kilobase messenger RNA derived by splicing of at least two introns. By means of S1 nuclease mapping of this RNA and nucleic acid sequence analysis of a complementary DNA clone, the complete primary structure of the x-gene product has been determined. It is encoded by sequences containing the env initiation codon and one nucleotide of the next codon spliced to the major open reading frame of the HTLV-I and HTLV-II x gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wachsman, W -- Golde, D W -- Temple, P A -- Orr, E C -- Clark, S C -- Chen, I S -- CA 30388/CA/NCI NIH HHS/ -- CA 32737/CA/NCI NIH HHS/ -- CA 38597/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 28;228(4707):1534-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990032" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Transformation, Viral ; Codon ; Deltaretrovirus/*genetics ; Electrophoresis, Polyacrylamide Gel ; Humans ; Methionine/*genetics ; Rats ; Viral Proteins/*analysis
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  • 24
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    A model for fibrinogen: domains and sequence (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-12-20
    Description: Electron microscopy of rotary-shadowed fibrinogen demonstrates that the molecules modified for crystallization by limited cleavage with a bacterial protease retain the major features of the native structure. This evidence, together with image processing and x-ray analysis of the crystals and of fibrin, has been used to develop a three-dimensional low resolution model for the molecule. The data indicate that the two large end domains of the molecule would be composed of the carboxyl-terminus of the B beta chain (proximal) and gamma chain (distal), respectively; the carboxyl-terminus of the A alpha chain would fold back to form an additional central domain. On this basis, the carboxyl-terminal region of each of the three chains of fibrinogen is folded independently into a globular domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weisel, J W -- Stauffacher, C V -- Bullitt, E -- Cohen, C -- AM17346/AM/NIADDK NIH HHS/ -- GM07596-07/GM/NIGMS NIH HHS/ -- HL30954/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Dec 20;230(4732):1388-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4071058" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Computers ; Fibrinogen/*metabolism ; Microscopy, Electron ; Models, Molecular ; Protein Conformation
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  • 25
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    Human immunoglobulin D: genomic sequence of the delta heavy chain (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-10
    Description: The DNA coding for the human immunoglobulin D(IgD) heavy chain (delta, delta) has been sequenced including the membrane and secreted termini. Human delta, like that of the mouse, has a separate exon for the carboxyl terminus of the secreted form. This feature of human and mouse IgD distinguishes it from all other immunoglobulins regardless of species or class. The human gene is different from that of the mouse; it has three, rather than two, constant region domains; and its lengthy hinge is encoded by two exons rather than one. Except for the third constant region, the human and mouse genes are only distantly related.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉White, M B -- Shen, A L -- Word, C J -- Tucker, P W -- Blattner, F R -- AI18016/AI/NIAID NIH HHS/ -- CA31013-04/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 10;228(4700):733-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3922054" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Humans ; Immunoglobulin D/*genetics ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin delta-Chains/*genetics ; Lymphocytes/metabolism ; Mice ; RNA, Messenger/genetics ; Species Specificity
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  • 26
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    Human GM-CSF: molecular cloning of the complementary DNA and purification of the natural and recombinant proteins (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-17
    Description: Clones of complementary DNA encoding the human lymphokine known as granulocyte-macrophage colony-stimulating factor (GM-CSF) were isolated by means of a mammalian cell (monkey COS cell) expression screening system. One of these clones was used to produce recombinant GM-CSF in mammalian cells. The recombinant hematopoietin was similar to the natural product that was purified to apparent homogeneity from medium conditioned by a human T-cell line. The human T-cell GM-CSF was found to be 60 percent homologous with the GM-CSF recently cloned from murine lung messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wong, G G -- Witek, J S -- Temple, P A -- Wilkens, K M -- Leary, A C -- Luxenberg, D P -- Jones, S S -- Brown, E L -- Kay, R M -- Orr, E C -- New York, N.Y. -- Science. 1985 May 17;228(4701):810-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3923623" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; *Cloning, Molecular ; Colony-Stimulating Factors/biosynthesis/*genetics/isolation & purification ; *Dna ; DNA, Recombinant ; *Granulocytes ; Haplorhini ; Humans ; *Macrophages ; RNA, Messenger/genetics ; T-Lymphocytes ; Transfection
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  • 27
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    Alignment of rat cardionatrin sequences with the preprocardionatrin sequence from complementary DNA (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-19
    Description: Mammalian atria contain peptides that promote the excretion of salt and water from the kidney. When rat atrial tissue is extracted under conditions known to inhibit proteolysis, four natriuretic peptides, cardionatrins I to IV, are consistently isolated. These peptides derive from a common precursor, preprocardionatrin, of 152 amino acids, whose sequence was determined by DNA sequencing of a complementary DNA clone. Amino acid sequencing located the start points of cardionatrins I, III, and IV in the overall sequence. Cardionatrin IV most closely resembles procardionatrin because it begins immediately after the signal sequence at residue 25. Cardionatrin III begins at residue 73, and cardionatrin I, sequenced previously, begins at residue 123. Compositional analysis indicated that each of these cardionatrins extends up to tyrosine at position 150 but lacks the terminal two arginine residues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flynn, T G -- Davies, P L -- Kennedy, B P -- de Bold, M L -- de Bold, A J -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):323-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3157217" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Atrial Function ; Atrial Natriuretic Factor ; Base Sequence ; Chromatography, High Pressure Liquid ; DNA/*genetics ; Electrophoresis, Polyacrylamide Gel ; Molecular Sequence Data ; Muscle Proteins/*genetics/isolation & purification ; *Peptide Fragments ; Protein Precursors/*genetics/isolation & purification ; Rats
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  • 28
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    Function and autoregulation of yeast copperthionein (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-10
    Description: The CUP1 gene of yeast encodes a small, metallothionein-like protein that binds to and is inducible by copper. A gene replacement experiment shows that this protein protects cells against copper poisoning but is dispensable for normal cellular growth and development throughout the yeast life cycle. The transcription of CUP1 is negatively autoregulated. This feedback mechanism, which is mediated through upstream control sequences, may play an important role in heavy metal homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamer, D H -- Thiele, D J -- Lemontt, J E -- New York, N.Y. -- Science. 1985 May 10;228(4700):685-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3887570" target="_blank"〉PubMed〈/a〉
    Keywords: Carrier Proteins ; Copper/metabolism ; Copper Sulfate ; Enzyme Induction ; Genes, Fungal ; Metallothionein/biosynthesis/genetics/*physiology ; Mutation ; Operon ; Plasmids ; RNA, Messenger/biosynthesis ; Saccharomyces cerevisiae/*enzymology/genetics
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    Mutation to herbicide resistance maps within the psbA gene of Anacystis nidulans R2 (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-13
    Description: A psbA gene encoding the target of photosystem II herbicide inhibition, the 32,000-dalton thylakoid membrane protein, has been cloned from a mutant of Anacystis nidulans R2, which is resistant to 3-(3,4-dichlorophenyl)-1,1-dimethylurea-(diuron). A cloned DNA fragment from within the coding region of this gene transforms wild-type cells to herbicide resistance, proving that mutation within psbA is responsible for that phenotype. The mutation consists of a single nucleotide change that replaces serine at position 264 of the wild-type protein with alanine in that of the diuron-resistant mutant.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Golden, S S -- Haselkorn, R -- New York, N.Y. -- Science. 1985 Sep 13;229(4718):1104-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3929379" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cyanobacteria/*genetics ; Diuron ; Drug Resistance ; Electrophoresis, Polyacrylamide Gel ; *Herbicides ; Membrane Proteins/genetics ; Molecular Weight ; *Mutation ; Phenotype
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    Three-dimensional structure of poliovirus at 2.9 A resolution (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-27
