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  • Amino Acid Sequence  (93)
  • Dose-Response Relationship, Drug  (89)
  • American Association for the Advancement of Science (AAAS)  (180)
  • Annual Reviews
  • International Union of Crystallography
  • 1980-1984  (180)
  • 1970-1974
  • 1955-1959
  • 1930-1934
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (180)
  • Annual Reviews
  • International Union of Crystallography
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
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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
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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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    Survival of mice receiving melanoma transplants is promoted by hydroquinone (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-04-25
    Description: In BALB/c female mice with melanoma transplants, the incidence of "takes" is decreased and survival is increased by hydroquinone, a melanocytolytic agent. The mechanism of drug action is suggested by via DNA. The significant and high degree of positive response to hydroquinone treatment in vivo is encouraging for the clinical management of melanoma with melanocytolytic agents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chavin, W -- Jelonek, E J Jr -- Reed, A H -- Binder, L R -- New York, N.Y. -- Science. 1980 Apr 25;208(4442):408-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7367868" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Disease Models, Animal ; Dose-Response Relationship, Drug ; Female ; Hydroquinones/metabolism/*therapeutic use ; Melanocytes/metabolism ; Melanoma/*drug therapy ; Mice ; Neoplasm Transplantation ; Neoplasms, Experimental/drug therapy
    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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    Oral contraceptives, lanosterol, and platelet hyperactivity in rat (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-11-07
    Description: Lanosterol, a cholesterol precursor that increases considerably in the platelets of rats treated with oral contraceptives, was incubated with either platelet-rich plasma or washed platelet suspension. After 2 minutes there was a remarkable dose-related increase in platelet activity. This platelet hyperactivity was measured by clotting time and platelet aggregation could not be reproduced by cholesterol or ethinylestradiol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ciavatti, M -- Dumont, E -- Benoit, C -- Renaud, S -- New York, N.Y. -- Science. 1980 Nov 7;210(4470):642-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7433990" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Coagulation/*drug effects ; Blood Platelets/*drug effects ; Contraceptives, Oral/*pharmacology ; Dose-Response Relationship, Drug ; Female ; Lanosterol/*pharmacology ; Platelet Aggregation/*drug effects ; Rats
    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
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    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
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  • 7
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    Mebendazole therapy of parenteral trichinellosis (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-03-14
    Description: Mebendazole was highly effective against the helminth parasite Trichinella spiralis in mice subjected to a 3-day course of treatment during the invasive and encystment phases of experimental trichinellosis. When treatment began either 2 or 4 weeks after the mice were inoculated with parasites, the number of larvae developing in the host musculature was greatly reduced by twice-daily oral administration of 3.125, 6.25, or 12.5 milligrams of mebendazole per kilogram of body weight.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCracken, R O -- Taylor, D D -- New York, N.Y. -- Science. 1980 Mar 14;207(4436):1220-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7355285" target="_blank"〉PubMed〈/a〉
    Keywords: Administration, Oral ; Animals ; Benzimidazoles/*therapeutic use ; Disease Models, Animal ; Dose-Response Relationship, Drug ; Larva ; Male ; Mebendazole/administration & dosage/*therapeutic use ; Mice ; Muscles/parasitology ; Trichinella/drug effects ; Trichinellosis/*drug therapy
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  • 8
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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
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  • 9
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    Substance P: does it produce analgesia or hyperalgesia? (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-04-18
    Description: In the hot plate test, substance P given intravenously at doses of 5 x 10-5 and 5 x 10-4 gram per kilogram caused analgesia, while lower doses caused hyperalgesia. The influence of substance P on nociception depended on the individual mouse's sensitivity to pain (control response latency). Analgesia was produced by substance P administered to mice with high sensitivity to thermic stimulation, whereas hyperalgesia occurred in mice whose control latencies were longer than normal. This result is interpreted as an indication that substance P is capable of normalizing responsiveness to pain and could be classified as a regulatory peptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oehme, P -- Hilse, H -- Morgenstern, E -- Gores, E -- New York, N.Y. -- Science. 1980 Apr 18;208(4441):305-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6154313" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates ; Animals ; Dose-Response Relationship, Drug ; Hot Temperature ; Hyperalgesia/*chemically induced ; Hyperesthesia/*chemically induced ; Mice ; Nociceptors/drug effects ; Pain/*physiopathology ; Perception/*drug effects ; Receptors, Drug/physiology ; Substance P/*pharmacology
    Print ISSN: 0036-8075
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  • 10
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    alpha-Lactalbumin-casein induction in virgin mouse mammary explants: dose-dependent differential action of cortisol (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-03-21
    Description: The interplay of insulin, cortisol, and prolactin induces synthesis of casein and alpha-lactalbumin in cultured mammary explants from mature virgin mice. A striking difference has been found between the optimal concentrations of cortisol required for maximal induction of the two milk proteins in vitro: 3 x 10(-8) molar for alpha-lactalbumin and 3 x 10(-6) molar for casein. Moreover, 10(-7) to 10(-5) molar cortisol caused progressive inhibition of alpha-lactalbumin accumulation. Such differential actions of cortisol may partly account for the asynchronous synthesis of the two proteins during pregnancy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ono, M -- Oka, T -- New York, N.Y. -- Science. 1980 Mar 21;207(4437):1367-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6986657" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caseins/*biosynthesis ; Dose-Response Relationship, Drug ; Drug Interactions ; Female ; Hydrocortisone/*pharmacology ; Insulin/pharmacology ; Lactalbumin/*biosynthesis ; Mammary Glands, Animal/drug effects/*metabolism ; Mice ; Organ Culture Techniques ; Pregnancy ; Prolactin/pharmacology
    Print ISSN: 0036-8075
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  • 11
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    Kindling induces long-lasting alterations in response of hippocampal neurons to elevated potassium levels in vitro (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-06-13
    Description: The cellular basis of kindling was studied electrophysiologically with slices of guinea pig hippocampus. Normally, epileptiform activity can be induced in the slices only by combined exposure to elevated potassium levels and a chemical convulsant such as penicillin. In hippocampal slices from pentylenetetrazole-kindled animals, however, elevated potassium alone can induce seizures. These data suggest that kindling elicits long-term changes in neuronal excitability that may involve ionic mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oliver, A P -- Hoffer, B J -- Wyatt, R J -- New York, N.Y. -- Science. 1980 Jun 13;208(4449):1264-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7375936" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Dose-Response Relationship, Drug ; Epilepsy/chemically induced/*physiopathology ; Guinea Pigs ; Hippocampus/drug effects/*physiology ; In Vitro Techniques ; Male ; Neurons/drug effects/physiology ; Pentylenetetrazole/administration & dosage/pharmacology ; Potassium/*pharmacology
    Print ISSN: 0036-8075
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  • 12
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    Food dyes impair performance of hyperactive children on a laboratory learning test (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-03-28
    Description: Forty children were given a diet free of artificial food dyes and other additives for 5 days. Twenty of the children had been classified as hyperactive by scores on the Conners Rating Scale and were reported to have favorable responses to stimulant medication. A diagnosis of hyperactivity had been rejected in the other 20 children. Oral challenges with large doses (100 or 150 milligrams) of a blend of FD & C approved food dyes or placebo were administered on days 4 and 5 of the experiment. The performance of the hyperactive children on paired-associate learning tests on the day they received the dye blend was impaired relative to their performance after they received the placebo, but the performance of the nonhyperactive group was not affected by the challenge with the food dye blend.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Swanson, J M -- Kinsbourne, M -- New York, N.Y. -- Science. 1980 Mar 28;207(4438):1485-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7361102" target="_blank"〉PubMed〈/a〉
    Keywords: Child ; Dose-Response Relationship, Drug ; Female ; Food Coloring Agents/*pharmacology ; Humans ; Hyperkinesis/*physiopathology ; Learning/*drug effects ; Male ; Time Factors
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  • 13
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    Genotoxicity of the antihypertensive drugs hydralazine and dihydralazine (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-10-17
    Description: The genotoxicity of the antihypertensive agents hydralazine and dihydralazine was tested in mammalian cells and bacteria. Both drugs elicited DNA repair in rat hepatocyte primary cultures. In the Ames test, both with and without an S-9 fraction, hydralazine was mutagenic in strains TA100 and TA1537, whereas dihydralazine was weakly mutagenic in strain TA1537. These findings support the observation that hydralazine is carcinogenic in mice. The carcinogenicity of many chemicals results from interaction with DNA. Since these studies demonstrate that hydralazine and dihydralazine damage DNA in mammalian cells, these drugs should be viewed as potential human carcinogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, G M -- Mazue, G -- McQueen, C A -- Shimada, T -- N 01-CP-55705/CP/NCI NIH HHS/ -- New York, N.Y. -- Science. 1980 Oct 17;210(4467):329-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7423193" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Animals ; Biotransformation ; *Carcinogens ; Cells, Cultured ; DNA Repair/*drug effects ; Dihydralazine/*toxicity ; Dose-Response Relationship, Drug ; Drug Evaluation, Preclinical ; Hydralazine/*analogs & derivatives/*toxicity ; Liver/metabolism ; *Mutagens ; Rats ; Salmonella typhi/drug effects
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  • 14
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    Multiple daily amphetamine administration: behavioral and neurochemical alterations (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-02-15
    Description: In rats, multiple daily amphetamine injections (2.5 milligrams per kilogram of body weight, injected subcutaneously every 4 hours for 5 days) resulted in a progressive augmentation in response, characterized by a more rapid onset and an increased magnitude of stereotypy. By contrast, offset times of both the stereotypy and the poststereotypy hyperactivity periods were markedly shortened. When the animals were retested with the same dose of amphetamine 8 days after the long-term treatment was discontinued, the time of offset of the stereotypy and hyperactivity phases had recovered to values found with short-term amphetamine treatment, whereas the more rapid onset of stereotypy persisted. Brain monoamine and amphetamine concentrations and tyrosine hydroxylase activity were determined in comparably treated rats at times corresponding to the behavioral observations. The behavioral data indicate that enhanced responsiveness to amphetamine following its repeated administration may contribute to the development of amphetamine psychosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Segal, D S -- Weinberger, S B -- Cahill, J -- McCunney, S J -- New York, N.Y. -- Science. 1980 Feb 15;207(4433):905-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7188815" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior/*drug effects ; Behavior, Animal/*drug effects ; Brain/metabolism ; Brain Chemistry/drug effects ; Dextroamphetamine/administration & dosage/*pharmacology ; Dopamine/metabolism ; Dose-Response Relationship, Drug ; Humans ; Male ; Motor Activity/drug effects ; Norepinephrine/metabolism ; Rats ; Serotonin/metabolism ; Stereotyped Behavior/*drug effects ; Time Factors
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  • 15
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    Cloned viral protein vaccine for foot-and-mouth disease: responses in cattle and swine (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-12-04
    Description: A DNA sequence coding for the immunogenic capsid protein VP3 of foot-and-mouth disease virus A12, prepared from the virion RNA, was ligated to a plasmid designed to express a chimeric protein from the Escherichia coli tryptophan promoter-operator system. When Escherichia coli transformed with this plasmid was grown in tryptophan-depleted media, approximately 17 percent of the total cellular protein was found to be an insoluble and stable chimeric protein. The purified chimeric protein competed equally on a molar basis with VP3 for specific antibodies to foot-and-mouth disease virus. When inoculated into six cattle and two swine, this protein elicited high levels of neutralizing antibody and protection against challenge with foot-and-mouth disease virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kleid, D G -- Yansura, D -- Small, B -- Dowbenko, D -- Moore, D M -- Grubman, M J -- McKercher, P D -- Morgan, D O -- Robertson, B H -- Bachrach, H L -- New York, N.Y. -- Science. 1981 Dec 4;214(4525):1125-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6272395" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibody Formation ; Base Sequence ; Cattle ; Cattle Diseases/*prevention & control ; *Cloning, Molecular ; DNA Restriction Enzymes ; DNA, Recombinant/metabolism ; Foot-and-Mouth Disease/*prevention & control ; Immunity, Cellular ; Protein Biosynthesis ; Swine ; Swine Diseases/*prevention & control ; Transcription, Genetic ; *Vaccines ; Viral Proteins/genetics/*therapeutic use
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  • 16
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    Calcitonin messenger RNA encodes multiple polypeptides in a single precursor (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-07-24
    Description: Recombinant DNA techniques were used to analyze the structure of the messenger RNA encoding a precursor of calcitonin, a small calcium-regulating hormone of 32 amino acids. Analyses of the nucleotide sequences of cloned complementary DNA's comprising the entire coding sequence of the messenger RNA revealed that calcitonin is flanked at both its amino and carboxyl termini by peptide extensions linked to the hormone by short sequences of basic amino acids. The location of glycine next to the carboxyl terminal prolinamide of calcitonin is consistent with indications that glycine is required for the enzymatic amidation of proline to the prolinamide. During cellular biosynthesis, calcitonin arises from a large precursor protein by cleavages at both amino and carboxyl terminal residues of the hormone. These findings raise questions concerning the regulation of these cleavages and the potential biological functions of the precursor extensions derived from these cleavages.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobs, J W -- Goodman, R H -- Chin, W W -- Dee, P C -- Habener, J F -- Bell, N H -- Potts, J T Jr -- AM 27781-01/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1981 Jul 24;213(4506):457-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6264603" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Calcitonin/*genetics ; Cloning, Molecular ; DNA Restriction Enzymes ; DNA, Recombinant/*metabolism ; Macromolecular Substances ; Neoplasms, Experimental/metabolism ; Nucleic Acid Hybridization ; Peptide Biosynthesis ; Plants/metabolism ; Protein Biosynthesis ; RNA, Messenger/*genetics ; Rats ; Thyroid Neoplasms/metabolism ; Triticum/metabolism
