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  • Articles  (62)
  • Molecular Weight  (39)
  • Mutation  (25)
  • American Association for the Advancement of Science (AAAS)  (62)
  • American Association for the Advancement of Science
  • American Chemical Society
  • American Institute of Physics
  • American Institute of Physics (AIP)
  • American Physical Society
  • Periodicals Archive Online (PAO)
  • 1985-1989  (62)
  • 1955-1959
  • 1940-1944
  • 1935-1939
  • 1993
  • 1985  (62)
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  • Articles  (62)
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  • American Association for the Advancement of Science (AAAS)  (62)
  • American Association for the Advancement of Science
  • American Chemical Society
  • American Institute of Physics
  • American Institute of Physics (AIP)
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  • 1985-1989  (62)
  • 1955-1959
  • 1940-1944
  • 1935-1939
  • 1990-1994  (83)
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  • 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
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  • 2
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    Major glycoprotein antigens that induce antibodies in AIDS patients are encoded by HTLV-III (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-31
    Description: Antibodies from the serum of patients with the acquired immune deficiency syndrome (AIDS) or with the AIDS-related complex and from the serum of seropositive healthy homosexuals, recognize two major glycoproteins in cells infected with human T-cell lymphotropic virus type III (HTLV III). These glycoproteins, gp160 and gp120, are encoded by the 2.5-kilobase open reading frame located in the 3' end of the HTLV-III genome, as determined by amino terminus sequence analysis of the radiolabeled forms of these proteins. It is hypothesized that gp160 and gp120 represent the major species of virus-encoded envelope gene products for HTLV-III.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allan, J S -- Coligan, J E -- Barin, F -- McLane, M F -- Sodroski, J G -- Rosen, C A -- Haseltine, W A -- Lee, T H -- Essex, M -- 2T32-CA09031/CA/NCI NIH HHS/ -- CA 13885/CA/NCI NIH HHS/ -- CA 37466/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 31;228(4703):1091-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2986290" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology ; Amino Acid Sequence ; Antibodies, Viral/immunology ; Antigens, Viral/genetics/*immunology ; Base Sequence ; Deltaretrovirus/*immunology ; Genes, Viral ; Glycoproteins/genetics/immunology ; Humans ; Molecular Weight ; Tunicamycin/pharmacology ; Viral Envelope Proteins/genetics/*immunology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    "Alz 50" recognizes an Alzheimer's protein (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barnes, D M -- New York, N.Y. -- Science. 1985 Dec 13;230(4731):1260.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4071048" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*diagnosis ; Antibodies, Monoclonal ; Humans ; Molecular Weight ; Nerve Tissue Proteins/immunology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Virus envelope protein of HTLV-III represents major target antigen for antibodies in AIDS patients (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-31
    Description: In this study, two glycoproteins (gp160 and gp120) that are encoded by human T-cell lymphoma virus type III (HTLV-III) were the antigens most consistently recognized by antibodies found in patients with the acquired immune deficiency syndrome (AIDS) and with the AIDS-related complex (ARC) and in healthy homosexual males. The techniques used to detect the glycoproteins were radioimmunoprecipitation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (RIP/SDS-PAGE). Although most antibody-positive samples from ARC patients and from healthy homosexual males also reacted with the virus core protein p24, less than half of the AIDS patients revealed a positive band with p24 under the same conditions. The ability to detect antibodies against a profile of both the major env gene encoded antigens and the gag gene encoded antigens suggests that the RIP/SDS-PAGE may be a valuable confirmatory assay for establishing the presence or absence of antibodies to HTLV-III in human serum samples.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barin, F -- McLane, M F -- Allan, J S -- Lee, T H -- Groopman, J E -- 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):1094-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2986291" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology/microbiology ; Antibodies, Viral/*immunology ; Antibody Specificity ; Antigens, Viral/*immunology ; Deltaretrovirus/*immunology ; Electrophoresis, Polyacrylamide Gel ; Humans ; Immunologic Techniques ; Molecular Weight ; Viral Envelope Proteins/*immunology
    Print ISSN: 0036-8075
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  • 5
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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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  • 6
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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
    Print ISSN: 0036-8075
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  • 7
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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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  • 8
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    Selective inhibition of fibronectin-mediated cell adhesion by monoclonal antibodies to a cell-surface glycoprotein (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-21
    Description: Fibroblasts possess several distinct mechanisms that control cellular adhesion to extracellular matrix macromolecules. Monoclonal antibodies to a 140-kilodalton (kD) cell surface glycoprotein inhibited the adhesion of fibroblastic Chinese hamster ovary cells to fibronectin-coated substrata but did not inhibit adhesion to substrata coated with vitronectin, laminin, serum, or other adhesive macromolecules. Thus the 140-kD glycoprotein appears to be involved in the fibronectin-mediated adhesion mechanism but not in other adhesion processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, P J -- Juliano, R L -- GM26165/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 21;228(4706):1448-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4012302" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; *Cell Adhesion ; Cell Membrane/immunology/*metabolism ; Cells, Cultured ; Cricetinae ; Cricetulus ; Fibroblasts/metabolism ; Fibronectins/*metabolism ; Glycoproteins/immunology/*metabolism ; Molecular Weight
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  • 9
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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
    Print ISSN: 0036-8075
