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  • Base Sequence  (179)
  • Amino Acid Sequence  (93)
  • American Association for the Advancement of Science (AAAS)  (234)
  • American Chemical Society
  • International Union of Crystallography (IUCr)
  • 1980-1984  (234)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (234)
  • American Chemical Society
  • International Union of Crystallography (IUCr)
Years
Year
  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-09-12
    Description: In the report by T. Kakunaga and J. D. Crow (25 July, p. 505), Fig. 1 on page 506 should have been printed as follows: [See figure in the PDF file]〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dayhoff, M O -- Schwartz, R M -- Chen, H R -- Hunt, L T -- Barker, W C -- Orcutt, B C -- New York, N.Y. -- Science. 1980 Sep 12;209(4462):1182.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7403878" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Information Systems ; *Nucleic Acids
    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: 1980-11-07
    Description: An analog of luteinizing hormone-releasing hormone containing a gamma-lactam as a conformational constraint has been prepared with the use of a novel cyclization of a methionine sulfonium salt. The analog is more active as a luteinizing hormone-releasing hormone agonist that the parent hormone, and provides evidence for a bioactive conformation containing a beta-turn.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freidinger, R M -- Veber, D F -- Perlow, D S -- Brooks, J R -- Saperstein, R -- New York, N.Y. -- Science. 1980 Nov 7;210(4470):656-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001627" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Assay ; Cells, Cultured ; Female ; *Gonadotropin-Releasing Hormone/analogs & derivatives ; Hydrogen Bonding ; Lactams ; Protein Conformation ; Rats ; Structure-Activity Relationship
    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
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-03-21
    Description: Intensive research in the last decade has revealed a wealth of detail on the mechanism of biosynthesis, molecular structure, and covalent cross-linking of collagen. Tissues of higher animals express a family of at least five genetically distinct types of collagen molecule, each apparently tailored for different construction work outside the cell. Within each genetic type of collagen, further chemical heterogeneity is also evident; the variations in hydroxylation, glycosylation, and cross-linking are dependent, for example, on tissue type, age, and hormonal status. The functional significance of collagen's molecular diversity and its control by different cells and tissues are not yet well understood but abnormalities of collagen in many human diseases keep this protein a focal molecule of medical research.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eyre, D R -- New York, N.Y. -- Science. 1980 Mar 21;207(4437):1315-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7355290" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcification, Physiologic ; Cartilage/ultrastructure ; *Collagen/genetics/metabolism ; Epithelium/ultrastructure ; Extracellular Space/ultrastructure ; Humans ; Hydrogen Bonding ; Polymorphism, Genetic ; Protein Biosynthesis ; Protein Conformation ; Vertebrates
    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
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-02-08
    Description: The distribution of active polyadenylate-messenger RNA sequences in fractionated chicken liver chromatin was examined. A portion of these active gene sequences is concentrated in a DNA fraction retained by tightly bound nonhistone chromosomal proteins, while the nonretained DNA fraction is substantially depleted of a portion of these sequences. These findings suggest that the tightly bound nonhistones are physically associated with a subset of active gene sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gates, D M -- Bekhor, I -- New York, N.Y. -- Science. 1980 Feb 8;207(4431):661-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7352280" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chickens ; Chromatin/ultrastructure ; Chromosomal Proteins, Non-Histone/*metabolism ; DNA/*metabolism ; *Genes ; Liver/*metabolism ; Nucleic Acid Hybridization ; Protein Binding ; RNA, Messenger/genetics ; Sodium Chloride
    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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  • 5
    Publication Date: 1980-07-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fox, G E -- Stackebrandt, E -- Hespell, R B -- Gibson, J -- Maniloff, J -- Dyer, T A -- Wolfe, R S -- Balch, W E -- Tanner, R S -- Magrum, L J -- Zablen, L B -- Blakemore, R -- Gupta, R -- Bonen, L -- Lewis, B J -- Stahl, D A -- Luehrsen, K R -- Chen, K N -- Woese, C R -- New York, N.Y. -- Science. 1980 Jul 25;209(4455):457-63.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6771870" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/*classification ; Base Sequence ; Biological Evolution ; Chloroplasts/analysis ; Clostridium/classification ; Cyanobacteria/classification ; DNA/analysis ; *Phylogeny ; RNA, Ribosomal/*analysis ; Species Specificity
    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: 1980-12-19
