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  • Amino Acid Sequence  (93)
  • Rabbits  (90)
  • American Association for the Advancement of Science (AAAS)  (180)
  • Annual Reviews
  • 1980-1984  (180)
  • 1930-1934
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (180)
  • Annual Reviews
  • Springer  (2)
Years
Year
  • 1
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    L-Ornithine decarboxylase:an essential role in early mammalian embryogenesis (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-05-02
    Description: The highly selective, enzyme-activated, irreversible inhibitor of L-ornithine decarboxylase, DL-alpha-difluoromethylornithine, suppresses the increase in uterine L-ornithine decarboxylase activity associated with early embryogenesis in the mouse and arrests embryonic development at that stage. Contragestational effects were confirmed in the rat and rabbit. An increase in L-ornithine decarboxylase activity that leads to a rapid increase in putrescine concentration appears to be essential during a critical period after implantation for continued mammalian embryonal growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fozard, J R -- Part, M L -- Prakash, N J -- Grove, J -- Schechter, P J -- Sjoerdsma, A -- Koch-Weser, J -- New York, N.Y. -- Science. 1980 May 2;208(4443):505-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6768132" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosylmethionine Decarboxylase/metabolism ; Animals ; Carboxy-Lyases/*physiology ; Eflornithine ; Embryo, Mammalian/drug effects/*physiology ; Female ; Gestational Age ; Mice ; Ornithine/*analogs & derivatives/pharmacology ; Ornithine Decarboxylase/*physiology ; Ornithine Decarboxylase Inhibitors ; Polyamines/metabolism ; Pregnancy ; Rabbits ; Rats ; Uterus/drug effects/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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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
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  • 3
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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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  • 4
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    Interaction of laminae of the cingulate cortex with the anteroventral thalamus during behavioral learning (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-05-30
    Description: Neurons in deep laminae of the rabbit cingulate cortex develop discriminative activity at an early stage of behavioral discrimination learning, whereas neurons in the anteroventral nucleus of thalamus and neurons in the superficial cortical laminae develop such activity in a late stage of behavioral learning. It is hypothesized that early-forming discriminative neuronal activity, relayed to anteroventral neurons via the corticothalamic pathway, contributes to the construction of changes underlying the late-forming neuronal discrimination in the anteroventral nucleus. The resultant late discriminative activity in the anteroventral nucleus is then relayed via the thalamocortical pathway back to the superficial cortical laminae, promoting disengagement of cortex from further task-processing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabriel, M -- Foster, K -- Orona, E -- New York, N.Y. -- Science. 1980 May 30;208(4447):1050-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7375917" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avoidance Learning/*physiology ; Brain Mapping ; Cerebral Cortex/cytology/*physiology ; Discrimination (Psychology)/*physiology ; Gyrus Cinguli/*physiology ; Neural Pathways/physiology ; Rabbits ; Thalamus/*physiology ; Time Factors
    Print ISSN: 0036-8075
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  • 5
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    DNA polymerases in parasitic protozoans differ from host enzymes (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-05-02
    Description: Analysis of extracts of the bloodstream forms of Trypanosoma brucei showed that both DNA polymerase-alpha and DNA polymerase-beta activities were present. The detection of DNA polymerase-beta in T. brucei demonstrates the presence of this enzyme in unicellular organisms. DNA polymerase-beta is present also in Leishmania mexicana. The DNA polymerases in T. brucei are immunologically distinct from the host enzymes. The structural differences between the parasite and the host enzymes could be exploited for the development of agents to combat parasitic diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, L M -- Cheriathundam, E -- Mahoney, E M -- Cerami, A -- New York, N.Y. -- Science. 1980 May 2;208(4443):510-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7367875" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Centrifugation, Density Gradient ; Chickens ; DNA Polymerase I/analysis ; DNA Polymerase II/analysis ; DNA Polymerase III/analysis ; DNA-Directed DNA Polymerase/*analysis ; Fishes ; Immune Sera ; Leishmania/*enzymology ; Molecular Weight ; Rabbits ; Rats ; Species Specificity ; Trypanosoma brucei brucei/*enzymology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    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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  • 7