    Description: The three-dimensional structure of poliovirus has been determined at 2.9 A resolution by x-ray crystallographic methods. Each of the three major capsid proteins (VP1, VP2, and VP3) contains a "core" consisting of an eight-stranded antiparallel beta barrel with two flanking helices. The arrangement of beta strands and helices is structurally similar and topologically identical to the folding pattern of the capsid proteins of several icosahedral plant viruses. In each of the major capsid proteins, the "connecting loops" and NH2- and COOH-terminal extensions are structurally dissimilar. The packing of the subunit "cores" to form the virion shell is reminiscent of the packing in the T = 3 plant viruses, but is significantly different in detail. Differences in the orientations of the subunits cause dissimilar contacts at protein-protein interfaces, and are also responsible for two major surface features of the poliovirion: prominent peaks at the fivefold and threefold axes of the particle. The positions and interactions of the NH2- and COOH-terminal strands of the capsid proteins have important implications for virion assembly. Several of the "connecting loops" and COOH-terminal strands form prominent radial projections which are the antigenic sites of the virion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hogle, J M -- Chow, M -- Filman, D J -- AI-20566/AI/NIAID NIH HHS/ -- AI-22346/AI/NIAID NIH HHS/ -- NS-07078/NS/NINDS NIH HHS/ -- R01 AI020566/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Sep 27;229(4720):1358-65.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994218" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/immunology ; Capsid/physiology ; Chemical Phenomena ; Chemistry ; HeLa Cells/microbiology ; Mutation ; Poliovirus/physiology/*ultrastructure ; Protein Conformation ; Virus Replication ; X-Ray Diffraction
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    The generative grammar of the immune system (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jerne, N K -- New York, N.Y. -- Science. 1985 Sep 13;229(4718):1057-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4035345" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies/analysis ; Humans ; *Immune System ; Lymphocytes/physiology ; Mice
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  • 32
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    Partial primary structure of the alpha and beta chains of human tumor T-cell receptors (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-01-18
    Description: The T-cell receptor for antigen (Ti) was purified from the human tumor cell line HPB-ALL. Amino-terminal sequence analysis of an acid-cleaved peptide of the Ti alpha chain showed that it is highly homologous to a putative murine alpha chain recently described. Amino-terminal sequence analysis of the Ti beta chain revealed that it shares 50 percent homology with the Ti beta chain amino acid sequences from two other human T-cell tumors. Nucleotide sequence analysis of a complementary DNA clone encoding the Ti beta chain from the HPB-MLT cell line showed that this chain represents a second human constant region gene segment and suggested that it arises from direct joining of the variable and joining gene segments without any intervening D region sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, N -- Leiden, J -- Dialynas, D -- Fraser, J -- Clabby, M -- Kishimoto, T -- Strominger, J L -- Andrews, D -- Lane, W -- Woody, J -- 5 R01 AI15669/AI/NIAID NIH HHS/ -- AI10736/AI/NIAID NIH HHS/ -- Y001CP00502/CP/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jan 18;227(4684):311-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3871253" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Humans ; Immunoglobulin Constant Regions/genetics ; Leukemia, Lymphoid/immunology ; Lymphoma/immunology ; Mice ; Nucleic Acid Hybridization ; Receptors, Antigen, T-Cell/*genetics ; T-Lymphocytes/*immunology
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  • 33
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    Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-04
    Description: A 2.7 angstrom resolution x-ray diffraction analysis of a trypsin-modified form of the Escherichia coli elongation factor Tu reveals that the GDP-binding domain has a structure similar to that of other nucleotide-binding proteins. The GDP ligand is located at the COOH-terminal end of the beta sheet and is linked to the protein via a Mg2+ ion salt bridge. The location of the guanine ring is unusual; the purine ring is located on the outer edge of the domain, not deep within a hydrophobic pocket. The amino acids from Pro10 to Arg44 and from Gly59 to Glu190 have been assigned to the electron density with computer graphic techniques, and the resulting model is consistent with all known biochemical data. An analysis of the structure reveals that four regions of the amino acid sequence that are homologous with the family of ras oncogene proteins, termed p21, are located in the vicinity of the GDP-binding site, and most of the invariant amino acids shared by the proteins interact directly with the GDP ligand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jurnak, F -- GM 26895/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Oct 4;230(4721):32-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3898365" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/*analysis ; Binding Sites ; Chemistry, Physical ; Computers ; Escherichia coli ; Fourier Analysis ; Guanine Nucleotides/*analysis ; Guanosine Diphosphate/*analysis ; Magnesium/metabolism ; *Oncogenes ; Peptide Elongation Factor Tu ; Peptide Elongation Factors/*analysis ; Physicochemical Phenomena ; Protein Conformation ; Trypsin/metabolism ; X-Ray Diffraction
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    Human dioxin-inducible cytochrome P1-450: complementary DNA and amino acid sequence (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-05
    Description: Induction of cytochrome P1-450 has been linked to susceptibility to certain chemically induced cancers in mouse and man. Treatment of the human cell line MCF-7 with 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) results in high levels of aryl hydrocarbon (benzo[a]pyrene) hydroxylase (P1-450) activity. This cell line was used to isolate a human P1-450 full-length complementary DNA (cDNA) clone. The cDNA is 2566 nucleotides in length, encodes a polyadenylated messenger RNA (2.8 kilobases in length), and has a continuous reading frame producing a protein with 512 residues (molecular weight, 58,151). The human P1-450 cDNA and protein are 63 percent and 80 percent similar to mouse P1-450 cDNA and protein, respectively. Whereas the mouse TCDD-inducible P-450 gene subfamily has two members (P1-450 and P3-450), the human TCDD-inducible gene subfamily appears to have only one gene (P1-450).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jaiswal, A K -- Gonzalez, F J -- Nebert, D W -- New York, N.Y. -- Science. 1985 Apr 5;228(4695):80-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3838385" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carcinogens/pharmacology ; Cell Line ; Cricetinae ; Cytochrome P-450 Enzyme System/*genetics ; DNA/*genetics ; Dioxins/*pharmacology ; Enzyme Induction ; Humans ; Mice ; Nucleic Acid Hybridization ; Rabbits ; Tetrachlorodibenzodioxin/*pharmacology
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  • 35
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    Molecular cloning of a complementary DNA encoding human macrophage-specific colony-stimulating factor (CSF-1) (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-18
    Description: Complementary DNA (cDNA) clones encoding human macrophage-specific specific colony-stimulating factor (CSF-1) were isolated. One cDNA clone codes for a mature polypeptide of 224 amino acids and a putative leader of 32 amino acids. This cDNA, which was cloned in the Okayama-Berg expression vector, specifies the synthesis of biologically active CSF-1 in COS cells, as determined by a specific radioreceptor assay, macrophage bone marrow colony formation, and antibody neutralization. Most of the cDNA isolates contain part of an intron sequence that changes the reading frame, resulting in an abrupt termination of translation; these cDNA's were inactive in COS cells. The CSF-1 appears to be encoded by a single-copy gene, but its expression results in the synthesis of several messenger RNA species, ranging in size from about 1.5 to 4.5 kilobases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawasaki, E S -- Ladner, M B -- Wang, A M -- Van Arsdell, J -- Warren, M K -- Coyne, M Y -- Schweickart, V L -- Lee, M T -- Wilson, K J -- Boosman, A -- C32551/PHS HHS/ -- New York, N.Y. -- Science. 1985 Oct 18;230(4723):291-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996129" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; *Cloning, Molecular ; Colony-Stimulating Factors/*genetics ; DNA/*metabolism ; DNA Restriction Enzymes ; *Genes ; Humans ; Macrophages/*metabolism ; Pancreatic Neoplasms ; RNA, Messenger/genetics ; Transcription, Genetic
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    Amplification of a novel v-erbB-related gene in a human mammary carcinoma (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-06
