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  • Time Factors  (127)
  • Amino Acid Sequence  (93)
  • American Association for the Advancement of Science (AAAS)  (220)
  • American Chemical Society
  • International Union of Crystallography (IUCr)
  • 1980-1984  (220)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (220)
  • American Chemical Society
  • International Union of Crystallography (IUCr)
Years
Year
  • 1
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    Bioactive conformation of luteinizing hormone-releasing hormone: evidence from a conformationally constrained analog (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Collagen: molecular diversity in the body's protein scaffold (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Interaction of laminae of the cingulate cortex with the anteroventral thalamus during behavioral learning (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-05-30
    Description: Neurons in deep laminae of the rabbit cingulate cortex develop discriminative activity at an early stage of behavioral discrimination learning, whereas neurons in the anteroventral nucleus of thalamus and neurons in the superficial cortical laminae develop such activity in a late stage of behavioral learning. It is hypothesized that early-forming discriminative neuronal activity, relayed to anteroventral neurons via the corticothalamic pathway, contributes to the construction of changes underlying the late-forming neuronal discrimination in the anteroventral nucleus. The resultant late discriminative activity in the anteroventral nucleus is then relayed via the thalamocortical pathway back to the superficial cortical laminae, promoting disengagement of cortex from further task-processing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabriel, M -- Foster, K -- Orona, E -- New York, N.Y. -- Science. 1980 May 30;208(4447):1050-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7375917" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avoidance Learning/*physiology ; Brain Mapping ; Cerebral Cortex/cytology/*physiology ; Discrimination (Psychology)/*physiology ; Gyrus Cinguli/*physiology ; Neural Pathways/physiology ; Rabbits ; Thalamus/*physiology ; Time Factors
    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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    Preserved learning and retention of pattern-analyzing skill in amnesia: dissociation of knowing how and knowing that (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-10-10
    Description: Amnesic patients acquired a mirror-reading skill at a rate equivalent to that of matched control subjects and retained it for at least 3 months. The results indicate that the class of preserved learning skills in amnesia is broader than previously reported. Amnesia seems to spare information that is based on rules or procedures, as contrasted with information that is data-based or declarative--"knowing how rather than "knowing that." The results support the hypothesis that such a distinction is honored by the nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, N J -- Squire, L R -- 1P50 MH 30914/MH/NIMH NIH HHS/ -- MH24600/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1980 Oct 10;210(4466):207-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7414331" target="_blank"〉PubMed〈/a〉
    Keywords: Alcohol Amnestic Disorder/physiopathology ; Amnesia/*physiopathology ; Electroconvulsive Therapy ; *Form Perception ; Humans ; Learning/*physiology ; *Pattern Recognition, Visual ; Reading ; Retention (Psychology)/physiology ; Time Factors
    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
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    Comparison of the nucleic acid sequence of anglerfish and mammalian insulin mRNA's from cloned cDNA's (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 6
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    High-molecular-weight immunoreactive beta-endorphin in extracts of human placenta is a fragment of immunoglobulin G (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 7
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    Computers, health care, and medical information science (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-10-17
    Description: The clinical laboratory is examined as a microcosm of the entire health care delivery system. The introduction of computers into the clinical laboratory raises issues that are difficult to resolve by the methods of information science or medical science applied in isolation. The melding of these two disciplines, together with the contributions of other disciplines, has created a new field of study called medical information science. The emergence of this new discipline and some specific problem-solving approaches used in its application in the clinical laboratory are examined.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lincoln, T L -- Korpman, R A -- New York, N.Y. -- Science. 1980 Oct 17;210(4467):257-63.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6999622" target="_blank"〉PubMed〈/a〉
    Keywords: Clinical Laboratory Techniques/*instrumentation ; Costs and Cost Analysis ; *Delivery of Health Care/economics ; Diagnosis, Computer-Assisted/*methods ; Humans ; Information Systems ; Time Factors
    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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    Specific reading disability: differences in contrast sensitivity as a function of spatial frequency (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-10-01
    Description: Contrast thresholds for sine-wave gratings of spatial frequencies of 2, 4, 12, and 16 cycles per degree were determined for normal and disabled readers at a range of stimulus durations. Normal readers demonstrated monotonically decreasing sensitivity with increasing spatial frequency at exposure durations between 40 and 100 milliseconds. At exposure durations of 150 to 1000 milliseconds, they showed peak sensitivity at 4 cycles per degree. In comparison, disabled readers showed monotonically decreasing sensitivity with increasing spatial frequency at all stimulus durations. The difference in sensitivity pattern across spatial frequencies was greatest at stimulus durations approximately equal to fixation durations during reading.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lovegrove, W J -- Bowling, A -- Badcock, D -- Blackwood, M -- New York, N.Y. -- Science. 1980 Oct;210(4468):439-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7433985" target="_blank"〉PubMed〈/a〉
    Keywords: Afterimage/physiology ; Dyslexia/*physiopathology ; Humans ; Space Perception/physiology ; Time Factors ; Visual Perception/*physiology
    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
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    Elevated cerebrospinal fuid norepinephrine in schizophrenics: confounding effects of treatment drugs (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-10-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lipsky, J J -- New York, N.Y. -- Science. 1980 Oct 3;210(4465):97.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6106286" target="_blank"〉PubMed〈/a〉
    Keywords: Antipsychotic Agents/*pharmacology ; Humans ; Norepinephrine/*cerebrospinal fluid ; Research Design ; Schizophrenia/*cerebrospinal fluid/drug therapy ; Time Factors
    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
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    Binding and factor XIIIa-mediated cross-linking of a 27-kilodalton fragment of fibronectin to Staphylococcus aureus (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Published by American Association for the Advancement of Science (AAAS)
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