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  • 10
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    A Plasmodium falciparum antigen that binds to host erythrocytes and merozoites (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-01
    Description: Antigens that bind to erythrocytes were identified in the supernatant fluids of a cultured human malaria parasite (Plasmodium falciparum). A 175-kilodalton (175K) antigen bound only to erythrocytes susceptible to invasion. The 175K antigen from the Camp or the FCR-3 strain also bound to merozoites. However, the antigen did not bind to merozoites when merozoites and supernatant antigens were from different strains unless proteinase inhibitors were present. Moreover, erythrocytes coated with supernatant antigens from the Camp or FCR-3 strain were invaded normally by merozoites of the homologous strain but were partially resistant to invasion by merozoites of the heterologous strain. The 175K antigen may be a receptor acting as a "bridge" between erythrocytes and merozoites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Camus, D -- Hadley, T J -- New York, N.Y. -- Science. 1985 Nov 1;230(4725):553-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3901257" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Protozoan/*metabolism ; Chymotrypsin/metabolism ; Electrophoresis, Polyacrylamide Gel ; Erythrocytes/*metabolism ; Guinea Pigs ; Humans ; Macaca mulatta ; Molecular Weight ; Neuraminidase/metabolism ; Plasmodium falciparum/*immunology ; Protease Inhibitors/pharmacology ; Rabbits ; Trypsin/metabolism
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  • 11
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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
    Print ISSN: 0036-8075
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  • 12
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    Atrotoxin: a specific agonist for calcium currents in heart (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-07-12
    Description: A specific label for voltage-dependent calcium channels is essential for the isolation and purification of the membrane protein that constitutes the calcium channel and for a better understanding of its function. A fraction of Crotalus atrox that increases voltage-dependent calcium currents in single, dispersed guinea pig ventricular cells was isolated. In the doses used, neither sodium nor potassium currents were changed. The fraction was active in the absence of detectable phospholipase or protease activity, and the active component, designated atrotoxin, produced its effect rapidly and reversibly. The effect was produced by extracellular but not intracellular application of the agent. The increase in Ca2+ current was blocked by the Ca2+ channel blockers cobalt and nitrendipine. The active fraction completely blocked specific [3H]nitrendipine binding to guinea pig ventricular membrane preparations. The inhibition of nitrendipine binding by atrotoxin was apparently via an allosteric mechanism. Thus atrotoxin was shown to bind to the Ca2+ channel and to act as a specific Ca2+ channel agonist.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamilton, S L -- Yatani, A -- Hawkes, M J -- Redding, K -- Brown, A M -- 1R01 HL3293S/HL/NHLBI NIH HHS/ -- 1R01-HL33662-01/HL/NHLBI NIH HHS/ -- 5R01-HL25145-05/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Jul 12;229(4709):182-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3160111" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/drug effects ; Animals ; Calcium/*metabolism ; Cell Membrane/metabolism ; Crotalid Venoms/*pharmacology ; Dose-Response Relationship, Drug ; Guinea Pigs ; In Vitro Techniques ; Molecular Weight ; Myocardium/*metabolism ; Nifedipine/analogs & derivatives/metabolism ; Nitrendipine ; Potassium/metabolism ; Rats ; Sodium/metabolism
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  • 13
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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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  • 14
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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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  • 15
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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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  • 16
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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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
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    The 36-kilodalton substrate of pp60v-src is myristylated in a transformation-sensitive manner (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-01
    Description: A primary intracellular substrate for pp60v-src kinase in a variety of avian and mammalian cells is a protein of 34 to 39 kilodaltons (kD). After incubation of chicken embryo fibroblasts (CEF) with [3H]myristic acid for 4 hours, the 36-kD protein contained covalently bound myristic acid by several criteria: (i) the radioactively labeled material comigrated with the 36-kD protein on sodium dodecyl sulfate-polyacrylamide gels in one and two dimensions, (ii) the labeled material was insoluble in chloroform-methanol, and (iii) radioactively labeled myristate could be recovered from the purified 36-kD protein. The resistance of the acyl fatty acid moiety to hydrolysis by hydroxylamine suggested that the covalent linkage to the 36-kD protein may be through an amide linkage. The [3H]myristic-acid labeling of the 36-kD protein in Rous sarcoma virus-transformed CEF showed a reduction of up to 45 percent when compared to an identical amount of 36-kD protein derived from normal cells; this reduction was not due to general changes in myristic acid metabolism in transformed cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Soric, J -- Gordon, J A -- CA-15823/CA/NCI NIH HHS/ -- CA-35378/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 1;230(4725):563-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996139" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avian Sarcoma Viruses ; *Cell Transformation, Viral ; Chick Embryo ; Electrophoresis, Polyacrylamide Gel ; Hydrolysis ; Hydroxylamine ; Hydroxylamines/pharmacology ; Methionine/metabolism ; Molecular Weight ; Myristic Acid ; Myristic Acids/*metabolism ; Oncogene Protein pp60(v-src) ; Retroviridae Proteins/*metabolism ; Time Factors
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  • 18
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    Circulating autoantibodies to the 200,000-dalton protein of neurofilaments in the serum of healthy individuals (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-31