    Description: The cellular gene encoding the receptor for epidermal growth factor (EGF) has considerable homology to the oncogene of avian erythroblastosis virus. In a human mammary carcinoma, a DNA sequence was identified that is related to v-erbB but amplified in a manner that appeared to distinguish it from the gene for the EGF receptor. Molecular cloning of this DNA segment and nucleotide sequence analysis revealed the presence of two putative exons in a DNA segment whose predicted amino acid sequence was closely related to, but different from, the corresponding sequence of the erbB/EGF receptor. Moreover, this DNA segment identified a 5-kilobase transcript distinct from the transcripts of the EGF receptor gene. Thus, a new member of the tyrosine kinase proto-oncogene family has been identified on the basis of its amplification in a human mammary carcinoma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, C R -- Kraus, M H -- Aaronson, S A -- New York, N.Y. -- Science. 1985 Sep 6;229(4717):974-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2992089" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Breast Neoplasms/*genetics ; Cell Line ; Cloning, Molecular ; DNA, Neoplasm/*genetics ; Female ; *Gene Amplification ; Gene Expression Regulation ; Humans ; *Oncogenes ; Protein Kinases/*genetics ; Protein-Tyrosine Kinases ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/*genetics
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    Human apolipoprotein B: structure of carboxyl-terminal domains, sites of gene expression, and chromosomal localization (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-04
    Description: Apolipoprotein (apo-) B is the ligand responsible for the receptor-mediated catabolism of low density lipoproteins, the principal cholesterol-transporting lipoproteins in plasma. The primary structure of the carboxyl-terminal 30 percent (1455 amino acids) of human apo-B (apo-B100) has been deduced from the nucleotide sequence of complementary DNA. Portions of the protein structure that may relate to its receptor binding function and lipid binding properties have been identified. The apo-B100 messenger RNA is about 19 kilobases in length. The apo-B100 gene is expressed primarily in liver and, to a lesser extent, in small intestine, but in no other tissues. The gene for apo-B100 is located in the p24 region (near the tip of the short arm) of chromosome 2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knott, T J -- Rall, S C Jr -- Innerarity, T L -- Jacobson, S F -- Urdea, M S -- Levy-Wilson, B -- Powell, L M -- Pease, R J -- Eddy, R -- Nakai, H -- GM 20454/GM/NIGMS NIH HHS/ -- HO 05196/HO/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 Oct 4;230(4721):37-43.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994225" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Apolipoprotein B-100 ; Apolipoproteins B/analysis/*genetics ; Apolipoproteins E/analysis ; Base Sequence ; *Chromosome Mapping ; Chromosomes, Human, 1-3 ; DNA/analysis ; DNA Restriction Enzymes/metabolism ; Female ; *Gene Expression Regulation ; Haplorhini ; Humans ; Intestine, Small/metabolism ; Lipid Metabolism ; Lipoproteins, LDL/metabolism ; Liver/metabolism ; Mice ; RNA, Messenger/analysis ; Receptors, LDL/metabolism ; Structure-Activity Relationship
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    How do proteins find mitochondria? (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G -- New York, N.Y. -- Science. 1985 Jun 28;228(4707):1517-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4012306" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Transport ; Enzyme Precursors/metabolism ; Mitochondria/*metabolism ; Mitochondria, Liver/enzymology ; Ornithine Carbamoyltransferase/metabolism ; Peptides/*metabolism ; Protein Sorting Signals ; Proteins/*metabolism
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    Enhanced immunogenicity of the pre-S region of hepatitis B surface antigen (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-07
    Description: The 55 codons upstream of the gene sequence encoding the hepatitis B surface antigen (HBsAg) are called the pre-S(2) region. It has been proposed that polypeptides of high molecular weight that contain the pre-S(2) region should be included in future hepatitis B virus (HBV) vaccines. The pre-S(2) region and the S gene product [25 kilodalton (kD)] together compose a polypeptide of high molecular weight (33 kD). As an initial attempt to determine the relevance of the 33-kD polypeptide to development of an HBV vaccine, the murine immune response to pre-S(2)-encoded determinants as compared to S-encoded determinants on the same polypeptide was examined. The results indicate (i) the pre-S(2) region is significantly more immunogenic than the S region of HBsAg, (ii) the 26 amino acid residues at the NH2-terminus of the 33-kD polypeptide represent a dominant antibody binding site on the pre-S(2) region, (iii) the immune response to the pre-S(2) region is regulated by H-2-linked genes distinct from those that regulate the response to the S region, and (iv) immunization of an S region nonresponder strain with HBV envelope particles that contain both the pre-S(2) and S regions can circumvent nonresponsiveness to the S region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milich, D R -- Thornton, G B -- Neurath, A R -- Kent, S B -- Michel, M L -- Tiollais, P -- Chisari, F V -- AI 00585/AI/NIAID NIH HHS/ -- AI 20001/AI/NIAID NIH HHS/ -- AI 20720/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1195-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2408336" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibody Formation ; Antibody Specificity ; Epitopes ; Genes, MHC Class II ; Genes, Viral ; Hepatitis B Antibodies/immunology ; Hepatitis B Surface Antigens/genetics/*immunology ; Mice ; Molecular Weight ; Protein Precursors/genetics/immunology ; Viral Hepatitis Vaccines/*immunology ; Viral Proteins/genetics/immunology
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  • 40
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    Sequence of the alpha subunit of photoreceptor G protein: homologies between transducin, ras, and elongation factors (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-05
    Description: A bovine retinal complementary DNA clone encoding the alpha subunit of transducin (T alpha) was isolated with the use of synthetic oligodeoxynucleotides as probes, and the complete nucleotide sequence of the insert was determined. THe predicted protein sequence of 354 amino acids includes the known sequences of four tryptic peptides and sequences adjacent to the residues that undergo adenosine diphosphate ribosylation by cholera toxin and pertussis toxin. On the basis of homologies to other proteins, such as the elongation factors of protein synthesis and the ras oncogene proteins, regions are identified that are predicted to be acylated and involved in guanine nucleotide binding and hydrolysis. Amino acid sequence similarity between T alpha and ras is confined to these regions of the molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lochrie, M A -- Hurley, J B -- Simon, M I -- New York, N.Y. -- Science. 1985 Apr 5;228(4695):96-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3856323" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Toxins/metabolism ; Base Sequence ; Cattle ; Cholera Toxin/metabolism ; Cloning, Molecular ; DNA/genetics ; Guanosine Triphosphate/metabolism ; Membrane Proteins/*genetics/metabolism ; *Oncogenes ; Peptide Elongation Factors/*genetics ; Pertussis Toxin ; Transducin ; Virulence Factors, Bordetella
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  • 41
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    Thermosensitivity of a DNA recognition site: activity of a truncated nutL antiterminator of coliphage lambda (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-05
    Description: Antitermination is an important transcriptional control. In bacteriophage lambda, the presence of the nut antiterminators between the promoters and terminators results in relatively unhindered transcription when the lambda N gene product and necessary host factors are supplied. This antitermination system has been rendered thermosensitivity by modification of the nut site. A fragment of lambda DNA [74 base pairs (bp) in length]that contained the 17-bp nutL core sequence, but lacked the 8-bp boxA sequence, was cloned in a pp-N-tL1-galK plasmid between the pp promoter and gene N. This fragment mediated antitermination of transcription at 30 degrees C, as measured by assaying galK gene expression in Escherichia coli. At 42 degrees C, however, antitermination at the lambda tL1 terminator was abolished. Antitermination at 42 degrees C was restored by replacing the 74-bp nutL fragment with longer sequences containing both nutL and boxA or by cloning a synthetic boxA sequence ahead of the 74-bp nutL fragment. Thus, efficient antitermination required both boxA and the 17-bp nutL core, with the latter becoming conditionally defective when the boxA sequence was deleted.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peltz, S W -- Brown, A L -- Hasan, N -- Podhajska, A J -- Szybalski, W -- 5-P30-CA-07175/CA/NCI NIH HHS/ -- 5-PO1-CA-23076/CA/NCI NIH HHS/ -- CA-09135/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Apr 5;228(4695):91-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3156406" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage lambda/*genetics ; DNA, Viral/*genetics/physiology ; Escherichia coli/genetics ; Hot Temperature ; Mutation ; Plasmids ; Promoter Regions, Genetic ; Terminator Regions, Genetic
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    Nucleotide sequence and expression of an AIDS-associated retrovirus (ARV-2) (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-02-01