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  • 17
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    2,4,5-trichlorophenoxyacetic acid causes behavioral effects in chickens at environmentally relevant doses (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-02-06
    Description: Administration of the herbicide 2,4,5-trichlorophenoxyacetic acid to incubating chicken eggs alters behavior after hatching. Single doses, with no morphological effects, retard learning (lowest dose, 7 milligrams per kilogram of body weight) and increase general activity (27 milligrams per kilogram) and jumping (13 milligrams per kilogram). Day 15 of incubation is the most susceptible stage of development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sanderson, C A -- Rogers, L J -- New York, N.Y. -- Science. 1981 Feb 6;211(4482):593-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7455699" target="_blank"〉PubMed〈/a〉
    Keywords: 2,4,5-Trichlorophenoxyacetic Acid/*pharmacology/toxicity ; Age Factors ; Animals ; Behavior, Animal/*drug effects ; Chick Embryo/drug effects ; Chickens ; Discrimination Learning/drug effects ; Dose-Response Relationship, Drug ; Motor Activity/drug effects
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  • 18
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    Determination of nucleotide sequences in DNA (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-12-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sanger, F -- New York, N.Y. -- Science. 1981 Dec 11;214(4526):1205-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7302589" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacteriophages/genetics ; *Base Sequence ; Cloning, Molecular ; DNA/*genetics ; DNA, Mitochondrial/genetics ; DNA, Single-Stranded/genetics ; DNA-Directed DNA Polymerase ; Humans ; Protein Biosynthesis ; Templates, Genetic
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  • 19
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    Bee venom enhances guanylate cyclase activity (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-07-17
    Description: Bee venom and phospholipase A2 extracted from bee venom enhanced guanylate cyclase (E.C. 4.6.1.2) activity two- to threefold in rat liver, lung, heart, kidney, ileum, and cerebellum. Dose-response relationships revealed that bee venom at concentrations as low as 1 microgram per milliliter and phospholipase A2 at 1 microunit per milliliter caused a maximal enhancement of guanylate cyclase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vesely, D L -- New York, N.Y. -- Science. 1981 Jul 17;213(4505):359-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6113689" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bee Venoms/*pharmacology ; Dose-Response Relationship, Drug ; Enzyme Activation ; Guanylate Cyclase/*metabolism ; Kinetics ; Organ Specificity ; Phospholipases/*pharmacology ; Phospholipases A/*pharmacology ; Phospholipases A2 ; Rats
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  • 20
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    Chemical impurity produces extra compound eyes and heads in crickets (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-04-03
    Description: A chemical impurity isolated from commercially purchased acridine causes cricket embryos to develop extra compound eyes, branched antennae, extra antennae, and extra heads. Purified acridine does not produce similar duplications of cricket heads or head structures nor do the substituted acridines proflavine, acriflavine, or acridine orange. A dose-response relation exists such that the number and severity of abnormalities increase with increasing concentration of the teratogen.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walton, B T -- New York, N.Y. -- Science. 1981 Apr 3;212(4490):51-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6782672" target="_blank"〉PubMed〈/a〉
    Keywords: Abnormalities, Multiple/chemically induced ; Acridines/*isolation & purification/pharmacology ; Animals ; Dose-Response Relationship, Drug ; Drug Contamination ; Embryo, Nonmammalian/drug effects ; Eye Abnormalities ; Head/abnormalities ; Orthoptera/*drug effects ; *Teratogens
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  • 21
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    Ethanol tolerance in the rat is learned (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-07-31
    Description: Rats were trained to walk on a treadmill to avoid foot shock. The animals developed tolerance for ethanol if given subsequent practice while ethanol intoxicated. Rats given equivalent doses of ethanol after practice did not develop tolerance, nor did saline-treated controls. These results challenge the hypothesis that mere repeated doses of ethanol are sufficient to induce tolerance. It seems that tolerance does not develop unless the response used to measure tolerance is performed while the subject is intoxicated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wenger, J R -- Tiffany, T M -- Bombardier, C -- Nicholls, K -- Woods, S C -- 03504/PHS HHS/ -- AA 04658/AA/NIAAA NIH HHS/ -- New York, N.Y. -- Science. 1981 Jul 31;213(4507):575-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7244656" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avoidance Learning/*drug effects ; Dose-Response Relationship, Drug ; Drug Tolerance ; Ethanol/blood/*pharmacology ; Rats
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  • 22
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    Calcium ionophore polarizes ooplasmic segregation in ascidian eggs (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-04-30
    Description: Calcium ionophore A23187 promotes ooplasmic segregation and orange crescent formation in eggs of the ascidian Boltenia villosa. When eggs were exposed to a gradient A23187 the orange crescent was induced to form in the region corresponding to the highest concentration of ionophore. This result is consistent with the hypothesis that a local increase in intracellular calcium polarizes cytoplasmic localization in the ascidian embryo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jeffery, W R -- 232-HDO-7098/HD/NICHD NIH HHS/ -- HD-13970/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1982 Apr 30;216(4545):545-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6803360" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Bacterial Agents/*pharmacology ; Calcimycin/*pharmacology ; Calcium/*physiology ; Cell Compartmentation/drug effects ; Cytoplasm/ultrastructure ; Dose-Response Relationship, Drug ; Female ; Ovum/*drug effects/ultrastructure ; Urochordata
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  • 23
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    Naloxone antagonism of the thermoregulatory effects of phencyclidine (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-09-24
    Description: Phencyclidine elicits hyperthermia at low doses and hypothermia at high doses in rats. Naloxone antagonizes both effects. Phencyclidine's effects on thermo-regulation are probably mediated by an interaction with a mu opiate receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Glick, S D -- Guido, R A -- DA 02534/DA/NIDA NIH HHS/ -- DA 70082/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1982 Sep 24;217(4566):1272-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6287581" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Temperature Regulation/*drug effects ; Dose-Response Relationship, Drug ; Female ; Naloxone/pharmacology ; Phencyclidine/antagonists & inhibitors/*pharmacology ; Rats ; Receptors, Opioid/*drug effects
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  • 24
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    alpha A-crystallin messenger RNA of the mouse lens: more noncoding than coding sequences (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-02-19
    Description: The 14S messenger RNA (1300 to 1500 nucleotides) for the alpha A chain of alpha-crystallin of the mammalian lens is nearly three times larger than required to code for the polypeptide that contains 173 amino acids. As a means of accounting for this anomaly, a complementary DNA clone for the mouse alpha A-crystallin messenger RNA was constructed in pBR322 and sequenced. Derivation of the protein sequence from the nucleic acid sequence showed that mouse alpha A-crystallin is similar to that of other organisms. The messenger RNA contains 536 nucleotides located on the 3' side of the coding region, excluding the polyadenylate stretch. This 3' sequence does not encode any other crystallin and has multiple termination codons in the three possible reading frames.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, C R -- Shinohara, T -- Piatigorsky, J -- New York, N.Y. -- Science. 1982 Feb 19;215(4535):985-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7156978" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; Crystallins/*genetics ; Mice ; RNA, Messenger/*genetics
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  • 25
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    Complete amino acid sequence of urotensin I, a hypotensive and corticotropin-releasing neuropeptide from Catostomus (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-10-08
    Description: Urotensin I, purified from extracts of the urophysis of a teleost fish (Catostomus commersoni), exhibits potent hypotensive activity (mammals and birds) and corticotropin-releasing activity (both fish and mammals). The primary structure of this 41-residue peptide was determined to be H-Asn-Asp-Asp-Pro-Pro-Ile-Ser-Ile-Asp-Leu-Thr-Phe-His-Leu-Leu-Arg-Asn-Met-Ile-Glu - Met-Ala-Arg-Ile-Glu-Asn-Glu-Arg-Glu-Gln-Ala-Gly-Leu-Asn-Arg-Lys-Tyr-Leu-Asp-Glu -Val-NH2. Extraction with 0.1N HCl at 100 degrees C cleaves the amino-terminal tripeptide, yeilding a fully active analog, urotensin I(4-41). The amino acid sequence was confirmed by measuring the biological activity of synthetic urotensin I(4-41). Urotensin I exhibits a striking sequence homology with ovine corticotropin-releasing factor and with frog sauvagine. These three peptides exhibit similar activities in biological test systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lederis, K -- Letter, A -- McMaster, D -- Moore, G -- Schlesinger, D -- New York, N.Y. -- Science. 1982 Oct 8;218(4568):162-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6981844" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Corticotropin-Releasing Hormone ; Fishes ; Peptides/*isolation & purification ; Species Specificity ; Urotensins/*isolation & purification
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  • 26
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    Somatic mutation in genes for the variable portion of the immunoglobulin heavy chain (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-04-16
    Description: The size of the gene pool potentially encoding antibodies to p-azophenyl arsonate has been examined. A heavy chain-specific full-length complementary DNA clone has been constructed with the use of messenger RNA from a hybridoma that produces antibodies to the arsonate hapten and bears nearly a full complement of the determinants comprising the cross-reactive idiotype (CRI). The sequences of both the complementary DNA clone and the corresponding immunoglobulin heavy chain have been independently determined. A probe for the variable region gene was prepared from the original heavy chain complementary DNA clone and used to analyze, by Southern filter hybridization, genomic DNA from both A/J (CRI positive) and BALB/c (CRI negative) mice. Approximately 20 to 25 restriction fragments containing "germline" variable region gene segments were detected in both strains, and many are shared by both, Since 35 CRI-positive heavy chains have been partially sequenced thus far and 31 are different, the results of the hybridization analysis suggest that somatic mutation events involving the variable region gene segments of the heavy chain play a role in the origin of the amino acid sequence diversity seen in this system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sims, J -- Rabbitts, T H -- Estess, P -- Slaughter, C -- Tucker, P W -- Capra, J D -- A112127/PHS HHS/ -- AI-06020/AI/NIAID NIH HHS/ -- AI18016/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1982 Apr 16;216(4543):309-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6801765" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites, Antibody/*genetics ; Genes ; Haptens ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin Idiotypes/genetics ; Immunoglobulin Variable Region/*genetics ; Mice ; *Mutation
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    Neuronal cell Thy-1 glycoprotein: homology with immunoglobulin (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-05-14
    Description: The amino acid sequences of mouse brain Thy-1 glycoproteins are shown to be homologous to those of variable-region immunoglobulin domains. There is also good homology with constant domains and beta 2-microglobulin; overall the results suggest that Thy-1 may be like the primordial immunoglobulin domain. Preliminary evidence for an invertebrate Thy-1 homolog supports this possibility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, A F -- Gagnon, J -- New York, N.Y. -- Science. 1982 May 14;216(4547):696-703.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6177036" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Surface/*immunology ; Antigens, Thy-1 ; Biological Evolution ; Epitopes ; Glycoproteins/*immunology ; Immunoglobulin Constant Regions/immunology ; Immunoglobulin Variable Region/immunology ; Immunoglobulins/*immunology ; Isoantibodies/biosynthesis ; Protein Conformation
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    Alcohol and pregnancy (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-09-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1983 Sep 23;221(4617):1244-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6684327" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Dose-Response Relationship, Drug ; Ethanol/*adverse effects ; Female ; Pregnancy ; Pregnancy, Animal/*drug effects
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  • 29
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    Human platelet-derived growth factor (PDGF): amino-terminal amino acid sequence (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-05-27
    Description: Human platelet-derived growth factor (PDGF) obtained from outdated human platelets was subjected to amino-terminal amino acid sequence analysis by automated Edman degradation. Despite the apparent presence of limited proteolytic degradation of the protein derived from this method, the sequence analysis reveals two primary peptide sequences and suggests that active PDGF is composed of two, possibly homologous, peptides linked by a disulfide bond or bonds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Antoniades, H N -- Hunkapiller, M W -- CA30101/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1983 May 27;220(4600):963-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6844921" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Electrophoresis, Polyacrylamide Gel ; Growth Substances/genetics/*metabolism ; Humans ; Molecular Weight ; Peptides/genetics/*metabolism ; Platelet-Derived Growth Factor
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  • 30
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    Platelet thromboxane synthetase inhibitors with low doses of aspirin: possible resolution of the "aspirin dilemma" (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-04-29
    Description: Selective pharmacological inhibition of thromboxane A2 synthesis did not prevent arachidonate-induced aggregation of human platelets in vitro. Prevention was instead achieved by a combination of thromboxane A2 inhibitors with low concentrations of aspirin. The latter partially reduced the proaggregatory cyclooxygenase products that accumulated when thromboxane A2 synthesis was blocked. The aspirin concentrations did not affect per se either platelet aggregation or prostacyclin synthesis in cultured human endothelial cells. The combination of thromboxane synthetase inhibitors with low doses of aspirin may offer greater antithrombotic potential than either drug alone.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bertele, V -- Falanga, A -- Tomasiak, M -- Dejana, E -- Cerletti, C -- de Gaetano, G -- New York, N.Y. -- Science. 1983 Apr 29;220(4596):517-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6682245" target="_blank"〉PubMed〈/a〉
