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  • Articles  (352)
  • Humans  (352)
  • 1995-1999
  • 1985-1989  (352)
  • 1985  (352)
  • Physics  (352)
Collection
  • Articles  (352)
Years
  • 1995-1999
  • 1985-1989  (352)
Year
  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-12-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1985 Dec 20;230(4732):1324-6, 1410.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4071054" target="_blank"〉PubMed〈/a〉
    Keywords: Humans ; *Nutritional Physiological Phenomena ; Nutritional Requirements ; *Societies, Scientific ; United States
    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
    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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  • 3
    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
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 1985-08-23
    Description: Mice were fed an ethanol-containing liquid diet for 9 days. On removal of the diet, exposure to 12 atmospheres absolute of a mixture of helium and oxygen precipitated earlier withdrawal, increased withdrawal scores for the first 6 hours, and increased the peak withdrawal intensity compared to dependent animals exposed to control conditions. The enhanced withdrawal did not appear to reflect alterations in ethanol elimination, oxygen or helium partial pressures, body temperature, or general excitability. These results extend to chronically treated animals the evidence that hyperbaric exposure antagonizes the membrane actions of ethanol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alkana, R L -- Finn, D A -- Galleisky, G G -- Syapin, P J -- Malcolm, R D -- R01AA03972/AA/NIAAA NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 23;229(4715):772-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4040651" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Atmospheric Pressure ; Cell Membrane/drug effects/physiology ; Ethanol/*adverse effects/pharmacology ; Humans ; Male ; Mice ; Substance Withdrawal Syndrome/*physiopathology
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 1985-08-02
    Description: Beta-galactosidase-deficient siblings in two litters of English springer spaniel puppies showed a progressive neurological impairment, dwarfism, orbital hypertelorism, and dysostosis multiplex. An excess of GM1-ganglioside was found in the brain. Three abnormal oligosaccharides were present in samples of urine, brain, liver, and cartilage. Light microscopy of selected tissue specimens revealed cytoplasmic vacuoles in neurons, circulating blood cells, macrophages, and chondrocytes. Ultrastructural studies demonstrated that these membrane-bound vacuoles were of two types--one containing lamellated membranes and the other, finely granular material. These clinical and pathological findings are similar to those observed in human patients affected by the infantile form of GM1-gangliosidosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alroy, J -- Orgad, U -- Ucci, A A -- Schelling, S H -- Schunk, K L -- Warren, C D -- Raghavan, S S -- Kolodny, E H -- HD 05515/HD/NICHD NIH HHS/ -- HD04147/HD/NICHD NIH HHS/ -- NS 21765/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 2;229(4712):470-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3925555" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Diseases, Metabolic/enzymology/genetics/*veterinary ; Dog Diseases/*enzymology/genetics/pathology ; Dogs ; Female ; G(M1) Ganglioside ; Gangliosidoses/enzymology/genetics/pathology/*veterinary ; Humans ; Lactose Intolerance/genetics/metabolism/*veterinary ; Male ; Neurons/pathology ; Oligosaccharides/metabolism ; Pedigree ; Vacuoles/pathology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    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
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 1985-12-06
    Description: Two transgenic mice were obtained that contain in their chromosomes the complete hepatitis B virus (HBV) genome except for the core gene. These mice secrete particles of HBV surface antigen (HBsAg) in the serum. In one mouse, HBV DNA sequences that had integrated at two different sites were shown to segregate independently in the first filial generation (F1) and only one of the sequences allowed expression of the surface antigen. Among these animals the males produced five to ten times more HBsAg than the females. A 2.1-kilobase messenger RNA species comigrating with the major surface gene messenger RNA is expressed specifically in the liver in the two original mice. The results suggest that the HBV sequences introduced into the mice are able to confer a tissue-specific expression to the S gene. In addition, the HBV transgenic mice represent a new model for the chronic carrier state of hepatitis B virus infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Babinet, C -- Farza, H -- Morello, D -- Hadchouel, M -- Pourcel, C -- CA37300-02/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Dec 6;230(4730):1160-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3865370" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier State ; DNA, Recombinant ; Female ; *Genetic Engineering ; Hepatitis B/genetics ; Hepatitis B Surface Antigens/*genetics ; Humans ; Male ; Mice ; Mice, Inbred C57BL/genetics ; Nucleic Acid Hybridization ; RNA, Messenger/genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
    Publication Date: 1985-07-05
    Description: Human T-lymphotropic virus type III (HTLV-III) encodes a trans-acting factor that activates the expression of genes linked to the HTLV-III long terminal repeat. By functional mapping of complementary DNA transcripts of viral messenger RNA's the major functional domain of the gene encoding this factor was localized to a region immediately before the env gene of the virus, a region previously thought to be noncoding. This newly identified gene consists of three exons, and its transcription into messenger RNA involves two splicing events bringing together sequences from the 5' part (287 base pairs), middle (268 base pairs), and 3'part (1258 base pairs) of the HTLV-III genome. A similar messenger RNA with a truncated second exon (70 base pairs) does not encode a trans-acting function. It is proposed that this second messenger RNA is the transcript of a gene (3'-orf) located after the env gene. Messenger RNA's were also identified for the env and gag-pol genes of HTLV-III.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arya, S K -- Guo, C -- Josephs, S F -- Wong-Staal, F -- New York, N.Y. -- Science. 1985 Jul 5;229(4708):69-73.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990040" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Deltaretrovirus/*genetics ; Gene Expression Regulation ; Genes, Regulator ; *Genes, Viral ; Humans ; RNA Splicing ; RNA, Messenger/genetics ; RNA, Viral/genetics ; Repetitive Sequences, Nucleic Acid ; Transcription Factors/*genetics ; Viral Proteins/genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
    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
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barnes, D M -- New York, N.Y. -- Science. 1985 Dec 13;230(4731):1260.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4071048" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*diagnosis ; Antibodies, Monoclonal ; Humans ; Molecular Weight ; Nerve Tissue Proteins/immunology
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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