    Description: The nucleotide sequence of molecular clones of DNA from a retrovirus, ARV-2, associated with the acquired immune deficiency syndrome (AIDS) was determined. Proviral DNA of ARV-2 (9737 base pairs) has long terminal repeat structures (636 base pairs) and long open reading frames encoding gag (506 codons), pol (1003 codons), and env (863 codons) genes. Two additional open reading frames were identified. Significant amino acid homology with several other retroviruses was noted in the predicted product of gag and pol, but ARV-2 was as closely related to murine and avian retroviruses as it was to human T-cell leukemia viruses (HTLV-I and HTLV-II). By means of an SV-40 vector in transfected simian cells, the cloned gag and env genes of ARV-2 were shown to express viral proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sanchez-Pescador, R -- Power, M D -- Barr, P J -- Steimer, K S -- Stempien, M M -- Brown-Shimer, S L -- Gee, W W -- Renard, A -- Randolph, A -- Levy, J A -- New York, N.Y. -- Science. 1985 Feb 1;227(4686):484-92.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2578227" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Codon ; DNA, Viral/*genetics ; Deltaretrovirus/genetics ; Gene Products, gag ; Genes, Viral ; Humans ; Nucleic Acid Conformation ; RNA-Directed DNA Polymerase/biosynthesis/genetics ; Repetitive Sequences, Nucleic Acid ; Retroviridae/*genetics ; Viral Envelope Proteins/biosynthesis/genetics ; Viral Proteins/biosynthesis/*genetics
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    A model for the tertiary structure of p21, the product of the ras oncogene (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-04
    Description: A model was developed for the structure of p21, the protein with a molecular weight of 21,000 that is produced by the ras genes. This model predicts that p21 consists of a central core of beta-sheet structure, connected by loops and alpha helices. Four of these loops comprise the guanine nucleotide binding site. The phosphoryl binding region is made up of amino acid sequences from 10 to 16 and from 57 to 63 of p21. The latter sequence may contain a site for magnesium binding. Amino acids defining guanine specificity are Asn-116 and Asp-119, and sequences around amino acid 145 may contribute to guanine binding. The model makes it possible to visualize how oncogenic mutations of p21 affect interaction with guanine nucleotides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCormick, F -- Clark, B F -- la Cour, T F -- Kjeldgaard, M -- Norskov-Lauritsen, L -- Nyborg, J -- New York, N.Y. -- Science. 1985 Oct 4;230(4721):78-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3898366" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/analysis ; Animals ; *Aspartate Carbamoyltransferase ; Base Sequence ; Binding Sites ; *Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) ; Cattle ; *Dihydroorotase ; Escherichia coli ; Guanine Nucleotides/metabolism ; Humans ; Macromolecular Substances ; Magnesium/metabolism ; Membrane Proteins/analysis ; Models, Chemical ; *Multienzyme Complexes ; Mutation ; *Oncogenes ; Peptide Elongation Factor Tu ; Peptide Elongation Factors/analysis ; Protein Conformation ; Proteins/*analysis ; RNA, Transfer, Amino Acyl/metabolism ; Saccharomyces cerevisiae ; Transducin
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    Molecular cloning of the complementary DNA for human tumor necrosis factor (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-12
    Description: Tumor necrosis factor (TNF) is a soluble protein that causes damage to tumor cells but has no effect on normal cells. Human TNF was purified to apparent homogeneity as a 17.3-kilodalton protein from HL-60 leukemia cells and showed cytotoxic and cytostatic activities against various human tumor cell lines. The amino acid sequence was determined for the amino terminal end of the purified protein, and oligodeoxyribonucleotide probes were synthesized on the basis of this sequence. Complementary DNA (cDNA) encoding human TNF was cloned from induced HL-60 messenger RNA and was confirmed by hybrid-selection assay, direct expression in COS-7 cells, and nucleotide sequence analysis. The human TNF cDNA is 1585 base pairs in length and encodes a protein of 233 amino acids. The mature protein begins at residue 77, leaving a long leader sequence of 76 amino acids. Expression of high levels of human TNF in Escherichia coli was accomplished under control of the bacteriophage lambda PL promoter and gene N ribosome binding site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, A M -- Creasey, A A -- Ladner, M B -- Lin, L S -- Strickler, J -- Van Arsdell, J N -- Yamamoto, R -- Mark, D F -- New York, N.Y. -- Science. 1985 Apr 12;228(4696):149-54.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3856324" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cells, Cultured ; *Cloning, Molecular ; DNA/*genetics ; DNA, Recombinant/metabolism ; Glycoproteins/*genetics/isolation & purification/pharmacology ; Humans ; Leukemia, Myeloid/metabolism ; Mice ; Mice, Nude ; Neoplasms, Experimental/drug therapy ; Nucleic Acid Hybridization ; RNA, Messenger/genetics ; Rabbits ; Rats ; Tumor Necrosis Factor-alpha ; Xenopus
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    Atrial natriuretic factor: a hormone produced by the heart (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-15
    Description: Systematic studies on the significance of the secretory-like morphological characteristic of cardiac atrial muscle cells of mammals led to the finding that these cells produce a polypeptide hormone. This hormone, described in 1981 as atrial natriuretic factor (ANF), is diuretic (natriuretic), hypotensive, and has an inhibitory effect on renin and aldosterone secretion. Thus, ANF probably intervenes in the short- and long-term control of water and electrolyte balance and of blood pressure. Phylogenetically, ANF appears early, suggesting different functions for this peptide in accordance with each species' environment. Knowledge of the properties of the hormone should provide insights into the pathophysiology of important clinical entities and lead to the development of new pharmaceutical products.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Bold, A J -- New York, N.Y. -- Science. 1985 Nov 15;230(4727):767-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2932797" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amphibians ; Animals ; Atrial Function ; Atrial Natriuretic Factor/genetics/*physiology ; Birds ; Cattle ; Cytoplasmic Granules/ultrastructure ; Fishes ; Heart/*physiology ; Humans ; Microscopy, Electron ; Myocardium/cytology/ultrastructure ; Rats ; Reptiles ; Rodentia ; Sinoatrial Node/cytology/physiology
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    Syrian hamster female protein: analysis of female protein primary structure and gene expression (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-07
    Description: The concentration in plasma of the female protein (FP) of the golden Syrian hamster is regulated by sex steroids and by mediators of the acute-phase response to tissue injury or inflammation. A complementary DNA (cDNA) clone corresponding to FP was isolated from a hamster liver cDNA library and used to determine the nucleotide sequence and derived amino acid sequence of native FP. The primary sequence of FP is 69 percent identical to human serum amyloid P component and 50 percent identical to human C-reactive protein. Evidence showed that sex-limited and acute-phase control of the FP gene is pretranslational. The FP protein is thus a useful model for investigating dual regulation of expression of a single gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dowton, S B -- Woods, D E -- Mantzouranis, E C -- Colten, H R -- AI20959/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1206-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2408337" target="_blank"〉PubMed〈/a〉
    Keywords: Acute-Phase Proteins ; Alpha-Globulins/*genetics ; Amino Acid Sequence ; Animals ; Base Sequence ; Blood Proteins/genetics ; *C-Reactive Protein ; Cricetinae/*physiology ; DNA/genetics ; Female ; Gene Expression Regulation ; Genes ; Liver/physiology ; Male ; Mesocricetus/*physiology ; RNA, Messenger/genetics
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  • 47
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    Redesigning trypsin: alteration of substrate specificity (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-04-19
    Description: A general method for modifying eukaryotic genes by site-specific mutagenesis and subsequent expression in mammalian cells was developed to study the relation between structure and function of the proteolytic enzyme trypsin. Glycine residues at positions 216 and 226 in the binding cavity of trypsin were replaced by alanine residues, resulting in three trypsin mutants. Computer graphic analysis suggested that these substitutions would differentially affect arginine and lysine substrate binding of the enzyme. Although the mutant enzymes were reduced in catalytic rate, they showed enhanced substrate specificity relative to the native enzyme. This increased specificity was achieved by the unexpected differential effects on the catalytic activity toward arginine and lysine substrates. Mutants containing alanine at position 226 exhibited an altered conformation that may be converted to a trypsin-like structure upon binding of a substrate analog.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Craik, C S -- Largman, C -- Fletcher, T -- Roczniak, S -- Barr, P J -- Fletterick, R -- Rutter, W J -- AM26081/AM/NIADDK NIH HHS/ -- GM07216/GM/NIGMS NIH HHS/ -- GM28520/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):291-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3838593" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; DNA/genetics ; Electrophoresis ; Mutation ; Rats ; Substrate Specificity ; Trypsin/biosynthesis/*genetics/metabolism ; Trypsinogen/metabolism