    Keywords: Aspirin/*pharmacology ; Blood Platelets/*drug effects/enzymology ; Dose-Response Relationship, Drug ; Drug Interactions ; Humans ; Imidazoles/pharmacology ; Methacrylates/pharmacology ; Oxidoreductases/*antagonists & inhibitors ; Platelet Aggregation/drug effects ; Thromboxane-A Synthase/*antagonists & inhibitors
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  • 31
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    Splice junctions: association with variation in protein structure (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-06-10
    Description: A comparison between eukaryotic gene sequences and protein sequences of homologous enzymes from bacterial and mammalian organisms shows that intron-exon junctions frequently coincide with variable surface loops of the protein structures. The altered surface structures can account for functional differences among the members of a family. Sliding of the intron-exon junctions may constitute one mechanism for generating length polymorphisms and divergent sequences found in protein families. Since intron-exon junctions map to protein surfaces, the alterations mediated by sliding of these junctions can be effected without disrupting the stability of the protein core.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Craik, C S -- Rutter, W J -- Fletterick, R -- AM21344/AM/NIADDK NIH HHS/ -- AM26081/AM/NIADDK NIH HHS/ -- GM28520/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Jun 10;220(4602):1125-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344214" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Proteins ; Base Sequence ; Biological Evolution ; DNA/genetics ; Endopeptidases/genetics ; Eukaryotic Cells/metabolism ; Genes ; Genes, Bacterial ; Protein Conformation ; Proteins/*genetics ; *Serine Endopeptidases ; Tetrahydrofolate Dehydrogenase/genetics
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  • 32
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    Bioactive cardiac substances: potent vasorelaxant activity in mammalian atria (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-07-01
    Description: Mammalian atrial extracts possess natriuretic and diuretic activity. In experiments reported here it was found that atrial, but not ventricular, extract also causes relaxation of isolated vascular and nonvascular smooth muscle preparations. The smooth muscle relaxant activity of atrial extract was heat-stable and concentration-dependent and could be destroyed with protease. Rabbit aortic and chick rectum strips were used for the detection of atrial biological activity. The atrial activity was separated by column chromatography into two peaks having apparent molecular weights of 20,000 to 30,000 and less than 10,000. The atrial substance that copurified with the smooth muscle relaxant activity in both peaks caused natriuresis when injected into conscious rats. It appears that atria possess at least two peptides that elicit smooth muscle relaxation and natriuresis, suggesting an endogenous system of fluid volume regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Currie, M G -- Geller, D M -- Cole, B R -- Boylan, J G -- YuSheng, W -- Holmberg, S W -- Needleman, P -- New York, N.Y. -- Science. 1983 Jul 1;221(4605):71-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6857267" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Atrial Function ; Chickens ; Chromatography, Gel ; Dogs ; Dose-Response Relationship, Drug ; Humans ; Molecular Weight ; Muscle, Smooth/drug effects ; Muscle, Smooth, Vascular/*drug effects ; Natriuresis/drug effects ; Rabbits ; Rats ; Swine ; Vasodilation/drug effects
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    Drug history modifies the behavioral effects of pentobarbital (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-04-15
    Description: Behavior of squirrel monkeys, maintained by the termination of stimuli associated with electric shock, was suppressed by response-dependent shock delivery. The effects of pentobarbital on this behavior depended on whether monkeys had previously received morphine. In monkeys without experience with drugs, pentobarbital increased responding. In monkeys with recent experience with morphine, however, pentobarbital resulted in a smaller increase or decrease in responding. The rate-decreasing effects of pentobarbital after a history of morphine administration could be reversed by the administration of d-amphetamine. These findings suggest that the behavioral effects of abused drugs may depend on previous experience with other drugs, even when those drugs are from a different pharmacological class.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Glowa, J R -- Barrett, J E -- DA 02658/DA/NIDA NIH HHS/ -- DA 02873/DA/NIDA NIH HHS/ -- MH 07658/MH/NIMH NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 Apr 15;220(4594):333-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6682244" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior, Animal/*drug effects ; Dextroamphetamine/pharmacology ; Dose-Response Relationship, Drug ; Drug Interactions ; Humans ; Macaca mulatta ; Male ; Morphine/pharmacology ; Pentobarbital/*pharmacology ; Saimiri ; Substance-Related Disorders/physiopathology
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    The thymus-adrenal connection: thymosin has corticotropin-releasing activity in primates (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-12-23
    Description: Endotoxin-free thymosin fraction 5 elevated corticotropin, beta-endorphin, and cortisol in a dose- and time-dependent fashion when administered intravenously to prepubertal cynomolgus monkeys. Two synthetic component peptides of thymosin fraction 5 had no acute effects on pituitary function, suggesting that some other peptides in thymosin fraction 5 were responsible for its corticotropin-releasing activity. In agreement with these observations, total thymectomy of juvenile macaques was associated with decreases in plasma cortisol, corticotropin, and beta-endorphin. These findings indicate that the prepubertal primate thymus contains corticotropin-releasing activity that may contribute to a physiological immunoregulatory circuit between the developing immunological and pituitary-adrenal systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Healy, D L -- Hodgen, G D -- Schulte, H M -- Chrousos, G P -- Loriaux, D L -- Hall, N R -- Goldstein, A L -- CA 24974/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1983 Dec 23;222(4630):1353-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6318312" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenocorticotropic Hormone/*blood ; Animals ; Dose-Response Relationship, Drug ; Endorphins/blood ; Female ; Hydrocortisone/blood ; Kinetics ; Macaca fascicularis ; Thymectomy ; Thymosin/analogs & derivatives/*pharmacology ; Thymus Gland/*physiology ; beta-Endorphin
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  • 35
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    Implication of nonlinear kinetics on risk estimation in carcinogenesis (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-03-04
    Description: Efforts in estimating carcinogenic risk in humans from long-term exposure to chemical carcinogens have centered on the problem of low-dose extrapolation. For chemicals with metabolites that interact with DNA, it may be more meaningful to relate tumor response to the concentration of the DNA adducts in the target organ rather than to the applied dose. Many data suggest that the relation between tumor response and concentration of DNA adducts in the target organ may be linear. This implies that the nonlinearities of the dose-response curve for tumor induction may be due to the kinetic processes involved in the formation of carcinogen metabolite--DNA adducts. Of particular importance is the possibility that the kinetic processes may show a nonlinear "hockey-stick" like behavior which results from saturation of detoxification or DNA repair processes. The mathematical models typically used for low-dose extrapolation are shown potentially to overestimate risk by several orders of magnitude when nonlinear kinetics are present.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoel, D G -- Kaplan, N L -- Anderson, M W -- New York, N.Y. -- Science. 1983 Mar 4;219(4588):1032-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6823565" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carcinogens/*administration & dosage ; Cell Transformation, Neoplastic/*drug effects ; DNA, Neoplasm/genetics ; Dose-Response Relationship, Drug ; Humans ; Kinetics ; Models, Biological ; Neoplasms/*chemically induced ; Risk
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  • 36
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    A parathyroid hormone inhibitor in vivo: design and biological evaluation of a hormone analog (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-06-03
    Description: A synthetic analog of bovine parathyroid hormone (bPTH), [tyrosine-34] bPTH-(7-34)NH2, was found to inhibit parathyroid hormone action in vivo. When the analog and parathyroid hormone were infused simultaneously to rats at a molar ratio of 200 to 1, the analog inhibited the excretion of urinary phosphate and adenosine 3',5'-monophosphate. When infused alone at the same dose rate, the analog was devoid of agonist activity. The compound was prepared by following design principles developed for inhibitors of parathyroid hormone, and is believed to be the first antagonist of parathyroid hormone that is effective in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Horiuchi, N -- Holick, M F -- Potts, J T Jr -- Rosenblatt, M -- AM11749/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1983 Jun 3;220(4601):1053-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6302844" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cyclic AMP/urine ; Dose-Response Relationship, Drug ; Male ; Parathyroid Hormone/*antagonists & inhibitors/*pharmacology ; Peptide Fragments/*pharmacology ; Phosphates/urine ; Rats
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  • 37
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    Requirement for signal peptide cleavage of Escherichia coli prolipoprotein (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-07-01
    Description: Oligonucleotide-directed site-specific mutagenesis was applied to alter the cleavage site in the signal peptide of the major outer membrane lipoprotein of Escherichia coli. Replacing the glycine residue at the cleavage site with an alanine residue did not affect the processing of the signal peptide. However, when the same cleavage site was constructed by the deletion of the glycine residue, the signal peptide was no longer cleaved. These results indicate that stringent structural integrity at the cleavage site in the lipoprotein signal sequence is required for correct processing of prolipoprotein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inouye, S -- Hsu, C P -- Itakura, K -- Inouye, M -- GM19043/GM/NIGMS NIH HHS/ -- GM30395/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 1;221(4605):59-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344218" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Bacterial Outer Membrane Proteins ; Base Sequence ; DNA, Bacterial/metabolism ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/*metabolism ; *Escherichia coli Proteins ; Lipoproteins/*biosynthesis ; Membrane Proteins/biosynthesis ; Mutation ; Protein Precursors/*biosynthesis
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  • 38
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    Fragile sites in chromosomes: possible model for the study of spontaneous chromosome breakage (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-04-01
    Description: The tissue culture condition that is required for the type of chromosome breakage seen at most fragile sites, namely, the absence of folic acid and thymidine in the medium, greatly enhanced micronucleus formation in proliferating lymphocyte cultures from normal individuals. This suggests that chromosome breakage at fragile sites and the apparently spontaneous damage that gives rise to micronuclei are controlled by the same mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacky, P B -- Beek, B -- Sutherland, G R -- New York, N.Y. -- Science. 1983 Apr 1;220(4592):69-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6828880" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Cell Nucleus/drug effects/ultrastructure ; Cells, Cultured ; Child ; *Chromosome Aberrations ; Chromosome Fragile Sites ; *Chromosome Fragility ; Culture Media ; Dose-Response Relationship, Drug ; Female ; Folic Acid/pharmacology ; Humans ; Lymphocytes/ultrastructure ; Male ; Middle Aged ; Thymidine/pharmacology
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  • 39
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    Inhibition of gastric acid secretion in rats by intracerebral injection of corticotropin-releasing factor (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-11-25
    Description: Intracisternal injection of ovine corticotropin-releasing factor (CRF) into the pylorus-ligated rat or the rat with gastric fistula resulted in a dose-dependent inhibition of gastric secretion stimulated with pentagastrin or thyrotropin-releasing hormone. When injected into the lateral hypothalamus--but not when injected into the cerebral cortex--CRF suppressed pentagastrin-stimulated acid secretion. The inhibitory effect of CRF was blocked by vagotomy and adrenalectomy but not by hypophysectomy or naloxone treatment. These results indicate that CRF acts within the brain to inhibit gastric acid secretion through vagal and adrenal mechanisms and not through hypophysiotropic effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tache, Y -- Goto, Y -- Gunion, M W -- Vale, W -- River, J -- Brown, M -- AM30110/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 25;222(4626):935-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6415815" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenalectomy ; Animals ; Brain/*drug effects ; Cerebral Cortex/drug effects ; Corticotropin-Releasing Hormone/administration & dosage/*pharmacology ; Dose-Response Relationship, Drug ; Gastric Acid/*secretion ; Hypophysectomy ; Hypothalamus/drug effects ; Male ; Pentagastrin/antagonists & inhibitors ; Rats ; Rats, Inbred Strains ; Thyrotropin-Releasing Hormone/antagonists & inhibitors ; Vagotomy
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    Monoclonal antibodies reveal the structural basis of antibody diversity (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-11-18
    Description: Hybridoma technology has made it possible to introduce into continuous culture normal antibody-forming cells and to obtain large amounts of the immunoglobulin produced by each of these cells. Examination of the structure of a number of monoclonal antibodies that react with a single antigen has provided new information on the structural basis of the specificity and affinity of antibodies. Comparisons of families of monoclonal antibodies derived from a single germ line gene revealed the importance of somatic mutation in generating antibody diversity. Monoclonal antibodies that react with variable regions of other monoclonals allow the further dissection and modulation of the immune response. Finally, the continued somatic instability of immunoglobulin genes in cultured antibody-forming cells makes it possible to determine the rate of somatic mutation and to generate mutant monoclonal antibodies that may be more effective serological reagents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teillaud, J L -- Desaymard, C -- Giusti, A M -- Haseltine, B -- Pollock, R R -- Yelton, D E -- Zack, D J -- Scharff, M D -- 5T32GM7288/GM/NIGMS NIH HHS/ -- AI05231/AI/NIAID NIH HHS/ -- AI10702/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):721-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356353" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/genetics/*immunology ; *Antibody Diversity ; Antibody Specificity ; Genes ; Hybridomas/immunology ; Immunoglobulin Idiotypes/immunology ; Immunoglobulin Variable Region/genetics ; Mice ; Mutation ; Protein Conformation ; Structure-Activity Relationship
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  • 41