    Description: There is substantial evidence that human serum contains antibodies to many autoantigens. For example, all healthy people have autoantibodies (immunoglobulin M) to some undefined brain antigens. In this study immunoblots and immunohistochemical staining were used to detect antibodies to neural tissues in serum samples from 200 healthy people and 200 patients with various neurological diseases. Ninety-nine percent of the 400 subjects had serum immunoglobulin M and 95 percent had immunoglobulin G that bound to a 200-kilodalton protein in homogenates of neural tissues. In most cases there were no antibodies to anything else in the homogenates. The 200-kilodalton protein was the heaviest of the neurofilament triplet proteins. These observations do not support a role for antibodies to the 200-kilodalton protein of neurofilaments in the pathogenesis of neurological diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stefansson, K -- Marton, L S -- Dieperink, M E -- Molnar, G K -- Schlaepfer, W W -- Helgason, C M -- New York, N.Y. -- Science. 1985 May 31;228(4703):1117-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4039466" target="_blank"〉PubMed〈/a〉
    Keywords: Autoantibodies/*analysis ; Cytoskeleton/*immunology ; Humans ; Immunoglobulin G/immunology ; Immunoglobulin M/immunology ; Intermediate Filament Proteins/*immunology ; Molecular Weight ; Nerve Tissue Proteins/immunology ; Nervous System Diseases/immunology
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  • 19
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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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  • 20
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    Neurotrophic factors (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-07-19
    Description: In addition to nerve growth factor (NGF), many proteins present in soluble tissue extracts and in the extracellular matrix influence the survival and development of cultured neurons. The structure, synthesis, and mechanism of action of NGF as a neurotrophic factor are considered along with the experiments on the new putative trophic molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thoenen, H -- Edgar, D -- New York, N.Y. -- Science. 1985 Jul 19;229(4710):238-42.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2409599" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cattle ; Cell Survival ; Cells, Cultured ; Chick Embryo ; Chickens ; Cyclic AMP/physiology ; DNA/genetics ; Extracellular Matrix/physiology ; Humans ; Ion Channels/physiology ; Male ; Mice ; Molecular Weight ; Myocardium/cytology ; Nerve Growth Factors/genetics/isolation & purification/*physiology ; Neurons/physiology ; Protein Precursors/genetics ; RNA, Messenger/metabolism ; Rats ; Receptors, Cell Surface/physiology ; Receptors, Nerve Growth Factor ; Sympathetic Nervous System/cytology
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  • 21
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    Chromosome-sized DNA molecules of Plasmodium falciparum (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-08-16
    Description: At least seven chromosome-sized DNA molecules (750 to 2000 kilobases in length and one fraction of undetermined molecular weight) from cultured clones and isolates of Plasmodium falciparum have been separated by pulsed-field gradient gel electrophoresis. Whereas asexual blood stages and sexual stages of the same line have identical molecular karyotypes, the length of chromosome-sized DNA molecules among different geographical isolates and several clones derived from a single patient is different. These length alterations of chromosomes are the result of DNA rearrangements that must occur unrelated to sexual differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Van der Ploeg, L H -- Smits, M -- Ponnudurai, T -- Vermeulen, A -- Meuwissen, J H -- Langsley, G -- New York, N.Y. -- Science. 1985 Aug 16;229(4714):658-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3895435" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosomes/*ultrastructure ; DNA/*isolation & purification ; Electrophoresis, Polyacrylamide Gel/methods ; Molecular Weight ; Plasmodium falciparum/*genetics ; Species Specificity
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  • 22
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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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  • 23
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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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  • 24
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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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  • 25
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    Stimulation of bone resorption in vitro by synthetic transforming growth factor-alpha (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-24
    Description: Experiments were conducted to test the hypothesis that tumor-derived transforming growth factor-alpha (TGF-alpha) is responsible for the increased bone resorption and hypercalcemia seen in some malignant diseases. Homogeneous synthetic TGF-alpha prepared by the solid-phase synthesis method stimulated bone resorption directly in vitro in a concentration-dependent manner. Incubation times of 72 hours or more were required to stimulate resorption, which is similar to the time course of bone resorption by epidermal growth factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ibbotson, K J -- Twardzik, D R -- D'Souza, S M -- Hargreaves, W R -- Todaro, G J -- Mundy, G R -- AM-28149/AM/NIADDK NIH HHS/ -- CA-29537/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 24;228(4702):1007-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3859011" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Resorption/*drug effects ; Bone and Bones/drug effects ; Dose-Response Relationship, Drug ; History, 20th Century ; Kinetics ; Molecular Weight ; Organ Culture Techniques ; Peptides/chemical synthesis/*pharmacology ; Rats ; Transforming Growth Factors
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  • 26
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    Expression of the Rous sarcoma virus pol gene by ribosomal frameshifting (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-13