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    Model structure for the inflammatory protein C5a (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-05-31
    Description: The complement cleavage product C5a is a potent stimulant of inflammatory processes; thus, inhibition of C5a activity is of therapeutic interest. The three-dimensional structure of the major portion of C5a was modeled from the homologous C3a crystal structure by comparative modeling techniques. The model shows that core residues of C5a are completely conserved, while external residues differ from C3a. Even though the amino-terminal 12 residues of C3a are disordered in the crystal, this sequence in C5a may form an amphipathic helix. The distribution of species sequence differences in the complete C5a structure suggests a possible receptor binding site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greer, J -- New York, N.Y. -- Science. 1985 May 31;228(4703):1055-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3992245" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Complement C5/metabolism ; Complement C5a ; Crystallography ; Humans ; Hydrogen Bonding ; Models, Molecular ; Protein Conformation ; Receptors, Complement/metabolism ; Thermodynamics
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  • 49
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    Molecular cloning of complementary DNA for the alpha subunit of the G protein that stimulates adenylate cyclase (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-20
    Description: A complementary DNA clone encoding the alpha subunit of the adenylate cyclase stimulatory G protein (Gs) was isolated and identified. A bovine brain complementary DNA library was screened with an oligonucleotide probe derived from amino acid sequence common to known G proteins. The only clone that was obtained with this probe has a complementary DNA insert of approximately 1670 base pairs. An antibody to a peptide synthesized according to deduced amino acid sequence reacts specifically with the alpha subunit of Gs. In addition, RNA that hybridizes with probes made from the clone is detected in wild-type S49 cells; however, cyc- S49 cells, which are deficient in Gs alpha activity, are devoid of this messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harris, B A -- Robishaw, J D -- Mumby, S M -- Gilman, A G -- GM09731/GM/NIGMS NIH HHS/ -- GM34497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Sep 20;229(4719):1274-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3839937" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/*metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Cattle ; Cerebral Cortex ; *Cloning, Molecular ; DNA/*analysis ; Enzyme Activation ; Nerve Tissue Proteins/*genetics ; Nucleic Acid Hybridization ; Protein Biosynthesis ; Retina
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    Amino acid replacements that compensate for a large polypeptide deletion in an enzyme (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-07-26
    Description: Deletion of more than 400 amino acids from the carboxyl terminus of an enzyme causes a severe reduction in catalytic activity. Selected point mutations within the residual protein partially reverse the effects of the missing segment. The selection can yield mutants with activities at least ten times as high as those of the starting polypeptides. One well-characterized mutation, a single amino acid replacement in the residual polypeptide, increases the catalytic activity of the polypeptide by a factor of 5. The results suggest substantial potential for design of protein elements to compensate for missing polypeptide sequences. They also may reflect that progenitors of large aminoacyl-tRNA (transfer RNA) synthetases--one of which was used in these studies--were themselves much smaller.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ho, C -- Jasin, M -- Schimmel, P -- New York, N.Y. -- Science. 1985 Jul 26;229(4711):389-93.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3892692" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine-tRNA Ligase/genetics ; *Amino Acid Sequence ; DNA, Recombinant ; Enzymes/*genetics/metabolism ; Escherichia coli/enzymology/genetics ; Genetic Engineering ; Genetic Vectors ; Mutation ; Nucleic Acid Heteroduplexes/genetics ; Plasmids
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    Mutation in LDL receptor: Alu-Alu recombination deletes exons encoding transmembrane and cytoplasmic domains (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-01-11
    Description: The molecular size of the plasma LDL (low density lipoprotein) receptor synthesized by cultured fibroblasts from a patient with the internalization-defective form of familial hypercholesterolemia (FH 274) was smaller by 10,000 daltons than the size of the normal LDL receptor. The segment of the gene encoding the truncated portion of the FH 274 receptor was cloned into bacteriophage lambda. Comparison of the nucleotide sequences of the normal and FH 274 genes revealed a 5-kilobase deletion, which eliminated the exons encoding the membrane-spanning region and the carboxyl terminal cytoplasmic domain of the receptor. The deletion appeared to be caused by a novel intrastrand recombination between two repetitive sequences of the Alu family that were oriented in opposite directions. The truncated receptors lack membrane-spanning regions and cytoplasmic domains; they are largely secreted into the culture medium, but a small fraction remains adherent to the cell surface. The surface-adherent receptors bind LDL, but they are unable to cluster in coated pits, thus explaining the internalization-defective phenotype.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4449727/" 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/PMC4449727/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lehrman, M A -- Schneider, W J -- Sudhof, T C -- Brown, M S -- Goldstein, J L -- Russell, D W -- HL 01287/HL/NHLBI NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- HL 31346/HL/NHLBI NIH HHS/ -- P01 HL020948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jan 11;227(4683):140-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3155573" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage lambda ; Base Sequence ; Cell Membrane ; Cloning, Molecular ; Coated Pits, Cell-Membrane/metabolism ; Cytoplasm ; Fibroblasts ; Genes ; Humans ; Hyperlipoproteinemia Type II/*genetics ; Male ; Molecular Weight ; Mutation ; Receptors, LDL/*genetics ; Recombination, Genetic ; *Repetitive Sequences, Nucleic Acid
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    Structure of the human interleukin-2 receptor gene (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-11-08
    Description: The gene encoding the human interleukin-2 (IL-2) receptor consists of 8 exons spanning more than 25 kilobases on chromosome 10. Exons 2 and 4 were derived from a gene duplication event and unexpectedly also are homologous to the recognition domain of human complement factor B. Alternative messenger RNA (mRNA) splicing may delete exon 4 sequences, resulting in a mRNA that does not encode a functional IL-2 receptor. Leukemic T cells infected with HTLV-I and normal activated T cells express IL-2 receptors with identical deduced protein sequences. Receptor gene transcription is initiated at two principal sites in normal activated T cells. Adult T cell leukemia cells infected with HTLV-I show activity at both of these sites, but also at a third transcription initiation site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leonard, W J -- Depper, J M -- Kanehisa, M -- Kronke, M -- Peffer, N J -- Svetlik, P B -- Sullivan, M -- Greene, W C -- New York, N.Y. -- Science. 1985 Nov 8;230(4726):633-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996141" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Complement Factor B/genetics ; DNA/genetics/isolation & purification ; DNA, Recombinant/isolation & purification ; Deltaretrovirus ; *Genes, MHC Class II ; Humans ; Peptide Chain Initiation, Translational ; RNA, Messenger/genetics ; Receptors, Immunologic/biosynthesis/*genetics ; Receptors, Interleukin-2 ; Repetitive Sequences, Nucleic Acid ; Retroviridae Infections/genetics ; T-Lymphocytes/microbiology ; Transcription, Genetic
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    Effects of genomic position on the expression of transduced copies of the white gene of Drosophila (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-08-09
    Description: The white gene of Drosophila is expressed normally when introduced at many different sites in the genome by P-element-mediated DNA transformation, but is expressed abnormally when inserted at two particular genomic positions. It is now demonstrated that the mutant expression in these two cases is caused by the surrounding chromosomal region into which the white gene has been inserted. The white gene could be moved from these two positions, where it confers a mutant phenotype, to other positions in the genome where it confers a wild-type phenotype. However, flies in which white has been moved to one new location have an unusual mosaic phenotype.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levis, R -- Hazelrigg, T -- Rubin, G M -- New York, N.Y. -- Science. 1985 Aug 9;229(4713):558-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2992080" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; DNA Transposable Elements ; Drosophila/*genetics ; *Gene Expression Regulation ; Mosaicism ; Mutation ; Phenotype ; Pigmentation ; *Transformation, Genetic
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    Peptide neurotoxins from fish-hunting cone snails (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-12-20
