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  • Articles  (92)
  • Amino Acid Sequence  (50)
  • Cell Line  (50)
  • 1985-1989  (92)
  • 1985  (92)
  • Biology  (92)
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  • Articles  (92)
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  • 1985-1989  (92)
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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
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Major glycoprotein antigens that induce antibodies in AIDS patients are encoded by HTLV-III (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-31
    Description: Antibodies from the serum of patients with the acquired immune deficiency syndrome (AIDS) or with the AIDS-related complex and from the serum of seropositive healthy homosexuals, recognize two major glycoproteins in cells infected with human T-cell lymphotropic virus type III (HTLV III). These glycoproteins, gp160 and gp120, are encoded by the 2.5-kilobase open reading frame located in the 3' end of the HTLV-III genome, as determined by amino terminus sequence analysis of the radiolabeled forms of these proteins. It is hypothesized that gp160 and gp120 represent the major species of virus-encoded envelope gene products for HTLV-III.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allan, J S -- Coligan, J E -- Barin, F -- McLane, M F -- Sodroski, J G -- Rosen, C A -- Haseltine, W A -- Lee, T H -- Essex, M -- 2T32-CA09031/CA/NCI NIH HHS/ -- CA 13885/CA/NCI NIH HHS/ -- CA 37466/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 31;228(4703):1091-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2986290" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology ; Amino Acid Sequence ; Antibodies, Viral/immunology ; Antigens, Viral/genetics/*immunology ; Base Sequence ; Deltaretrovirus/*immunology ; Genes, Viral ; Glycoproteins/genetics/immunology ; Humans ; Molecular Weight ; Tunicamycin/pharmacology ; Viral Envelope Proteins/genetics/*immunology
    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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    Identification of the protein encoded by the E6 transforming gene of bovine papillomavirus (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-25
    Description: Papillomaviruses (PV) contain several conserved genes that may encode nonstructural proteins; however, none of these predicted gene products have been identified. Papillomavirus E6 genes are retained and expressed as RNA in PV-associated human and animal carcinomas and cell lines. This suggests that the E6 gene product may be important in the maintenance of the malignant phenotype. The E6 open reading frame of the bovine papillomavirus (BPV) genome has been identified as one of two BPV genes that can independently transform mouse cells in vitro. A polypeptide encoded by this region of BPV was produced in a bacterial expression vector and used to raise antisera. The antisera specifically immunoprecipitated the predicted 15.5-kilodalton BPV E6 protein from cells transformed by the E6 gene. The E6 protein was identified in both the nuclear and membrane fractions of these transformed cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Androphy, E J -- Schiller, J T -- Lowy, D R -- 5-F32-CA-07237/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Oct 25;230(4724):442-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996134" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bovine papillomavirus 1/*genetics ; Cell Line ; Cell Transformation, Viral ; *Genes, Viral ; Mice ; Oncogenes ; Papillomaviridae/*genetics ; RNA, Messenger/genetics ; Rabbits ; Rats ; Tumor Virus Infections/genetics ; Viral Proteins/*genetics/isolation & purification
    Print ISSN: 0036-8075
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  • 4
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    Circumsporozoite protein of Plasmodium vivax: gene cloning and characterization of the immunodominant epitope (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-15
    Description: The gene encoding the circumsporozoite (CS) protein of the human malaria parasite Plasmodium vivax has been cloned. The deduced sequence of the protein consists of 373 amino acids with a central region of 19 tandem repeats of the nonapeptide Asp-Arg-Ala-Asp/Ala-Gly-Gln-Pro-Ala-Gly. A synthetic 18-amino acid peptide containing two tandem repeats binds to a monoclonal antibody directed to the CS protein of Plasmodium vivax and inhibits the interaction of this antibody with the native protein in sporozoite extracts. The portions of the CS gene that do not contain repeats are closely related to the corresponding regions of the CS genes of two simian malarias, Plasmodium cynomolgi and Plasmodium knowlesi. In contrast, the homology between the CS genes of Plasmodium vivax and Plasmodium falciparum, another malaria parasite of humans, is very limited.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arnot, D E -- Barnwell, J W -- Tam, J P -- Nussenzweig, V -- Nussenzweig, R S -- Enea, V -- New York, N.Y. -- Science. 1985 Nov 15;230(4727):815-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2414847" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Antigens, Surface/*genetics/immunology ; Cloning, Molecular ; Epitopes/*genetics/immunology ; Haplorhini/parasitology ; Humans ; Malaria/parasitology ; Nucleic Acid Hybridization ; Plasmodium/immunology ; Plasmodium vivax/*genetics/immunology ; *Protozoan Proteins ; Repetitive Sequences, Nucleic Acid
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Trans-activator gene of human T-lymphotropic virus type III (HTLV-III) (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-07-05
    Description: Human T-lymphotropic virus type III (HTLV-III) encodes a trans-acting factor that activates the expression of genes linked to the HTLV-III long terminal repeat. By functional mapping of complementary DNA transcripts of viral messenger RNA's the major functional domain of the gene encoding this factor was localized to a region immediately before the env gene of the virus, a region previously thought to be noncoding. This newly identified gene consists of three exons, and its transcription into messenger RNA involves two splicing events bringing together sequences from the 5' part (287 base pairs), middle (268 base pairs), and 3'part (1258 base pairs) of the HTLV-III genome. A similar messenger RNA with a truncated second exon (70 base pairs) does not encode a trans-acting function. It is proposed that this second messenger RNA is the transcript of a gene (3'-orf) located after the env gene. Messenger RNA's were also identified for the env and gag-pol genes of HTLV-III.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arya, S K -- Guo, C -- Josephs, S F -- Wong-Staal, F -- New York, N.Y. -- Science. 1985 Jul 5;229(4708):69-73.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990040" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Deltaretrovirus/*genetics ; Gene Expression Regulation ; Genes, Regulator ; *Genes, Viral ; Humans ; RNA Splicing ; RNA, Messenger/genetics ; RNA, Viral/genetics ; Repetitive Sequences, Nucleic Acid ; Transcription Factors/*genetics ; Viral Proteins/genetics
    Print ISSN: 0036-8075
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  • 6
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    Immunogenicity of synthetic peptides from circumsporozoite protein of Plasmodium falciparum (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-24
    Description: In a study of recombinant proteins that might be useful in developing a vaccine against malaria, synthetic peptides from the circumsporozoite (CS) protein of Plasmodium falciparum were found to be immunogenic for mice and rabbits. Antibody to peptides from the repeating region of the CS protein recognized native CS protein and blocked sporozoite invasion of human hepatoma cells in vitro. Antibodies to peptides from regions I and II had no biologic activity, although antibody to region I recognized processed CS protein by Western blot analysis. These data support the feasibility of developing a vaccine against the sporozoite stage of the malaria parasite by using synthetic peptides of the repeating region of the CS protein conjugated to a carrier protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ballou, W R -- Rothbard, J -- Wirtz, R A -- Gordon, D M -- Williams, J S -- Gore, R W -- Schneider, I -- Hollingdale, M R -- Beaudoin, R L -- Maloy, W L -- New York, N.Y. -- Science. 1985 May 24;228(4702):996-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2988126" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies/immunology ; Antibody Formation ; Antigens, Surface/*immunology ; Carcinoma, Hepatocellular ; Cell Line ; Cross Reactions ; Fluorescent Antibody Technique ; Humans ; Immune Sera/immunology ; Liver Neoplasms ; Malaria/prevention & control ; Mice ; Peptides/chemical synthesis/*immunology ; Plasmodium/immunology ; Plasmodium falciparum/*immunology/physiology ; Precipitin Tests ; *Protozoan Proteins ; Rabbits ; Vaccines/immunology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Active T-cell receptor genes have intron deoxyribonuclease hypersensitive sites (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-08-09
    Description: The T-cell receptor beta-chain gene has a nuclease hypersensitive site in several kinds of T cells, which does not appear in B cells expressing immunoglobulins. Conversely, the kappa immunoglobulin gene shows a known hypersensitive site at its enhancer element in B cells, as expected, but this site is absent in T cells. As is the case with immunoglobulin genes, the T-cell receptor site lies within the gene, in the intron separating joining and constant region segments. These nuclease hypersensitive DNA configurations in the introns of active T-cell receptor and immunoglobulin genes may arise from control elements that share ancestry but have diverged to the extent that each normally acts only in lymphoid cells which use the proximal gene product.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bier, E -- Hashimoto, Y -- Greene, M I -- Maxam, A M -- AI 19901/AI/NIAID NIH HHS/ -- CA 22427/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 9;229(4713):528-34.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3927483" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/metabolism ; Base Sequence ; Binding Sites ; Cell Line ; Chromosome Mapping ; Collodion ; Deoxyribonuclease I/*metabolism ; Enhancer Elements, Genetic ; Gene Expression Regulation ; Humans ; Hybridomas ; Immunochemistry ; Immunoglobulin Fragments/*genetics ; Immunoglobulin Heavy Chains/genetics ; Immunoglobulin kappa-Chains/genetics ; Mice ; Receptors, Antigen, T-Cell/*genetics ; T-Lymphocytes/*metabolism ; Transcription, Genetic
    Print ISSN: 0036-8075
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  • 8
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    Biosynthesis and secretion of proatrial natriuretic factor by cultured rat cardiocytes (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-06
    Description: Rat atrial natriuretic factor (ANF) is translated as a 152-amino acid precursor preproANF. PreproANF is converted to the 126-amino acid proANF, the storage form of ANF in the atria. ANF isolated from the blood is approximately 25 amino acids long. It is demonstrated here that rat cardiocytes in culture store and secrete proANF. Incubation of proANF with serum produced a smaller ANF peptide. PreproANF seems to be processed to proANF in the atria, and proANF appears to be released into the blood, where it is converted by a protease to a smaller peptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bloch, K D -- Scott, J A -- Zisfein, J B -- Fallon, J T -- Margolies, M N -- Seidman, C E -- Matsueda, G R -- Homcy, C J -- Graham, R M -- Seidman, J G -- 1R23CA33570/CA/NCI NIH HHS/ -- HL07208/HL/NHLBI NIH HHS/ -- HL26215/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Dec 6;230(4730):1168-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2933808" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Atrial Natriuretic Factor/*biosynthesis/genetics/secretion ; Autoradiography ; Cells, Cultured ; Electrophoresis, Polyacrylamide Gel ; Heart/physiology ; Immune Sera/immunology ; Myocardium/*cytology/metabolism ; Protein Precursors/*biosynthesis/genetics/secretion ; RNA, Messenger/genetics ; Rabbits/immunology ; Rats
    Print ISSN: 0036-8075
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  • 9
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    Association of crossover points with topoisomerase I cleavage sites: a model for nonhomologous recombination (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-22
    Description: Nonhomologous DNA recombination is frequently observed in somatic cells upon the introduction of DNA into cells or in chromosomal events involving sequences already stably carried by the genome. In this report, the DNA sequences at the crossover points for excision of SV40 from chromosomes were shown to be associated with eukaryotic topoisomerase I cleavage sites in vitro. The precise location of the cleavage sites relative to the crossover points has suggested a general model for nonhomologous recombination mediated by topoisomerase I.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bullock, P -- Champoux, J J -- Botchan, M -- CA 30490/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 22;230(4728):954-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2997924" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Line ; Cell Transformation, Viral ; Chromatin/ultrastructure ; Chromosome Mapping ; DNA Topoisomerases, Type I/*metabolism ; Rats ; *Recombination, Genetic ; Simian virus 40/*genetics
    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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  • 10
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    A new class of endogenous human retroviral genomes (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-07
    Description: Human DNA contains multiple copies of a novel class of endogenous retroviral genomes. Analysis of a human recombinant DNA clone (HLM-2) containing one such proviral genome revealed that it is a mosaic of retroviral-related sequences with the organization and length of known endogenous retroviral genomes. The HLM-2 long terminal repeat hybridized with the long terminal repeat of the squirrel monkey virus, a type D retrovirus. The HLM-2 gag and pol genes share extensive nucleotide sequence homology with those of the M432 retrovirus (a type A-related retrovirus), mouse mammary tumor virus (a type B retrovirus), and the avian Rous sarcoma virus (a type C retrovirus). Nucleotide sequence analysis revealed regions in the HLM-2 pol gene that were as much as 70 percent identical to the mouse mammary tumor virus pol gene. A portion of the putative HLM-2 env gene hybridized with the corresponding region of the M432 viral genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Callahan, R -- Chiu, I M -- Wong, J F -- Tronick, S R -- Roe, B A -- Aaronson, S A -- Schlom, J -- GM30400/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1208-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2408338" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/genetics ; Base Sequence ; Cloning, Molecular ; DNA Restriction Enzymes ; Gene Products, gag ; Genes, Viral ; Humans ; RNA-Directed DNA Polymerase/genetics ; Retroviridae/classification/*genetics ; Viral Proteins/genetics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 11
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    Imaging elemental distribution and ion transport in cultured cells with ion microscopy (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-28
    Description: Both elemental distribution and ion transport in cultured cells have been imaged by ion microscopy. Morphological and chemical information was obtained with a spatial resolution of approximately 0.5 micron for sodium, potassium, calcium, and magnesium in freeze-fixed, cryofractured, and freeze-dried normal rat kidney cells and Chinese hamster ovary cells. Ion transport was successfully demonstrated by imaging Na+-K+ fluxes after the inhibition of Na+- and K+ -dependent adenosine triphosphatase with ouabain. This method allows measurements of elemental (isotopic) distribution to be related to cell morphology, thereby providing the means for studying ion distribution and ion transport under different physiological, pathological, and toxicological conditions in cell culture systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chandra, S -- Morrison, G H -- R01GM24314/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 28;228(4707):1543-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990033" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/analysis ; Cell Line ; Cells, Cultured ; Cricetinae ; Elements/*analysis ; Female ; Freeze Fracturing ; Kidney/*ultrastructure ; Magnesium/analysis ; Microscopy/methods ; Ouabain/pharmacology ; Ovary/*ultrastructure ; Potassium/analysis ; Rats ; Sodium/analysis ; Sodium-Potassium-Exchanging ATPase/antagonists & inhibitors ; Tissue Distribution
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  • 12
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    Disorganization of cultured vascular endothelial cell monolayers by fibrinogen fragment D (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-03-22