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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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  • 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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    Social environment as a factor in diet-induced atherosclerosis (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-06-27
    Description: Rabbits on a 2 percent cholesterol diet were individually petted, held, talked to, and played with on a regular basis. Measurements of aortic affinity for a Sudan stain, serum cholesterol levels, heart rate, and blood pressure were made at the end of the experimental period. Compared to control groups, which were given the same diet and normal laboratory animal care, the experimental groups showed more than a 60 percent reduction in the percentage of aortic surface area exhibiting sudanophilic lesions, even though serum cholesterol levels, heart rate, and blood pressure were comparable.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nerem, R M -- Levesque, M J -- Cornhill, J F -- New York, N.Y. -- Science. 1980 Jun 27;208(4451):1475-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7384790" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta/pathology ; Arteriosclerosis/*etiology/physiopathology/psychology ; Blood Pressure ; Cholesterol/blood ; *Diet, Atherogenic ; Heart Rate ; Male ; Rabbits ; *Social Environment
    Print ISSN: 0036-8075
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  • 10
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    DDT contamination at Wheeler National Wildlife Refuge (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-07-25
    Description: Disposal of industrial waste resulted in massive DDT contamination at Wheeler National Wildlife Refuge, Alabama. Nearly a decade after the cessation of DDT manufacturing at the facility responsible, concentrations of DDT residues in the local fauna are still high enough to suggest avian reproductive impairment and mortality. Populations of fish-eating birds are low, endangered species are being exposed, and muscle lipids of game birds contain up to 6900 parts of DDT (isomers and metabolites) per million.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Shea, T J -- Fleming, W J -- Cromartie, E -- New York, N.Y. -- Science. 1980 Jul 25;209(4455):509-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7394517" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Birds ; DDT/*analysis ; Ducks ; *Industrial Waste ; Lipids/analysis ; Muscles/analysis ; Rabbits ; Species Specificity
    Print ISSN: 0036-8075
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  • 11
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    Bladder-surface glycosaminoglycans: an efficient mechanism of environmental adaptation (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-05-09
    Description: The transitional epithelium of the urinary bladder secretes and binds to its surface a glycosaminoglycan than inhibits the adherence of bacteria. Synthetic sulfonated glycosaminoglycans instilled intraluminally into bladders whose natural mucin layer has been removed are as effective as the natural mucin in preventing bacterial adherence. It also appears that adherence of calcium and protein is reduced in the presence of both the natural mucin layer and the synthetic sulfonated glycosaminoglycan sodium pentosanpolysulfate, suggesting that the antiadherence activity of both natural and synthetic surface glycosaminoglycans in the bladder extends to the molecular and ionic levels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parsons, C L -- Stauffer, C -- Schmidt, J D -- New York, N.Y. -- Science. 1980 May 9;208(4444):605-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6154316" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; Animals ; Calcium/metabolism ; Cell Adhesion ; Environmental Exposure ; Epithelium/physiology ; Glycosaminoglycans/*physiology ; Male ; Mucins/pharmacology ; Pentosan Sulfuric Polyester/pharmacology ; Protein Binding/drug effects ; Proteins/metabolism ; Rabbits ; Urinary Bladder/microbiology/*physiology
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  • 12
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    Cytochrome p-450: localization in rabbit lung (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-03-28
