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  • Articles  (13)
  • Amino Acid Sequence
  • American Association for the Advancement of Science (AAAS)  (13)
  • American Meteorological Society
  • American Physical Society (APS)
  • Elsevier
  • Public Library of Science
  • Springer Nature
  • 2000-2004
  • 1980-1984  (13)
  • 1955-1959
  • 1935-1939
  • 1930-1934
  • 1999
  • 1998
  • 1996
  • 1982  (13)
  • Natural Sciences in General  (13)
  • Geosciences
Collection
  • Articles  (13)
Publisher
  • American Association for the Advancement of Science (AAAS)  (13)
  • American Meteorological Society
  • American Physical Society (APS)
  • Elsevier
  • Public Library of Science
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Years
  • 2000-2004
  • 1980-1984  (13)
  • 1955-1959
  • 1935-1939
  • 1930-1934
  • +
Year
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  • 11
    Publication Date: 1982-10-22
    Description: The protein coding region of the herpes simplex virus type-1 glycoprotein D (gD) gene was mapped, and the nucleotide sequence was determined. The predicted amino acid sequence of the gD polypeptide was found to contain a number of features in common with other virus glycoproteins. Insertion of this protein coding region into a bacterial expressor plasmid enabled synthesis in Escherichia coli of an immunoreactive gD-related polypeptide. The potential of this system for preparation of a type-common herpes simplex virus vaccine is discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watson, R J -- Weis, J H -- Salstrom, J S -- Enquist, L W -- New York, N.Y. -- Science. 1982 Oct 22;218(4570):381-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6289440" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/genetics ; Base Sequence ; Escherichia coli/genetics ; Gene Expression Regulation ; Genes ; Genes, Viral ; Glycoproteins/*genetics ; Peptides/genetics ; Protein Sorting Signals ; Simplexvirus/*genetics ; Viral Proteins/*genetics/immunology ; Viral Vaccines
    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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  • 12
    Publication Date: 1982-08-27
    Description: A pituitary glycopeptide whose amino acid sequence was previously identified has now been recognized as the final portion of the precursor to arginine vasopressin and its associated neurophysin. Immunocytochemical techniques with antiserums against this 39 amino acid peptide and vasopressin were used to study their distribution in the rat central nervous system. The peptide is located in vasopressin-synthesizing cells in the neurosecretory magnocellular nuclei. Positively stained fibers project from the magnocellular nuclei through the median eminence to the posterior pituitary. Studies of the homozygous Brattleboro rat, which is known to be deficient in the production of vasopressin and its related neurophysin, also show the absence of immunoreactivity to this peptide. These immunocytochemical data strongly indicate that the peptide is synthesized with vasopressin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watson, S J -- Seidah, N G -- Chretien, M -- DA00154/DA/NIDA NIH HHS/ -- DA02265/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1982 Aug 27;217(4562):853-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6125034" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arginine Vasopressin/*metabolism ; Brain/*metabolism ; Dynorphins ; Endorphins/metabolism ; Hypothalamus/metabolism ; Male ; Neurophysins/*metabolism ; Peptide Fragments ; Pituitary Gland, Posterior/metabolism ; Protein Precursors/analysis/*metabolism ; Rats ; Rats, Inbred Strains
    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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  • 13
    Publication Date: 1982-11-05
    Description: A 44 amino acid peptide with growth hormone-releasing activity has been isolated from a human tumor of the pancreas that had caused acromegaly. The primary structure of the tumor-derived peptide is H-Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala- Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Gln-Gln-Gly-Glu-Ser-Asn-Gln-Glu-Arg-Gly -Ala-Arg-Ala-Arg-Leu-NH2. The synthetic replicate has full biological activity in vitro and in vivo specifically to stimulate the secretion of immunoreactive growth hormone. The tumor-derived peptide is identical in biological activity and similar in physiochemical properties to the still uncharacterized growth hormone-releasing factor present in extracts of hypothalamic tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guillemin, R -- Brazeau, P -- Bohlen, P -- Esch, F -- Ling, N -- Wehrenberg, W B -- AM-18811/AM/NIADDK NIH HHS/ -- HD-09690/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1982 Nov 5;218(4572):585-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6812220" target="_blank"〉PubMed〈/a〉
    Keywords: Acromegaly/*physiopathology ; Amino Acid Sequence ; Biological Assay ; Growth Hormone-Releasing Hormone/chemical synthesis/*isolation & purification ; Hormones, Ectopic/*isolation & purification ; Humans ; Pancreatic Neoplasms/*chemistry
    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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