    Description: Fibrinogen fragment D, which is heterogeneous, has several important biological functions. Human fibrinogen fragments D94 (molecular weight, 94,000), D78 (78,000), and E (52,000) were purified. Fragments D78 and D94 but not purified fibrinogen or fragment E specifically caused disorganization of bovine aortic endothelial cells cultured as monolayers. Within 2 hours of exposure to pathophysiological concentrations of fragment D, the confluent endothelial cells retracted from each other and projected pseudopodia. These disturbed cells subsequently became rounded and detached from the substrate. The actin present in stress fibers in stationary monolayer cells was diffusely redistributed in cells with fragment D-induced alterations in morphology. This effect was not observed in monolayers of kidney epithelial cells. The results demonstrate a specific effect of fibrinogen fragment D on the disorganization of cultured vascular endothelial cell monolayers and suggest that fragment D plays a role in the pathogenesis of syndromes with vascular endothelial damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dang, C V -- Bell, W R -- Kaiser, D -- Wong, A -- New York, N.Y. -- Science. 1985 Mar 22;227(4693):1487-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4038818" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/analysis ; Animals ; Aorta ; Cattle ; Cell Adhesion/drug effects ; Cell Line ; Cells, Cultured ; Cytoskeleton/drug effects ; Endothelium/analysis/*cytology/drug effects/ultrastructure ; Epithelial Cells ; Fibrin Fibrinogen Degradation Products/*pharmacology ; Humans ; Kidney ; Pseudopodia/drug effects
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  • 13
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    Inhibition of lymphocyte proliferation by a synthetic peptide homologous to retroviral envelope proteins (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-25
    Description: The retroviral transmembrane envelope protein p15E is immunosuppressive in that it inhibits immune responses of lymphocytes, monocytes, and macrophages. A region of p15E has been conserved among murine and feline retroviruses; a homologous region is also found in the transmembrane envelope proteins of the human retroviruses HTLV-I and HTLV-II and in a putative envelope protein encoded by an endogenous C-type human retroviral DNA. A peptide (CKS-17) was synthesized to correspond to this region of homology and was examined for its effects on lymphocyte proliferation. CKS-17 inhibited the proliferation of an interleukin-2-dependent murine cytotoxic T-cell line as well as alloantigen-stimulated proliferation of murine and human lymphocytes. Four other peptides, representing different regions of virus proteins, were inactive. These results suggest that the immunosuppressive portion of retroviral transmembrane envelope proteins may reside, at least in part, in a-conserved sequence represented by the CKS-17 peptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cianciolo, G J -- Copeland, T D -- Oroszlan, S -- Snyderman, R -- P01-CA29589-02/CA/NCI NIH HHS/ -- R23-CA34671-02/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Oct 25;230(4724):453-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996136" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Deltaretrovirus/genetics ; Humans ; Leukemia Virus, Feline/genetics ; Leukemia Virus, Murine/genetics ; Lymphocyte Activation/*drug effects ; Lymphocyte Culture Test, Mixed ; Lymphocytes/drug effects ; Mice ; Mice, Inbred BALB C ; Peptides/*pharmacology ; Retroviridae/*genetics ; Spleen/cytology ; Viral Envelope Proteins/genetics/*pharmacology
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  • 14
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    Amino acid homology between the encephalitogenic site of myelin basic protein and virus: mechanism for autoimmunity (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-29
    Description: Amino acid sequence homology was found between viral and host encephalitogenic protein. Immune responses were then generated in rabbits by using the viral peptide that cross-reacts with the self protein. Mononuclear cell infiltration was observed in the central nervous systems of animals immunized with the viral peptide. Myelin basic protein (MBP) is a host protein whose encephalitogenic site of ten amino acids induces experimental allergic encephalomyelitis. By computer analysis, hepatitis B virus polymerase (HBVP) was found to share six consecutive amino acids with the encephalitogenic site of rabbit MBP. Rabbits given injections of a selected eight- or ten-amino acid peptide from HBVP made antibody that reacted with the predetermined sequences of HBVP and also with native MBP. Peripheral blood mononuclear cells from the immunized rabbits proliferated when incubated with either MBP or HBVP. Central nervous system tissue taken from these rabbits had a histologic picture reminiscent of experimental allergic encephalomyelitis. Thus, viral infection may trigger the production of antibodies and mononuclear cells that cross-react with self proteins by a mechanism termed molecular mimicry. Tissue injury from the resultant autoallergic event can take place in the absence of the infectious virus that initiated the immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fujinami, R S -- Oldstone, M B -- AG-04342/AG/NIA NIH HHS/ -- AI-07007/AI/NIAID NIH HHS/ -- NS-12428/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 29;230(4729):1043-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2414848" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Autoimmune Diseases/immunology ; Cross Reactions ; *DNA-Directed RNA Polymerases/immunology ; Encephalomyelitis, Autoimmune, Experimental/immunology/*microbiology ; Hepatitis B virus/analysis/*immunology ; *Myelin Basic Protein/immunology ; *Viral Proteins/immunology
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  • 15
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    Immunoglobulin heavy-chain enhancer requires one or more tissue-specific factors (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-01-18
    Description: Enhancer sequences are regulatory regions that greatly increase transcription of certain eukaryotic genes. An immunoglobulin heavy-chain variable gene segment is moved from a region lacking enhancer activity to a position adjacent to the known heavy-chain enhancer early in B-cell maturation. In lymphoid cells, the heavy-chain and SV40 enhancers bind a common factor essential for enhancer function. In contrast, fibroblast cells contain a functionally distinct factor that is used by the SV40 but not by the heavy-chain enhancer. The existence of different factors in these cells may explain the previously described lymphoid cell specificity of the heavy-chain enhancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mercola, M -- Goverman, J -- Mirell, C -- Calame, K -- GM29361/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jan 18;227(4684):266-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3917575" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibody Formation ; B-Lymphocytes/immunology ; Base Sequence ; Cell Line ; *Enhancer Elements, Genetic ; Fibroblasts/immunology ; *Genes, Regulator ; Humans ; Immunoglobulin Constant Regions/genetics ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin Variable Region/genetics ; Mice ; Transcription, Genetic
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  • 16
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    AIDS virology: a battle on many fronts (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Norman, C -- New York, N.Y. -- Science. 1985 Nov 1;230(4725):518-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2413546" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/diagnosis/*microbiology ; Antibodies, Monoclonal ; Antibodies, Viral/analysis ; Antigens, Viral/analysis/immunology ; Cell Line ; Cross Reactions ; Culture Techniques/methods ; Cytopathogenic Effect, Viral ; Deltaretrovirus/immunology/*isolation & purification ; Homosexuality ; Humans ; Lymphatic Diseases/microbiology ; Microscopy, Electron ; Patents as Topic/legislation & jurisprudence ; RNA-Directed DNA Polymerase/analysis ; Reagent Kits, Diagnostic ; T-Lymphocytes/microbiology ; Terminology as Topic ; United States ; Viral Core Proteins/immunology ; Viral Envelope Proteins/immunology
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  • 17
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    Differential control of U1 small nuclear RNA expression during mouse development (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-20
    Description: During normal mouse development the relative amounts of two types of U1 small nuclear RNA's (U1 RNA) change significantly. Fetal tissues have comparable levels of the two major types of mouse U1 RNA's, mU1a and mU1b, whereas most differentiated adult tissues contain only mU1a RNA's. Those adult tissues that also accumulate detectable amounts of embryonic (mU1b) RNA's (for example, testis, spleen, and thymus) contain a significant proportion of stem cells capable of further differentiation. Several strains of mice express minor sequence variants of U1 RNA's that are subject to the same developmental controls as the major types of adult and embryonic U1 RNA. The differential accumulation of embryonic U1 RNA's may influence the pattern of gene expression during early development and differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lund, E -- Kahan, B -- Dahlberg, J E -- CA 33453/CA/NCI NIH HHS/ -- GM 30220/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Sep 20;229(4719):1271-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2412294" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Animals ; Base Sequence ; Brain/*growth & development/metabolism ; Cell Line ; Embryonic and Fetal Development ; Liver/*growth & development/metabolism ; Male ; Mice ; Mice, Inbred ICR ; Neoplastic Stem Cells/metabolism ; Nucleic Acid Hybridization ; RNA/*biosynthesis ; RNA, Messenger/biosynthesis ; RNA, Small Nuclear ; Testis/*growth & development/metabolism
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  • 18
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    U1 small nuclear RNA genes are subject to dosage compensation in mouse cells (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-07-19
    Description: Multiple copies of a gene that encodes human U1 small nuclear RNA were introduced into mouse C127 cells with bovine papilloma virus as the vector. For some recombinant constructions, the human U1 gene copies were maintained extrachromosomally on the viral episome in an unrearranged fashion. The relative abundance of human and mouse U1 small nuclear RNA varied from one cell line to another, but in some lines human U1 RNA accounted for as much as one-third of the total U1. Regardless of the level of human U1 expression, the total amount of U1 RNA (both mouse and human) in each cell line was nearly the same relative to endogenous mouse 5S or U2 RNA. This result was obtained whether measurements were made of total cellular U1 or of only the U1 in small nuclear ribonucleoprotein particles that could be precipitated with antibody directed against the Sm antigen. The data suggest that the multigene families encoding mammalian U1 RNA are subject to some form of dosage compensation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mangin, M -- Ares, M Jr -- Weiner, A M -- GM09148/GM/NIGMS NIH HHS/ -- GM31073/GM/NIGMS NIH HHS/ -- GM31335/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jul 19;229(4710):272-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2409601" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoradiography ; Bovine papillomavirus 1/genetics ; Cell Line ; DNA, Recombinant ; *Dosage Compensation, Genetic ; Electrophoresis, Polyacrylamide Gel ; Genetic Vectors ; Humans ; Mice ; Plasmids ; RNA/*genetics/isolation & purification ; RNA, Small Nuclear ; Xenopus
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  • 19
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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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
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    Studies of the putative transforming protein of the type I human T-cell leukemia virus (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-21
    Description: The putative transforming protein of the type I human T-cell leukemia virus (HTLV-1) is a 40-kilodalton protein encoded by the X region and is termed p40XI. On the basis of both subcellular fractionation techniques and immunocytochemical analysis, it is now shown that p40XI is a nuclear protein with a relatively short half-life (120 minutes). It is synthesized de novo in considerable quantities in a human T-cell line infected with and transformed by the virus in vitro, and it is not packaged in detectable amounts in the extracellular virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Slamon, D J -- Press, M F -- Souza, L M -- Murdock, D C -- Cline, M J -- Golde, D W -- Gasson, J C -- Chen, I S -- CA 32737/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 21;228(4706):1427-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990027" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Polyomavirus Transforming ; Antigens, Viral, Tumor/immunology/*metabolism ; Cell Fractionation ; Cell Line ; Cell Nucleus/metabolism ; Cell Transformation, Viral ; Deltaretrovirus/*metabolism ; Half-Life ; Humans ; Immune Sera ; Precipitin Tests ; Viral Proteins/immunology/*metabolism
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  • 21
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    Diversity of circumsporozoite antigen genes from two strains of the malarial parasite Plasmodium knowlesi (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-08-23
    Description: The complete nucleotide sequence of the coding region of the circumsporozoite antigen gene (CS gene) of the Nuri strain of the malarial parasite Plasmodium knowlesi is presented. The gene from the Nuri strain exhibits a novel form of sequence diversity when compared to the CS gene from the H strain. Instead of the 12 tandem repeating 36-base pair units of the H strain, the Nuri strain contains 16 tandem repeating 27-base pair units of a different nucleotide sequence that encodes a different repeating peptide. In contrast, the 5' and 3' coding and noncoding sequences flanking the repeats are 98 percent conserved in both strains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharma, S -- Svec, P -- Mitchell, G H -- Godson, G N -- 1 R01 AI21496-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 23;229(4715):779-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4023712" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Protozoan/*genetics ; Antigens, Surface/genetics ; Base Sequence ; Genes ; Molecular Sequence Data ; Plasmodium/*genetics/immunology ; Protozoan Proteins/*genetics ; Repetitive Sequences, Nucleic Acid
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  • 22
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    Dissociation of antitumor potency from anthracycline cardiotoxicity in a doxorubicin analog (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-28
    Description: The search for new congeners of the leading anticancer drug doxorubicin has led to an analog that is approximately 1000 times more potent, noncardiotoxic at therapeutic dose levels, and non-cross-resistant with doxorubicin. The new anthracycline, 3'-deamino-3'-(3-cyano-4-morpholinyl)doxorubicin (MRA-CN), is produced by incorporation of the 3' amino group of doxorubicin in a new cyanomorpholinyl ring. The marked increase in potency was observed against human ovarian and breast carcinomas in vitro; it was not accompanied by an increase in cardiotoxicity in fetal mouse heart cultures. Doxorubicin and MRA-CN both produced typical cardiac ultrastructural and biochemical changes, but at equimolar concentrations. In addition, MRA-CN was not cross-resistant with doxorubicin in a variant of the human sarcoma cell line MES-SA selected for resistance to doxorubicin. Thus antitumor efficacy was dissociated from both cardiotoxicity and cross-resistance by this modification of anthracycline structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sikic, B I -- Ehsan, M N -- Harker, W G -- Friend, N F -- Brown, B W -- Newman, R A -- Hacker, M P -- Acton, E M -- CA 24543/CA/NCI NIH HHS/ -- CA 32250/CA/NCI NIH HHS/ -- CA 33303/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 28;228(4707):1544-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4012308" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antineoplastic Agents ; Breast Neoplasms/drug therapy ; Cell Line ; Chemical Phenomena ; Chemistry ; Dose-Response Relationship, Drug ; Doxorubicin/adverse effects/*analogs & derivatives/therapeutic use ; Female ; Heart/drug effects ; Humans ; Isoenzymes ; L-Lactate Dehydrogenase/analysis ; Mice ; Myocardium/enzymology ; Ovarian Neoplasms/drug therapy ; Pregnancy
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  • 23
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    Sequence of the immunodominant epitope for the surface protein on sporozoites of Plasmodium vivax (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-20
    Description: Plasmodium vivax is one of the four malaria parasites that cause disease in humans. The structure of the immunodominant repeating peptide of the circumsporozoite (CS) protein of P. vivax was determined. A fragment of P. vivax DNA that encodes this tandemly repeating epitope was isolated by use of an oligonucleotide probe whose sequence is thought to be conserved in CS protein genes. DNA sequence analysis of the P. vivax clone indicates that the CS repeat is nine amino acids in length (Gly-Asp-Arg-Ala-Asp-Gly-Gln-Pro-Ala). The structure of the repeating region was confirmed with synthetic peptides and monoclonal antibodies directed against P. vivax sporozoites. This information should allow synthesis of a vaccine for P. vivax that is similar to the one being tested for P. falciparum.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCutchan, T F -- Lal, A A -- de la Cruz, V F -- Miller, L H -- Maloy, W L -- Charoenvit, Y -- Beaudoin, R L -- Guerry, P -- Wistar, R Jr -- Hoffman, S L -- New York, N.Y. -- Science. 1985 Dec 20;230(4732):1381-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2416057" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Surface/*genetics ; Base Sequence ; DNA Restriction Enzymes ; Epitopes/*genetics ; *Genes ; Plasmodium vivax/*immunology ; Species Specificity