    Description: Cytochrome P-450-dependent monooxygenase systems, which metabolize endogenous as well as foriegn compounds, are found in hepatic and several extrahepatic tissues of mammals, including humans. A form of cytochrome P-450 is localized in the nonciliated bronchiolar epithelial cells (Clara cells) of the small airways of rabbit lung. The apparent high concentration of the cytochrome in this pulmonary cell type compared to liver may be an important determinant in the susceptibility of the lung to a number of toxic chemicals that undergo metabolic activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Serabjit-Singh, C J -- Wolf, C R -- Philpot, R M -- Plopper, C G -- New York, N.Y. -- Science. 1980 Mar 28;207(4438):1469-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6767272" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biotransformation ; Bronchi/enzymology ; Cytochrome P-450 Enzyme System/immunology/*metabolism ; Epithelium/enzymology ; Fluorescent Antibody Technique ; Inactivation, Metabolic ; Lung/cytology/*enzymology/metabolism ; Rabbits
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  • 13
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    A new laser scanning system for measuring action potential propagation in the heart (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-10-23
    Description: A rapid laser scanning system was developed to map the spread of excitation in amphibian and mammalian hearts stained with fluorescent dye. Isochronic maps of conduction were constructed by timing the upstroke of the optical action potential; 128 sites could be scanned in 4 milliseconds. The accuracy of this technique was verified by recording simultaneously from 16 unipolar electrodes placed in different areas of the heart. Conducted action potentials in normal frog heart propagated at 0.1 meter per second. Propagation of action potentials was also monitored in ischemic cat heart, in which both driven and arrhythmic action potential upstrokes could be tracked. The results suggest that this system is capable of scanning the normal and abnormal spread of electrical activity in the heart.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dillon, S -- Morad, M -- New York, N.Y. -- Science. 1981 Oct 23;214(4519):453-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6974891" target="_blank"〉PubMed〈/a〉
    Keywords: *Action Potentials ; Animals ; *Benzenesulfonates ; Cats ; Coronary Disease/physiopathology ; Fluorescent Dyes ; Guinea Pigs ; Heart/*physiology ; *Lasers ; Rabbits ; Rana catesbeiana ; Spectrometry, Fluorescence/methods
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  • 14
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    Fertilizability of ova ovulated and recovered from rabbit ovaries perfused in vitro (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-09-04
    Description: Ovaries removed from New Zealand White rabbits were perfused and exposed to gonadotropin in vitro. The ova ovulated in vitro (N = 56) were recovered and cultured and then transferred to the oviducts of six previously mated Dutch Belted hosts. Twelve of the resulting 36 offspring (33.3 percent) were white. In control matings between 12 Dutch Belted females (six randomly selected and the six hosts) and New Zealand White males, only one of 80 (1.2 percent) offspring was white. These data indicate that ova ovulated in vitro can be transferred to the oviduct of a host rabbit where they may be fertilized and after implantation may develop into viable embryos.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kobayashi, Y -- Santulli, R -- Wright, K H -- Wallach, E E -- HD-05948/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1981 Sep 4;213(4512):1127-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7268420" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chorionic Gonadotropin/*pharmacology ; Embryo Transfer ; Female ; *Fertilization in Vitro ; Ovary/drug effects/*physiology ; *Ovulation/drug effects ; Pregnancy ; Rabbits
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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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    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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  • 18
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    The hormonal control of sexual development (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-03-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, J D -- George, F W -- Griffin, J E -- AM03892/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1981 Mar 20;211(4488):1278-84.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7010602" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Mullerian Hormone ; Estradiol/metabolism/*physiology ; Female ; *Glycoproteins ; Gonadotropins/physiology ; *Growth Inhibitors ; Humans ; Male ; Morphogenesis ; Mullerian Ducts ; Ovary/embryology ; Rabbits ; Receptors, Androgen/metabolism ; *Sex Differentiation ; Testicular Hormones/*physiology ; Testis/embryology/secretion ; Testosterone/metabolism/*physiology ; Time Factors ; Urogenital System/embryology ; Wolffian Ducts
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  • 19