    Description: Anglerfish (Lophius americanus) insulin complementary DNA was cloned in bacterial plasmids, and its sequence was determined. Fish insulin messenger RNA is larger (1.5 times) than the messenger RNA encoding mammalian (rat and human) insulin, in part because of a larger C peptide (an additional six amino acids or 18 nucleotides in length) but mainly because of increases in the 5' and 3' untranslated regions. Comparison of the fish, rat, and human insulin messenger RNA (from the complementary DNA) reveals that, in addition to the regions coding for the A and B peptides, sequence conservation is limited to a segment within the 5' untranslated region which may be involved in ribosomal binding, two small segments of the signal peptide, and two stretches of sequence in the 3' untranslated region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hobart, P M -- Shen, L P -- Crawford, R -- Pictet, R L -- Rutter, W J -- AM 21344/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1980 Dec 19;210(4476):1360-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001633" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Biological Evolution ; Cloning, Molecular ; Codon ; Fishes/*genetics ; Insulin/*genetics ; Nucleic Acid Conformation ; Proinsulin/genetics ; Protein Biosynthesis ; Protein Precursors/genetics ; RNA, Messenger/*genetics
    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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  • 7
    Publication Date: 1980-04-11
    Description: A high-molecular-weight protein with beta-endorphin- and adrenocorticotropin-immunoreactivities was isolated from extracts of human placenta after several purification steps, including immunoadsorption with a well-characterized antiserum raised to beta-endorphin. This protein was identified as the heavy chain of the human immunoglobulin class IgG1. These results have led to the recognition of homologies in the amino acid sequences of these physiologically unrelated molecules. They also suggest caution in accepting immunological competence as the sole criterion of the chemical identity of a ligand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Julliard, J H -- Shibasaki, T -- Ling, N -- Guillemin, R -- New York, N.Y. -- Science. 1980 Apr 11;208(4440):183-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6244620" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Electrophoresis, Polyacrylamide Gel ; Endorphins/*analysis ; Female ; Humans ; Immunoglobulin G/*analysis ; Placental Extracts/*analysis ; Pregnancy ; Radioimmunoassay ; beta-Endorphin
    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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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-11-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G B -- New York, N.Y. -- Science. 1980 Nov 21;210(4472):887-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001629" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chemistry/history ; DNA/genetics ; DNA, Recombinant ; History, 20th Century ; Molecular Biology/*history ; *Nobel Prize
    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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  • 9
    Publication Date: 1980-05-30
    Description: Cloned repetitive DNA sequences were used to determine the number of homologous RNA transcripts in the eggs of two sea urchin species, Strongylocentrotus purpuratus and S. franciscanus. The eggs of these species contain different amounts of RNA, and their genomes contain different numbers of copies of the cloned repeats. The specific pattern of repetitive sequence representation in the two egg RNA's is nonetheless quantitatively similar. The evolutionary conservation of this pattern suggests the functional importance of repeat sequence expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, G P -- Costantini, F D -- Posakony, J W -- Davidson, E H -- Britten, R J -- New York, N.Y. -- Science. 1980 May 30;208(4447):1046-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6154974" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Evolution ; DNA, Recombinant ; Female ; Nucleic Acid Hybridization ; Ovum/physiology ; Plasmids ; RNA/*genetics ; Sea Urchins/*genetics ; Species Specificity ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
    Publication Date: 1980-08-22
    Description: A 27-kilodalton tryptic fragment, derived from the amino terminus of the 200-kilodalton fibronectin subunit, inhibited binding of intact fibronectin to Staphylococcus aureus and could be cross-linked to Staphylococcus aureus by blood coagulation Factor XIIIa. Interactions of fibronectin with Staphylococcus aureus via this fragment may be important for bacterial opsonization and attachment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mosher, D F -- Proctor, R A -- New York, N.Y. -- Science. 1980 Aug 22;209(4459):927-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7403857" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Factor XIII/*metabolism ; Fibronectins/*metabolism ; Humans ; Molecular Weight ; Opsonin Proteins ; Peptide Fragments ; Protein Binding ; Staphylococcus aureus/immunology/*metabolism ; Trypsin/metabolism
    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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