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  • 24
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    Trans-acting transcriptional regulation of human T-cell leukemia virus type III long terminal repeat (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-01-11
    Description: Human T-cell leukemia virus type III (HTLV-III) was recently identified as the probable etiologic agent of the acquired immune deficiency syndrome (AIDS). Here it is shown that, in human T-cell lines infected with HTLV-III, gene expression directed by the long terminal repeat sequence of this virus is stimulated by more than two orders of magnitude compared to matched uninfected cells. The rate of transcription of the HTLV-III long terminal repeat is more than 1000 times that of the SV40 early promoter in one infected cell line. Thus, HTLV-III, like HTLV-I, HTLV-II, and the bovine leukemia virus, is characterized by trans-activation of transcription in infected cells. The efficiency of trans-activation in the case of HTLV-III may account, at least in part, for the virulent nature of HTLV-III infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sodroski, J -- Rosen, C -- Wong-Staal, F -- Salahuddin, S Z -- Popovic, M -- Arya, S -- Gallo, R C -- Haseltine, W A -- CA07094/CA/NCI NIH HHS/ -- CA07580/CA/NCI NIH HHS/ -- CA36974/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jan 11;227(4683):171-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2981427" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/genetics/metabolism ; Cell Line ; Chloramphenicol O-Acetyltransferase ; DNA, Recombinant ; Deltaretrovirus/*genetics ; *Gene Expression Regulation ; Humans ; Operon ; Plasmids ; Transcription, Genetic ; Transfection
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  • 25
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    Cassette of eight exons shared by genes for LDL receptor and EGF precursor (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-17
    Description: The amino acid sequences of the human low-density lipoprotein (LDL) receptor and the human precursor for epidermal growth factor (EGF) show 33 percent identity over a stretch of 400 residues. This region of homologous is encoded by eight contiguous exons in each respective gene. Of the nine introns that separate these exons, five are located in identical positions in the two protein sequences. This finding suggests that the homologous region may have resulted from a duplication of an ancestral gene and that the two genes evolved further by recruitment of exons from other genes, which provided the specific functional domains of the LDL receptor and the EGF precursor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sudhof, T C -- Russell, D W -- Goldstein, J L -- Brown, M S -- Sanchez-Pescador, R -- Bell, G I -- HL 01287/HL/NHLBI NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- HL 31346/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 17;228(4701):893-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3873704" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Base Sequence ; Biological Evolution ; Cloning, Molecular ; Epidermal Growth Factor/*genetics ; Genes ; Humans ; Protein Precursors/genetics ; Receptors, LDL/*genetics ; Repetitive Sequences, Nucleic Acid
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  • 26
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    Recombinant human tumor necrosis factor-alpha: effects on proliferation of normal and transformed cells in vitro (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-22
    Description: Modulation of the growth of human and murine cell lines in vitro by recombinant human tumor necrosis factor-alpha (rTNF-alpha) and recombinant human interferon-gamma (rIFN-gamma) was investigated. rTNF-alpha had cytostatic or cytolytic effects on only some tumor cell lines. When administered together with rIFN-gamma, rTNF-alpha showed enhanced antiproliferative effects on a subset of the cell lines tested. In contrast to its effects on sensitive tumor cells, rTNF-alpha augmented the growth of normal diploid fibroblasts. Variations in the proliferative response induced by rTNF-alpha were apparently not due to differences in either the number of binding sites per cell or their affinity for rTNF-alpha. These observations indicate that the effects of rTNF-alpha on cell growth are not limited to tumor cells, but rather that this protein may have a broad spectrum of activities in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sugarman, B J -- Aggarwal, B B -- Hass, P E -- Figari, I S -- Palladino, M A Jr -- Shepard, H M -- New York, N.Y. -- Science. 1985 Nov 22;230(4728):943-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3933111" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division/*drug effects ; Cell Line ; Cell Survival/drug effects ; Cell Transformation, Neoplastic/pathology ; Drug Synergism ; Glycoproteins/*pharmacology ; Humans ; Interferon-gamma/pharmacology ; Mice ; Recombinant Proteins/*pharmacology ; Tumor Necrosis Factor-alpha
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  • 27
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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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    Reversal of oncogenesis by the expression of a major histocompatibility complex class I gene (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-04-05
    Description: The classical transplantation antigens (the major histocompatibility complex class I antigens) play a key role in host defense against cells expressing foreign antigens. Several naturally occurring tumors and virally transformed cells show an overall suppression of these surface antigens. Since the class I molecules are required in the presentation of neoantigens on tumor cells to the cytotoxic T lymphocytes, their absence from the cell surface may lead to the escape of these tumors from immunosurveillance. To test this possibility, a functional class I gene was transfected into human adenovirus 12-transformed mouse cells that do not express detectable levels of class I antigens; the transformants were tested for expression of the transfected gene and for changes in oncogenicity. The expression of a single class I gene, introduced by DNA-mediated gene transfer into highly tumorigenic adenovirus 12-transformed cells, was sufficient to abrogate the oncogenicity of these cells. This finding has important implications for the regulation of the malignant phenotype in certain tumors and for the potential modulation of oncogenicity through derepression of the endogenous class I genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanaka, K -- Isselbacher, K J -- Khoury, G -- Jay, G -- New York, N.Y. -- Science. 1985 Apr 5;228(4695):26-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3975631" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Neoplasm/immunology ; Cell Line ; Immunization ; *Major Histocompatibility Complex ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Neoplasm Transplantation ; Neoplasms, Experimental/genetics/*immunology ; Rats
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    Bovine leukemia virus-related antigens in lymphocyte cultures infected with AIDS-associated viruses (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-03-22
    Description: An earlier finding that lymphocytes from African patients with the acquired immune deficiency syndrome (AIDS) react with rabbit antiserum to purified antigens of bovine leukemia virus (BLV) prompted a study of the possible cross-reactions between a BLV-infected ovine cell line and human lymphocytes inoculated with a strain of lymphadenopathy syndrome-associated virus (LAV). A solid-phase radioimmunoassay was used to detect antigenic markers of the retroviruses. Crude extracts from short-term cultures of lymphocytes infected with LAV bound rabbit antisera to the LAV glycoprotein gp13 (molecular weight 13,000) and the BLV proteins p24 and gp51, but did not bind antibodies to the p24 of human T-cell leukemia virus type I (HTLV-I). Antiserum to LAV gp13 reacted with an ovine cell line producing BLV but also weakly with virus-free ovine cells. Lymphocyte cultures from four African patients with AIDS expressed BLV-related antigens within 6 to 10 days of culture, at the moment when particle-bound reverse transcriptase was produced. BLV-related antigens were induced in lymphocyte cultures from healthy individuals by addition of filtered supernatant or irradiated cells of the original culture. The antisera to BLV used in this study may prove useful for the detection of AIDS-associated viruses in short-term cultures of lymphocytes from AIDS patients or their contacts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thiry, L -- Sprecher-Goldberger, S -- Jacquemin, P -- Cogniaux, J -- Burny, A -- Bruck, C -- Portetelle, D -- Cran, S -- Clumeck, N -- New York, N.Y. -- Science. 1985 Mar 22;227(4693):1482-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2579433" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; Animals ; Antigens, Viral/analysis/*immunology ; Cell Line ; Cells, Cultured ; Cross Reactions ; Deltaretrovirus/*immunology ; Epitopes/immunology ; Humans ; Leukemia Virus, Bovine/*immunology ; Lymph Nodes/microbiology ; Lymphocytes/immunology/*microbiology ; Radioimmunoassay ; Retroviridae/*immunology ; Sheep ; Viral Proteins/immunology
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    HTLV x-gene product: requirement for the env methionine initiation codon (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-06-28
    Description: The human T-cell leukemia viruses (HTLV) are replication-competent retroviruses whose genomes contain gag, pol, and env genes as well as a fourth gene, termed x, which is believed to be the transforming gene of HTLV. The product of the x gene is now shown to be encoded by a 2.1-kilobase messenger RNA derived by splicing of at least two introns. By means of S1 nuclease mapping of this RNA and nucleic acid sequence analysis of a complementary DNA clone, the complete primary structure of the x-gene product has been determined. It is encoded by sequences containing the env initiation codon and one nucleotide of the next codon spliced to the major open reading frame of the HTLV-I and HTLV-II x gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wachsman, W -- Golde, D W -- Temple, P A -- Orr, E C -- Clark, S C -- Chen, I S -- CA 30388/CA/NCI NIH HHS/ -- CA 32737/CA/NCI NIH HHS/ -- CA 38597/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 28;228(4707):1534-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990032" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Transformation, Viral ; Codon ; Deltaretrovirus/*genetics ; Electrophoresis, Polyacrylamide Gel ; Humans ; Methionine/*genetics ; Rats ; Viral Proteins/*analysis
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    A model for fibrinogen: domains and sequence (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-12-20
    Description: Electron microscopy of rotary-shadowed fibrinogen demonstrates that the molecules modified for crystallization by limited cleavage with a bacterial protease retain the major features of the native structure. This evidence, together with image processing and x-ray analysis of the crystals and of fibrin, has been used to develop a three-dimensional low resolution model for the molecule. The data indicate that the two large end domains of the molecule would be composed of the carboxyl-terminus of the B beta chain (proximal) and gamma chain (distal), respectively; the carboxyl-terminus of the A alpha chain would fold back to form an additional central domain. On this basis, the carboxyl-terminal region of each of the three chains of fibrinogen is folded independently into a globular domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weisel, J W -- Stauffacher, C V -- Bullitt, E -- Cohen, C -- AM17346/AM/NIADDK NIH HHS/ -- GM07596-07/GM/NIGMS NIH HHS/ -- HL30954/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Dec 20;230(4732):1388-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4071058" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Computers ; Fibrinogen/*metabolism ; Microscopy, Electron ; Models, Molecular ; Protein Conformation
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    Human immunoglobulin D: genomic sequence of the delta heavy chain (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-05-10
    Description: The DNA coding for the human immunoglobulin D(IgD) heavy chain (delta, delta) has been sequenced including the membrane and secreted termini. Human delta, like that of the mouse, has a separate exon for the carboxyl terminus of the secreted form. This feature of human and mouse IgD distinguishes it from all other immunoglobulins regardless of species or class. The human gene is different from that of the mouse; it has three, rather than two, constant region domains; and its lengthy hinge is encoded by two exons rather than one. Except for the third constant region, the human and mouse genes are only distantly related.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉White, M B -- Shen, A L -- Word, C J -- Tucker, P W -- Blattner, F R -- AI18016/AI/NIAID NIH HHS/ -- CA31013-04/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 10;228(4700):733-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3922054" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Humans ; Immunoglobulin D/*genetics ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin delta-Chains/*genetics ; Lymphocytes/metabolism ; Mice ; RNA, Messenger/genetics ; Species Specificity
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  • 33
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    Human GM-CSF: molecular cloning of the complementary DNA and purification of the natural and recombinant proteins (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-05-17
    Description: Clones of complementary DNA encoding the human lymphokine known as granulocyte-macrophage colony-stimulating factor (GM-CSF) were isolated by means of a mammalian cell (monkey COS cell) expression screening system. One of these clones was used to produce recombinant GM-CSF in mammalian cells. The recombinant hematopoietin was similar to the natural product that was purified to apparent homogeneity from medium conditioned by a human T-cell line. The human T-cell GM-CSF was found to be 60 percent homologous with the GM-CSF recently cloned from murine lung messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wong, G G -- Witek, J S -- Temple, P A -- Wilkens, K M -- Leary, A C -- Luxenberg, D P -- Jones, S S -- Brown, E L -- Kay, R M -- Orr, E C -- New York, N.Y. -- Science. 1985 May 17;228(4701):810-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3923623" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; *Cloning, Molecular ; Colony-Stimulating Factors/biosynthesis/*genetics/isolation & purification ; *Dna ; DNA, Recombinant ; *Granulocytes ; Haplorhini ; Humans ; *Macrophages ; RNA, Messenger/genetics ; T-Lymphocytes ; Transfection
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  • 34
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    Transformation of human bronchial epithelial cells transfected by Harvey ras oncogene (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-03-08
    Description: Transfection of normal human bronchial epithelial (NHBE) cells with a plasmid carrying the ras oncogene of Harvey murine sarcoma virus (v-Ha ras) changed the growth requirements, terminal differentiation, and tumorigenicity of the recipient cells. One of the cell lines isolated after transfection (TBE-1) was studied extensively and shown to contain v-Ha ras DNA. Total cellular RNA from TBE-1 cells hybridized to v-Ha ras structural gene fragment probes five to eight times more than RNA from parental NHBE cells. The TBE-1 cells expressed phosphorylated v-Ha ras polypeptide p21, showed a reduced requirement for growth-factor supplements, and became aneuploid as an early cellular response to v-Ha ras expression. As the transfectants acquire an indefinite life-span and anchorage independence they became transplantable tumor cells and showed many phenotypic changes suggesting a pleiotropic mechanism for the role of Ha ras in human carcinogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoakum, G H -- Lechner, J F -- Gabrielson, E W -- Korba, B E -- Malan-Shibley, L -- Willey, J C -- Valerio, M G -- Shamsuddin, A M -- Trump, B F -- Harris, C C -- New York, N.Y. -- Science. 1985 Mar 8;227(4691):1174-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3975607" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bronchi/*cytology/microbiology ; Carcinoma, Bronchogenic/genetics ; Cell Line ; Cell Transformation, Neoplastic/metabolism ; *Cell Transformation, Viral ; Culture Media ; DNA, Neoplasm/genetics ; Epithelial Cells ; Epithelium/microbiology ; Humans ; Lung Neoplasms/genetics ; Mice ; Mice, Nude ; Nucleic Acid Hybridization ; *Oncogenes ; Rats ; *Transfection
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  • 35
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    Expression of Plasmodium falciparum circumsporozoite proteins in Escherichia coli for potential use in a human malaria vaccine (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-05-24