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    Rabies virus glycoprotein analogs: biosynthesis in Escherichia coli (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-02-11
    Description: The surface of rabies virus is composed of an approximately 60,000 dalton glycoprotein, in which most of the antigenic and immunogenic determinants of the virus reside. We have constructed plasmids for the direct expression in Escherichia coli of the mature full length rabies glycoprotein gene and also for the expression of a glycoprotein gene which has been truncated to exclude the coding region for a hydrophobic, possibly transmembrane, domain of the protein. Escherichia coli harboring the plasmids synthesize analog proteins which conform by several biochemical and antigenic criteria to rabies glycoprotein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yelverton, E -- Norton, S -- Obijeski, J F -- Goeddel, D V -- New York, N.Y. -- Science. 1983 Feb 11;219(4585):614-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6297004" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cloning, Molecular ; Escherichia coli ; Genes, Viral ; Genetic Vectors ; Glycoproteins/*genetics/immunology ; Plasmids ; Rabies virus/*genetics/immunology ; Viral Proteins/immunology
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  • 42
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    Criteria for evidence of chemical carcinogenicity. Interdisciplinary Panel on Carcinogenicity (1984)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1984-08-17
    Description: The Interdisciplinary Panel on Carcinogenicity reviewed and reevaluated criteria for assessing evidence of carcinogenicity of chemical substances. The panel reviewed criteria applicable to data derived from human epidemiological studies and from both in vivo and in vitro laboratory studies. A critical appraisal of all these sources of information led to the conclusion that the characterization of human risk always requires interdisciplinary evaluation of the entire array of data on a case-by-case basis. Animal studies, whenever possible, should be augmented by studies of mechanisms, metabolism, and pharmacodynamics. Such studies may assist in assessing risk to man. Recognizing the utility of such data should point the way for better assessment in the future.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1984 Aug 17;225(4663):682-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6463646" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Assay ; *Carcinogens/metabolism/pharmacology ; Carcinogens, Environmental ; Cell Transformation, Neoplastic ; Dose-Response Relationship, Drug ; Environmental Exposure ; Epidemiologic Methods ; Humans ; In Vitro Techniques ; Mixed Function Oxygenases/metabolism ; Mutagenicity Tests ; Neoplasms/chemically induced ; Risk ; Time Factors ; United States
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  • 43
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    Structure of a mouse submaxillary messenger RNA encoding epidermal growth factor and seven related proteins (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-07-15
    Description: The structure of the messenger RNA (mRNA) encoding the precursor to mouse submaxillary epidermal growth factor (EGF) was determined from the sequence of a set of overlapping complementary DNA's (cDNA). The mRNA is unexpectedly large, about 4750 nucleotide bases, and predicts the sequence of preproEGF, a protein of 1217 amino acids (133,000 molecular weight). The EGF moiety (53 amino acids) is flanked by polypeptide segments of 976 and 188 amino acids at its amino and carboyxl termini, respectively. The amino terminal segment of the precursor contains seven peptides with sequences that are similar but not identical to EGF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, J -- Urdea, M -- Quiroga, M -- Sanchez-Pescador, R -- Fong, N -- Selby, M -- Rutter, W J -- Bell, G I -- 21344/PHS HHS/ -- New York, N.Y. -- Science. 1983 Jul 15;221(4607):236-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6602382" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Epidermal Growth Factor/biosynthesis/*genetics ; Humans ; Male ; Mice ; RNA, Messenger/*genetics ; Submandibular Gland/metabolism
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  • 44
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    Structure of the gene encoding the immunodominant surface antigen on the sporozoite of the human malaria parasite Plasmodium falciparum (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-08-10
    Description: The gene for the circumsporozoite (CS) protein of Plasmodium falciparum has been cloned and its nucleotide sequence determined. The gene encodes a protein of 412 amino acids as deduced from the nucleotide sequence. The protein contains 41 tandem repeats of a tetrapeptide, 37 of which are Asn-Ala-Asn-Pro and four of which are Asn-Val-Asp-Pro. Monoclonal antibodies against the CS protein of Plasmodium falciparum were inhibited from binding to the protein by synthetic peptides of the repeat sequence. The CS protein of Plasmodium falciparum and the CS protein of a simian malaria parasite, Plasmodium knowlesi, have two regions of homology, one of which is present on either side of the repeat. One region contains 12 of 13 identical amino acids. Within the nucleotide sequence of this region, 25 of 27 nucleotides are conserved. The conservation of these regions in parasites widely separated in evolution suggests that they may have a function such as binding to liver cells and may represent an invariant target for immunity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dame, J B -- Williams, J L -- McCutchan, T F -- Weber, J L -- Wirtz, R A -- Hockmeyer, W T -- Maloy, W L -- Haynes, J D -- Schneider, I -- Roberts, D -- New York, N.Y. -- Science. 1984 Aug 10;225(4662):593-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6204383" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal/immunology ; Antigens, Surface/*genetics/immunology ; Base Sequence ; Epitopes/genetics ; *Genes ; Humans ; Liver/parasitology ; Malaria/*immunology ; Plasmodium/genetics ; Plasmodium falciparum/*genetics/immunology ; *Protozoan Proteins
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    Nucleotide sequence of a human Blym transforming gene activated in a Burkitt's lymphoma (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-08-03
    Description: The nucleotide sequence of a human Blym-1 transforming gene activated in a Burkitt's lymphoma cell line was determined. This sequence predicts a small protein of 58 amino acids that is 33 percent identical to the predicted product of chicken Blym-1, the activated transforming gene of chicken B cell lymphomas. Both the human and chicken Blym-1 genes exhibit significant identity to an amino-terminal region of transferrins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diamond, A -- Devine, J M -- Cooper, G M -- CA 07250/CA/NCI NIH HHS/ -- CA 28946/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Aug 3;225(4661):516-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6330897" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Burkitt Lymphoma/*genetics ; Cell Line ; *Cell Transformation, Neoplastic ; DNA Restriction Enzymes ; Humans ; *Oncogenes ; Structure-Activity Relationship ; Transcription, Genetic ; Transferrin/genetics
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    Human-proto-oncogene nucleotide sequences corresponding to the transforming region of simian sarcoma virus (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-02-03
    Description: The nucleotide sequences of the six regions within the normal human cellular locus (c-sis) that correspond to the entire transforming region of the simian sarcoma virus (SSV) genome (v-sis) were determined. The regions are bounded by acceptor and donor splice sites and, except for region 6, resemble exons. Region 6 lacks a 3' donor splice site and terminates -5 base pairs from the 3' v-sis-helper-viral junction. This is consistent with a model proposing that SSV was generated by recombination between proviral DNA of a simian sarcoma associated virus and proto-sis and that introns were spliced out subsequently from a fused viral-sis messenger RNA. This also suggests that the 3' recombination occurred within an exon of the woolly monkey (Lagothrix) genome. The open reading frames predicting the v-sis and c-sis gene products coincide with the stop codon of c-sis located 123 nucleotides into the fifth region of homology. The overall nucleotide homology was 91 percent with substitutions mainly in the third codon positions within the open reading frame and with greatest divergence within the untranslated 3' portion of the sequences. The predicted protein products for v-sis and c-sis are 93 percent homologous. The predicted c-sis gene product is identical in 31 of 31 amino acids to one of the published sequences of platelet-derived growth factor. Thus, c-sis encodes one chain of human platelet-derived growth factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Josephs, S F -- Guo, C -- Ratner, L -- Wong-Staal, F -- New York, N.Y. -- Science. 1984 Feb 3;223(4635):487-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6318322" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Transformation, Neoplastic ; Cell Transformation, Viral ; Codon ; *Genes, Viral ; Humans ; *Oncogenes ; Platelet-Derived Growth Factor/*genetics ; RNA Splicing ; RNA, Messenger/genetics ; Recombination, Genetic ; Retroviridae/*genetics ; Sarcoma Virus, Woolly Monkey/*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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    Amphiphilic secondary structure: design of peptide hormones (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-20
    Description: Peptide synthesis can be used for elucidating the roles of secondary structures in the specificity of hormones, antigens, and toxins. Intermediate sized peptides with these activities assume amphiphilic secondary structures in the presence of membranes. When models are designed to optimize the amphiphilicity of the secondary structure, stronger interactions can be observed with the synthetic peptides than with the naturally occurring analogs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, E T -- Kezdy, F J -- HL-18577/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1984 Jan 20;223(4633):249-55.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6322295" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apolipoprotein A-I ; Apolipoproteins ; Binding Sites ; Calcitonin ; Chemical Phenomena ; Chemistry ; Corticotropin-Releasing Hormone ; Endorphins ; Glucagon ; Growth Hormone-Releasing Hormone ; *Hormones/pharmacology ; Lipoproteins, HDL ; Melitten ; Models, Structural ; *Peptides/chemical synthesis/metabolism/pharmacology ; Protein Conformation ; Structure-Activity Relationship ; beta-Endorphin
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  • 48
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    Antigens encoded by the 3'-terminal region of human T-cell leukemia virus: evidence for a functional gene (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-10-05
    Description: Antibodies in sera from patients with adult T-cell leukemia-lymphoma or from healthy carriers of type I human T-cell leukemia virus (HTLV) recognize an antigen of approximately 42 kilodaltons (p42) in cell lines infected with HTLV-I. Radiolabel sequence analysis of cyanogen bromide fragments of p42 led to the conclusion that this antigen is encoded in part by LOR, a conserved portion of the "X" region that is flanked by the envelope gene and the 3' long terminal repeat of HTLV-I. It is possible that this novel product mediates the unique transformation properties of the HTLV family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, T H -- Coligan, J E -- Sodroski, J G -- Haseltine, W A -- Salahuddin, S Z -- Wong-Staal, F -- Gallo, R C -- Essex, M -- 2-T32-CA0903/CA/NCI NIH HHS/ -- CA07094/CA/NCI NIH HHS/ -- CA13885/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1984 Oct 5;226(4670):57-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089350" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/*genetics ; Base Sequence ; Cell Line ; Cyanogen Bromide ; Deltaretrovirus/*genetics/immunology ; *Genes, Viral ; Humans ; Peptide Fragments ; Trans-Activators ; Viral Proteins/*genetics
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  • 49
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    Oncogene linked to growth factor receptor (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-02-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1984 Feb 24;223(4638):806.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6320370" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Cycle ; Humans ; *Oncogenes ; Receptor, Epidermal Growth Factor ; *Receptors, Cell Surface
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  • 50
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    Total synthesis and cloning of a gene coding for the ribonuclease S protein (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-03-23
    Description: A gene for ribonuclease S protein, has been chemically synthesized and cloned. The gene is designed to have 25 specific restriction endonuclease sites spaced at short intervals, permitting its structure to be rapidly modified. This flexibility facilitates tests of hypotheses relating the primary structure of the enzyme to its physical and catalytic behavior.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nambiar, K P -- Stackhouse, J -- Stauffer, D M -- Kennedy, W P -- Eldredge, J K -- Benner, S A -- 1 RO1 GM 30110-01A2/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Mar 23;223(4642):1299-301.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6322300" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Cloning, Molecular ; DNA Restriction Enzymes ; Escherichia coli/genetics ; *Genes, Synthetic ; Oligodeoxyribonucleotides/chemical synthesis ; Peptide Fragments/*genetics ; Ribonucleases/*genetics
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  • 51
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    Gene product of v-fgr onc: hybrid protein containing a portion of actin and a tyrosine-specific protein kinase (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-06
    Description: The nucleotide sequence of the region of Gardner-Rasheed feline sarcoma virus (GR-FeSV) encoding its primary translation product, p70gag-fgr, has been determined. From the nucleotide sequence, the amino acid sequence of this transforming protein was deduced. Computer analysis indicates that a portion of P70gag-fgr has extensive amino acid sequence homology with actin, a eukaryotic cytoskeletal protein. A second region of P70gag-fgr is closely related to the tyrosine-specific kinase gene family. Thus, the v-fgr oncogene appears to have arisen as a result of recombinational events involving two distinct cellular genes, one coding for a structural protein and the other for a protein kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Naharro, G -- Robbins, K C -- Reddy, E P -- New York, N.Y. -- Science. 1984 Jan 6;223(4631):63-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6318314" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/analysis ; Amino Acid Sequence ; Base Sequence ; Computers ; Gene Products, gag ; *Genes, Viral ; *Oncogenes ; Protein Kinases/analysis ; Protein-Tyrosine Kinases ; Recombination, Genetic ; Retroviridae/*genetics ; Sarcoma Viruses, Feline/*genetics ; Viral Proteins/analysis/*genetics
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  • 52
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    Location and chemical synthesis of a pre-S gene coded immunodominant epitope of hepatitis B virus (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-04-27
    Description: Immunodominant, disulfide-bond independent epitopes recognized by human antibodies to hepatitis B virus (HBV) are located within the 55-residue amino terminal portion (coded for by the pre-S region of HBV DNA) of minor HBV envelope components larger than the major protein constituents encoded by the S gene. A peptide having the sequence of the first 26 amino acids from the amino terminal methionine was synthesized and elicited antibodies (at dilutions of greater than or equal to 1 to 10(5) ) to the HBV envelope. These antibodies can be utilized for diagnostic tests. The immunogenicity of the peptide was substantially increased by covalent attachment to liposomes. The disulfide bond-independent determinants on sequences coded for by the pre-S gene may be more easily mimicked by peptide analogs than "conformational" determinants on the S-gene product.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neurath, A R -- Kent, S B -- Strick, N -- 9011/PHS HHS/ -- New York, N.Y. -- Science. 1984 Apr 27;224(4647):392-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6200931" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Epitopes/*analysis/genetics/immunology ; *Genes, Viral ; Hepatitis B Antibodies/biosynthesis ; Hepatitis B Surface Antigens/analysis/genetics/*immunology ; Hepatitis B virus/genetics/*immunology ; Immunization ; Liposomes ; Peptides/chemical synthesis/genetics/*immunology ; Rabbits