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    Role for the adenosine triphosphate-dependent proteolytic pathway in reticulocyte maturation (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-02-19
    Description: As reticulocytes mature into erythrocytes, organelles and many enzymes are lost. Protein degradation during reticulocyte maturation was measured by monitoring the release of tyrosine from cell proteins. Proteolysis in rabbit red blood cells was directly proportional to the number of reticulocytes and was low in erythrocytes. This process was inhibited by blockers of cellular adenosine triphosphate production and by agents, such as o-phenanthroline, N-ethylmaleimide, and hemin, which inhibit the soluble adenosine triphosphate-dependent proteolytic system. The breakdown of endogenous proteins in reticulocyte extracts was also inhibited by these agents and required adenosine triphosphate. Inhibitors of lysosomal function, however, did not affect proteolysis. Thus, the proteolytic system that degrades abnormal proteins also catalyzes the elimination of proteins during red cell development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boches, F S -- Goldberg, A L -- New York, N.Y. -- Science. 1982 Feb 19;215(4535):978-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7156977" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/*physiology ; Animals ; Blood Proteins/*metabolism ; Cell Differentiation ; Cyclophosphamide/pharmacology ; Deoxyglucose/pharmacology ; Dinitrophenols/pharmacology ; Lysosomes/enzymology ; Rabbits ; Reticulocytes/*physiology ; Tyrosine/analysis
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  • 20
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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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 21
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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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  • 22
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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)
    Details
    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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  • 23
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    Significance of tissue myo-inositol concentrations in metabolic regulation in nerve (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-08-27
    Description: Approximately 25 percent of resting energy utilization in isolated nerve endoneurium is inhibited by medium containing defatted albumin and selectively restored by arachidonic acid but is unaffected by indomethacin or nordihydroguaiaretic acid. The same component of energy utilization is inhibited by small decreases in endoneurial myo-inositol, which decrease incorporation of carbon-14-labeled arachidonic acid into phosphatidylinositol. The fraction of the resting oxygen uptake inhibited by ouabain is decreased 40 to 50 percent by a reduced tissue myo-inositol concentration or by defatted albumin. Metabolic regulation by rapid, basal phosphatidylinositol turnover is dependent on the maintenance of normal tissue myoinositol concentrations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simmons, D A -- Winegrad, A I -- Martin, D B -- T32 AMO7314/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1982 Aug 27;217(4562):848-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6285474" target="_blank"〉PubMed〈/a〉
    Keywords: Albumins/pharmacology ; Animals ; Arachidonic Acid ; Arachidonic Acids/pharmacology ; Catechols/pharmacology ; Indomethacin/pharmacology ; Inositol/*metabolism ; Linolenic Acids/pharmacology ; Masoprocol ; Ouabain/pharmacology ; Oxygen Consumption ; Palmitic Acids/pharmacology ; Peripheral Nerves/*metabolism ; Phosphatidylinositols/metabolism ; Rabbits ; gamma-Linolenic Acid
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  • 24
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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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  • 25
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    Human platelet-derived growth factor (PDGF): amino-terminal amino acid sequence (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 26
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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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  • 27
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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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  • 28
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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)
    Details
    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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  • 29
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    Protein phosphatases: properties and role in cellular regulation (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-07-22