    Description: The circumsporozoite (CS) protein of the human malaria parasite Plasmodium falciparum may be the most promising target for the development of a malaria vaccine. In this study, proteins composed of 16, 32, or 48 tandem copies of a tetrapeptide repeating sequence found in the CS protein were efficiently expressed in the bacterium Escherichia coli. When injected into mice, these recombinant products resulted in the production of high titers of antibodies that reacted with the authentic CS protein on live sporozoites and blocked sporozoite invasion of human hepatoma cells in vitro. These CS protein derivatives are therefore candidates for a human malaria vaccine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Young, J F -- Hockmeyer, W T -- Gross, M -- Ballou, W R -- Wirtz, R A -- Trosper, J H -- Beaudoin, R L -- Hollingdale, M R -- Miller, L H -- Diggs, C L -- New York, N.Y. -- Science. 1985 May 24;228(4702):958-62.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2988125" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antibody Formation ; Antigens, Surface/genetics/*immunology ; Carcinoma, Hepatocellular ; Cell Line ; Cloning, Molecular ; Cross Reactions ; DNA, Recombinant ; Escherichia coli/genetics ; Humans ; Liver Neoplasms ; Malaria/*prevention & control ; Mice ; Plasmodium/immunology ; Plasmodium falciparum/genetics/*immunology/physiology ; *Protozoan Proteins ; Vaccines/*immunology
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  • 36
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    Superinduction of c-fos by nerve growth factor in the presence of peripherally active benzodiazepines (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-09-20
    Description: Alterations in proto-oncogene expression after stimulation of rat pheochromocytoma (PC12) cells by nerve growth factor (NGF) have been investigated. A specific stimulation of c-fos messenger RNA and protein was detected 30 minutes after treatment. This induction was enhanced more than 100-fold in the presence of peripherally active benzodiazepines. The effect was specific as very little change was observed in the levels of c-rasHa, c-rasKi, c-myc, and N-myc messenger RNA's. Under the conditions used here, NGF treatment ultimately results in neurite outgrowth, with a reduction or cessation of cell division. Thus, stimulation of the c-fos gene in this system appeared to be associated with differentiation and not with cellular proliferation. The effect of benzodiazepines was stereospecific and represents a novel action of these compounds at the level of gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Curran, T -- Morgan, J I -- New York, N.Y. -- Science. 1985 Sep 20;229(4719):1265-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4035354" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Benzodiazepines/*pharmacology ; Cell Line ; Cell Transformation, Neoplastic/drug effects ; Gene Expression Regulation/*drug effects ; Nerve Growth Factors/*pharmacology ; *Oncogenes ; Pheochromocytoma/genetics/metabolism ; RNA, Messenger/biosynthesis ; Rats
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  • 37
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    Alignment of rat cardionatrin sequences with the preprocardionatrin sequence from complementary DNA (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-04-19
    Description: Mammalian atria contain peptides that promote the excretion of salt and water from the kidney. When rat atrial tissue is extracted under conditions known to inhibit proteolysis, four natriuretic peptides, cardionatrins I to IV, are consistently isolated. These peptides derive from a common precursor, preprocardionatrin, of 152 amino acids, whose sequence was determined by DNA sequencing of a complementary DNA clone. Amino acid sequencing located the start points of cardionatrins I, III, and IV in the overall sequence. Cardionatrin IV most closely resembles procardionatrin because it begins immediately after the signal sequence at residue 25. Cardionatrin III begins at residue 73, and cardionatrin I, sequenced previously, begins at residue 123. Compositional analysis indicated that each of these cardionatrins extends up to tyrosine at position 150 but lacks the terminal two arginine residues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flynn, T G -- Davies, P L -- Kennedy, B P -- de Bold, M L -- de Bold, A J -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):323-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3157217" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Atrial Function ; Atrial Natriuretic Factor ; Base Sequence ; Chromatography, High Pressure Liquid ; DNA/*genetics ; Electrophoresis, Polyacrylamide Gel ; Molecular Sequence Data ; Muscle Proteins/*genetics/isolation & purification ; *Peptide Fragments ; Protein Precursors/*genetics/isolation & purification ; Rats
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    Contribution of promoter to tissue-specific expression of the mouse immunoglobulin kappa gene (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-09-13
    Description: The immunoglobulin kappa (kappa) gene promoter was activated by a "neutral" enhancer derived from Harvey murine sarcoma virus (HaMuSV) in immunoglobulin-producing myeloma cells, regardless of the enhancer's orientation or position in the vector. In one fibroblast line (3T3) the immunoglobulin kappa gene promoter was completely inactive when linked to the HaMuSV enhancer, whereas in mouse L cells, promoter activity was observed only with the HaMuSV enhancer in tandem with the immunoglobulin kappa gene promoter. The differential behavior of the gene promoter, when activated by a neutral enhancer in these three murine cell lines, suggests that promoter sequences contribute to the tissue-specific expression of this gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gopal, T V -- Shimada, T -- Baur, A W -- Nienhuis, A W -- New York, N.Y. -- Science. 1985 Sep 13;229(4718):1102-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994213" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Transformation, Viral ; Fibroblasts/analysis ; *Gene Expression Regulation ; Immunoglobulin Light Chains/*genetics ; Immunoglobulin kappa-Chains/*genetics ; Mice ; Multiple Myeloma/metabolism ; *Operon ; Sarcoma Viruses, Murine
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  • 39
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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)
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    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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  • 40
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    cis- and trans-acting transcriptional regulation of visna virus (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-08-02
    Description: Visna virus is a pathogenic lentivirus of sheep that is related to human T-cell lymphotropic virus type III (HTLV-III), the probable etiologic agent of the acquired immune deficiency syndrome (AIDS). The transcriptional activity of visna virus promoter and enhancer sequences was studied by means of an assay based on the transient expression of the bacterial gene chloramphenicol acetyltransferase (CAT). The results suggest that the high level of expression of visna virus is due in part to cis-acting enhancer sequences that give the viral promoter a high level of transcriptional activity. In addition, the rate of transcription from the visna virus promoter situated in a plasmid expressing the CAT gene was much greater in infected than uninfected cells. This phenomenon of trans-acting transcriptional activation may involve either virally or cellularly encoded factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hess, J L -- Clements, J E -- Narayan, O -- NS-15721/NS/NINDS NIH HHS/ -- NS-16145/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 2;229(4712):482-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990051" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/genetics ; Animals ; Base Sequence ; Cell Line ; Chloramphenicol O-Acetyltransferase ; Choroid Plexus ; Chromosome Mapping ; Enhancer Elements, Genetic ; *Genes, Regulator ; Goats ; Humans ; L Cells (Cell Line) ; Macrophages ; Mice ; Plasmids ; Promoter Regions, Genetic ; Sheep ; Synovial Membrane ; T-Lymphocytes ; *Transcription, Genetic ; Transfection ; Visna-maedi virus/*genetics
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    Three-dimensional structure of poliovirus at 2.9 A resolution (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-27
    Description: The three-dimensional structure of poliovirus has been determined at 2.9 A resolution by x-ray crystallographic methods. Each of the three major capsid proteins (VP1, VP2, and VP3) contains a "core" consisting of an eight-stranded antiparallel beta barrel with two flanking helices. The arrangement of beta strands and helices is structurally similar and topologically identical to the folding pattern of the capsid proteins of several icosahedral plant viruses. In each of the major capsid proteins, the "connecting loops" and NH2- and COOH-terminal extensions are structurally dissimilar. The packing of the subunit "cores" to form the virion shell is reminiscent of the packing in the T = 3 plant viruses, but is significantly different in detail. Differences in the orientations of the subunits cause dissimilar contacts at protein-protein interfaces, and are also responsible for two major surface features of the poliovirion: prominent peaks at the fivefold and threefold axes of the particle. The positions and interactions of the NH2- and COOH-terminal strands of the capsid proteins have important implications for virion assembly. Several of the "connecting loops" and COOH-terminal strands form prominent radial projections which are the antigenic sites of the virion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hogle, J M -- Chow, M -- Filman, D J -- AI-20566/AI/NIAID NIH HHS/ -- AI-22346/AI/NIAID NIH HHS/ -- NS-07078/NS/NINDS NIH HHS/ -- R01 AI020566/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Sep 27;229(4720):1358-65.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994218" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/immunology ; Capsid/physiology ; Chemical Phenomena ; Chemistry ; HeLa Cells/microbiology ; Mutation ; Poliovirus/physiology/*ultrastructure ; Protein Conformation ; Virus Replication ; X-Ray Diffraction
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    The human gene encoding GM-CSF is at 5q21-q32, the chromosome region deleted in the 5q- anomaly (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-13
    Description: Human granulocyte-macrophage colony-stimulating factor (GM-CSF) is a 22,000-dalton glycoprotein that stimulates the growth of myeloid progenitor cells and acts directly on mature neutrophils. A full-length complementary DNA clone encoding human GM-CSF was used as a probe to screen a human genomic library and isolate the gene encoding human GM-CSF. The human GM-CSF gene is approximately 2.5 kilobase pairs in length with at least three intervening sequences. The GM-CSF gene was localized by somatic cell hybrid analysis and in situ hybridization to human chromosome region 5q21-5q32, which is involved in interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. An established, human promyelocytic leukemia cell line, HL60, contains a rearranged, partially deleted GM-CSF allele and a candidate 5q- marker chromosome, indicating that the truncated GM-CSF allele may reside at the rejoining point for the interstitial deletion on the HL60 marker chromosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huebner, K -- Isobe, M -- Croce, C M -- Golde, D W -- Kaufman, S E -- Gasson, J C -- CA-10805/CA/NCI NIH HHS/ -- CA-16685/CA/NCI NIH HHS/ -- CA-21124/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Dec 13;230(4731):1282-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2999978" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia/genetics ; Base Sequence ; Cell Line ; Chromosome Aberrations/*genetics ; Chromosome Deletion ; Chromosome Disorders ; Chromosome Mapping ; *Chromosomes, Human, 4-5 ; Colony-Stimulating Factors/*genetics ; DNA Restriction Enzymes ; Genes ; Granulocytes ; Humans ; Leukemia, Myeloid, Acute/genetics ; Macrophages ; Syndrome
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    The generative grammar of the immune system (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jerne, N K -- New York, N.Y. -- Science. 1985 Sep 13;229(4718):1057-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4035345" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies/analysis ; Humans ; *Immune System ; Lymphocytes/physiology ; Mice
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  • 44
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    Partial primary structure of the alpha and beta chains of human tumor T-cell receptors (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-01-18
    Description: The T-cell receptor for antigen (Ti) was purified from the human tumor cell line HPB-ALL. Amino-terminal sequence analysis of an acid-cleaved peptide of the Ti alpha chain showed that it is highly homologous to a putative murine alpha chain recently described. Amino-terminal sequence analysis of the Ti beta chain revealed that it shares 50 percent homology with the Ti beta chain amino acid sequences from two other human T-cell tumors. Nucleotide sequence analysis of a complementary DNA clone encoding the Ti beta chain from the HPB-MLT cell line showed that this chain represents a second human constant region gene segment and suggested that it arises from direct joining of the variable and joining gene segments without any intervening D region sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, N -- Leiden, J -- Dialynas, D -- Fraser, J -- Clabby, M -- Kishimoto, T -- Strominger, J L -- Andrews, D -- Lane, W -- Woody, J -- 5 R01 AI15669/AI/NIAID NIH HHS/ -- AI10736/AI/NIAID NIH HHS/ -- Y001CP00502/CP/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jan 18;227(4684):311-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3871253" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Humans ; Immunoglobulin Constant Regions/genetics ; Leukemia, Lymphoid/immunology ; Lymphoma/immunology ; Mice ; Nucleic Acid Hybridization ; Receptors, Antigen, T-Cell/*genetics ; T-Lymphocytes/*immunology
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  • 45
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    Control of cytochrome P1-450 gene expression by dioxin (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-03-22
    Description: The environmental contaminant 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) may produce its effects by altering gene expression in susceptible cells. In mouse hepatoma cells, TCDD induces the transcription of the cytochrome P1-450 gene, whose product, aryl hydrocarbon hydroxylase, contributes both to the detoxification and to the metabolic activation of carcinogenic polycyclic aromatic hydrocarbons. A DNA fragment containing sequences flanking the 5' end of the cytochrome P1-450 gene was isolated and analyzed. This DNA fragment contains a cis-acting control element with at least three functional domains: a putative promoter, an inhibitory domain upstream from the promoter that blocks its function, and a TCDD-responsive domain still farther (1265 to 1535 base pairs) upstream of the promoter. These findings, together with results from earlier studies, imply that transcription of the cytochrome P1-450 gene is under both positive and negative control by at least two trans-acting regulatory factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, P B -- Galeazzi, D R -- Fisher, J M -- Whitlock, J P Jr -- CA09302/CA/NCI NIH HHS/ -- CA32786/CA/NCI NIH HHS/ -- GM07149/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Mar 22;227(4693):1499-502.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3856321" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/biosynthesis/genetics ; Animals ; Cell Line ; Chloramphenicol O-Acetyltransferase ; Cytochrome P-450 Enzyme System/*genetics ; DNA, Recombinant ; Dioxins/*pharmacology ; Enzyme Induction ; Gene Expression Regulation/*drug effects ; *Genes, Regulator ; Liver Neoplasms, Experimental ; Mice ; *Promoter Regions, Genetic ; Tetrachlorodibenzodioxin/*pharmacology ; Transcription Factors/metabolism ; Transcription, Genetic/drug effects ; Transfection
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  • 46
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    Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-04
    Description: A 2.7 angstrom resolution x-ray diffraction analysis of a trypsin-modified form of the Escherichia coli elongation factor Tu reveals that the GDP-binding domain has a structure similar to that of other nucleotide-binding proteins. The GDP ligand is located at the COOH-terminal end of the beta sheet and is linked to the protein via a Mg2+ ion salt bridge. The location of the guanine ring is unusual; the purine ring is located on the outer edge of the domain, not deep within a hydrophobic pocket. The amino acids from Pro10 to Arg44 and from Gly59 to Glu190 have been assigned to the electron density with computer graphic techniques, and the resulting model is consistent with all known biochemical data. An analysis of the structure reveals that four regions of the amino acid sequence that are homologous with the family of ras oncogene proteins, termed p21, are located in the vicinity of the GDP-binding site, and most of the invariant amino acids shared by the proteins interact directly with the GDP ligand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jurnak, F -- GM 26895/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Oct 4;230(4721):32-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3898365" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/*analysis ; Binding Sites ; Chemistry, Physical ; Computers ; Escherichia coli ; Fourier Analysis ; Guanine Nucleotides/*analysis ; Guanosine Diphosphate/*analysis ; Magnesium/metabolism ; *Oncogenes ; Peptide Elongation Factor Tu ; Peptide Elongation Factors/*analysis ; Physicochemical Phenomena ; Protein Conformation ; Trypsin/metabolism ; X-Ray Diffraction