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  • 53
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    Antibodies to human c-myc oncogene product: evidence of an evolutionarily conserved protein induced during cell proliferation (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-08-17
    Description: Antisera to a synthetic c-myc peptide and to c-myc antigens synthesized from various portions of the human gene expressed in Escherichia coli were used in order to characterize the protein product of the human c-myc oncogene. Although the deduced molecular weight of the human c-myc protein is 49,000, these antisera precipitate a protein from human cells that migrates in sodium dodecyl sulfate-polyacrylamide gel as if its molecular weight were 65,000. In addition, the mouse c-myc protein, whether synthesized in cells or in a cell-free system directed by pure, synthetic messenger RNA, has analogous properties and is immunoprecipitated by the antiserum to the human c-myc protein. Similar proteins are immunoprecipitated from monkey, rat, hamster, and frog cells, suggesting evolutionary conservation of antigenic structure of the c-myc protein among vertebrates. In addition, and in a manner consistent with the behavior of its messenger RNA, the immunoprecipitable c-myc protein is sharply induced by the action of mitogens on resting human T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Persson, H -- Hennighausen, L -- Taub, R -- DeGrado, W -- Leder, P -- New York, N.Y. -- Science. 1984 Aug 17;225(4663):687-93.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6431612" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Neoplasm/*immunology ; Base Sequence ; *Cell Division ; Chickens ; Cricetinae ; DNA, Neoplasm/genetics ; DNA, Recombinant/metabolism ; Electrophoresis, Polyacrylamide Gel ; Haplorhini ; Humans ; Mice ; Mitogens/pharmacology ; Molecular Weight ; Neoplasm Proteins/genetics/*immunology ; *Oncogenes ; RNA, Messenger/genetics ; Rabbits ; Rats
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  • 54
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    Opioid peptides mediate the suppressive effect of stress on natural killer cell cytotoxicity (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-13
    Description: The cytotoxic activity of natural killer cells was investigated in rats subjected to one of two inescapable footshock stress paradigms, both of which induce analgesia, but only one via activation of opioid mechanisms. Splenic natural killer cell activity was suppressed by the opioid, but not the nonopioid, form of stress. This suppression was blocked by the opioid antagonist naltrexone. Similar suppression of natural killer activity was induced by high doses of morphine. These results suggest that endogenous opioid peptides mediate the suppressive effect of certain forms of stress on natural killer cell cytotoxicity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shavit, Y -- Lewis, J W -- Terman, G W -- Gale, R P -- Liebeskind, J C -- MH15795/MH/NIMH NIH HHS/ -- NS07628/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1984 Jan 13;223(4632):188-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6691146" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cytotoxicity, Immunologic/drug effects ; Dose-Response Relationship, Drug ; Endorphins/*physiology ; Female ; Killer Cells, Natural/*immunology ; Morphine/*pharmacology ; Naltrexone/pharmacology ; Rats ; Rats, Inbred F344 ; Stress, Physiological/*immunology
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  • 55
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    Insect prothoracicotropic hormone: evidence for two molecular forms (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-06-15
    Description: In an insect, the tobacco hornworm Manduca sexta, the cerebral neuropeptide prothoracicotropic hormone (PTTH), the primary effector of postembryonic development, exists as two molecular forms. These two PTTH's elicit characteristic in vitro dose responses of activation of prothoracic glands from different developmental stages, an indication that during development the glands change in their sensitivity to the neurohormones. Both PTTH's are active in a specific in situ bioassay. Since they may be released in situ at stage-specific times to evoke distinctly different developmental responses, the PTTH neuroendocrine axis appears to be an effective system for determining the functions of molecular forms of a neurohormone in the regulation of growth and development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bollenbacher, W E -- Katahira, E J -- O'Brien, M -- Gilbert, L I -- Thomas, M K -- Agui, N -- Baumhover, A H -- AM-30118/AM/NIADDK NIH HHS/ -- AM-31642/AM/NIADDK NIH HHS/ -- NS-18791/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1984 Jun 15;224(4654):1243-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6732895" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Assay ; Bombyx ; Chromatography, Gel ; Dose-Response Relationship, Drug ; Insect Hormones/pharmacology/*physiology ; Insects/drug effects/growth & development/physiology ; Isoelectric Focusing ; Larva
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  • 56
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    Separation of signal transduction and adaptation functions of the aspartate receptor in bacterial sensing (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-06-03
    Description: In order to investigate the functions of stimulus recognition, signal transduction, and adaptation, the aspartate receptor gene for bacterial chemotaxis in Salmonella typhimurium has been sequenced and modified. A carboxyl-terminal truncated receptor was shown to bind aspartate and to transmit a signal to change motility behavior. However, the truncated receptor showed greatly reduced methyl-accepting capacity, and did not allow adaptation to the sensory stimulation. The separation of receptor functions by alteration of primary structure emphasizes that the receptor is directly involved in adaptation and is not solely a device for transmitting a signal across a membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russo, A F -- Koshland, D E Jr -- New York, N.Y. -- Science. 1983 Jun 3;220(4601):1016-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6302843" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Amino Acid Sequence ; Aspartic Acid ; *Bacterial Physiological Phenomena ; Base Sequence ; *Chemotaxis ; Escherichia coli/physiology ; Methylation ; *Receptors, Amino Acid ; Receptors, Cell Surface/genetics/*physiology ; Salmonella typhimurium/physiology ; Serine
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  • 57
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    Acetylcholine receptor: an allosteric protein (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-09-21
    Description: The nicotine receptor for the neurotransmitter acetylcholine is an allosteric protein composed of four different subunits assembled in a transmembrane pentamer alpha 2 beta gamma delta. The protein carries two acetylcholine sites at the level of the alpha subunits and contains the ion channel. The complete sequence of the four subunits is known. The membrane-bound protein undergoes conformational transitions that regulate the opening of the ion channel and are affected by various categories of pharmacologically active ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Changeux, J P -- Devillers-Thiery, A -- Chemouilli, P -- New York, N.Y. -- Science. 1984 Sep 21;225(4668):1335-45.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6382611" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Sequence ; Animals ; Binding Sites ; Cell Membrane/ultrastructure ; Cloning, Molecular ; DNA/analysis ; Electric Organ/metabolism ; Electrophorus ; Macromolecular Substances ; Protein Conformation ; *Receptors, Nicotinic/genetics/metabolism ; Torpedo
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  • 58
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    Potentiation of bleomycin lethality by anticalmodulin drugs: a role for calmodulin in DNA repair (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-06-22
    Description: Treatment of exponentially growing Chinese hamster ovary cells with bleomycin causes a dose-dependent decrease in cell survival due to DNA damage. This lethal effect can be potentiated by the addition of a nonlethal dose of the anticalmodulin drug N-(4-aminobutyl)-5-chloro-2-naphthalenesulfonamide ( W13 ) but not its inactive analog N-(4-aminobutyl)-2-naphthalenesulfonamide ( W12 ). By preventing the repair of damaged DNA, W13 also inhibits recovery from potentially lethal damage induced by bleomycin. These data suggest a role for calmodulin in the DNA repair pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chafouleas, J G -- Bolton, W E -- Means, A R -- RR-05425/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1984 Jun 22;224(4655):1346-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6203171" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bleomycin/*pharmacology ; Calmodulin/*antagonists & inhibitors/*physiology ; Cell Division/drug effects ; Cell Line ; Cell Survival/drug effects ; Cricetinae ; Cricetulus ; DNA Repair/*drug effects ; Dose-Response Relationship, Drug ; Drug Synergism ; Sulfonamides/pharmacology
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  • 59
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    Major pol gene progenitors in the evolution of oncoviruses (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-27
    Description: The genetic relationships among molecularly cloned prototype viruses representing all of the major oncovirus genera were investigated by molecular hybridization and nucleotide sequence analysis. One of the major progenitors of the pol genes of such viruses gives rise to mammalian type C viruses and another gives rise to type A, B, D, and avian type C oncoviruses. Evidence of unusual patterns of homology among the env genes of mammalian type C and D oncoviruses illustrates that genetic interactions between their progenitors contributed to the evolution of oncoviruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chiu, I M -- Callahan, R -- Tronick, S R -- Schlom, J -- Aaronson, S A -- New York, N.Y. -- Science. 1984 Jan 27;223(4634):364-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6197754" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Avian Sarcoma Viruses/genetics ; Base Sequence ; *Biological Evolution ; Cloning, Molecular ; DNA Restriction Enzymes ; *Genes, Viral ; Nucleic Acid Heteroduplexes ; Nucleic Acid Hybridization ; RNA-Directed DNA Polymerase/*genetics/metabolism ; Recombination, Genetic ; Retroviridae/classification/*genetics ; Viral Envelope Proteins/genetics
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  • 60
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    Expression of the c-fos gene and of an fos-related gene is stimulated by platelet-derived growth factor (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-30
    Description: Complementary DNA clones of genes induced by platelet-derived growth factor (PDGF) in BALB/c-3T3 cells were isolated; one such clone contains a domain having nucleotide sequence homology with the third exon of c-fos. This nucleotide sequence homology is reflected in the predicted amino acid sequences of the gene products. Under low stringency conditions, the mouse v-fos gene cross-hybridizes with the PDGF-inducible complementary DNA clone. However, the messenger RNA transcripts of mouse c-fos and the new fos-related gene can be distinguished by gel electrophoresis and by S1 nuclease analysis. Expression of the authentic c-fos gene is induced by PDGF and superinduced by the combination of PDGF and cycloheximide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cochran, B H -- Zullo, J -- Verma, I M -- Stiles, C D -- New York, N.Y. -- Science. 1984 Nov 30;226(4678):1080-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6093261" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cells, Cultured ; *Cloning, Molecular ; DNA/analysis ; DNA Restriction Enzymes ; DNA Transposable Elements ; Endonucleases ; Genes/drug effects ; Mice ; Mice, Inbred BALB C ; Nucleic Acid Hybridization ; Oncogenes/*drug effects ; Platelet-Derived Growth Factor/*pharmacology ; Single-Strand Specific DNA and RNA Endonucleases ; Transcription, Genetic/drug effects
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  • 61
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    Amiloride directly inhibits the Na,K-ATPase activity of rabbit kidney proximal tubules (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-05-27
    Description: Amiloride inhibited the ouabain-sensitive rate of oxygen consumption (QO2) of a suspension of rabbit intact proximal tubules in the presence of different concentrations of extracellular sodium. Measurements of the ouabain-sensitive QO2 in the presence of nystatin, the tissue sodium and potassium contents of the tubules in suspension, and the sodium- and potassium-dependent adenosinetriphosphatase (Na,K-ATPase) activity of lysed tubule membranes indicated that the effect of amiloride was due to a direct inhibition of the Na,K-ATPase activity of the proximal tubule.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Soltoff, S P -- Mandel, L J -- AM26816/AM/NIADDK NIH HHS/ -- GM29256/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 May 27;220(4600):957-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6302840" target="_blank"〉PubMed〈/a〉
    Keywords: Amiloride/*pharmacology ; Animals ; Dose-Response Relationship, Drug ; Female ; Ion Channels/drug effects ; Kidney Tubules, Proximal/drug effects/*enzymology ; Nystatin/pharmacology ; Ouabain/pharmacology ; Oxygen Consumption/drug effects ; Pyrazines/*pharmacology ; Rabbits ; Rats ; Sodium/metabolism ; Sodium-Potassium-Exchanging ATPase/*antagonists & inhibitors/metabolism
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  • 62
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    Purification and sequence analysis of bioactive atrial peptides (atriopeptins) (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-06
    Description: Mammalian cardiac atria have several biologically active peptides that exert profound effects on sodium excretion, urine volume, and smooth muscle tone. In the present study two such peptides of low molecular weight were purified and separated from each other on the basis of differences in charge, hydrophobicity, and biological profile. The first peptide, designated atriopeptin I, exhibits natriuretic and diuretic activity and selectivity relaxes intestinal smooth muscle but not vascular smooth muscle strips. The second peptide, atriopeptin II, is a potent natriuretic and diuretic that relaxes both intestinal and vascular strips. Sequence analysis of atriopeptin I indicates that it is composed of 21 amino acids, of which serine and glycine residues predominate. The amino terminal sequence of atriopeptin II up to residue 21 is the same as that of atriopeptin I, with the addition of the Phe-Arg extension at the carboxyl terminus. Both peptides appear to be derived from a common high molecular weight precursor (designated atriopeptigen); their biological selectivity and potency may be determined by the site of carboxyl terminal cleavage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Currie, M G -- Geller, D M -- Cole, B R -- Siegel, N R -- Fok, K F -- Adams, S P -- Eubanks, S R -- Galluppi, G R -- Needleman, P -- New York, N.Y. -- Science. 1984 Jan 6;223(4631):67-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6419347" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arginine/analysis ; Chromatography, High Pressure Liquid ; Chromatography, Ion Exchange ; Diuresis/drug effects ; Glycine/analysis ; Heart Atria/*analysis ; Muscle Contraction/drug effects ; Muscle, Smooth/drug effects ; Muscle, Smooth, Vascular/drug effects ; Natriuresis/drug effects ; Peptides/analysis/*isolation & purification/pharmacology ; Phenylalanine/analysis ; Rats ; Serine/analysis
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    DNA cloning of Plasmodium falciparum circumsporozoite gene: amino acid sequence of repetitive epitope (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-08-10