    Description: The pol gene of Rous sarcoma virus is positioned downstream of the gag gene in a different, briefly overlapping reading frame; nevertheless, the primary translation product of pol is a gag-pol fusion protein. Two mechanisms, ribosomal frameshifting and RNA splicing, have been considered to explain this phenomenon. The frameshifting model is supported by synthesis of both gag protein and gag-pol fusion protein in a cell-free mammalian translation system programmed by a single RNA species that was synthesized from cloned viral DNA with a bacteriophage RNA polymerase. Under these conditions, the ratio of the gag protein to the fusion protein (about 20 to 1) is similar to that previously observed in infected cells, the frameshifting is specific for the gag-pol junction, and it is unaffected by large deletions in gag. In addition, synthesis of the fusion protein is ten times less efficient in an Escherichia coli cell-free translation system and cannot be explained by transcriptional errors or in vitro modification of the RNA. Ribosomal frameshifting may affect production of other proteins in higher eukaryotes, including proteins encoded by several retroviruses and transposable elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacks, T -- Varmus, H E -- New York, N.Y. -- Science. 1985 Dec 13;230(4731):1237-42.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2416054" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avian Sarcoma Viruses/*genetics ; Base Sequence ; Cell-Free System ; *Gene Expression Regulation ; Gene Products, gag ; Molecular Weight ; *Protein Biosynthesis ; RNA, Messenger/genetics ; RNA, Viral/genetics ; RNA-Directed DNA Polymerase/*genetics ; Rabbits ; Retroviridae Proteins/genetics ; Ribosomes/*metabolism
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  • 27
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    Serologic identification and characterization of a macaque T-lymphotropic retrovirus closely related to HTLV-III (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-07
    Description: Human T-lymphotropic virus type III (HTLV-III) is thought to play an etiologic role in the development of the acquired immune deficiency syndrome (AIDS). In this study the serologic characterization of a new simian retrovirus that is related to HTLV-III is described. This new virus, here referred to as STLV-III, was isolated from sick macaques at the New England Regional Primate Research Center. Radioimmunoprecipitation analysis revealed STLV-III-specific proteins of 160, 120, 55, and 24 kilodaltons, all similar in size to the major gag and env proteins of HTLV-III. These antigens were recognized by representative macaque serum samples and human reference serum samples positive for HTLV-III antibodies. Monoclonal antibodies directed to p24, the major core protein of HTLV-III, also immunoprecipitated a 24-kilodalton species in lysates of cells infected with the macaque virus. This HTLV-III-related virus, which naturally infects a nonhuman primate species, may provide a useful model for the study of HTLV-III and the pathogenesis of AIDS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kanki, P J -- McLane, M F -- King, N W Jr -- Letvin, N L -- Hunt, R D -- Sehgal, P -- Daniel, M D -- Desrosiers, R C -- Essex, M -- 5TRRR07000/RR/NCRR NIH HHS/ -- CA18216/CA/NCI NIH HHS/ -- CA37466/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1199-201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3873705" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*veterinary ; Animals ; Antigens, Viral/analysis ; Glycoproteins/immunology ; Lymphoma/microbiology ; Macaca/*microbiology ; Molecular Weight ; Monkey Diseases/microbiology ; Retroviridae/*immunology/isolation & purification ; T-Lymphocytes/*microbiology ; Viral Proteins/immunology
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  • 28
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    Deregulation of interleukin-2 receptor gene expression in HTLV-I-induced adult T-cell leukemia (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-07
    Description: Infection of human T cells by human T-lymphotropic virus, type I (HTLV-I), a retrovirus, is uniformly associated with the constitutive expression of large numbers of cellular receptors for interleukin-2 (IL-2). Comparison with normal T cells shows that neither IL-2 receptor gene organization nor IL-2 receptor messenger RNA processing are altered in the leukemic cells. However, mitogenic stimuli activate IL-2 receptor gene expression in normal T cells, whereas these stimuli paradoxically inhibit IL-2 receptor gene transcription in HTLV-I-infected leukemic T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kronke, M -- Leonard, W J -- Depper, J M -- Greene, W C -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1215-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2988127" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Nucleus/physiology ; Cells, Cultured ; DNA/genetics ; Deltaretrovirus ; Humans ; Leukemia/*genetics ; Molecular Weight ; Poly A/genetics ; RNA, Messenger/genetics ; Receptors, Immunologic/*genetics ; Receptors, Interleukin-2 ; T-Lymphocytes/microbiology/*physiology ; Transcription, Genetic
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  • 29
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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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    Antibodies to peptides detect new hepatitis B antigen: serological correlation with hepatocellular carcinoma (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-01-25
    Description: The expression of a previously unidentified gene product, encoded by the hepatitis B virus (HBV) genome, has been achieved with a recombinant SV40 expression vector. Antibodies against synthetic peptides representing defined regions of this protein were used to screen cells infected with recombinant virus as well as tissues naturally infected with HBV. A 24,000-dalton protein (p24) was detected in cells infected with recombinant virus and a 28,000-dalton protein (p28) was detected in tissues infected with HBV. The peptides or recombinant-derived protein were used as antigens to screen sera from individuals infected with HBV. Specific antibodies were detected predominantly in sera from patients with hepatocellular carcinoma. The presence of p28 in tissues infected with HBV and the appearance of specific antibodies in infectious sera establish the existence of an additional marker for HBV infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moriarty, A M -- Alexander, H -- Lerner, R A -- Thornton, G B -- New York, N.Y. -- Science. 1985 Jan 25;227(4685):429-33.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2981434" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carcinoma, Hepatocellular/diagnosis/*immunology ; Cell Line ; Cloning, Molecular ; Enzyme-Linked Immunosorbent Assay ; Genetic Vectors ; Hepatitis B/diagnosis/*immunology ; Hepatitis B Antibodies/*analysis/immunology ; Hepatitis B Antigens/*analysis/immunology ; Humans ; Liver/*immunology ; Liver Neoplasms/diagnosis/*immunology ; Molecular Weight ; Peptides/immunology ; Simian virus 40/genetics ; Viral Proteins/immunology
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    Uromodulin: a unique 85-kilodalton immunosuppressive glycoprotein isolated from urine of pregnant women (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-08-02