    Description: To paralyze their more agile prey, the venomous fish-hunting cone snails (Conus) have developed a potent biochemical strategy. They produce several classes of toxic peptides (conotoxins) that attack a series of successive physiological targets in the neuromuscular system of the fish. The peptides include presynaptic omega-conotoxins that prevent the voltage-activated entry of calcium into the nerve terminal and release of acetylcholine, postsynaptic alpha-conotoxins that inhibit the acetylcholine receptor, and muscle sodium channel inhibitors, the mu-conotoxins, which directly abolish muscle action potentials. These distinct peptide toxins share several common features: they are relatively small (13 to 29 amino acids), are highly cross-linked by disulfide bonds, and strongly basic. The fact that they inhibit sequential steps in neuromuscular transmission suggests that their action is synergistic rather than additive. Five new omega-conotoxins that block presynaptic calcium channels are described. They vary in their activity against different vertebrate classes, and also in their actions against different synapses from the same animal. There are susceptible forms of the target molecule in peripheral synapses of fish and amphibians, but those of mice are resistant. However, the mammalian central nervous system is clearly affected, and these toxins are thus of potential significance for investigating the presynaptic calcium channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olivera, B M -- Gray, W R -- Zeikus, R -- McIntosh, J M -- Varga, J -- Rivier, J -- de Santos, V -- Cruz, L J -- GM 22737/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Dec 20;230(4732):1338-43.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4071055" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Feeding Behavior ; Fishes ; Mice ; Mollusk Venoms/*isolation & purification/toxicity ; Neurotoxins/*isolation & purification ; Peptide Fragments/analysis ; Snails/*physiology ; Species Specificity ; Structure-Activity Relationship
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    Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-19
    Description: The milk protein beta-lactoglobulin has been extensively studied but its function has not been identified. A clue regarding the function of a protein can be obtained by discovering a genetic relationship with a protein of known function through comparisons of amino acid sequence. Such comparisons revealed that beta-lactoglobulin is similar to human serum retinol-binding protein and to another human protein of unknown function known as complex-forming glycoprotein heterogeneous in charge (protein HC). beta-Lactoglobulins from several species have been found to bind retinol, while the absorption and fluorescence properties reported for the unidentified heterogeneous prosthetic group of protein HC are retinoid-like. The role of serum retinol-binding protein in vitamin A transport in the circulation suggests that the other two homologous proteins may function in the binding and transport of retinoids; beta-lactoglobulin may facilitate the absorption of vitamin A from milk and protein HC may mediate the excretion of retinol-derived metabolites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pervaiz, S -- Brew, K -- GM 21363/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):335-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2580349" target="_blank"〉PubMed〈/a〉
    Keywords: Alpha-Globulins/*genetics ; Amino Acid Sequence ; Animals ; Cattle ; Dolphins ; Humans ; Lactoglobulins/*genetics/metabolism ; Lagomorpha ; Mammals ; Milk/metabolism ; Primates ; Protein Conformation ; Proteinuria/metabolism ; Retinol-Binding Proteins/*genetics/metabolism ; Rodentia ; Swine ; Vitamin A/metabolism
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    The 23-million-dollar quest pays off (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1985 Oct 11;230(4722):161.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4035360" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Angiogenesis Inducing Agents/genetics/*isolation & purification ; Animals ; Growth Substances/*isolation & purification ; Humans ; Neoplasm Proteins/genetics/*isolation & purification ; Neoplasms/blood supply/metabolism ; Rats ; *Ribonuclease, Pancreatic
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    A glycophospholipid tail at the carboxyl terminus of the Thy-1 glycoprotein of neurons and thymocytes (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-29
    Description: Cell surface molecules of eukaryotic cells have been considered to be integrated into the membrane bilayer by a transmembrane protein sequence. The Thy-1 antigen of rodent thymocytes and brain was the first eukaryotic membrane molecule for which biochemical data clearly suggested membrane integration via a nonprotein tail. Direct evidence is now presented showing that a glycophospholipid structure is attached to the carboxyl-terminal cysteine residue and that 31 carboxyl-terminal amino acids predicted from the Thy-1 complementary DNA sequence are not present in the mature glycoprotein. These experimental results raise questions concerning signaling across a cell membrane since antibodies to Thy-1 can stimulate T lymphocytes to release lymphokines and undergo cell division.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tse, A G -- Barclay, A N -- Watts, A -- Williams, A F -- New York, N.Y. -- Science. 1985 Nov 29;230(4729):1003-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2865810" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antigens, Surface/isolation & purification ; Antigens, Thy-1 ; Brain/*metabolism ; Ethanolamines/metabolism ; Galactosamine/metabolism ; Glucosamine/metabolism ; Glycolipids/*metabolism ; Membrane Proteins/*metabolism ; Nerve Tissue Proteins/*metabolism ; Rats ; Stearic Acids/metabolism ; T-Lymphocytes/*metabolism
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    Antigenic variation and resistance to neutralization in poliovirus type 1 (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-13
    Description: Mutations have been identified in variants of poliovirus, type 1 (Mahoney) on the basis of their resistance to neutralization by individual monoclonal antibodies. The phenotypes of these variants were defined in terms of antibody binding; the pattern of epitopes expressed or able to be exploited for neutralization were complex. Single amino acid changes can have distant (in terms of linear sequence) and generalized effects on the antigenic structure of poliovirus and similarly constituted virions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diamond, D C -- Jameson, B A -- Bonin, J -- Kohara, M -- Abe, S -- Itoh, H -- Komatsu, T -- Arita, M -- Kuge, S -- Nomoto, A -- AI-15122/AI/NIAID NIH HHS/ -- CA-28146/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Sep 13;229(4718):1090-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2412292" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Antibodies, Monoclonal ; Epitopes/*analysis ; Immunity, Innate ; Mutation ; Phenotype ; Poliovirus/genetics/*immunology ; Virion/immunology
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    The x gene is essential for HTLV replication (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-07-05
    Description: The human T-cell leukemia viruses (HTLV) are associated with T-cell malignancies in man and will transform normal human T cells in vitro. The mechanism of malignant transformation by HTLV is unknown but appears to be distinct from that of other classes of retroviruses, which induce malignant transformation through viral or cellular oncogenes. Recently a new gene, termed x, was identified in HTLV. This gene has been hypothesized to be the transforming gene of HTLV because of its conservation within the HTLV class of retroviruses. By in vitro mutagenesis of the HTLV-II x gene, it is now demonstrated that the presence of a functional x gene product is necessary for efficient HTLV transcription. Therefore, these studies provide direct evidence for an important function of the x gene in HTLV replication. The functional analogies between the x gene and transcriptional regulatory genes of some DNA viruses suggest that these viruses share similar mechanisms for cellular transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, I S -- Slamon, D J -- Rosenblatt, J D -- Shah, N P -- Quan, S G -- Wachsman, W -- CA 09297/CA/NCI NIH HHS/ -- CA 32737/CA/NCI NIH HHS/ -- CA 38597/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Jul 5;229(4708):54-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990037" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Deltaretrovirus/*genetics/growth & development ; Genes, Viral ; Humans ; Mutation ; RNA, Viral/*biosynthesis ; Transcription, Genetic ; *Virus Replication
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    Prooxidant states and tumor promotion (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-01-25