    Description: A clone of complementary DNA encoding the circumsporozoite (CS) protein of the human malaria parasite Plasmodium falciparum has been isolated by screening an Escherichia coli complementary DNA library with a monoclonal antibody to the CS protein. The DNA sequence of the complementary DNA insert encodes a four-amino acid sequence: proline-asparagine-alanine-asparagine, tandemly repeated 23 times. The CS beta-lactamase fusion protein specifically binds monoclonal antibodies to the CS protein and inhibits the binding of these antibodies to native Plasmodium falciparum CS protein. These findings provide a basis for the development of a vaccine against Plasmodium falciparum malaria.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Enea, V -- Ellis, J -- Zavala, F -- Arnot, D E -- Asavanich, A -- Masuda, A -- Quakyi, I -- Nussenzweig, R S -- New York, N.Y. -- Science. 1984 Aug 10;225(4662):628-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6204384" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal/immunology ; Antigens, Surface/*genetics/immunology ; *Cloning, Molecular ; DNA/genetics ; Epitopes/*genetics ; *Genes ; Malaria/immunology ; Plasmodium falciparum/*genetics ; *Protozoan Proteins ; *Repetitive Sequences, Nucleic Acid
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    The structural gene for tetanus neurotoxin is on a plasmid (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-05-25
    Description: A pool of synthetic oligonucleotides was prepared based on the amino terminal amino acid sequence of tetanus toxin. This probe hybridized to plasmid DNA isolated from three toxigenic strains of Clostridium tetani but not to plasmid DNA from a nontoxigenic strain. These results show that the structural gene for the toxin is on the plasmid. The pCL1 plasmid from one of the toxigenic strains spontaneously deleted 22 kilobase pairs of DNA to form pCL2. Strains harboring this deleted plasmid are nontoxigenic. However, the probe mixture hybridized to pCL2, indicating that the DNA encoding the amino terminus of the toxin had not been deleted. Restriction endonuclease cleavage maps of pCL1 and pCL2 were constructed and indicate the approximate location and orientation of the structural gene for tetanus toxin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finn, C W Jr -- Silver, R P -- Habig, W H -- Hardegree, M C -- Zon, G -- Garon, C F -- New York, N.Y. -- Science. 1984 May 25;224(4651):881-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6326263" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; DNA Restriction Enzymes ; *Genes ; Nucleic Acid Hybridization ; *Plasmids ; Tetanus Toxin/*genetics
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    Cyclophilin: a specific cytosolic binding protein for cyclosporin A (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-02
    Description: Cyclophilin, a specific cytosolic binding protein responsible for the concentration of the immunosuppressant cyclosporin A by lymphoid cells, was purified to homogeneity from bovine thymocytes. Cation-exchange high-performance liquid chromatography resolved a major and minor cyclophilin species that bind cyclosporin A with a dissociation constant of about 2 X 10(-7) moles per liter and specific activities of 77 and 67 micrograms per milligram of protein, respectively. Both cyclophilin species have an apparent molecular weight of 15,000, an isoelectric point of 9.6, and nearly identical amino acid compositions. A portion of the NH2-terminal amino acid sequence of the major species was determined. The cyclosporin A-binding activity of cyclophilin is sulfhydryl dependent, unstable at 56 degrees C and at pH 4 or 9.5, and sensitive to trypsin but not to chymotrypsin digestion. Cyclophilin specifically binds a series of cyclosporin analogs in proportion to their activity in a mixed lymphocyte reaction. Isolation of cyclophilin from the cytosol of thymocytes suggests that the immunosuppressive activity of cyclosporin A is mediated by an intracellular mechanism, not by a membrane-associated mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Handschumacher, R E -- Harding, M W -- Rice, J -- Drugge, R J -- Speicher, D W -- New York, N.Y. -- Science. 1984 Nov 2;226(4674):544-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6238408" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/*isolation & purification/metabolism ; Cattle ; Chromatography, High Pressure Liquid ; Cyclosporins/*metabolism ; Electrophoresis, Polyacrylamide Gel ; Humans ; Isoelectric Point ; Kinetics ; Lymphocyte Culture Test, Mixed ; Mice ; Molecular Weight ; Peptidylprolyl Isomerase
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    Structure and expression of a complementary DNA for the nuclear coded precursor of human mitochondrial ornithine transcarbamylase (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-06-08
    Description: Most mitochondrial proteins are encoded in the nucleus and are translated on free cytoplasmic ribosomes as larger precursors containing amino-terminal "leader" sequences, which are removed after the precursors are taken up by mitochondria. We have deduced the complete primary structure of the precursor of a human mitochondrial matrix enzyme, ornithine transcarbamylase (OTC), from the nucleotide sequence of cloned complementary DNA. The amino-terminal leader peptide of OTC is 32 amino acids in length and contains four arginines but no acidic residues. Cleavage of the leader peptide from the "mature" protein occurs between glutamine and asparagine residues. The sequence of mature human OTC resembles that of the subunits of both OTC and aspartate transcarbamylase from Escherichia coli. The biological activity of the cloned OTC complementary DNA was tested by joining it with SV40 (an animal virus) regulatory elements and transfecting cultured HeLa cells, which do not normally express OTC. Both the precursor and mature forms of the OTC subunit were identified; in stable transformants, enzymatic activity was also detected.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Horwich, A L -- Fenton, W A -- Williams, K R -- Kalousek, F -- Kraus, J P -- Doolittle, R F -- Konigsberg, W -- Rosenberg, L E -- AM 09527/AM/NIADDK NIH HHS/ -- AM 12579/AM/NIADDK NIH HHS/ -- GM 31539/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1984 Jun 8;224(4653):1068-74.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6372096" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; DNA, Mitochondrial/*genetics ; DNA, Recombinant/metabolism ; Escherichia coli/enzymology ; HeLa Cells/metabolism ; Humans ; Mitochondria/enzymology ; Ornithine Carbamoyltransferase/*genetics ; Protein Biosynthesis ; Rats
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    Homologies between signal transducing G proteins and ras gene products (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-16
    Description: The guanosine triphosphate-binding proteins (G proteins) found in a variety of tissues transduce signals generated by ligand binding to cell surface receptors into changes in intracellular metabolism. Amino acid sequences of peptides prepared by partial proteolysis of the alpha subunit of a bovine brain G protein and the alpha subunit of rod outer-segment transducin were determined. The two proteins show regions of sequence identity as well as regions of diversity. A portion of the amino-terminal peptide sequence of each protein is highly homologous with the corresponding region in the ras protein (a protooncogene product). These similarities suggest that G proteins and ras proteins may have analogous functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hurley, J B -- Simon, M I -- Teplow, D B -- Robishaw, J D -- Gilman, A G -- GM 09731-02/GM/NIGMS NIH HHS/ -- NS 18153/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 16;226(4676):860-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6436980" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cattle ; GTP-Binding Proteins/*metabolism ; Neoplasm Proteins/*metabolism ; Oncogenes ; Protein Conformation ; Proto-Oncogene Proteins p21(ras) ; Transduction, Genetic
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    Amino acid sequence similarity between rabies virus glycoprotein and snake venom curaremimetic neurotoxins (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-16
    Description: Evidence was presented earlier that a host-cell receptor for the highly neurotropic rabies virus might be the acetylcholine receptor. The amino acid sequence of the glycoprotein of rabies virus was compared by computer analysis with that of snake venom curaremimetic neurotoxins, potent ligands of the acetylcholine receptor. A statistically significant sequence relation was found between a segment of the rabies glycoprotein and the entire sequence of long neurotoxins. The greatest identity occurs with residues considered most important in neurotoxicity, including those interacting with the acetylcholine binding site of the acetylcholine receptor. Because of the similarity between the glycoprotein and the receptor-binding region of the neurotoxins, this region of the viral glycoprotein may function as a recognition site for the acetylcholine receptor. Direct binding of the rabies virus glycoprotein to the acetylcholine receptor could contribute to the neurotropism of this virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lentz, T L -- Wilson, P T -- Hawrot, E -- Speicher, D W -- GM 32629/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 16;226(4676):847-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6494916" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Glycoproteins/*genetics ; Neurotoxins/*genetics ; Rabies virus/*genetics ; Receptors, Cholinergic/metabolism ; Snake Venoms/*genetics ; Snakes ; Viral Proteins/*genetics
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    Rat transforming growth factor type 1: structure and relation to epidermal growth factor (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-03-09
    Description: The complete amino acid sequence of rat transforming growth factor type 1 has been determined. This growth factor, obtained from retrovirus-transformed fibroblasts, is structurally and functionally related to mouse epidermal growth factor and human urogastrone. Production of this polypeptide by various neoplastic cells might contribute to the continued expression of the transformed phenotype.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marquardt, H -- Hunkapiller, M W -- Hood, L E -- Todaro, G J -- New York, N.Y. -- Science. 1984 Mar 9;223(4640):1079-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6320373" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; *Cell Transformation, Neoplastic ; DNA/biosynthesis ; Epidermal Growth Factor/*metabolism/pharmacology ; Humans ; Idoxuridine/metabolism ; Mice ; Peptide Biosynthesis ; Peptides/*metabolism/pharmacology ; Rats ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/metabolism ; Structure-Activity Relationship ; Transforming Growth Factors
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    Primary structure of v-raf: relatedness to the src family of oncogenes (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-04-20
    Description: A replication-defective, acute transforming retrovirus (murine sarcoma virus 3611) was isolated from mouse and molecularly cloned. The nucleotide sequence of 1.5 kilobases encompassing the transforming gene (v-raf) was determined. This sequence, which predicts the amino acid sequence of a gag-raf fusion protein, terminates 180 nucleotides from the 3' end of the acquired cellular sequence. Comparison of the predicted amino acid sequence of v-raf with the predicted amino acid sequences of other oncogenes reveals significant homologies to the src family of oncogenes. There is a lack of homology within the sequence of the tyrosine acceptor domain described for the phosphotyrosine kinase members of the src family of transforming proteins. Phylogenetic arrangement of this family of oncogenes suggests that tyrosine-specific phosphorylation may be a recently acquired activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mark, G E -- Rapp, U R -- New York, N.Y. -- Science. 1984 Apr 20;224(4646):285-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6324342" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Biological Evolution ; Cell Transformation, Neoplastic ; Cell Transformation, Viral ; DNA Restriction Enzymes ; Gene Products, gag ; *Genes, Viral ; Mice ; *Oncogenes ; Protein Biosynthesis ; Protein Kinases/metabolism ; Protein-Tyrosine Kinases ; Sarcoma Viruses, Murine/*genetics ; Transcription, Genetic ; Tyrosine/metabolism ; Viral Proteins/analysis/*genetics
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    More progress on the T cell receptor (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-05-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1984 May 25;224(4651):859-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6426056" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; Cloning, Molecular ; Dna ; *Genes, MHC Class II ; Humans ; Mice ; Receptors, Antigen, T-Cell/*genetics
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    More on the T-cell receptor (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1984 Nov 30;226(4678):1065.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6494924" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Cloning, Molecular ; Genes ; Humans ; Receptors, Antigen, T-Cell/*genetics
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    Need a catalyst? Design an enzyme (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maugh, T H 2nd -- New York, N.Y. -- Science. 1984 Jan 20;223(4633):269-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6608147" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Biochemistry/*methods ; Catalysis ; *Cloning, Molecular ; Enzymes/genetics/*metabolism ; Mutation ; Structure-Activity Relationship ; Substrate Specificity ; Tetrahydrofolate Dehydrogenase/metabolism ; Tyrosine-tRNA Ligase/metabolism ; beta-Lactamases/metabolism
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    A potential second messenger role for unsaturated fatty acids: activation of Ca2+-dependent protein kinase (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-05-11
    Description: Arachidonate and other unsaturated long-chain fatty acids were found to activate protein kinase C from human neutrophils. Kinase activation by arachidonate required calcium and was enhanced by diolein but did not require exogenous phosphatidylserine. Submaximal levels of arachidonate also enhanced the affinity of the kinase for calcium during activation by phosphatidylserine. Thus the release of arachidonate, which is triggered in many cell types by ligand-receptor interactions, could play a second messenger role in the regulation of cellular function by activation of protein kinase C.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McPhail, L C -- Clayton, C C -- Snyderman, R -- 5PO1CA29589/CA/NCI NIH HHS/ -- 5RO-1DEO3738/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 1984 May 11;224(4649):622-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6231726" target="_blank"〉PubMed〈/a〉
    Keywords: Arachidonic Acid ; Arachidonic Acids/pharmacology ; Dose-Response Relationship, Drug ; Enzyme Activation ; Fatty Acids, Unsaturated/pharmacology/*physiology ; Humans ; Kinetics ; Neutrophils/enzymology ; Phosphatidylserines/pharmacology ; Protein Kinase C ; Protein Kinases/*metabolism
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    Evolution of proteolytic enzymes (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-04-27
    Description: Proteolytic enzymes have many physiological functions, ranging from generalized protein digestion to more specific regulated processes such as the activation of zymogens, blood coagulation and the lysis of fibrin clots, the release of hormones and pharmacologically active peptides from precursor proteins, and the transport of secretory proteins across membranes. They are present in all forms of living organisms. Comparisons of amino acid sequences, three-dimensional structures, and enzymatic reaction mechanisms of proteases indicate that there are distinct families of these proteins. Changes in molecular structure and function have accompanied the evolution of proteolytic enzymes and their inhibitors, each having relatively simple roles in primitive organisms and more diverse and more complex functions in higher organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neurath, H -- GM-15731/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 27;224(4647):350-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6369538" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; *Biological Evolution ; Blood Coagulation ; Chemistry, Physical ; Enzyme Activation ; Enzyme Precursors/metabolism ; Genes ; Humans ; Mutation ; *Peptide Hydrolases/analysis/genetics/metabolism ; Peptides/metabolism ; Physicochemical Phenomena ; Protease Inhibitors/analysis/metabolism ; Protein Conformation ; Protein Sorting Signals ; Substrate Specificity