    Description: Protein phosphorylation is a principal regulatory mechanism in the control of almost all cellular processes. The nature of the protein phosphatases that participate in these reactions has been a subject of controversy. Four enzymes, termed protein phosphatases 1, 2A, 2B, and 2C, account for virtually all of the phosphatase activity toward phosphoproteins involved in controlling glycogen metabolism, glycolysis, gluconeogenesis, fatty acid synthesis, cholesterol synthesis, and protein synthesis. The properties, physiological roles, and mechanisms for regulating the four protein phosphatases are reviewed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ingebritsen, T S -- Cohen, P -- New York, N.Y. -- Science. 1983 Jul 22;221(4608):331-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6306765" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/physiology ; Cyclic AMP/metabolism ; Glycogen/metabolism ; Liver/enzymology ; Muscles/enzymology ; Phosphoprotein Phosphatases/classification/*physiology ; Phosphoproteins/metabolism ; Phosphorylase Phosphatase/metabolism ; Phosphorylation ; Protein Biosynthesis ; Protein Kinases/physiology ; Rabbits ; Rats
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  • 30
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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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  • 31
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    Oxygen tension regulates the expression of angiogenesis factor by macrophages (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-09-23
    Description: When cultured in a hypoxic environment similar to that found in the center of a wound, macrophages secreted active angiogenesis factor into the medium. Under conditions similar to those of well-oxygenated tissue, macrophages did not secrete active angiogenesis factor. Macrophages that secreted the factor at hypoxic conditions stopped secreting it when returned to room air. Thus the control of angiogenesis in wound healing may be the result of macrophages responding to tissue oxygen tension without the necessity of interacting with other cell types or biochemical signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knighton, D R -- Hunt, T K -- Scheuenstuhl, H -- Halliday, B J -- Werb, Z -- Banda, M J -- GM27345/GM/NIGMS NIH HHS/ -- HL26323/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1983 Sep 23;221(4617):1283-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6612342" target="_blank"〉PubMed〈/a〉
    Keywords: Angiogenesis Inducing Agents/*biosynthesis ; Animals ; Anoxia/physiopathology ; Cells, Cultured ; Cornea ; Growth Substances/*biosynthesis ; Macrophages/*physiology ; Models, Biological ; Oxygen/*physiology ; Rabbits ; *Wound Healing
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    Cholesterol--heart disease link illuminated. New findings explain how blood cholesterol levels are controlled and how to lower them substantially in persons at high risk of heart disease (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-09-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G -- New York, N.Y. -- Science. 1983 Sep 16;221(4616):1164-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6310747" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anticholesteremic Agents/therapeutic use ; Cholesterol/*blood ; Coronary Disease/drug therapy/*etiology ; Humans ; Lovastatin ; Naphthalenes/therapeutic use ; Rabbits ; Receptors, Cell Surface/physiology ; Receptors, LDL
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    Monoclonal antibodies reveal the structural basis of antibody diversity (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Bone cell differentiation and growth factors (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-05-13
    Description: Bone morphogenetic protein and bone-derived growth factors are biochemical tools for research on induced cell differentiation and local mechanisms controlling cell proliferation. Bone morphogenetic protein irreversibly induces differentiation of perivascular mesenchymal-type cells into osteoprogenitor cells. Bone-derived growth factors are secreted by and for osteoprogenitor cells and stimulate DNA synthesis. Bone generation and regeneration are attributable to the co-efficiency of bone morphogenetic protein and bone-derived growth factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Urist, M R -- DeLange, R J -- Finerman, G A -- DEO2103-17/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 1983 May 13;220(4598):680-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6403986" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Bone Development ; Bone Matrix/drug effects/physiology ; Bone Morphogenetic Proteins ; Bone Neoplasms/physiopathology ; Cattle ; Cell Differentiation ; DNA, Neoplasm/metabolism ; Dogs ; Growth Substances/*physiology ; Guinea Pigs ; Haplorhini ; Humans ; Insulin-Like Growth Factor II ; Mice ; *Osteogenesis ; Osteosarcoma/physiopathology ; Proteins/pharmacology/physiology ; Rabbits ; Rats