    Description: There is convincing evidence that cellular prooxidant states--that is, increased concentrations of active oxygen and organic peroxides and radicals--can promote initiated cells to neoplastic growth. Prooxidant states can be caused by different classes of agents, including hyperbaric oxygen, radiation, xenobiotic metabolites and Fenton-type reagents, modulators of the cytochrome P-450 electron-transport chain, peroxisome proliferators, inhibitors of the antioxidant defense, and membrane-active agents. Many of these agents are promoters or complete carcinogens. They cause chromosomal damage by indirect action, but the role of this damage in carcinogenesis remains unclear. Prooxidant states can be prevented or suppressed by the enzymes of the cellular antioxidant defense and low molecular weight scavenger molecules, and many antioxidants are antipromoters and anticarcinogens. Finally, prooxidant states may modulate the expression of a family of prooxidant genes, which are related to cell growth and differentiation, by inducing alterations in DNA structure or by epigenetic mechanisms, for example, by polyadenosine diphosphate-ribosylation of chromosomal proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cerutti, P A -- New York, N.Y. -- Science. 1985 Jan 25;227(4685):375-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2981433" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antioxidants/pharmacology ; *Carcinogens/metabolism/pharmacology ; Cations/metabolism ; Cell Differentiation ; Cell Division ; Cell Line ; Cell Membrane/physiology ; *Cell Transformation, Neoplastic ; Chromosome Aberrations ; Chromosomes/drug effects ; Cytochrome P-450 Enzyme System/metabolism ; DNA/metabolism ; Electron Transport ; Gene Expression Regulation ; Humans ; Hydrogen Peroxide/metabolism ; Hydroxides/metabolism ; Hydroxyl Radical ; Lipid Peroxides/metabolism ; Microbodies/metabolism ; Mutation ; Neoplasms/*chemically induced ; Oxidation-Reduction ; Oxygen/*metabolism/physiology ; Poly Adenosine Diphosphate Ribose/metabolism ; Singlet Oxygen ; Sulfhydryl Compounds/physiology ; Superoxides/metabolism ; Ultraviolet Rays
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    Cell interactions in myxobacterial growth and development (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-04
    Description: During their complex life cycle, myxobacteria manifest a number of cell interactions. These include contact-mediated interactions as well as those mediated by soluble extracellular signals. Some of these interactions are well-defined; in addition, the tools for molecular and genetic analysis of these interactions in Myxococcus xanthus are now available.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dworkin, M -- Kaiser, D -- GM19957/GM/NIGMS NIH HHS/ -- GM23441/GM/NIGMS NIH HHS/ -- GM34317/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Oct 4;230(4721):18-24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3929384" target="_blank"〉PubMed〈/a〉
    Keywords: Microscopy, Electron, Scanning ; Movement ; Mutation ; Myxococcales/genetics/*growth & development ; Spores, Bacterial ; Transduction, Genetic
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    Cyanobacterial light-harvesting complex subunits encoded in two red light-induced transcripts (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-01
    Description: The major light-harvesting complex in cyanobacteria and red algae, the phycobilisome, is composed of chromophoric and nonchromophoric polypeptides. Two linked genes encoding major chromophoric components, the polypeptide subunits of phycocyanin, were isolated from the cyanobacterium Fremyella diplosiphon. Transcripts from this phycocyanin subunit gene cluster were present as major species in the cyanobacterium grown in red light, but not in cultures maintained in green light. The genes for the subunits of the red light-induced phycocyanin were transcribed together (beta-phycocyanin followed by alpha-phycocyanin) on two messenger RNA species; one contained 1600 bases while the other had 3800 bases. The latter, which encompassed the smaller transcript, contained additional sequences extending from the 3' end of the coding region of the alpha-phycocyanin gene. It may encode other light-induced components of the phycobilisome. Since phycocyanin, which effectively absorbs red light, becomes a dominant constituent of the phycobilisome in red light, these different levels may reflect an important adaptive mechanism of these organisms to their environment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Conley, P B -- Lemaux, P G -- Grossman, A R -- GM 33436-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 1;230(4725):550-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3931221" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cyanobacteria/*genetics ; Light ; Nucleic Acid Hybridization ; Phycobilisomes ; Phycocyanin/genetics ; RNA, Messenger/metabolism ; *Transcription, Genetic
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    Evolution in inbred strains of mice appears rapid (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-07
    Description: Genetic variation at 97 loci in ten commonly used inbred strains of mice is greatly in excess of that expected under current assumptions. Evidence against all of the readily apparent explanations is presented and the possibility of early selection for heterozygosity or of conversion is suggested. The common ancestor of these strains is estimated to have occurred about 150 years ago.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fitch, W M -- Atchley, W R -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1169-75.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4001935" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Heterozygote ; Mice ; Mice, Inbred Strains/*genetics ; Mutation ; Species Specificity ; Time Factors
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    Measuring gene expression with light (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-03-15
    Description: Light is produced by recombinant Escherichia coli that contain lux genes cloned from the marine bacterium Vibrio fischeri. The bioluminescence phenotype requires genes for regulatory and biochemical functions, the latter encoded by five lux genes contained in a single operon. These lux genes were disconnected from their native promoter and inserted into the transposon mini-Mu. The resulting transposon, mini-Mulux, could induce mutations by insertional inactivation of a target gene, and the lux DNA was oriented to align target gene transcription with that of the lux genes. Genes in Escherichia coli and Vibrio parahaemolyticus were mutagenized, and mutants containing transposon-generated lux gene fusions produced light as a function of target gene transcription. Light production offers a simple, sensitive, in vivo indicator of gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Engebrecht, J -- Simon, M -- Silverman, M -- New York, N.Y. -- Science. 1985 Mar 15;227(4692):1345-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2983423" target="_blank"〉PubMed〈/a〉
    Keywords: DNA Transposable Elements ; DNA, Recombinant/*metabolism ; Escherichia coli/genetics ; *Gene Expression Regulation ; Luciferases/genetics ; Luminescence ; Luminescent Proteins/*genetics ; Mutation ; Phenotype ; Protein Biosynthesis ; Vibrio/genetics ; Vibrio parahaemolyticus/metabolism
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    Brain-derived acidic fibroblast growth factor: complete amino acid sequence and homologies (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-20
    Description: Bovine brain-derived acidic fibroblast growth factor (aFGF) is a protein mitogen originally identified in partially purified preparations of whole brain. The protein was purified to homogeneity and shown to be a potent vascular endothelial cell mitogen in culture and angiogenic substance in vivo. The homology of aFGF to human interleukin-1 beta was inferred from partial sequence data. The complete amino acid sequence of aFGF has now been determined and observed to be similar to both basic FGF and interleukin-1's. A neuropeptide-like sequence, flanked by basic dipeptides, was observed within the aFGF sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gimenez-Gallego, G -- Rodkey, J -- Bennett, C -- Rios-Candelore, M -- DiSalvo, J -- Thomas, K -- New York, N.Y. -- Science. 1985 Dec 20;230(4732):1385-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4071057" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Brain Chemistry ; Cattle ; Fibroblast Growth Factors/*isolation & purification ; Hormones ; Humans ; Hydrogen-Ion Concentration ; Nerve Tissue Proteins ; Sequence Homology, Nucleic Acid ; Species Specificity
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    Sequence and structure of a human glucose transporter (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-06
    Description: The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone. Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical. The protein lacks a cleavable amino-terminal signal sequence. Analysis of the primary structure suggests the presence of 12 membrane-spanning domains. Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves. The amino terminus, carboxyl terminus, and a highly hydrophilic domain in the center of the protein are all predicted to lie on the cytoplasmic face. Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mueckler, M -- Caruso, C -- Baldwin, S A -- Panico, M -- Blench, I -- Morris, H R -- Allard, W J -- Lienhard, G E -- Lodish, H F -- GM22996/GM/NIGMS NIH HHS/ -- HL32262/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 Sep 6;229(4717):941-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3839598" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Carrier Proteins/genetics/metabolism ; Cell Membrane/ultrastructure ; Cloning, Molecular ; DNA/genetics ; Erythrocytes/metabolism ; Glucose/*metabolism ; Humans ; Liver Neoplasms, Experimental/metabolism ; *Membrane Proteins/genetics/metabolism ; Molecular Weight ; Monosaccharide Transport Proteins ; Protein Conformation ; RNA, Messenger/genetics ; Tissue Distribution
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    The structure of arthropod hemocyanins (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-08-09