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  • 47
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    Human dioxin-inducible cytochrome P1-450: complementary DNA and amino acid sequence (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-05
    Description: Induction of cytochrome P1-450 has been linked to susceptibility to certain chemically induced cancers in mouse and man. Treatment of the human cell line MCF-7 with 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) results in high levels of aryl hydrocarbon (benzo[a]pyrene) hydroxylase (P1-450) activity. This cell line was used to isolate a human P1-450 full-length complementary DNA (cDNA) clone. The cDNA is 2566 nucleotides in length, encodes a polyadenylated messenger RNA (2.8 kilobases in length), and has a continuous reading frame producing a protein with 512 residues (molecular weight, 58,151). The human P1-450 cDNA and protein are 63 percent and 80 percent similar to mouse P1-450 cDNA and protein, respectively. Whereas the mouse TCDD-inducible P-450 gene subfamily has two members (P1-450 and P3-450), the human TCDD-inducible gene subfamily appears to have only one gene (P1-450).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jaiswal, A K -- Gonzalez, F J -- Nebert, D W -- New York, N.Y. -- Science. 1985 Apr 5;228(4695):80-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3838385" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carcinogens/pharmacology ; Cell Line ; Cricetinae ; Cytochrome P-450 Enzyme System/*genetics ; DNA/*genetics ; Dioxins/*pharmacology ; Enzyme Induction ; Humans ; Mice ; Nucleic Acid Hybridization ; Rabbits ; Tetrachlorodibenzodioxin/*pharmacology
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  • 48
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    Transfection of v-rasH DNA into MCF-7 human breast cancer cells bypasses dependence on estrogen for tumorigenicity (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-10
    Description: The natural history of estrogen-responsive breast cancers often involves a phenotypic change to an estrogen-unresponsive, more aggressive tumor. The human breast cancer cell line, MCF-7, which requires estradiol for tumor formation in vivo and shows growth stimulation in response to estradiol in vitro, is a model for hormone-responsive tumors. The v-rasH onc gene was transfected into MCF-7 cells. The cloned MCF-7ras transfectants, which expressed the v-rasH messenger RNA and v-rasH p21 protein (21,000 daltons), were characterized. In contrast to the parental cell line, MCF-7ras cells no longer responded to exogenous estrogen in culture and their growth was minimally inhibited by exogenous antiestrogens. When tested in the nude mouse, the MCF-7ras cells were fully tumorigenic in the absence of estrogen supplementation. Thus, cells acquiring an activated onc gene can bypass the hormonal regulatory signals that trigger the neoplastic growth of a human breast cancer cell line.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kasid, A -- Lippman, M E -- Papageorge, A G -- Lowy, D R -- Gelmann, E P -- New York, N.Y. -- Science. 1985 May 10;228(4700):725-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4039465" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Breast Neoplasms/chemically induced/*genetics ; Cell Line ; Cell Transformation, Neoplastic/*chemically induced ; DNA, Neoplasm/genetics ; Estrogens/*pharmacology ; Female ; Humans ; Mice ; Mice, Nude ; Neoplasms, Experimental/chemically induced/genetics ; *Oncogenes ; Pyrrolidines/pharmacology ; Repetitive Sequences, Nucleic Acid ; Thiophenes/pharmacology ; *Transfection
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    Molecular cloning of a complementary DNA encoding human macrophage-specific colony-stimulating factor (CSF-1) (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-18
    Description: Complementary DNA (cDNA) clones encoding human macrophage-specific specific colony-stimulating factor (CSF-1) were isolated. One cDNA clone codes for a mature polypeptide of 224 amino acids and a putative leader of 32 amino acids. This cDNA, which was cloned in the Okayama-Berg expression vector, specifies the synthesis of biologically active CSF-1 in COS cells, as determined by a specific radioreceptor assay, macrophage bone marrow colony formation, and antibody neutralization. Most of the cDNA isolates contain part of an intron sequence that changes the reading frame, resulting in an abrupt termination of translation; these cDNA's were inactive in COS cells. The CSF-1 appears to be encoded by a single-copy gene, but its expression results in the synthesis of several messenger RNA species, ranging in size from about 1.5 to 4.5 kilobases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawasaki, E S -- Ladner, M B -- Wang, A M -- Van Arsdell, J -- Warren, M K -- Coyne, M Y -- Schweickart, V L -- Lee, M T -- Wilson, K J -- Boosman, A -- C32551/PHS HHS/ -- New York, N.Y. -- Science. 1985 Oct 18;230(4723):291-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996129" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; *Cloning, Molecular ; Colony-Stimulating Factors/*genetics ; DNA/*metabolism ; DNA Restriction Enzymes ; *Genes ; Humans ; Macrophages/*metabolism ; Pancreatic Neoplasms ; RNA, Messenger/genetics ; Transcription, Genetic
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    Pathways of protein secretion in eukaryotes (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-10-04
    Description: Protein secretion from cells can take several forms. Secretion is constitutive if proteins are secreted as fast as they are synthesized. In regulated secretion newly synthesized proteins destined for secretion are stored at high concentration in secretory vesicles until the cell receives an appropriate stimulus. When both constitutive and regulated protein secretion can take place in the same cell a mechanism must exist for sorting the correct secretory protein into the correct secretory vesicle. The secretory vesicle must then be delivered to the appropriate region of plasma membrane. Transfection of DNA encoding foreign secretory proteins into regulated secretory cells has provided insight into the specificity of sorting into secretory vesicles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kelly, R B -- New York, N.Y. -- Science. 1985 Oct 4;230(4721):25-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994224" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenocorticotropic Hormone/secretion ; Animals ; Calcium/metabolism ; Calmodulin/metabolism ; Carrier Proteins/physiology ; Cell Compartmentation ; Cell Fusion ; Cell Line ; Cells/*secretion ; Cytoplasmic Granules/metabolism ; Eukaryotic Cells/cytology/*secretion ; Exocytosis ; Golgi Apparatus/ultrastructure ; Half-Life ; Leukemia Virus, Murine/genetics ; Lysosomes/enzymology ; Membrane Proteins/genetics/metabolism ; Microscopy, Electron ; Models, Biological ; Peptide Hydrolases/metabolism ; Pituitary Gland/cytology ; Pro-Opiomelanocortin/secretion ; Proteins/*secretion ; Transfection
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    Amplification of a novel v-erbB-related gene in a human mammary carcinoma (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-06
    Description: The cellular gene encoding the receptor for epidermal growth factor (EGF) has considerable homology to the oncogene of avian erythroblastosis virus. In a human mammary carcinoma, a DNA sequence was identified that is related to v-erbB but amplified in a manner that appeared to distinguish it from the gene for the EGF receptor. Molecular cloning of this DNA segment and nucleotide sequence analysis revealed the presence of two putative exons in a DNA segment whose predicted amino acid sequence was closely related to, but different from, the corresponding sequence of the erbB/EGF receptor. Moreover, this DNA segment identified a 5-kilobase transcript distinct from the transcripts of the EGF receptor gene. Thus, a new member of the tyrosine kinase proto-oncogene family has been identified on the basis of its amplification in a human mammary carcinoma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, C R -- Kraus, M H -- Aaronson, S A -- New York, N.Y. -- Science. 1985 Sep 6;229(4717):974-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2992089" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Breast Neoplasms/*genetics ; Cell Line ; Cloning, Molecular ; DNA, Neoplasm/*genetics ; Female ; *Gene Amplification ; Gene Expression Regulation ; Humans ; *Oncogenes ; Protein Kinases/*genetics ; Protein-Tyrosine Kinases ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/*genetics
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    Insertion mutagenesis of embryonal carcinoma cells by retroviruses (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-03
    Description: Mutagenesis was studied in cultured F9 embryonal carcinoma cells infected with a variant of Moloney murine leukemia virus. Proviral insertion induced the inactivation of the hypoxanthine phosphoribosyltransferase locus, and the virus was used to isolate the mutated genes rapidly. Mutagenesis by these methods may be useful for the genetic dissection of the various mammalian cell phenotypes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, W -- Patel, M D -- Lobel, L I -- Goff, S P -- Nguyen-Huu, M C -- New York, N.Y. -- Science. 1985 May 3;228(4699):554-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3838595" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Line ; DNA/genetics ; DNA, Neoplasm/genetics ; DNA, Recombinant/metabolism ; DNA, Viral/genetics ; Mice ; Moloney murine leukemia virus/physiology ; *Mutation ; Nucleic Acid Hybridization ; Rats ; Retroviridae/*physiology ; Teratoma/*genetics/microbiology
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    Human apolipoprotein B: structure of carboxyl-terminal domains, sites of gene expression, and chromosomal localization (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-04
    Description: Apolipoprotein (apo-) B is the ligand responsible for the receptor-mediated catabolism of low density lipoproteins, the principal cholesterol-transporting lipoproteins in plasma. The primary structure of the carboxyl-terminal 30 percent (1455 amino acids) of human apo-B (apo-B100) has been deduced from the nucleotide sequence of complementary DNA. Portions of the protein structure that may relate to its receptor binding function and lipid binding properties have been identified. The apo-B100 messenger RNA is about 19 kilobases in length. The apo-B100 gene is expressed primarily in liver and, to a lesser extent, in small intestine, but in no other tissues. The gene for apo-B100 is located in the p24 region (near the tip of the short arm) of chromosome 2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knott, T J -- Rall, S C Jr -- Innerarity, T L -- Jacobson, S F -- Urdea, M S -- Levy-Wilson, B -- Powell, L M -- Pease, R J -- Eddy, R -- Nakai, H -- GM 20454/GM/NIGMS NIH HHS/ -- HO 05196/HO/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 Oct 4;230(4721):37-43.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994225" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Apolipoprotein B-100 ; Apolipoproteins B/analysis/*genetics ; Apolipoproteins E/analysis ; Base Sequence ; *Chromosome Mapping ; Chromosomes, Human, 1-3 ; DNA/analysis ; DNA Restriction Enzymes/metabolism ; Female ; *Gene Expression Regulation ; Haplorhini ; Humans ; Intestine, Small/metabolism ; Lipid Metabolism ; Lipoproteins, LDL/metabolism ; Liver/metabolism ; Mice ; RNA, Messenger/analysis ; Receptors, LDL/metabolism ; Structure-Activity Relationship
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    How do proteins find mitochondria? (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G -- New York, N.Y. -- Science. 1985 Jun 28;228(4707):1517-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4012306" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Transport ; Enzyme Precursors/metabolism ; Mitochondria/*metabolism ; Mitochondria, Liver/enzymology ; Ornithine Carbamoyltransferase/metabolism ; Peptides/*metabolism ; Protein Sorting Signals ; Proteins/*metabolism
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    Enhanced immunogenicity of the pre-S region of hepatitis B surface antigen (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-07
    Description: The 55 codons upstream of the gene sequence encoding the hepatitis B surface antigen (HBsAg) are called the pre-S(2) region. It has been proposed that polypeptides of high molecular weight that contain the pre-S(2) region should be included in future hepatitis B virus (HBV) vaccines. The pre-S(2) region and the S gene product [25 kilodalton (kD)] together compose a polypeptide of high molecular weight (33 kD). As an initial attempt to determine the relevance of the 33-kD polypeptide to development of an HBV vaccine, the murine immune response to pre-S(2)-encoded determinants as compared to S-encoded determinants on the same polypeptide was examined. The results indicate (i) the pre-S(2) region is significantly more immunogenic than the S region of HBsAg, (ii) the 26 amino acid residues at the NH2-terminus of the 33-kD polypeptide represent a dominant antibody binding site on the pre-S(2) region, (iii) the immune response to the pre-S(2) region is regulated by H-2-linked genes distinct from those that regulate the response to the S region, and (iv) immunization of an S region nonresponder strain with HBV envelope particles that contain both the pre-S(2) and S regions can circumvent nonresponsiveness to the S region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milich, D R -- Thornton, G B -- Neurath, A R -- Kent, S B -- Michel, M L -- Tiollais, P -- Chisari, F V -- AI 00585/AI/NIAID NIH HHS/ -- AI 20001/AI/NIAID NIH HHS/ -- AI 20720/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1195-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2408336" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibody Formation ; Antibody Specificity ; Epitopes ; Genes, MHC Class II ; Genes, Viral ; Hepatitis B Antibodies/immunology ; Hepatitis B Surface Antigens/genetics/*immunology ; Mice ; Molecular Weight ; Protein Precursors/genetics/immunology ; Viral Hepatitis Vaccines/*immunology ; Viral Proteins/genetics/immunology
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    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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    Enhanced transcription of c-myc in bursal lymphoma cells requires continuous protein synthesis (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-06
    Description: In several bursal lymphoma cell lines in which c-myc transcription is regulated by avian leukosis virus (ALV) long terminal repeat (LTR) sequences, protein synthesis inhibition decreases the transcriptional activity of c-myc as well as other LTR driven viral genes. This decrease in transcription is associated with a change in the chromatin structure of c-myc, as measured by deoxyribonuclease I (DNase I) hypersensitivity, and a shift of transcription from the LTR to the normal c-myc promoter. In contrast, cycloheximide had little or no effect on the transcription of LTR driven genes in infected chicken embryo fibroblasts treated with the drug. These results suggest that a labile, cell type-specific protein may interact with the retroviral LTR and regulate transcription of genes under LTR control. Further, the results demonstrate that the increase in intracellular concentration of c-myc RNA induced by cycloheximide treatment of normal cells is the result of stabilization of this message.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Linial, M -- Gunderson, N -- Groudine, M -- CA 18282/CA/NCI NIH HHS/ -- CA 28151/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Dec 6;230(4730):1126-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2999973" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avian Leukosis/genetics ; Avian Leukosis Virus ; Bursa of Fabricius/cytology ; Cell Line ; Chick Embryo ; Chickens ; Chromatin/drug effects ; Cycloheximide/pharmacology ; Dactinomycin/pharmacology ; Emetine/pharmacology ; Lymphoma/*genetics ; Neoplasm Proteins/*biosynthesis ; *Oncogenes ; RNA, Neoplasm/metabolism ; Repetitive Sequences, Nucleic Acid ; *Transcription, Genetic/drug effects
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    Sequence of the alpha subunit of photoreceptor G protein: homologies between transducin, ras, and elongation factors (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-05
    Description: A bovine retinal complementary DNA clone encoding the alpha subunit of transducin (T alpha) was isolated with the use of synthetic oligodeoxynucleotides as probes, and the complete nucleotide sequence of the insert was determined. THe predicted protein sequence of 354 amino acids includes the known sequences of four tryptic peptides and sequences adjacent to the residues that undergo adenosine diphosphate ribosylation by cholera toxin and pertussis toxin. On the basis of homologies to other proteins, such as the elongation factors of protein synthesis and the ras oncogene proteins, regions are identified that are predicted to be acylated and involved in guanine nucleotide binding and hydrolysis. Amino acid sequence similarity between T alpha and ras is confined to these regions of the molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lochrie, M A -- Hurley, J B -- Simon, M I -- New York, N.Y. -- Science. 1985 Apr 5;228(4695):96-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3856323" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Toxins/metabolism ; Base Sequence ; Cattle ; Cholera Toxin/metabolism ; Cloning, Molecular ; DNA/genetics ; Guanosine Triphosphate/metabolism ; Membrane Proteins/*genetics/metabolism ; *Oncogenes ; Peptide Elongation Factors/*genetics ; Pertussis Toxin ; Transducin ; Virulence Factors, Bordetella