    Description: Crude fractions of urine from pregnant women are immunosuppressive in vitro. An 85-kilodalton immunosuppressive glycoprotein purified to homogeneity from such urine inhibited in vitro assays of human T-cell and monocyte activity at concentrations of 10(-9) to 10(-11) molar. This material was nontoxic and blocked early events required for normal T-cell proliferation in vitro. On the basis of its tissue source and its in vitro activity, the name "uromodulin" is proposed for this glycoprotein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muchmore, A V -- Decker, J M -- New York, N.Y. -- Science. 1985 Aug 2;229(4712):479-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2409603" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocytes/drug effects ; Chromatography/methods ; Collodion ; Cytotoxicity, Immunologic/drug effects ; Electrophoresis, Polyacrylamide Gel ; Epitopes ; Female ; Hemolytic Plaque Technique ; Humans ; Immunosuppressive Agents/isolation & purification/*urine ; In Vitro Techniques ; Isoelectric Focusing ; Lymphocyte Activation/drug effects ; Molecular Weight ; *Mucoproteins ; Pregnancy ; Pregnancy Proteins/isolation & purification/pharmacology/*urine ; T-Lymphocytes/drug effects ; Uromodulin
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    A test of clathrin function in protein secretion and cell growth (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-29
    Description: Clathrin-coated membranes are intimately associated with a variety of protein transport processes in eukaryotic cells, yet no direct test of clathrin function has been possible. The data presented demonstrate that Saccharomyces cerevisiae does not require clathrin for either cell growth or protein secretion. Antiserum to the yeast clathrin heavy chain has been used to isolate a molecular clone of the heavy chain gene (CHC1) from a library of yeast DNA in lambda gt11. Clathrin-deficient mutant yeast have been obtained by replacing the single chromosomal CHC1 gene with a disrupted version of the cloned DNA. Cells harboring a nonfunctional chc1 allele produce no immunoreactive heavy chain polypeptide, and vesicles prepared from mutant cells are devoid of clathrin heavy and light chains. Although clathrin-deficient cells grow two to three times more slowly than normal, secretion of invertase occurs at a nearly normal rate. Therefore protein transport through the secretory pathway is not obligately coupled to the formation of clathrin-coated vesicles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Payne, G S -- Schekman, R -- New York, N.Y. -- Science. 1985 Nov 29;230(4729):1009-14.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2865811" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Transport ; *Cell Physiological Phenomena ; Clathrin/genetics/immunology/*physiology ; Coated Pits, Cell-Membrane/*physiology ; Endosomes/*physiology ; Eukaryotic Cells/*physiology ; Genes ; Genes, Fungal ; Genetic Engineering ; Glycoside Hydrolases/secretion ; Macromolecular Substances ; Molecular Weight ; Proteins/*secretion ; Saccharomyces cerevisiae/genetics ; beta-Fructofuranosidase
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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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    Retinal S antigen identified as the 48K protein regulating light-dependent phosphodiesterase in rods (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-17
    Description: Retinal S antigen chromatographically purified from whole retina, induces experimental autoimmune uveoretinitis in laboratory animals. The 48K protein, a soluble protein found in rod outer segments, is purified through its specific binding to photoexcited rhodopsin and is involved in the quenching of light-induced guanosine 3',5'-monophosphate-phosphodiesterase activity. Biochemical, immunological, functional, and pathological tests showed that retinal S antigen and the 48K protein are identical.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pfister, C -- Chabre, M -- Plouet, J -- Tuyen, V V -- De Kozak, Y -- Faure, J P -- Kuhn, H -- New York, N.Y. -- Science. 1985 May 17;228(4701):891-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2988124" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-GMP Phosphodiesterases/*metabolism ; Animals ; *Antigens/isolation & purification ; Arrestin ; Autoimmune Diseases/etiology ; Cattle ; Eye Proteins/immunology/isolation & purification/pharmacology ; Light ; Molecular Weight ; Photoreceptor Cells/*enzymology ; Rats ; Retina/analysis/*immunology ; Rod Cell Outer Segment/analysis/immunology ; Uveitis/etiology
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    Isolation and propagation of a human enteric coronavirus (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-09-06
    Description: Coronavirus-like particles were found by electron microscopy in stools from infants with necrotizing enterocolitis. Stool samples from these infants as well as control specimens were passaged in cultures of human fetal intestinal organs. Two samples yielded virus-like particles and these have now been passaged 14 times (HEC 14). Gradient-purified HEC 14 strains had typical coronavirus morphology on electron microscopy and contained five major proteins with molecular sizes ranging from 190 to 23 kilodaltons. Infants with necrotizing enterocolitis developed specific antibody to the viral antigens between the acute and convalescent stages of the disease, as shown by examining serum specimens by single radial hemolysis, immunoenzymatic assay, and Western immunoblotting. No cross-reactivity was shown with other coronavirus strains tested, or with the newly isolated viruses of the Breda-Berne group, responsible for calf or horse diarrhea.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Resta, S -- Luby, J P -- Rosenfeld, C R -- Siegel, J D -- New York, N.Y. -- Science. 1985 Sep 6;229(4717):978-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2992091" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Viral/analysis ; Coronaviridae/immunology/*isolation & purification ; Coronaviridae Infections/*microbiology ; Cross Infection ; Disease Outbreaks ; Enterocolitis, Pseudomembranous/*microbiology ; Feces/microbiology ; Humans ; Infant ; Microscopy, Electron ; Molecular Weight ; Viral Proteins/immunology
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    Vaccination against Schistosoma mansoni with purified surface antigens (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-02-01
    Description: Two surface antigens were isolated from young or adult schistosomes by affinity chromatography with monoclonal antibodies. Vaccination with an antigen having a molecular weight of 155,000 gave partial protection against challenge in some batches of mice and in a group of cynomolgus monkeys. Vaccination with an antigen having a molecular weight of 53,000 gave similar levels of protection in mice. The results demonstrate that protection can be obtained with single antigens, but the precise requirements for reproducible vaccination are as yet unknown.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, M A -- Clegg, J A -- New York, N.Y. -- Science. 1985 Feb 1;227(4686):535-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3966161" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Antigens, Helminth/*immunology/isolation & purification ; Antigens, Surface/*immunology/isolation & purification ; Chromatography, Affinity ; Immunoglobulin E/biosynthesis ; Immunoglobulin G/biosynthesis ; Immunoglobulin M/biosynthesis ; Macaca fascicularis ; Macrophage Activation ; Mice ; Molecular Weight ; Schistosoma mansoni/*immunology ; Schistosomiasis/immunology/*prevention & control ; *Vaccination ; Vaccines