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    Detection of high molecular weight forms of platelet-derived growth factor by sequence-specific antisera (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-09
    Description: Antisera to synthetic peptides representing sequences of both chains of platelet-derived growth factor (PDGF) were used to structurally analyze PDGF isolated from outdated human platelets and PDGF-like proteins in normal and transformed cells. Most PDGF isolated from platelets did not contain the carboxyl portion of PDGF-2 in contrast to p20sis, the major form of p28sis detected in simian sarcoma virus-transformed cells. In addition, higher molecular weight forms of molecules containing PDGF-1 and PDGF-2 sequences were detected in all cell lines tested. These lines were heterogeneous with respect to species, cell type, and transforming agent.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Niman, H L -- Houghten, R A -- Bowen-Pope, D F -- CA 25803/CA/NCI NIH HHS/ -- HL 18645/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 9;226(4675):701-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6494905" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Electrophoresis, Polyacrylamide Gel ; Humans ; Immune Sera/immunology ; Molecular Weight ; Platelet-Derived Growth Factor/*immunology/isolation & purification ; Rats
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    Kainic acid induces sprouting of retinal neurons (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-02-03
    Description: The neurotoxin kainic acid caused dose-dependent morphological changes in horizontal cells of the retinas of adult cats and rabbits. High concentrations of kainic acid killed the cells, but when exposed to sublethal doses they contracted their dendritic fields and sent sprouting processes into the inner retina. It appears that kainic acid can induce neuronal growth as well as degeneration and that the potential for morphological plasticity is still present in neurons of the adult mammalian retina.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peichl, L -- Bolz, J -- New York, N.Y. -- Science. 1984 Feb 3;223(4635):503-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6691162" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cats ; Dendrites/ultrastructure ; Dose-Response Relationship, Drug ; Kainic Acid/*pharmacology ; Nerve Degeneration/drug effects ; Neurons/cytology/*drug effects ; Pyrrolidines/*pharmacology ; Rabbits ; Retina/cytology/*drug effects
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    Isolation, structure, and synthesis of a human seminal plasma peptide with inhibin-like activity (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-03-16
    Description: A basic peptide isolated from pooled human seminal plasma exhibited inhibin-like activity by suppressing pituitary follicle-stimulating hormone secretion in vitro and in vivo. The peptide has been characterized and sequenced, and a 31-amino-acid synthetic replicate showed full biological activity in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ramasharma, K -- Sairam, M R -- Seidah, N G -- Chretien, M -- Manjunath, P -- Schiller, P W -- Yamashiro, D -- Li, C H -- New York, N.Y. -- Science. 1984 Mar 16;223(4641):1199-202.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6422553" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Animals ; Follicle Stimulating Hormone/secretion ; Gonadotropin-Releasing Hormone/antagonists & inhibitors ; Humans ; Inhibins/*isolation & purification/pharmacology ; Luteinizing Hormone/secretion ; Male ; Mice ; Molecular Weight ; Peptides/chemical synthesis/isolation & purification ; Pituitary Gland/secretion ; *Prostatic Secretory Proteins ; Proteins/chemical synthesis/*isolation & purification/pharmacology ; Rats ; Semen/*analysis ; Seminal Plasma Proteins
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    DNA-binding proteins (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-09-09
    Description: The structures of three proteins that regulate gene expression have been determined recently and suggest how these proteins may bind to their specific recognition sites on the DNA. One protein (Cro) is a repressor of gene expression, the second (CAP) usually stimulates gene expression, and the third (lambda repressor) can act as either a repressor or an activator. The three proteins contain a substructure consisting of two consecutive alpha helices that is virtually identical in each case. Structural and amino acid sequence comparisons suggest that this bihelical fold occurs in a number of proteins that regulate gene expression, and is an intrinsic part of the DNA-protein recognition event. The modes of repression and activation by Cro and lambda repressor are understood reasonably well, but the mode of action of CAP is still unclear.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takeda, Y -- Ohlendorf, D H -- Anderson, W F -- Matthews, B W -- GM20066/GM/NIGMS NIH HHS/ -- GM28138/GM/NIGMS NIH HHS/ -- GM30894/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Sep 9;221(4615):1020-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6308768" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chemical Phenomena ; Chemistry ; *DNA Helicases ; DNA-Binding Proteins ; Escherichia coli/genetics ; Gene Expression Regulation ; Models, Chemical ; Protein Conformation
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  • 80
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    Identification of the putative transforming protein of the human T-cell leukemia viruses HTLV-I and HTLV-II (1984)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1984-10-05
    Description: The human T-cell leukemia viruses HTLV-I and HTLV-II are unique among the transforming retroviruses of vertebrates in their ability to transform human T cells in vitro and in their close association with human malignancies (T-cell lymphomas and leukemia). Their genomes are relatively simple, containing the genes gag, pol, env, and a 3' region termed "X." This 3' region may be responsible for the transforming potential of the viruses. The existence of proteins encoded by the 3' region has been postulated on the basis of multiple open reading frames. In the present study this region is shown to contain a gene encoding a protein of 40 kilodaltons in HTLV-I and 37 kilodaltons in HTLV-II. It is proposed that these proteins be called, respectively, p40xI and p37xII.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Slamon, D J -- Shimotohno, K -- Cline, M J -- Golde, D W -- Chen, I S -- CA 16042/CA/NCI NIH HHS/ -- CA 32737/CA/NCI NIH HHS/ -- RR 00865/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1984 Oct 5;226(4670):61-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089351" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; B-Lymphocytes/microbiology ; Cell Line ; *Cell Transformation, Viral ; Deltaretrovirus/analysis/*genetics/physiology ; *Genes, Viral ; Humans ; Immune Sera ; Molecular Weight ; T-Lymphocytes/*microbiology ; Trans-Activators ; Viral Proteins/genetics/immunology/*physiology
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  • 81
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    Interchangeability of stress and amphetamine in sensitization (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-01-18
    Description: In view of similarities between the behavioral, biochemical, and electrophysiological effects of amphetamine and stress, we tested the hypothesis that presentation of a stressor, mild tail pressure, can sensitize an animal to the later effects of amphetamine, and vice versa. Our findings supported this hypothesis and suggest that amphetamine and at least some stressors may be interchangeable in their ability to induce a sensitization. The data raise the possibility that stress might be a common variable contributing to both amphetamine psychosis and some forms of schizophrenia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Antelman, S M -- Eichler, A J -- Black, C A -- Kocan, D -- New York, N.Y. -- Science. 1980 Jan 18;207(4428):329-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7188649" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior, Animal/drug effects/*physiology ; Dextroamphetamine/*pharmacology ; Dopamine/physiology ; Dose-Response Relationship, Drug ; Haloperidol/pharmacology ; Humans ; Male ; Rats ; Schizophrenia/physiopathology ; Stereotyped Behavior/drug effects ; Stress, Physiological/*physiopathology
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  • 82
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    Excitatory and inhibitory effects of serotonin on sensorimotor reactivity measured with acoustic startle (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-07-25
    Description: Serotonin infused into the lateral ventricle in rats produced a dose-dependent depression of the acoustic startle reflex. When infused onto the spinal cord, serotonin produced a dose-dependent increase in startle. Thus the same neurotransmitter can modulate the same behavior in opposite ways, depending on which part of the central nervous system is involved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, M -- Strachan, D I -- Kass, E -- New York, N.Y. -- Science. 1980 Jul 25;209(4455):521-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7394520" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Dose-Response Relationship, Drug ; Kinetics ; Male ; Rats ; Reflex, Acoustic/*drug effects ; Reflex, Startle/*drug effects ; Serotonin/*pharmacology
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  • 83
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    Endorphin-mediated increases in pain threshold during pregnancy (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-10-10
    Description: Maternal pain thresholds in rats were determined during various stages of pregnancy and parturition by measuring the intensity of electric shock that elicited reflexive jumping. There was a gradual rise in the pain threshold between 16 and 4 days prior to parturition and a more abrupt rise 1 to 2 days before that event. This increase was abolished by long-term administration of the narcotic antagonist naltrexone. The endorphin system is thus an important component of intrinsic mechanisms that modulate responsiveness to aversive stimuli. The data also demonstrate the activation during pregnancy of an endorphin system that is apparently quiescent in nonpregnant female rats treated the same way.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gintzler, A R -- NIMH GRANT DA01771/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1980 Oct 10;210(4466):193-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7414330" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Dose-Response Relationship, Drug ; Endorphins/antagonists & inhibitors/*physiology ; Female ; Naltrexone/pharmacology ; Pain/*physiopathology ; Pregnancy ; *Pregnancy, Animal ; Rats ; Time Factors
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  • 84
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    Ala-Gly- and Val-Asp-[Arg8]-vasopressin: bovine storage forms of arginine vasopressin with natriuretic activity (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-02-22
    Description: Extracts of fresh-frozen bovine neurohypophysis were purified by chromatographic techniques to isolate and characterize the components that produce natriuresis in nondiuretic dogs. Two compounds with natiuretic properties similar to those of synthetic arginine vasopressin accounted for most of the natriuretic activity and appeared to be the prevalent vasopressin-like molecules in the extract. These peptides were Ala-Gly-[Arg8]-vasopressin and Val-Asp-[Arg8]-vasopressin; the natriuretic potency of each appeared to be similar to synthetic arginine vasopressin and could be observed with doses in the range of 50 picomoles. In the dog the most conspicuous difference between synthetic arginine vasopressin and the new vasopressin peptides was the smaller pressor responses to natriuretic doses of the new compounds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gitelman, H J -- Klapper, D G -- Alderman, F R -- Blythe, W B -- New York, N.Y. -- Science. 1980 Feb 22;207(4433):893-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7355269" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arginine Vasopressin/analogs & derivatives/*metabolism/pharmacology ; Biological Assay ; Blood Pressure/drug effects ; Cattle ; Dogs ; Male ; Natriuresis/*drug effects ; Pituitary Gland, Posterior/*metabolism ; Protein Precursors/metabolism ; Structure-Activity Relationship
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    Phase variation: evolution of a controlling element (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-09-19
    Description: Phase variation in bacteria is regulated by homologous recombination at a specific DNA site. This recombinational event causes the inversion of a 970-base-pair DNA sequence that includes the promoter necessary for transcription of a flagellar gene. The invertible segment is flanked by two sites that are necessary for the inversion and contains a gene (hin) whose product mediates the inversion event. The hin gene shows extensive homology with the TnpR gene carried on the Tn3 transposon. It is also homologous with the gin gene carried on bacteriophage mu. These relationships suggest that the phase variation system may have evolved by the association of a transposon with a resident gene and the subsequent specialization of these elements to regulate flagellar antigen expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simon, M -- Zieg, J -- Silverman, M -- Mandel, G -- Doolittle, R -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1370-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6251543" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*genetics ; Base Sequence ; *DNA Transposable Elements ; DNA, Bacterial/genetics ; Flagellin/*genetics ; Genes ; Recombination, Genetic ; Salmonella/*genetics
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  • 86
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    Tumor-promoting phorbol esters stimulate hematopoietic colony formation in vitro (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-04-25
    Description: Tumor-promoting phorbol esters stimulated mouse bone marrow cells to form myeloid colonies in agar cultures without added colony-stimulating factors. The colony-stimulating ability of various phorbol esters correlated well with their ability to promote skin tumors in vivo. These results suggest that phorbol esters mimic the action of specific colony-stimulating factors that regulate growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stuart, R K -- Hamilton, J A -- New York, N.Y. -- Science. 1980 Apr 25;208(4442):402-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6245446" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division/drug effects ; Cells, Cultured ; *Colony-Forming Units Assay ; Colony-Stimulating Factors/pharmacology ; Dose-Response Relationship, Drug ; Hematopoietic Stem Cells/*drug effects ; Macrophages/physiology ; Mice ; Monocytes/physiology ; Phorbol Esters/pharmacology ; Phorbols/*pharmacology ; Receptors, Cell Surface/drug effects ; Structure-Activity Relationship ; Tetradecanoylphorbol Acetate/*pharmacology
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  • 87
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    Genetic variation in the human insulin gene (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-08-01
    Description: Four recombinant lambda phages containing nucleotide sequences complementary to a cloned human preproinsulin DNA probe have been isolated from human DNA. Restriction analyses in conjunction with Southern hybridizations reveal two types of gene sequences. One isolate of each type was subjected to complete nucleotide sequence determination. The sequences contain the entire preproinsulin messenger RNA region, two intervening sequence. 260 nucleotides upstream from the messenger RNA capping site, and 35 nucleotides beyond the polyadenylate attachment site. Our results strongly suggest that these two gene types are allelic variants of a single insulin gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ullrich, A -- Dull, T J -- Gray, A -- Brosius, J -- Sures, I -- New York, N.Y. -- Science. 1980 Aug 1;209(4456):612-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6248962" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; *Dna ; DNA Restriction Enzymes ; DNA, Recombinant/metabolism ; *Genes ; Genetic Code ; *Genetic Variation ; Humans ; Insulin/*biosynthesis ; Nucleic Acid Hybridization ; Proinsulin/biosynthesis ; Rats ; Species Specificity