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    Nucleotide sequence and expression of an AIDS-associated retrovirus (ARV-2) (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-02-01
    Description: The nucleotide sequence of molecular clones of DNA from a retrovirus, ARV-2, associated with the acquired immune deficiency syndrome (AIDS) was determined. Proviral DNA of ARV-2 (9737 base pairs) has long terminal repeat structures (636 base pairs) and long open reading frames encoding gag (506 codons), pol (1003 codons), and env (863 codons) genes. Two additional open reading frames were identified. Significant amino acid homology with several other retroviruses was noted in the predicted product of gag and pol, but ARV-2 was as closely related to murine and avian retroviruses as it was to human T-cell leukemia viruses (HTLV-I and HTLV-II). By means of an SV-40 vector in transfected simian cells, the cloned gag and env genes of ARV-2 were shown to express viral proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sanchez-Pescador, R -- Power, M D -- Barr, P J -- Steimer, K S -- Stempien, M M -- Brown-Shimer, S L -- Gee, W W -- Renard, A -- Randolph, A -- Levy, J A -- New York, N.Y. -- Science. 1985 Feb 1;227(4686):484-92.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2578227" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Codon ; DNA, Viral/*genetics ; Deltaretrovirus/genetics ; Gene Products, gag ; Genes, Viral ; Humans ; Nucleic Acid Conformation ; RNA-Directed DNA Polymerase/biosynthesis/genetics ; Repetitive Sequences, Nucleic Acid ; Retroviridae/*genetics ; Viral Envelope Proteins/biosynthesis/genetics ; Viral Proteins/biosynthesis/*genetics
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    Molecular cloning of the complementary DNA for human tumor necrosis factor (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-12
    Description: Tumor necrosis factor (TNF) is a soluble protein that causes damage to tumor cells but has no effect on normal cells. Human TNF was purified to apparent homogeneity as a 17.3-kilodalton protein from HL-60 leukemia cells and showed cytotoxic and cytostatic activities against various human tumor cell lines. The amino acid sequence was determined for the amino terminal end of the purified protein, and oligodeoxyribonucleotide probes were synthesized on the basis of this sequence. Complementary DNA (cDNA) encoding human TNF was cloned from induced HL-60 messenger RNA and was confirmed by hybrid-selection assay, direct expression in COS-7 cells, and nucleotide sequence analysis. The human TNF cDNA is 1585 base pairs in length and encodes a protein of 233 amino acids. The mature protein begins at residue 77, leaving a long leader sequence of 76 amino acids. Expression of high levels of human TNF in Escherichia coli was accomplished under control of the bacteriophage lambda PL promoter and gene N ribosome binding site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, A M -- Creasey, A A -- Ladner, M B -- Lin, L S -- Strickler, J -- Van Arsdell, J N -- Yamamoto, R -- Mark, D F -- New York, N.Y. -- Science. 1985 Apr 12;228(4696):149-54.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3856324" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cells, Cultured ; *Cloning, Molecular ; DNA/*genetics ; DNA, Recombinant/metabolism ; Glycoproteins/*genetics/isolation & purification/pharmacology ; Humans ; Leukemia, Myeloid/metabolism ; Mice ; Mice, Nude ; Neoplasms, Experimental/drug therapy ; Nucleic Acid Hybridization ; RNA, Messenger/genetics ; Rabbits ; Rats ; Tumor Necrosis Factor-alpha ; Xenopus
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    Atrial natriuretic factor: a hormone produced by the heart (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-15
    Description: Systematic studies on the significance of the secretory-like morphological characteristic of cardiac atrial muscle cells of mammals led to the finding that these cells produce a polypeptide hormone. This hormone, described in 1981 as atrial natriuretic factor (ANF), is diuretic (natriuretic), hypotensive, and has an inhibitory effect on renin and aldosterone secretion. Thus, ANF probably intervenes in the short- and long-term control of water and electrolyte balance and of blood pressure. Phylogenetically, ANF appears early, suggesting different functions for this peptide in accordance with each species' environment. Knowledge of the properties of the hormone should provide insights into the pathophysiology of important clinical entities and lead to the development of new pharmaceutical products.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Bold, A J -- New York, N.Y. -- Science. 1985 Nov 15;230(4727):767-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2932797" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amphibians ; Animals ; Atrial Function ; Atrial Natriuretic Factor/genetics/*physiology ; Birds ; Cattle ; Cytoplasmic Granules/ultrastructure ; Fishes ; Heart/*physiology ; Humans ; Microscopy, Electron ; Myocardium/cytology/ultrastructure ; Rats ; Reptiles ; Rodentia ; Sinoatrial Node/cytology/physiology
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    Bovine leukemia virus long terminal repeat: a cell type-specific promoter (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-01-18
    Description: The functional activity of the promoter unit contained within the long terminal repeat (LTR) of bovine leukemia virus (BLV) was examined by monitoring transient expression of a heterologous gene placed under its control. Various cell lines were transfected with recombinant plasmids carrying the bacterial chloramphenicol acetyltransferase (CAT) gene coupled to the BLV LTR (pBL-cat). Transient expression of CAT activity directed by the BLV LTR was observed only in the established BLV-producer cell lines derived from fetal lamb kidney (FLK) cells and bat lung cells. The amount of CAT activity transiently expressed in FLK-BLV cells was decreased approximately tenfold by deletion of LTR sequences located within a region 100 to 170 nucleotides upstream of the RNA start site. Surprisingly, removal of the region 50 base pairs downstream of the RNA initiation site to the 3'-end of the LTR reduced the expression of CAT activity by 87 percent. The BLV LTR thus appears to be an unusual promoter unit, functioning in a cell type-specific manner and possessing sequences on both the 5' and 3' sides of the RNA start site that influence gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Derse, D -- Caradonna, S J -- Casey, J W -- CA07392/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jan 18;227(4684):317-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2981431" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Cell Line ; Chiroptera ; DNA, Recombinant/metabolism ; Deltaretrovirus/genetics ; Genes, Regulator ; Haplorhini ; Humans ; Leukemia Virus, Bovine/*genetics ; *Promoter Regions, Genetic ; RNA, Viral/*genetics ; *Repetitive Sequences, Nucleic Acid ; Retroviridae/*genetics ; Sheep ; Transcription, Genetic
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    Individual tumors of multifocal EB virus-induced malignant lymphomas in tamarins arise from different B-cell clones (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-05-10
    Description: Cotton-top tamarins were inoculated with sufficient Epstein-Barr virus to induce multiple tumors in each animal within 14 to 21 days. The tumors consisted of large-cell lymphomas that contained multiple copies of the Epstein-Barr virus genome and generated Epstein-Barr virus-carrying cell lines showing no detectable consistent chromosomal abnormality. Hybridization of tumor DNA with immunoglobulin gene probes revealed that each lymphoma was oligo- or monoclonal in origin and that individual tumors from the same animal arose from different B-cell clones. Thus the virus induced multiple transformation events in tamarins in vivo to cause malignant tumors resembling the Epstein-Barr virus-associated lymphomas of patients with organ transplants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cleary, M L -- Epstein, M A -- Finerty, S -- Dorfman, R F -- Bornkamm, G W -- Kirkwood, J K -- Morgan, A J -- Sklar, J -- CA 34233/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 10;228(4700):722-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2986287" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/*microbiology ; Burkitt Lymphoma/genetics/*microbiology ; Cell Line ; DNA, Neoplasm/genetics ; Heart Transplantation ; Herpesvirus 4, Human ; Humans ; Neoplasms, Experimental/genetics/microbiology ; Nucleic Acid Hybridization ; Saguinus
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    Syrian hamster female protein: analysis of female protein primary structure and gene expression (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-07
    Description: The concentration in plasma of the female protein (FP) of the golden Syrian hamster is regulated by sex steroids and by mediators of the acute-phase response to tissue injury or inflammation. A complementary DNA (cDNA) clone corresponding to FP was isolated from a hamster liver cDNA library and used to determine the nucleotide sequence and derived amino acid sequence of native FP. The primary sequence of FP is 69 percent identical to human serum amyloid P component and 50 percent identical to human C-reactive protein. Evidence showed that sex-limited and acute-phase control of the FP gene is pretranslational. The FP protein is thus a useful model for investigating dual regulation of expression of a single gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dowton, S B -- Woods, D E -- Mantzouranis, E C -- Colten, H R -- AI20959/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1206-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2408337" target="_blank"〉PubMed〈/a〉
    Keywords: Acute-Phase Proteins ; Alpha-Globulins/*genetics ; Amino Acid Sequence ; Animals ; Base Sequence ; Blood Proteins/genetics ; *C-Reactive Protein ; Cricetinae/*physiology ; DNA/genetics ; Female ; Gene Expression Regulation ; Genes ; Liver/physiology ; Male ; Mesocricetus/*physiology ; RNA, Messenger/genetics
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    Redesigning trypsin: alteration of substrate specificity (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-04-19
    Description: A general method for modifying eukaryotic genes by site-specific mutagenesis and subsequent expression in mammalian cells was developed to study the relation between structure and function of the proteolytic enzyme trypsin. Glycine residues at positions 216 and 226 in the binding cavity of trypsin were replaced by alanine residues, resulting in three trypsin mutants. Computer graphic analysis suggested that these substitutions would differentially affect arginine and lysine substrate binding of the enzyme. Although the mutant enzymes were reduced in catalytic rate, they showed enhanced substrate specificity relative to the native enzyme. This increased specificity was achieved by the unexpected differential effects on the catalytic activity toward arginine and lysine substrates. Mutants containing alanine at position 226 exhibited an altered conformation that may be converted to a trypsin-like structure upon binding of a substrate analog.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Craik, C S -- Largman, C -- Fletcher, T -- Roczniak, S -- Barr, P J -- Fletterick, R -- Rutter, W J -- AM26081/AM/NIADDK NIH HHS/ -- GM07216/GM/NIGMS NIH HHS/ -- GM28520/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):291-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3838593" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; DNA/genetics ; Electrophoresis ; Mutation ; Rats ; Substrate Specificity ; Trypsin/biosynthesis/*genetics/metabolism ; Trypsinogen/metabolism
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    Model structure for the inflammatory protein C5a (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-05-31
    Description: The complement cleavage product C5a is a potent stimulant of inflammatory processes; thus, inhibition of C5a activity is of therapeutic interest. The three-dimensional structure of the major portion of C5a was modeled from the homologous C3a crystal structure by comparative modeling techniques. The model shows that core residues of C5a are completely conserved, while external residues differ from C3a. Even though the amino-terminal 12 residues of C3a are disordered in the crystal, this sequence in C5a may form an amphipathic helix. The distribution of species sequence differences in the complete C5a structure suggests a possible receptor binding site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greer, J -- New York, N.Y. -- Science. 1985 May 31;228(4703):1055-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3992245" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Complement C5/metabolism ; Complement C5a ; Crystallography ; Humans ; Hydrogen Bonding ; Models, Molecular ; Protein Conformation ; Receptors, Complement/metabolism ; Thermodynamics
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    Molecular cloning of complementary DNA for the alpha subunit of the G protein that stimulates adenylate cyclase (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-20
    Description: A complementary DNA clone encoding the alpha subunit of the adenylate cyclase stimulatory G protein (Gs) was isolated and identified. A bovine brain complementary DNA library was screened with an oligonucleotide probe derived from amino acid sequence common to known G proteins. The only clone that was obtained with this probe has a complementary DNA insert of approximately 1670 base pairs. An antibody to a peptide synthesized according to deduced amino acid sequence reacts specifically with the alpha subunit of Gs. In addition, RNA that hybridizes with probes made from the clone is detected in wild-type S49 cells; however, cyc- S49 cells, which are deficient in Gs alpha activity, are devoid of this messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harris, B A -- Robishaw, J D -- Mumby, S M -- Gilman, A G -- GM09731/GM/NIGMS NIH HHS/ -- GM34497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Sep 20;229(4719):1274-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3839937" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/*metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Cattle ; Cerebral Cortex ; *Cloning, Molecular ; DNA/*analysis ; Enzyme Activation ; Nerve Tissue Proteins/*genetics ; Nucleic Acid Hybridization ; Protein Biosynthesis ; Retina
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    Gene transfer and expression of human phenylalanine hydroxylase (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-05
    Description: Phenylketonuria (PKU) is caused by a genetic deficiency of the enzyme phenylalanine hydroxylase (PAH). A full-length complementary DNA clone of human PAH was inserted into a eukaryotic expression vector and transferred into mouse NIH3T3 cells which do not normally express PAH. The transformed mouse cells expressed PAH messenger RNA, immunoreactive protein, and enzymatic activity that are characteristic of the normal human liver products, demonstrating that a single gene contains all of the necessary genetic information to code for functional PAH. These results support the use of the human PAH probe in prenatal diagnosis and detection of carriers, to provide new opportunities for the biochemical characterization of normal and mutant enzymes, and in the investigation of alternative genetic therapies for PKU.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ledley, F D -- Grenett, H E -- DiLella, A G -- Kwok, S C -- Woo, S L -- HD-06495/HD/NICHD NIH HHS/ -- HD-17711/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 5;228(4695):77-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3856322" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cloning, Molecular ; DNA, Recombinant/metabolism ; *Genetic Engineering ; Humans ; Mice ; Nucleic Acid Hybridization ; Phenylalanine Hydroxylase/*genetics ; Phenylketonurias/diagnosis/genetics ; Prenatal Diagnosis ; Rats
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 69
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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
    Print ISSN: 0036-8075
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    Structure of the human interleukin-2 receptor gene (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-08