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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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  • 38
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    Colocalization of band 3 with ankyrin and spectrin at the basal membrane of intercalated cells in the rat kidney (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-13
    Description: An immunoreactive form of the anion channel protein of erythrocytes, band 3, has been identified in the rat kidney. It is found in the intercalated cells of the distal tubule and collecting ducts. Immunostaining specific for band 3 is confined to the basolateral plasma membrane of these cells, where this protein probably mediates the transport of bicarbonate across the tubular wall. Double-immunolabeling studies demonstrate that band 3 is colocalized with immunoreactive forms of ankyrin and spectrin along the basolateral plasma membrane. The polarized distribution of band 3 may be the result of the association of its cytoplasmic domain with ankyrin, which in turn links band 3 to spectrin and the cytoskeleton. These observations help to explain how the collecting ducts of the kidney can direct the transport of bicarbonate ions, thus maintaining the acid-base balance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Drenckhahn, D -- Schluter, K -- Allen, D P -- Bennett, V -- K04 AM00926/AM/NIADDK NIH HHS/ -- R01 AM29808/AM/NIADDK NIH HHS/ -- R01 GM33996/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Dec 13;230(4731):1287-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2933809" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anion Exchange Protein 1, Erythrocyte/*metabolism ; Ankyrins ; Bicarbonates/*metabolism ; Cell Membrane/metabolism ; Fluorescent Antibody Technique ; Immunosorbent Techniques ; Kidney/metabolism/*ultrastructure ; Kidney Tubules, Collecting/metabolism/ultrastructure ; Kidney Tubules, Distal/metabolism/ultrastructure ; Macromolecular Substances ; Membrane Proteins/*metabolism ; Molecular Weight ; Rats ; Spectrin/*metabolism
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    Gonadotropin-releasing hormone binding sites in human breast carcinoma (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-09-06
    Description: Gonadotropin-releasing hormone analogs can cause regression of hormone-dependent breast carcinomas. These effects are thought to be mediated through the inhibition of gonadotropic and steroid hormones. These analogs may also act directly on the tumor because they are effective in treating breast cancer in some postmenopausal women. The presence of specific binding sites for gonadotropin-releasing hormone was demonstrated in human breast carcinomas by means of a novel approach of ligand immunoblotting. The results indicate a possible mechanism by which the peptide has direct effects on this tissue. These binding proteins were not detectable in non-neoplastic breast tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eidne, K A -- Flanagan, C A -- Millar, R P -- New York, N.Y. -- Science. 1985 Sep 6;229(4717):989-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2992093" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Breast Neoplasms/*metabolism ; Female ; Gonadotropin-Releasing Hormone/*metabolism ; Humans ; Membrane Proteins/metabolism ; Menopause ; Middle Aged ; Molecular Weight ; Receptors, Cell Surface/*metabolism ; Receptors, LHRH
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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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  • 41
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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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  • 42
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    The granulocyte-macrophage colony-stimulating factors (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-07-05
    Description: The granulocyte-macrophage colony-stimulating factors are well-characterized specific glycoproteins that interact to control the production, differentiation, and function of two related white cell populations of the blood, the granulocytes and monocyte-macrophages. Widely produced in the body, these regulators probably play an important role in resistance to infections. The proliferation of myeloid leukemia cells remains dependent on stimulation by colony-stimulating factors, although one of them also has the ability to suppress leukemic populations by inducing terminal differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Metcalf, D -- CA-22556/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jul 5;229(4708):16-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990035" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Marrow Cells ; Cell Differentiation ; Cell Division ; Cell Survival ; Cloning, Molecular ; Colony-Stimulating Factors/*physiology ; Granulocytes/*physiology ; *Hematopoiesis ; Humans ; Leukemia, Myeloid, Acute/physiopathology ; Macrophages/*physiology ; Mice ; Molecular Weight ; Receptors, Cell Surface/physiology ; Receptors, Colony-Stimulating Factor ; Species Specificity
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    Evidence that the v-sis gene product transforms by interaction with the receptor for platelet-derived growth factor (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-18
    Description: A scheme for partial purification of biologically active v-sis-coded protein from cells transformed with simian sarcoma virus (SSV) has made possible a functional comparison of the transforming protein with platelet-derived growth factor (PDGF). The SSV-transforming gene product is capable of specifically binding PDGF receptors, stimulating tyrosine phosphorylation of PDGF receptors, and inducing DNA synthesis in quiescent fibroblasts. Each of these activities was specifically inhibited by antibodies to different regions of the v-sis gene product. Moreover, viral infection of a variety of cell types revealed a strict correlation between those cells possessing PDGF receptors and those susceptible to transformation by SSV. These findings provide evidence that SSV-transforming activity is mediated by the interaction of a virus-coded mitogen with PDGF receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leal, F -- Williams, L T -- Robbins, K C -- Aaronson, S A -- New York, N.Y. -- Science. 1985 Oct 18;230(4723):327-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996133" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta/metabolism ; Cattle ; Cell Line ; *Cell Transformation, Viral ; Cells, Cultured ; Fibroblasts/metabolism ; *Genes ; *Genes, Viral ; Humans ; Kinetics ; Mink ; Molecular Weight ; Muscle, Smooth/metabolism ; Muscle, Smooth, Vascular/metabolism ; Platelet-Derived Growth Factor/*metabolism ; Receptors, Cell Surface/isolation & purification/*metabolism ; Receptors, Platelet-Derived Growth Factor ; Retroviridae/*genetics ; Sarcoma Virus, Woolly Monkey/*genetics ; Viral Proteins/genetics/*metabolism