    Description: Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. Comparison of the amino acid sequence data for seven different subunits of arthropod hemocyanins from crustaceans and chelicerates shows many highly conserved residues and extensive regions of near identity. This correspondence can be matched closely with the three domain structure established by x-ray crystallography for spiny lobster hemocyanin. The degree of identity is particularly striking in the second domain of the subunit that contains the six histidines which ligate the two oxygen-binding copper atoms. The polypeptide architecture of spiny lobster hemocyanin appears to be the same in all arthropods. This structure must therefore be at least as old as the estimated time of divergence of crustaceans and chelicerates, about 540 to 600 million years ago.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Linzen, B -- Soeter, N M -- Riggs, A F -- Schneider, H J -- Schartau, W -- Moore, M D -- Yokota, E -- Behrens, P Q -- Nakashima, H -- Takagi, T -- GM 21314/GM/NIGMS NIH HHS/ -- GM 28410/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 9;229(4713):519-24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4023698" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arachnida/genetics ; *Arthropods/genetics ; Binding Sites ; Biological Evolution ; Chemical Phenomena ; Chemistry ; Copper ; Crustacea/genetics ; *Hemocyanin/genetics ; Models, Molecular ; Protein Conformation ; Species Specificity
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    Construction and recovery of viable retroviral genomes carrying a bacterial suppressor transfer RNA gene (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-04-19
    Description: The integration of retroviral genomes into cellular DNA can induce mutations by altering the expression of nearby cellular genes and can serve to identify the gene affected. The construction of a retrovirus that stably carries a suppressor transfer RNA gene from Escherichia coli has allowed facile recovery of the viral genome in vectors marked with amber mutations. This virus can be used for rapid isolation of cellular sequences at the site of proviral insertion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lobel, L I -- Patel, M -- King, W -- Nguyen-Huu, M C -- Goff, S P -- 2 P30 CA 23767/CA/NCI NIH HHS/ -- R01 CA 37176/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):329-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2984770" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA Transposable Elements ; DNA, Recombinant/metabolism ; DNA, Viral/genetics ; Escherichia coli/genetics ; *Genes, Bacterial ; *Genes, Viral ; Moloney murine leukemia virus/genetics ; Mutation ; Nucleic Acid Hybridization ; RNA, Transfer/*genetics ; Retroviridae/*genetics ; *Suppression, Genetic
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    Amino terminal myristylation of the protein kinase p60src, a retroviral transforming protein (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-01-25
    Description: The transforming protein of Rous sarcoma virus, p60src, was shown to be acylated at its amino terminus with the long-chain fatty acid myristic acid by isolation of a tryptic peptide with the following structure: myristylglycylserylseryllysine. The occurrence of this unusual posttranslational modification in the cyclic adenosine monophosphate-dependent protein kinase and in several transforming protein kinases of mammalian retroviruses suggests that myristylation of the amino terminal glycyl residue may be critical for the function of certain proteins related to cell transformation and growth control.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schultz, A M -- Henderson, L E -- Oroszlan, S -- Garber, E A -- Hanafusa, H -- CA-14935/CA/NCI NIH HHS/ -- N01-CO-23909/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jan 25;227(4685):427-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3917576" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Amino Acid Sequence ; Cell Transformation, Neoplastic ; Cell Transformation, Viral ; Myristic Acid ; Myristic Acids/*analysis/metabolism ; Oncogene Protein pp60(v-src) ; Protein Kinases/*analysis/metabolism ; Protein Processing, Post-Translational ; Viral Proteins/*analysis/metabolism
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    A hydrophobic transmembrane segment at the carboxyl terminus of thy-1 (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-02-08
    Description: The mode of integration of the glycoprotein thy-1 within the cell membrane has been controversial due to an apparent lack of a transmembrane hydrophobic segment. Rat and mouse complementary DNA and genomic clones encoding the thy-1 molecule have been isolated and sequenced. These studies have enabled us to determine the intron-exon organization of the thy-1 gene. Furthermore, they have revealed the existence of a sequence which would encode an extra segment (31 amino acids) at the carboxyl terminus of the thy-1 molecule. These extra amino acids include a 20-amino acid hydrophobic segment which may be responsible for integration of thy-1 within the plasma membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seki, T -- Chang, H C -- Moriuchi, T -- Denome, R -- Ploegh, H -- Silver, J -- CA38404/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Feb 8;227(4687):649-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2857501" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Surface/*genetics ; Antigens, Thy-1 ; Base Sequence ; Cloning, Molecular ; DNA, Recombinant/metabolism ; Membrane Proteins/*genetics/metabolism ; Mice ; Molecular Weight ; Nucleic Acid Hybridization ; Rats
    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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  • 71
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    Characterization of gp41 as the transmembrane protein coded by the HTLV-III/LAV envelope gene (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-27
    Description: Radiolabeled amino acid sequencing was used to characterize gp41, an antigen of HTLV-III/LAV, the virus believed to be the etiological agent of the acquired immune deficiency syndrome. This antigen is the one most commonly detected in immunoblot assays by sera of patients with AIDS or AIDS-related complex (ARC) and other individuals infected with HTLV-III/LAV. A mouse monoclonal antibody that was reactive with gp41 precipitated a 160-kilodalton protein (gp160) in addition to gp41, but did not precipitate a 120-kilodalton protein (gp120) from extracts of metabolically labeled cells producing HTLV-III. Extracts of infected cells that had been labeled with tritiated leucine or isoleucine were immunoprecipitated with the monoclonal antibody. The immunoprecipitates were fractionated by polyacrylamide gel electrophoresis and the p41 was eluted from the gel bands and subjected to amino-terminal radiolabeled amino acid sequencing by the semiautomated Edman degradation. Leucine residues occurred in cycles 7, 9, 12, 26, 33, and 34 among 40 cycles and isoleucine occurred in cycle 4 among 24 cycles analyzed. Comparison of the data with the deduced amino acid sequence of the env gene product of HTLV-III precisely placed gp41 in the COOH-terminal region of the env gene product. Gp160 is thus the primary env gene product and it is processed into gp120 and gp41.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Veronese, F D -- DeVico, A L -- Copeland, T D -- Oroszlan, S -- Gallo, R C -- Sarngadharan, M G -- New York, N.Y. -- Science. 1985 Sep 27;229(4720):1402-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994223" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/microbiology ; Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Antigens, Viral/genetics/immunology ; Deltaretrovirus/*genetics ; *Genes, Viral ; Humans ; Mice ; Mice, Inbred BALB C ; Viral Envelope Proteins/*genetics
    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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  • 72
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    The action of oncogenes in the cytoplasm and nucleus (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-15
    Description: As many as 40 distinct oncogenes of viral and cellular origin have been identified to date. Many of these genes can be grouped into functional classes on the basis of their effects on cellular phenotype. These groupings suggest a small number of mechanisms of action of the oncogene-encoded proteins. Some data suggest that, in the cytoplasm, these proteins may regulate levels of critical second messenger molecules; in the nucleus, these proteins may modulate the activity of the cell's transcriptional machinery. Many of the gene products can also be related to a signaling pathway that determines the cell's response to growth-stimulating factors. Because some of these genes are expressed in nongrowing, differentiated cells, the encoded proteins may in certain tissues mediate functions that are unrelated to cellular growth control.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weinberg, R A -- CA39826/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 15;230(4727):770-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2997917" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Birds ; Cell Nucleus/metabolism ; Cell Transformation, Neoplastic/metabolism ; Chickens ; Cytoplasm/metabolism ; DNA Tumor Viruses/genetics ; Deltaretrovirus/genetics ; Drosophila ; Epidermal Growth Factor/physiology ; Growth Substances/physiology ; Guanosine Triphosphate/metabolism ; Humans ; Mutation ; Neoplasms/genetics ; *Oncogenes ; Platelet-Derived Growth Factor/physiology ; Polyomavirus/genetics ; Proto-Oncogenes ; Rats ; Repetitive Sequences, Nucleic Acid ; Retroviridae/genetics ; Simian virus 40/genetics ; Transcription, Genetic
    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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