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  • 35
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    Potentiation of glucocorticoid activity by 5 beta-dihydrocortisol: its role in glaucoma (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-10-14
    Description: 5 beta-Dihydrocortisol potentiated the threshold level (the smallest dose producing a measurable effect) of topically applied cortisol (0.02 percent) and dexamethasone (0.003 percent) in causing nuclear translocation of the cytosolic glucocorticoid receptor in rabbit iris-ciliary body tissue. 5 beta-Dihydrocortisol accumulates in cells cultured from trabecular meshwork specimens from patients with primary open-angle glaucoma, but not in similar cells derived from nonglaucomatous patients. In view of the sensitivity of patients with primary open-angle glaucoma to the effects of glucocorticoids in raising intraocular pressure, this potentiation may be responsible for the steroid sensitivity and for the ocular hypertension seen in this disorder.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weinstein, B I -- Gordon, G G -- Southren, A L -- EY 01313/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1983 Oct 14;222(4620):172-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6623065" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/metabolism ; Ciliary Body/metabolism ; Cytoplasm/metabolism ; Dexamethasone/pharmacology ; Glaucoma, Open-Angle/*physiopathology ; Hydrocortisone/pharmacology ; Intraocular Pressure/*drug effects ; Iris/metabolism ; Rabbits ; Receptors, Glucocorticoid/*drug effects/metabolism ; Receptors, Steroid/*drug effects
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    Rabies virus glycoprotein analogs: biosynthesis in Escherichia coli (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Noninvasive observations of fluorinated anesthetics in rabbit brain by fluorine-19 nuclear magnetic resonance (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-10-28
    Description: Fluorinated anesthetics were observed noninvasively in the brain of intact rabbits with fluorine-19 nuclear magnetic resonance spectroscopy. High-resolution fluorine-19 spectra of halothane, methoxyflurane, and isoflurane were obtained with a surface coil centered over the calvarium. Elimination of halothane from the brain was also monitored by this technique. Residual fluorine-19 signals from halothane (or a metabolite) could be detected as long as 98 hours after termination of anesthesia. These observations demonstrate the feasibility of using this technique to study the fate of fluorinated anesthetics in live mammals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wyrwicz, A M -- Pszenny, M H -- Schofield, J C -- Tillman, P C -- Gordon, R E -- Martin, P A -- GM 29520/GM/NIGMS NIH HHS/ -- K04 GM 00503/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Oct 28;222(4622):428-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6623084" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*metabolism ; Halothane/*metabolism ; Isoflurane/*metabolism ; Kinetics ; Magnetic Resonance Spectroscopy ; Methoxyflurane/*metabolism ; Methyl Ethers/*metabolism ; Rabbits
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    Leukotrienes: mediators of immediate hypersensitivity reactions and inflammation (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-05-06
    Description: Arachidonic acid plays a central role in a biological control system where such oxygenated derivatives as prostaglandins, thromboxanes, and leukotrienes are mediators. The leukotrienes are formed by transformation of arachidonic acid into an unstable epoxide intermediate, leukotriene A4, which can be converted enzymatically by hydration to leukotriene B4, and by addition of glutathione to leukotriene C4. This last compound is metabolized to leukotrienes D4 and E4 by successive elimination of a gamma-glutamyl residue and glycine. Slow-reacting substance of anaphylaxis consists of leukotrienes C4, D4, and E4. The cysteinyl-containing leukotrienes are potent bronchoconstrictors, increase vascular permeability in postcapillary venules, and stimulate mucus secretion. Leukotriene B4 causes adhesion and chemotactic movement of leukocytes and stimulates aggregation, enzyme release, and generation of superoxide in neutrophils. Leukotrienes C4, D4, and E4, which are released from the lung tissue of asthmatic subjects exposed to specific allergens, seem to play a pathophysiological role in immediate hypersensitivity reactions. These leukotrienes, as well as leukotriene B4, have pro-inflammatory effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Samuelsson, B -- New York, N.Y. -- Science. 1983 May 6;220(4597):568-75.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6301011" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arachidonic Acids/metabolism/pharmacology/physiology ; Bronchi/drug effects ; Cats ; Chemical Phenomena ; Chemistry ; Cricetinae ; Guinea Pigs ; Haplorhini ; Humans ; Hypersensitivity, Immediate/*physiopathology ; Inflammation/*physiopathology ; Leukocytes/drug effects/metabolism ; Leukotriene B4/pharmacology/*physiology ; Mice ; Microcirculation/drug effects ; Rabbits ; Rats ; SRS-A/*physiology