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  • 44
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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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  • 45
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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)
    Details
    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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  • 46
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    A specific 37,000-dalton protein that accumulates in regenerating but not in nonregenerating mammalian nerves (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-26
    Description: A 37-kilodalton protein is synthesized at higher rates in the peripheral and central nervous system of newborn rats than in adult animals. As a specific response to denervation, the synthesis of the 37-kilodalton protein is increased in the mature peripheral and central nervous system; however, this protein accumulates only in the peripheral nervous system. The differences in accumulation of the protein correlate with the apparent differences in the ability of peripheral and central axons to regenerate. The synthesis of the 37-kilodalton protein is inhibited when proper innervation or reinnervation is established.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muller, H W -- Gebicke-Harter, P J -- Hangen, D H -- Shooter, E M -- NS 04270/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 26;228(4698):499-501.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3983637" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Animals ; Animals, Newborn/physiology ; Axons/physiology ; Brain/physiology ; Central Nervous System/metabolism/*physiology ; Molecular Weight ; *Nerve Regeneration ; Nerve Tissue Proteins/*biosynthesis ; Optic Nerve/physiology ; Peripheral Nerves/metabolism/*physiology ; Photofluorography ; Rats ; Rats, Inbred Strains ; Sciatic Nerve/physiology ; Spinal Cord/physiology
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  • 47
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    Immunoprecipitation of insulin receptors from cultured human lymphocytes (IM-9 cells) by antibodies to pp60src (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-02-15
    Description: The family of tyrosine-specific protein kinases includes proteins encoded by retroviral oncogenes as well as receptors for insulin and several growth factors. Antibodies to pp60src, the protein encoded by the src oncogene of Rous sarcoma virus (RSV), can specifically immunoprecipitate affinity-labeled insulin receptors from cultured human lymphocytes (IM-9 cells). This precipitation is specifically inhibited by the src gene product purified from RSV-transformed rat cells. These observations provide evidence that there is structural homology between the insulin receptors and pp60src.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perrotti, N -- Taylor, S I -- Richert, N D -- Rapp, U R -- Pastan, I H -- Roth, J -- New York, N.Y. -- Science. 1985 Feb 15;227(4688):761-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3918346" target="_blank"〉PubMed〈/a〉
    Keywords: Cross Reactions ; Humans ; Molecular Weight ; Oncogene Protein pp60(v-src) ; *Oncogenes ; Protein Kinases/*immunology ; Protein-Tyrosine Kinases ; Receptor, Insulin/*immunology ; Viral Proteins/*immunology
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  • 48
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    The product of the c-fms proto-oncogene: a glycoprotein with associated tyrosine kinase activity (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-04-19
    Description: The c-fms proto-oncogene is a member of a gene family that has been implicated in tumorigenesis. Glycoproteins encoded by c-fms were identified in cat spleen cells by means of an immune-complex kinase assay performed with monoclonal antibodies to v-fms-coded epitopes. The major form of the normal cellular glycoprotein has an apparent molecular weight of 170,000 and, like the product of the viral oncogene, serves as a substrate for an associated tyrosine-specific protein kinase activity in vitro. The results suggest that the transforming glycoprotein specified by v-fms is a truncated form of a c-fms-coded growth factor receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rettenmier, C W -- Chen, J H -- Roussel, M F -- Sherr, C J -- 1 RO1 CA 38187/CA/NCI NIH HHS/ -- RR-05584-20/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):320-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2580348" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology ; Cats ; Glycoproteins/immunology/*metabolism ; Humans ; Mice ; Molecular Weight ; Neoplasm Proteins/immunology/*metabolism ; *Oncogenes ; Phosphorylation ; Protein Kinases/*metabolism ; Protein-Tyrosine Kinases ; RNA/metabolism ; Rats
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  • 49
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    Characterization of envelope and core structural gene products of HTLV-III with sera from AIDS patients (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-03
    Description: The envelope (env) and structural (gag) gene products of human T-cell leukemia (lymphotropic) virus type III were identified by immunoaffinity chromatography, immunoprecipitation, and two-dimensional oligopeptide mapping methods. The env gene specifies a glycosylated polypeptide with a molecular weight of 160,000 (gp160) that is processed to gp120 and smaller gene products. The gag gene specifies two polypeptides of 70,000 and 55,000 molecular weight (p70 and p55), both of which contain p24, the major structural protein of the mature virion. The techniques in this study can be used to define the extent of variability of the env gene product among different virus isolates and may identify the nature and patterns of the humoral immune response that lead to an immunologically protected state.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Robey, W G -- Safai, B -- Oroszlan, S -- Arthur, L O -- Gonda, M A -- Gallo, R C -- Fischinger, P J -- N01-CO-23909/CO/NCI NIH HHS/ -- N01-CO-23910/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 3;228(4699):593-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2984774" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; Animals ; Antibodies, Viral/immunology ; Chromatography, Affinity ; Deltaretrovirus/*metabolism ; Genes, Viral ; Humans ; Molecular Weight ; Pan troglodytes ; Sarcoma, Kaposi/microbiology ; Viral Envelope Proteins/*isolation & purification ; Viral Proteins/isolation & purification