    Description: The gene encoding the human interleukin-2 (IL-2) receptor consists of 8 exons spanning more than 25 kilobases on chromosome 10. Exons 2 and 4 were derived from a gene duplication event and unexpectedly also are homologous to the recognition domain of human complement factor B. Alternative messenger RNA (mRNA) splicing may delete exon 4 sequences, resulting in a mRNA that does not encode a functional IL-2 receptor. Leukemic T cells infected with HTLV-I and normal activated T cells express IL-2 receptors with identical deduced protein sequences. Receptor gene transcription is initiated at two principal sites in normal activated T cells. Adult T cell leukemia cells infected with HTLV-I show activity at both of these sites, but also at a third transcription initiation site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leonard, W J -- Depper, J M -- Kanehisa, M -- Kronke, M -- Peffer, N J -- Svetlik, P B -- Sullivan, M -- Greene, W C -- New York, N.Y. -- Science. 1985 Nov 8;230(4726):633-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996141" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Complement Factor B/genetics ; DNA/genetics/isolation & purification ; DNA, Recombinant/isolation & purification ; Deltaretrovirus ; *Genes, MHC Class II ; Humans ; Peptide Chain Initiation, Translational ; RNA, Messenger/genetics ; Receptors, Immunologic/biosynthesis/*genetics ; Receptors, Interleukin-2 ; Repetitive Sequences, Nucleic Acid ; Retroviridae Infections/genetics ; T-Lymphocytes/microbiology ; Transcription, Genetic
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  • 71
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    Localization of the gene encoding the human interleukin-2 receptor on chromosome 10 (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-28
    Description: The human interleukin-2 receptor is an inducible growth factor receptor present on the surface of activated T lymphocytes. The receptor is required for a normal T-cell immune response. High-resolution fluorescence-activated chromosome sorting and DNA spot-blot analysis with complementary DNA's for the interleukin-2 receptor indicated that the receptor gene was located on chromosome 9, 10, 11, or 12. In situ hybridization studies showed that the interleukin-2 receptor gene is on the short arm of chromosome 10, p14----15.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leonard, W J -- Donlon, T A -- Lebo, R V -- Greene, W C -- New York, N.Y. -- Science. 1985 Jun 28;228(4707):1547-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3925551" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; *Chromosomes, Human, 6-12 and X ; DNA/analysis ; Humans ; Lymphocyte Activation ; Male ; Nucleic Acid Hybridization ; Phytohemagglutinins/pharmacology ; Receptors, Immunologic/*genetics ; Receptors, Interleukin-2 ; T-Lymphocytes/analysis/immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 72
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    Molecular cloning of a gene sequence regulated by nerve growth factor (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-07-26
    Description: Nerve growth factor (NGF) is essential for the development and differentiation of sympathetic or sensory neurons. A complementary DNA was cloned that corresponds to a gene sequence induced more than 50-fold in a cultured target cell line of pheochromocytoma cells (PC12 cells) 5 hours after the addition of NGF. The induced messenger RNA encodes a 90,000-dalton polypeptide that may represent one of the primary events in NGF-induced differentiation of neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levi, A -- Eldridge, J D -- Paterson, B M -- New York, N.Y. -- Science. 1985 Jul 26;229(4711):393-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3839317" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/genetics ; Adrenal Gland Neoplasms/genetics ; Animals ; Base Sequence ; Cell Line ; Chickens ; *Cloning, Molecular ; DNA/genetics ; Gene Expression Regulation ; *Genes ; Nerve Growth Factors/*physiology ; Nucleic Acid Hybridization ; Pheochromocytoma/genetics ; RNA, Messenger/genetics ; Rabbits ; Rats
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 73
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    Peptide neurotoxins from fish-hunting cone snails (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-20
    Description: To paralyze their more agile prey, the venomous fish-hunting cone snails (Conus) have developed a potent biochemical strategy. They produce several classes of toxic peptides (conotoxins) that attack a series of successive physiological targets in the neuromuscular system of the fish. The peptides include presynaptic omega-conotoxins that prevent the voltage-activated entry of calcium into the nerve terminal and release of acetylcholine, postsynaptic alpha-conotoxins that inhibit the acetylcholine receptor, and muscle sodium channel inhibitors, the mu-conotoxins, which directly abolish muscle action potentials. These distinct peptide toxins share several common features: they are relatively small (13 to 29 amino acids), are highly cross-linked by disulfide bonds, and strongly basic. The fact that they inhibit sequential steps in neuromuscular transmission suggests that their action is synergistic rather than additive. Five new omega-conotoxins that block presynaptic calcium channels are described. They vary in their activity against different vertebrate classes, and also in their actions against different synapses from the same animal. There are susceptible forms of the target molecule in peripheral synapses of fish and amphibians, but those of mice are resistant. However, the mammalian central nervous system is clearly affected, and these toxins are thus of potential significance for investigating the presynaptic calcium channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olivera, B M -- Gray, W R -- Zeikus, R -- McIntosh, J M -- Varga, J -- Rivier, J -- de Santos, V -- Cruz, L J -- GM 22737/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Dec 20;230(4732):1338-43.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4071055" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Feeding Behavior ; Fishes ; Mice ; Mollusk Venoms/*isolation & purification/toxicity ; Neurotoxins/*isolation & purification ; Peptide Fragments/analysis ; Snails/*physiology ; Species Specificity ; Structure-Activity Relationship
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  • 74
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    Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-19
    Description: The milk protein beta-lactoglobulin has been extensively studied but its function has not been identified. A clue regarding the function of a protein can be obtained by discovering a genetic relationship with a protein of known function through comparisons of amino acid sequence. Such comparisons revealed that beta-lactoglobulin is similar to human serum retinol-binding protein and to another human protein of unknown function known as complex-forming glycoprotein heterogeneous in charge (protein HC). beta-Lactoglobulins from several species have been found to bind retinol, while the absorption and fluorescence properties reported for the unidentified heterogeneous prosthetic group of protein HC are retinoid-like. The role of serum retinol-binding protein in vitamin A transport in the circulation suggests that the other two homologous proteins may function in the binding and transport of retinoids; beta-lactoglobulin may facilitate the absorption of vitamin A from milk and protein HC may mediate the excretion of retinol-derived metabolites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pervaiz, S -- Brew, K -- GM 21363/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):335-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2580349" target="_blank"〉PubMed〈/a〉
    Keywords: Alpha-Globulins/*genetics ; Amino Acid Sequence ; Animals ; Cattle ; Dolphins ; Humans ; Lactoglobulins/*genetics/metabolism ; Lagomorpha ; Mammals ; Milk/metabolism ; Primates ; Protein Conformation ; Proteinuria/metabolism ; Retinol-Binding Proteins/*genetics/metabolism ; Rodentia ; Swine ; Vitamin A/metabolism
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    The 23-million-dollar quest pays off (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1985 Oct 11;230(4722):161.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4035360" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Angiogenesis Inducing Agents/genetics/*isolation & purification ; Animals ; Growth Substances/*isolation & purification ; Humans ; Neoplasm Proteins/genetics/*isolation & purification ; Neoplasms/blood supply/metabolism ; Rats ; *Ribonuclease, Pancreatic
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  • 76
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    A glycophospholipid tail at the carboxyl terminus of the Thy-1 glycoprotein of neurons and thymocytes (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-29
    Description: Cell surface molecules of eukaryotic cells have been considered to be integrated into the membrane bilayer by a transmembrane protein sequence. The Thy-1 antigen of rodent thymocytes and brain was the first eukaryotic membrane molecule for which biochemical data clearly suggested membrane integration via a nonprotein tail. Direct evidence is now presented showing that a glycophospholipid structure is attached to the carboxyl-terminal cysteine residue and that 31 carboxyl-terminal amino acids predicted from the Thy-1 complementary DNA sequence are not present in the mature glycoprotein. These experimental results raise questions concerning signaling across a cell membrane since antibodies to Thy-1 can stimulate T lymphocytes to release lymphokines and undergo cell division.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tse, A G -- Barclay, A N -- Watts, A -- Williams, A F -- New York, N.Y. -- Science. 1985 Nov 29;230(4729):1003-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2865810" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antigens, Surface/isolation & purification ; Antigens, Thy-1 ; Brain/*metabolism ; Ethanolamines/metabolism ; Galactosamine/metabolism ; Glucosamine/metabolism ; Glycolipids/*metabolism ; Membrane Proteins/*metabolism ; Nerve Tissue Proteins/*metabolism ; Rats ; Stearic Acids/metabolism ; T-Lymphocytes/*metabolism
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  • 77
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    Involvement of the bcl-2 gene in human follicular lymphoma (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-21
    Description: Recombinant DNA probes were cloned for the areas flanking the breakpoint on chromosome 18 in cells from a patient with acute lymphocytic leukemia of the B-cell type; cells of this line carry the t(14;18) chromosomal translocation. Two of the probes detected DNA rearrangements in approximately 60 percent of the cases of follicular lymphoma screened. In follicular lymphoma, most of the breakpoints in band q21 of chromosome 18 were clustered within a short stretch of DNA, approximately 2.1 kilobases in length. Chromosome 18-specific DNA probes for the areas flanking the breakpoints also detected RNA transcripts 6 kilobases in length in various cell types. The gene coding for these transcript (the bcl-2 gene) seems to be interrupted in most cases of follicular lymphomas carrying the t(14;18) chromosomal translocation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsujimoto, Y -- Cossman, J -- Jaffe, E -- Croce, C M -- CA16685/CA/NCI NIH HHS/ -- CA36521/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 21;228(4706):1440-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3874430" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocytes/ultrastructure ; Cell Line ; *Chromosomes, Human, 16-18 ; Cloning, Molecular ; Humans ; Leukemia, Lymphoid/genetics ; Lymphoma/*genetics ; *Oncogenes ; *Translocation, Genetic
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    Antigenic variation and resistance to neutralization in poliovirus type 1 (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-13
    Description: Mutations have been identified in variants of poliovirus, type 1 (Mahoney) on the basis of their resistance to neutralization by individual monoclonal antibodies. The phenotypes of these variants were defined in terms of antibody binding; the pattern of epitopes expressed or able to be exploited for neutralization were complex. Single amino acid changes can have distant (in terms of linear sequence) and generalized effects on the antigenic structure of poliovirus and similarly constituted virions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diamond, D C -- Jameson, B A -- Bonin, J -- Kohara, M -- Abe, S -- Itoh, H -- Komatsu, T -- Arita, M -- Kuge, S -- Nomoto, A -- AI-15122/AI/NIAID NIH HHS/ -- CA-28146/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Sep 13;229(4718):1090-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2412292" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Antibodies, Monoclonal ; Epitopes/*analysis ; Immunity, Innate ; Mutation ; Phenotype ; Poliovirus/genetics/*immunology ; Virion/immunology
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    Prooxidant states and tumor promotion (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-01-25
    Description: There is convincing evidence that cellular prooxidant states--that is, increased concentrations of active oxygen and organic peroxides and radicals--can promote initiated cells to neoplastic growth. Prooxidant states can be caused by different classes of agents, including hyperbaric oxygen, radiation, xenobiotic metabolites and Fenton-type reagents, modulators of the cytochrome P-450 electron-transport chain, peroxisome proliferators, inhibitors of the antioxidant defense, and membrane-active agents. Many of these agents are promoters or complete carcinogens. They cause chromosomal damage by indirect action, but the role of this damage in carcinogenesis remains unclear. Prooxidant states can be prevented or suppressed by the enzymes of the cellular antioxidant defense and low molecular weight scavenger molecules, and many antioxidants are antipromoters and anticarcinogens. Finally, prooxidant states may modulate the expression of a family of prooxidant genes, which are related to cell growth and differentiation, by inducing alterations in DNA structure or by epigenetic mechanisms, for example, by polyadenosine diphosphate-ribosylation of chromosomal proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cerutti, P A -- New York, N.Y. -- Science. 1985 Jan 25;227(4685):375-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2981433" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antioxidants/pharmacology ; *Carcinogens/metabolism/pharmacology ; Cations/metabolism ; Cell Differentiation ; Cell Division ; Cell Line ; Cell Membrane/physiology ; *Cell Transformation, Neoplastic ; Chromosome Aberrations ; Chromosomes/drug effects ; Cytochrome P-450 Enzyme System/metabolism ; DNA/metabolism ; Electron Transport ; Gene Expression Regulation ; Humans ; Hydrogen Peroxide/metabolism ; Hydroxides/metabolism ; Hydroxyl Radical ; Lipid Peroxides/metabolism ; Microbodies/metabolism ; Mutation ; Neoplasms/*chemically induced ; Oxidation-Reduction ; Oxygen/*metabolism/physiology ; Poly Adenosine Diphosphate Ribose/metabolism ; Singlet Oxygen ; Sulfhydryl Compounds/physiology ; Superoxides/metabolism ; Ultraviolet Rays
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  • 80
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    Growth regulation of human melanocytes: mitogenic factors in extracts of melanoma, astrocytoma, and fibroblast cell lines (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-06
    Description: Melanocytes derived from fetal or adult skin do not propagate in vitro unless cultured in the presence of factors such as 12-O-tetradecanoylphorbol 13-acetate (TPA). In a search for physiological factors regulating the growth of melanocytes, extracts of various cultured cell types were tested. Factors produced by melanoma and astrocytoma cell lines support continued proliferation of melanocytes in the absence of TPA. WI-38, a fibroblast cell line derived from human embryonic lung, was the most active source of melanocyte growth factors. No melanocyte growth-promoting activity was found in extracts of cultured neuroblastoma, renal cancer, normal keratinocytes, or renal epithelium. Nerve growth factor, epidermal growth factor, melanocyte-stimulating hormone, transforming growth factor-beta, and platelet-derived growth factor did not have growth-promoting activity for melanocytes. The presence of melanocyte growth factors and TPA together resulted in the strongest mitogenic activity for melanocytes, permitting the recovery (at 20 days) of 4 to 20 times as many cells as in growth factor or TPA alone.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eisinger, M -- Marko, O -- Ogata, S -- Old, L J -- 1R01 CA-32152/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Sep 6;229(4717):984-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4023718" target="_blank"〉PubMed〈/a〉
    Keywords: Astrocytoma/physiopathology ; Cell Division/drug effects ; Cell Line ; Cholera Toxin/pharmacology ; Fibroblasts/physiology ; Growth Substances/isolation & purification/*pharmacology ; Humans ; Melanocytes/*cytology ; Melanoma/physiopathology ; Tetradecanoylphorbol Acetate/pharmacology
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    B lineage--specific interactions of an immunoglobulin enhancer with cellular factors in vivo (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-01-11
    Description: The mouse heavy chain immunoglobulin gene contains a tissue-specific enhancer. The enhancer and flanking sequences were studied in vivo by carrying out dimethyl sulfate protection experiments on living cells, in combination with genomic sequencing. Relative to reactions on naked DNA, there are changes (protections and enhancements) in the reactivity of guanine residues to dimethyl sulfate within the enhancer sequence in myeloma, B, and early B cells, whereas virtually no alterations appear in cells of non-B lineage. Most of the affected residues are in four clusters, in sequences homologous to the octamer 5'CAGGTGGC 3' (C, cytosine; A, adenine; G. guanine; T, thymine). The alterations in the pattern of G reactivity are consistent with the tissue-specific binding of molecules to the mouse immunoglobulin heavy chain enhancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ephrussi, A -- Church, G M -- Tonegawa, S -- Gilbert, W -- 2T 32 CA 09255/CA/NCI NIH HHS/ -- CA 14041/CA/NCI NIH HHS/ -- GM-09541-22/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jan 11;227(4683):134-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3917574" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/*metabolism ; Base Sequence ; Cell Line ; *Enhancer Elements, Genetic ; *Genes, Regulator ; Guanine/metabolism ; Immunoglobulin Heavy Chains/*genetics ; Methylation ; Mice ; Multiple Myeloma/genetics ; RNA, Messenger/metabolism ; Sulfuric Acid Esters/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 82