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  • 88
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    Conversion of 3T3-L1 fibroblasts to fat cells by an inhibitor of methylation: effect of 3-deazaadenosine (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-03-13
    Description: 3-Deazaadenosine, an inhibitor of methylation, increased the frequency of conversion of 3T3-L1 fibroblasts to fat cells in a dose-dependent manner. Once converted, the 3T3-L1 fat cells retained their adipose morphology and accumulated triglycerides even when 3-deazaadenosine was removed from the culture medium. 3-Deazaadenosine may perturb cellular methylation and thereby lead to an increase in the frequency of differentiation of 3T3-L1 fibroblasts to fat cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chiang, P K -- New York, N.Y. -- Science. 1981 Mar 13;211(4487):1164-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7466386" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/*cytology ; Animals ; Carnitine/pharmacology ; Cell Differentiation/*drug effects ; Cells, Cultured ; Dose-Response Relationship, Drug ; Fibroblasts/cytology ; Methylation ; Mice ; Ribonucleosides/*pharmacology ; Tubercidin/*pharmacology
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  • 89
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    Detection of circulating metallothionein in rats injected with zinc or cadmium (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-11-13
    Description: Circulating metallothionein was measured by radioimmunoassay over a 13-day period in male Sprague-Dawley rats that received a sequence of three intraperitoneal injections (at 3-day intervals) of either 5 milligrams of zinc or 0.8 milligrams of cadmium per kilogram of body weight. These amounts of zinc and cadmium produced metallothionein concentrations in the range of 2 to 5 nanograms per milliliter of serum (zinc) and 2 to 15 nanograms per milliliter of serum (cadmium). In control rats given saline injections over the same period the metallothionein concentration ranged from 1 to 3 nanograms per milliliter of serum.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garvey, J S -- Chang, C C -- ES 01629/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1981 Nov 13;214(4522):805-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7292012" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cadmium/*pharmacology ; Dose-Response Relationship, Drug ; Male ; Metalloproteins/*blood ; Metallothionein/*blood/immunology ; Radioimmunoassay ; Rats ; Rats, Inbred Strains ; Zinc/*pharmacology
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  • 90
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    Hemoglobin Parchman: double crossover within a single human gene (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-10-15
    Description: Structural analysis of a new variant hemoglobin revealed tryptic peptides with the amino acid composition of normal delta-globin, except for two internal peptides, which had the compositions of normal beta-globin. The most likely explanation for these findings is that a double, nonhomologous crossover between the delta-and beta-globin genes had occurred.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adams, J G 3rd -- Morrison, W T -- Steinberg, M H -- New York, N.Y. -- Science. 1982 Oct 15;218(4569):291-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7123235" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crossing Over, Genetic ; Globins/genetics ; Hemoglobins, Abnormal/*genetics ; Humans
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  • 91
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    Mammalian muscle acetylcholine receptor: a supramolecular structure formed by four related proteins (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-12-17
    Description: The nicotinic acetylcholine receptor has been purified from fetal calf muscle. Amino terminal amino acid sequence data indicate that the mammalian receptor is formed from closely related but distinct subunits. A cytoskeletal component, actin, may be associated with the receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Conti-Tronconi, B M -- Gotti, C M -- Hunkapiller, M W -- Raftery, M A -- GM-06965/GM/NIGMS NIH HHS/ -- NS-10294/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1982 Dec 17;218(4578):1227-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7146904" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/isolation & purification ; Amino Acid Sequence ; Animals ; Cattle ; Macromolecular Substances ; Molecular Weight ; Receptors, Cholinergic/*isolation & purification
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  • 92
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    Nucleotide sequence of the p21 transforming protein of Harvey murine sarcoma virus (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-09-03
    Description: Harvey murine sarcoma virus is a retrovirus which transforms cells by means of a single virally encoded protein called p21 has. We have determined the nucleotide sequence of 1.0 kilobase in the 5' half of the viral genome which encompasses the has coding sequences and its associated regulatory signals. The nucleotide sequence has identified the amino acid sequence of two additional overlapping polypeptides which share their reading frames and the carboxyl termini with p21 but which contain additional NH2-terminal amino acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dhar, R -- Ellis, R W -- Shih, T Y -- Oroszlan, S -- Shapiro, B -- Maizel, J -- Lowy, D -- Scolnick, E -- New York, N.Y. -- Science. 1982 Sep 3;217(4563):934-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6287572" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Transformation, Viral ; Cells, Cultured ; Defective Viruses/*genetics ; Genes, Viral ; Oncogene Protein p21(ras) ; Peptide Fragments ; Protein Biosynthesis ; Protein Conformation ; RNA, Viral/genetics ; Sarcoma Viruses, Murine/*genetics ; Viral Proteins/analysis/*genetics
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  • 93
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    Circulating somatostatin acts on the islets of Langerhans by way of a somatostatin-poor compartment (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-10-29
    Description: Somatostatin perfused in canine pancreases at 10 to 20 picograms per milliliter or 10 to 20 percent of the pancreatic vein somatostatin concentration inhibited insulin and glucagon secretion. This suggests that the high local concentration of endogenous somatostatin is not in contact with somatostatin receptors of the islets. The integrity of this separation may determine the sensitivity of islet cells to circulating somatostatin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawai, K -- Ipp, E -- Orci, L -- Perrelet, A -- Unger, R H -- New York, N.Y. -- Science. 1982 Oct 29;218(4571):477-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6126931" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Dogs ; Dose-Response Relationship, Drug ; Glucagon/secretion ; Insulin/secretion ; Intercellular Junctions/physiology ; Islets of Langerhans/*secretion ; Receptors, Cell Surface/physiology ; Receptors, Somatostatin ; Somatostatin/*blood/metabolism
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  • 94
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    Homologous regulation of gonadotropin-releasing hormone receptors in cultured pituitary cells (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-02-19
    Description: Specific receptors for gonadotropin-releasing hormone (GnRH) in cultured rat pituitary cells were increased by subnanomolar concentrations of GnRH agonists and decreased by high concentrations of these peptides. The antagonist [D-Phe2, Pro3, D-Phe6]GnRH did not alter GnRH binding capacity and blocked the increase in sites induced by GnRH. These findings provide direct evidence for the homologous regulation of GnRH receptors by physiological concentrations of the hypothalamic peptide, an action that could mediate the cyclical and postcastration increases in GnRH receptors and responsiveness of the pituitary gonadotrophs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Loumaye, E -- Catt, K J -- New York, N.Y. -- Science. 1982 Feb 19;215(4535):983-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6296998" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Dose-Response Relationship, Drug ; Feedback ; Female ; Gonadotropin-Releasing Hormone/analogs & derivatives/metabolism/pharmacology ; Pituitary Gland/secretion ; Pituitary Hormone-Releasing Hormones/*metabolism/pharmacology ; Rats ; Receptors, Cell Surface/*pharmacology ; Receptors, LHRH
    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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  • 95
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    Rat pro-opiomelanocortin contains sulfate (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-07-02
    Description: Intermediate lobes isolated from rat pituitary glands incorporated [35S]sulfate into pro-opiomelanocortin and other adrenocorticotropic hormone-containing peptides. Incubation of intermediate lobes in medium containing the arginine analog canavanine inhibited the cleavage of pro-opiomelanocortin into smaller products. Pro-opiomelanocortin that accumulated in the presence of canavanine was also sulfated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoshina, H -- Hortin, G -- Boime, I -- New York, N.Y. -- Science. 1982 Jul 2;217(4554):63-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6283633" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenocorticotropic Hormone/*biosynthesis ; Amino Acid Sequence ; Animals ; In Vitro Techniques ; Kinetics ; Leucine ; Pituitary Gland/*metabolism ; Pituitary Hormones, Anterior/*biosynthesis ; Pro-Opiomelanocortin ; Protein Precursors/*biosynthesis ; Radioisotope Dilution Technique ; Rats ; Sulfur Radioisotopes ; Sulfuric Acids/*metabolism ; Tritium
    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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  • 96
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    Cysteamine: a potent and specific depletor of pituitary prolactin (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-07-30
    Description: Cysteamine rapidly reduces the concentration of prolactin in pituitary tissue in vivo and in vitro. The effect is dose-dependent, reversible, and cannot be accounted for by prolactin release. Cysteamine does not appear to exert its effect through dopamine receptors and does not alter lactotrope morphology, as determined by electron microscopy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Millard, W J -- Sagar, S M -- Landis, D M -- Martin, J B -- AM 26252/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1982 Jul 30;217(4558):452-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7089575" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Cysteamine/*pharmacology ; Domperidone/pharmacology ; Dose-Response Relationship, Drug ; Kinetics ; Male ; Pituitary Gland, Anterior/*metabolism ; Prolactin/analysis/*metabolism/secretion ; Rats ; Receptors, Dopamine/physiology ; Spiperone/pharmacology
    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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  • 97
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    DNA sequence of a gene encoding a BALB/c mouse Ld transplantation antigen (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-02-05
    Description: The sequence of a gene, denoted 27.5, encoding a transplantation antigen for the BALB/c mouse has been determined. Gene transfer studies and comparison of the translated sequence with the partial amino acid sequence of the Ld transplantation antigen establish that gene 27.5 encodes an Ld polypeptide. A comparison of the gene 27.5 sequence with several complementary DNA sequences suggests that the BALB/c mouse may contain a number of closely related L-like genes. Gene 27.5 has eight exons that correlate with the structural domains of the transplantation antigen.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, K W -- Sher, B T -- Sun, Y H -- Eakle, K A -- Hood, L -- 1 T32 GM07616/GM/NIGMS NIH HHS/ -- GM 06965/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 Feb 5;215(4533):679-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7058332" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular/methods ; Genes ; H-2 Antigens/*genetics ; *Major Histocompatibility Complex ; Mice ; Mice, Inbred BALB C/*genetics ; Plasmids ; 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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  • 98
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    Heroin "overdose" death: contribution of drug-associated environmental cues (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-04-23
    Description: A model of "overdose" deaths among heroin addicts is proposed which emphasizes recent findings concerning the contribution of drug-associated environmental cues to drug tolerance. Results of animal experiments performed to evaluate this model suggest that conditioned drug-anticipatory responses, in addition to pharmacological factors, affect heroin-induced mortality.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Siegel, S -- Hinson, R E -- Krank, M D -- McCully, J -- New York, N.Y. -- Science. 1982 Apr 23;216(4544):436-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7200260" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Disease Models, Animal ; Dose-Response Relationship, Drug ; Drug Tolerance ; Environment ; Heroin/*pharmacology ; Humans ; Male ; Rats ; Substance-Related Disorders/*physiopathology
    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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  • 99
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    Diazepam impairs lateral position control in highway driving (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-07-02
    Description: Nine expert drivers operated an instrumented vehicle in tests over a highway at night after being treated with diazepam (5 and 10 milligrams), a placebo, and nothing. They reacted to 10 milligrams of diazepam with increased lateral position variability. Potentially dangerous impairment was inferred from the reactions of some subjects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Hanlon, J F -- Haak, T W -- Blaauw, G J -- Riemersma, J B -- New York, N.Y. -- Science. 1982 Jul 2;217(4554):79-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7089544" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; *Automobile Driving ; Diazepam/*pharmacology ; Dose-Response Relationship, Drug ; Double-Blind Method ; Functional Laterality ; Humans ; Male ; Motor Activity/*drug effects ; Placebos
    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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  • 100
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    Nonopiate effects of dynorphin and des-Tyr-dynorphin (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-12-10
    Description: Intracerebroventricular administration of dynorphin produced potent and long-lasting effects on motor function and the electroencephalogram in rats. In addition, local iontophoretic or pressure ejection of dynorphin consistently inhibited hippocampal unit activity. None of these effects were significantly affected by naloxone even at high doses. Moreover, a fragment of dynorphin that failed to displace any of a number of tritiated narcotics from rat brain homogenates produced similar effects on these physiological measures in vivo. On the basis of a variety of criteria for "opiate action," the results suggest that a second biologically active site within the dynorphin sequence is capable of quite potent but nonopiate effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walker, J M -- Moises, H C -- Coy, D H -- Baldrighi, G -- Akil, H -- 1F32DA04183/DA/NIDA NIH HHS/ -- DA02265/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1982 Dec 10;218(4577):1136-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6128791" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Amino Acid Sequence ; Animals ; Dynorphins ; Endorphins/*physiology ; Hippocampus/*physiology ; Male ; Pain/*physiopathology ; Rats ; Structure-Activity Relationship
    Print ISSN: 0036-8075
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    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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