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  • 50
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    Naturally occurring antibodies reactive with sperm proteins: apparent deficiency in AIDS sera (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-07
    Description: A set of naturally occurring immunoglobulin M (IgM) antibodies that are reactive with a defined subset of proteins in the acrosomal cap region of human sperm has been identified. These antibodies are present in a broad spectrum of human sera from males and females, 1 day to 40 years of age, and are absent or markedly deficient in a large proportion of sera from individuals with the acquired immune deficiency syndrome (AIDS) or at risk for AIDS. The subset of proteins with which the IgM antibodies are reactive includes a factor (or factors) capable of inhibiting lectin-induced T-lymphocyte proliferation. The prevalence of the sperm-reactive IgM antibodies indicates that they are not elicited by sperm. Further, immunoreactivity of the sperm proteins resulting in depletion of specific circulating IgM antibodies, or other interactions between the sperm proteins and elements of the immune system, may be a factor in the suppressed state of the immune system in AIDS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rodman, T C -- Laurence, J -- Pruslin, F H -- Chiorazzi, N -- Winston, R -- CA 35018-02/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1211-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3890184" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology ; Acrosome/*immunology ; Adolescent ; Adult ; Antibodies/analysis ; Child ; Child, Preschool ; Female ; Fluorescent Antibody Technique ; Humans ; Immunoglobulin M/analysis ; Infant ; Male ; Molecular Weight ; Spermatozoa/*immunology ; T-Lymphocytes/immunology
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    Antigenic variation and resistance to neutralization in poliovirus type 1 (1985)
    American Association for the Advancement of Science (AAAS)
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    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)
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    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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  • 53
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    Prooxidant states and tumor promotion (1985)
    American Association for the Advancement of Science (AAAS)
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    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)
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    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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  • 55
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    Evolution in inbred strains of mice appears rapid (1985)
    American Association for the Advancement of Science (AAAS)
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    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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  • 56
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    Measuring gene expression with light (1985)
    American Association for the Advancement of Science (AAAS)
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    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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    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
    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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  • 58
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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)
    Details
    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
    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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  • 59
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    Expression of the major surface antigen of Plasmodium knowlesi sporozoites in yeast (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-17
    Description: The circumsporozite protein, a surface antigen of the sporozoite stage of the monkey malarial parasite Plasmodium knowlesi, was expressed in the yeast Saccharomyces cerevisiae by using an expression vector containing the 5' regulatory region of the yeast alcohol dehydrogenase I gene. It was necessary to eliminate the entire 5' upstream region of the parasite DNA to obtain the expression of this protein. Only the circumsporozoite precursor was produced by the yeast transformants, as detected by immunoblotting. About 55 and 20 percent of the circumsporozoite protein produced in yeast was associated wtih the 25,000 g and 150,000 g particulate fractions, respectively. The protein could be solubilized in Triton X-100 and was stable in solubilized extracts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharma, S -- Godson, G N -- 1 R01 AI21496-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 May 17;228(4701):879-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3890178" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Protozoan/*genetics ; Antigens, Surface/*genetics ; Cloning, Molecular ; DNA, Recombinant ; Genes ; Molecular Weight ; Plasmodium/genetics/*immunology ; Protein Precursors/biosynthesis/genetics ; Protozoan Proteins/*genetics ; Saccharomyces cerevisiae/*genetics ; Transformation, Genetic
    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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  • 60
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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
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  • 61
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    Effects of extracellular egg factors on sperm guanylate cyclase (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-02-15
    Description: Extracellular factors from the sea urchin egg induce a change in the electrophoretic mobility of an abundant sperm membrane phosphoprotein. The modified protein was identified as guanylate cyclase. The mobility shift of the cyclase was shown to be associated with a decrease in its enzymatic activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ward, G E -- Garbers, D L -- Vacquier, V D -- HD-10254/HD/NICHD NIH HHS/ -- HD-12986/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1985 Feb 15;227(4688):768-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2857502" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Enzyme Activation ; Female ; Fertilization ; Guanylate Cyclase/*metabolism ; Male ; Membrane Proteins/metabolism ; Molecular Weight ; Phosphoproteins/metabolism ; Sea Urchins ; Sperm Maturation ; *Sperm-Ovum Interactions ; Spermatozoa/*enzymology
    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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  • 62
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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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