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    Cyanobacterial light-harvesting complex subunits encoded in two red light-induced transcripts (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-01
    Description: The major light-harvesting complex in cyanobacteria and red algae, the phycobilisome, is composed of chromophoric and nonchromophoric polypeptides. Two linked genes encoding major chromophoric components, the polypeptide subunits of phycocyanin, were isolated from the cyanobacterium Fremyella diplosiphon. Transcripts from this phycocyanin subunit gene cluster were present as major species in the cyanobacterium grown in red light, but not in cultures maintained in green light. The genes for the subunits of the red light-induced phycocyanin were transcribed together (beta-phycocyanin followed by alpha-phycocyanin) on two messenger RNA species; one contained 1600 bases while the other had 3800 bases. The latter, which encompassed the smaller transcript, contained additional sequences extending from the 3' end of the coding region of the alpha-phycocyanin gene. It may encode other light-induced components of the phycobilisome. Since phycocyanin, which effectively absorbs red light, becomes a dominant constituent of the phycobilisome in red light, these different levels may reflect an important adaptive mechanism of these organisms to their environment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Conley, P B -- Lemaux, P G -- Grossman, A R -- GM 33436-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 1;230(4725):550-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3931221" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cyanobacteria/*genetics ; Light ; Nucleic Acid Hybridization ; Phycobilisomes ; Phycocyanin/genetics ; RNA, Messenger/metabolism ; *Transcription, Genetic
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  • 83
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    Brain-derived acidic fibroblast growth factor: complete amino acid sequence and homologies (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-20
    Description: Bovine brain-derived acidic fibroblast growth factor (aFGF) is a protein mitogen originally identified in partially purified preparations of whole brain. The protein was purified to homogeneity and shown to be a potent vascular endothelial cell mitogen in culture and angiogenic substance in vivo. The homology of aFGF to human interleukin-1 beta was inferred from partial sequence data. The complete amino acid sequence of aFGF has now been determined and observed to be similar to both basic FGF and interleukin-1's. A neuropeptide-like sequence, flanked by basic dipeptides, was observed within the aFGF sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gimenez-Gallego, G -- Rodkey, J -- Bennett, C -- Rios-Candelore, M -- DiSalvo, J -- Thomas, K -- New York, N.Y. -- Science. 1985 Dec 20;230(4732):1385-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4071057" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Brain Chemistry ; Cattle ; Fibroblast Growth Factors/*isolation & purification ; Hormones ; Humans ; Hydrogen-Ion Concentration ; Nerve Tissue Proteins ; Sequence Homology, Nucleic Acid ; Species Specificity
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  • 84
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    Sequence and structure of a human glucose transporter (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-06
    Description: The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone. Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical. The protein lacks a cleavable amino-terminal signal sequence. Analysis of the primary structure suggests the presence of 12 membrane-spanning domains. Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves. The amino terminus, carboxyl terminus, and a highly hydrophilic domain in the center of the protein are all predicted to lie on the cytoplasmic face. Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mueckler, M -- Caruso, C -- Baldwin, S A -- Panico, M -- Blench, I -- Morris, H R -- Allard, W J -- Lienhard, G E -- Lodish, H F -- GM22996/GM/NIGMS NIH HHS/ -- HL32262/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 Sep 6;229(4717):941-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3839598" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Carrier Proteins/genetics/metabolism ; Cell Membrane/ultrastructure ; Cloning, Molecular ; DNA/genetics ; Erythrocytes/metabolism ; Glucose/*metabolism ; Humans ; Liver Neoplasms, Experimental/metabolism ; *Membrane Proteins/genetics/metabolism ; Molecular Weight ; Monosaccharide Transport Proteins ; Protein Conformation ; RNA, Messenger/genetics ; Tissue Distribution
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  • 85
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    A new role for DNA virus early proteins in viral carcinogenesis (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-01-04
    Description: The T antigen proteins encoded by DNA tumor virus early genes are involved in the transformation of normal cells to immortalized neoplastic cells that may or may not be tumorigenic in immunocompetent animals. Studies have been made of the tumorigenicity of DNA virus-transformed cells and the interactions of these cells in vivo and in vitro with immunologically nonspecific host effector cells such as natural killer cells and macrophages. The results imply that the T proteins determine the capacity of transformed cells to induce tumors by governing the level of susceptibility that transformed cells express to destruction by such host cellular defenses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewis, A M Jr -- Cook, J L -- CA 31732/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jan 4;227(4682):15-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3843807" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Polyomavirus Transforming ; Antigens, Viral, Tumor/*metabolism ; Cell Line ; Cell Transformation, Neoplastic/immunology/*metabolism ; *Cell Transformation, Viral ; Cricetinae ; Cytotoxicity, Immunologic ; DNA Viruses/*metabolism ; Humans ; Immunity, Cellular ; Killer Cells, Natural/immunology ; Major Histocompatibility Complex ; Mesocricetus ; Mice ; Mice, Nude ; Neoplasm Transplantation ; Neoplasms, Experimental/immunology ; Rats ; Viral Proteins/*metabolism
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  • 86
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    The structure of arthropod hemocyanins (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-08-09
    Description: Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. Comparison of the amino acid sequence data for seven different subunits of arthropod hemocyanins from crustaceans and chelicerates shows many highly conserved residues and extensive regions of near identity. This correspondence can be matched closely with the three domain structure established by x-ray crystallography for spiny lobster hemocyanin. The degree of identity is particularly striking in the second domain of the subunit that contains the six histidines which ligate the two oxygen-binding copper atoms. The polypeptide architecture of spiny lobster hemocyanin appears to be the same in all arthropods. This structure must therefore be at least as old as the estimated time of divergence of crustaceans and chelicerates, about 540 to 600 million years ago.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Linzen, B -- Soeter, N M -- Riggs, A F -- Schneider, H J -- Schartau, W -- Moore, M D -- Yokota, E -- Behrens, P Q -- Nakashima, H -- Takagi, T -- GM 21314/GM/NIGMS NIH HHS/ -- GM 28410/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 9;229(4713):519-24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4023698" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arachnida/genetics ; *Arthropods/genetics ; Binding Sites ; Biological Evolution ; Chemical Phenomena ; Chemistry ; Copper ; Crustacea/genetics ; *Hemocyanin/genetics ; Models, Molecular ; Protein Conformation ; Species Specificity
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  • 87
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    A mammalian host-vector system that regulates expression and amplification of transfected genes by temperature induction (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-01-04
    Description: SV40-transformed simian cells that permit temperature-dependent regulation of vector DNA replication were isolated and characterized. These cell lines (ts COS cells) produce high levels of thermolabile large T antigen under the transcriptional control of the Rous sarcoma virus long terminal repeat. The ts COS cell lines can complement SV40 A gene mutants and support replication of SV40-origin containing vectors at 33 degrees C but not at 40 degrees C. It should now be possible to regulate the copy number of transfected plasmid DNA's and also maintain selectable vector sequences either as integrated DNA or as autonomously replicating episomes by modulating T antigen activity in ts COS cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rio, D C -- Clark, S G -- Tjian, R -- New York, N.Y. -- Science. 1985 Jan 4;227(4682):23-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2981116" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Viral, Tumor/genetics ; Cell Line ; Cell Transformation, Viral ; DNA Replication ; *Gene Amplification ; *Gene Expression Regulation ; *Genetic Vectors ; Haplorhini ; Plasmids ; RNA, Messenger/metabolism ; Simian virus 40/physiology ; Temperature ; *Transfection ; Virus Replication
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  • 88
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    Amino terminal myristylation of the protein kinase p60src, a retroviral transforming protein (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-01-25
    Description: The transforming protein of Rous sarcoma virus, p60src, was shown to be acylated at its amino terminus with the long-chain fatty acid myristic acid by isolation of a tryptic peptide with the following structure: myristylglycylserylseryllysine. The occurrence of this unusual posttranslational modification in the cyclic adenosine monophosphate-dependent protein kinase and in several transforming protein kinases of mammalian retroviruses suggests that myristylation of the amino terminal glycyl residue may be critical for the function of certain proteins related to cell transformation and growth control.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schultz, A M -- Henderson, L E -- Oroszlan, S -- Garber, E A -- Hanafusa, H -- CA-14935/CA/NCI NIH HHS/ -- N01-CO-23909/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jan 25;227(4685):427-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3917576" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Amino Acid Sequence ; Cell Transformation, Neoplastic ; Cell Transformation, Viral ; Myristic Acid ; Myristic Acids/*analysis/metabolism ; Oncogene Protein pp60(v-src) ; Protein Kinases/*analysis/metabolism ; Protein Processing, Post-Translational ; Viral Proteins/*analysis/metabolism
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  • 89
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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
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  • 90
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    A macrophage factor inhibits adipocyte gene expression: an in vitro model of cachexia (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-08-30
    Description: Certain infections and malignancies in mammals cause the development of a condition known as cachexia in which the animal continues to lose weight, often while consuming an adequate diet. When macrophages are stimulated with an endotoxin, they produce a factor or factors, termed cachectin, that inhibits the activity of fat-producing (lipogenic) enzymes in cultured adipocytes. This effect may reflect one of the physiological bases for cachexia. In the present study, clones of complementary DNA from genes whose expression is increased during the differentiation of adipocytes were used to study the molecular basis of cachectin's actions. In the presence of cachectin, the expression of the corresponding genes was reversibly and specifically inhibited. Furthermore, when mature adipocytes were exposed to cachectin, the messenger RNA's of those genes diminished and rapidly approached the levels present before differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Torti, F M -- Dieckmann, B -- Beutler, B -- Cerami, A -- Ringold, G M -- AM0131401/AM/NIADDK NIH HHS/ -- GM25821/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 30;229(4716):867-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3839597" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/genetics ; Adipose Tissue/cytology/*enzymology ; Animals ; Cachexia/*etiology ; Cell Differentiation ; Cell Division/drug effects ; Cell Line ; Cell Survival/drug effects ; Dna ; Endotoxins/pharmacology ; Gene Expression Regulation/drug effects ; Glycerolphosphate Dehydrogenase/genetics ; Lipids/*biosynthesis ; Macrophages/*metabolism ; Models, Biological ; Proteins/*pharmacology ; RNA, Messenger/genetics ; Tumor Necrosis Factor-alpha
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  • 91
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    Characterization of gp41 as the transmembrane protein coded by the HTLV-III/LAV envelope gene (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-27
    Description: Radiolabeled amino acid sequencing was used to characterize gp41, an antigen of HTLV-III/LAV, the virus believed to be the etiological agent of the acquired immune deficiency syndrome. This antigen is the one most commonly detected in immunoblot assays by sera of patients with AIDS or AIDS-related complex (ARC) and other individuals infected with HTLV-III/LAV. A mouse monoclonal antibody that was reactive with gp41 precipitated a 160-kilodalton protein (gp160) in addition to gp41, but did not precipitate a 120-kilodalton protein (gp120) from extracts of metabolically labeled cells producing HTLV-III. Extracts of infected cells that had been labeled with tritiated leucine or isoleucine were immunoprecipitated with the monoclonal antibody. The immunoprecipitates were fractionated by polyacrylamide gel electrophoresis and the p41 was eluted from the gel bands and subjected to amino-terminal radiolabeled amino acid sequencing by the semiautomated Edman degradation. Leucine residues occurred in cycles 7, 9, 12, 26, 33, and 34 among 40 cycles and isoleucine occurred in cycle 4 among 24 cycles analyzed. Comparison of the data with the deduced amino acid sequence of the env gene product of HTLV-III precisely placed gp41 in the COOH-terminal region of the env gene product. Gp160 is thus the primary env gene product and it is processed into gp120 and gp41.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Veronese, F D -- DeVico, A L -- Copeland, T D -- Oroszlan, S -- Gallo, R C -- Sarngadharan, M G -- New York, N.Y. -- Science. 1985 Sep 27;229(4720):1402-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994223" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/microbiology ; Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Antigens, Viral/genetics/immunology ; Deltaretrovirus/*genetics ; *Genes, Viral ; Humans ; Mice ; Mice, Inbred BALB C ; Viral Envelope Proteins/*genetics
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  • 92
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    Cyclic AMP regulation of eukaryotic gene transcription by two discrete molecular mechanisms (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-07-19
    Description: In experiments designed to study the mechanism by which peptide hormones binding to their plasma membrane receptors stimulate the expression of specific genes, the transcription of two neuroendocrine genes, prolactin and growth hormone, was analyzed in a rat pituitary cell line. The results showed that cyclic adenosine monophosphate (cyclic AMP) stimulates the transcription of discrete subsets of eukaryotic genes by at least two independent molecular mechanisms. Cyclic AMP stimulated growth hormone gene transcription and phosphorylation of a 19,000-dalton nuclear protein; this appears to reflect direct nuclear actions of the cyclic AMP-dependent protein kinase. In contrast, the stimulation by cyclic AMP of prolactin gene transcription appears to reflect activation of a discrete calcium-dependent event.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Waterman, M -- Murdoch, G H -- Evans, R M -- Rosenfeld, M G -- New York, N.Y. -- Science. 1985 Jul 19;229(4710):267-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990047" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Membrane/metabolism ; Cobalt/pharmacology ; Colforsin ; Cyclic AMP/*physiology ; Diterpenes/pharmacology ; Growth Hormone/biosynthesis/genetics ; Phosphorylation ; Pituitary Gland/cytology ; Prolactin/biosynthesis/genetics ; Protein Kinases/physiology ; Rats ; Thyrotropin-Releasing Hormone/pharmacology ; *Transcription, Genetic/drug effects
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