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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)
    Details
    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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    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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    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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    Initiation of angiogenesis by human follicular fluid (1984)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1984-04-27
    Description: Angiogenesis was observed and measured after injection of human follicular fluid into rabbit corneas. Undiluted human follicular fluid stimulated angiogenesis in every case, with new blood vessels visible 3 days after injection and extending 2.0 millimeters from the corneal scleral limbus into the injection site by day 15. Stimulation of angiogenesis was lost by heating or diluting the follicular fluid but was retained after charcoal stripping or dialysis. Human follicular fluid contains an angiogenic factor that may be associated with perifollicular neovascularization during folliculogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frederick, J L -- Shimanuki, T -- diZerega, G S -- New York, N.Y. -- Science. 1984 Apr 27;224(4647):389-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6200930" target="_blank"〉PubMed〈/a〉
    Keywords: Angiogenesis Inducing Agents/*analysis ; Animals ; Body Fluids/*analysis ; Chorionic Gonadotropin/pharmacology ; Cornea/blood supply ; Dialysis ; Female ; Growth Substances/*analysis ; Hot Temperature ; Humans ; Menstruation ; *Neovascularization, Pathologic ; Ovarian Follicle/*analysis ; Rabbits
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    Identification and location of brain protein 4.1 (1984)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1984-06-29
    Description: Protein 4.1 is a membrane skeletal protein that converts the low-affinity interaction between spectrin and actin into a high-affinity ternary complex of spectrin, protein 4.1, and actin that is essential to the structural stability of the erythrocyte. Pig brain was shown to contain an 87-kilodalton immunoreactive analog of protein 4.1 that has partial sequence homology with pig erythrocyte protein 4.1 and the same location as spectrin in the cortical cytoplasm of neuronal and glial cell types of the cerebellum.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goodman, S R -- Casoria, L A -- Coleman, D B -- Zagon, I S -- HL 26059/HL/NHLBI NIH HHS/ -- NS19357/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1984 Jun 29;224(4656):1433-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6374897" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Animals ; Blood Proteins/*metabolism ; Brain/*metabolism ; *Cytoskeletal Proteins ; Erythrocytes/metabolism ; Fluorescent Antibody Technique ; Immunoglobulin G/immunology ; Male ; *Membrane Proteins ; *Neuropeptides ; Rabbits ; Spectrin/metabolism ; Swine
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  • 46
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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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    The biochemistry of memory: a new and specific hypothesis (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-06-08
    Description: Recent studies have uncovered a synaptic process with properties required for an intermediate step in memory storage. Calcium rapidly and irreversibly increases the number of receptors for glutamate (a probable neurotransmitter) in forebrain synaptic membranes by activating a proteinase (calpain) that degrades fodrin, a spectrin-like protein. This process provides a means through which physiological activity could produce long-lasting changes in synaptic chemistry and ultrastructure. Since the process is only poorly represented in the brain stem, it is hypothesized to be responsible for those forms of memory localized in the telencephalon.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lynch, G -- Baudry, M -- AG 00538/AG/NIA NIH HHS/ -- MH 19793-12/MH/NIMH NIH HHS/ -- NH 00358-03/NH/NIH HHS/ -- New York, N.Y. -- Science. 1984 Jun 8;224(4653):1057-63.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6144182" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/physiology ; Calpain ; Carrier Proteins/physiology ; Cerebral Cortex/physiology ; Endopeptidases/physiology ; Glutamates/physiology ; Glutamic Acid ; Hippocampus/physiology ; Humans ; Learning/physiology ; Leupeptins/pharmacology ; Memory/*physiology ; *Microfilament Proteins ; Neuronal Plasticity ; Rabbits ; Rats ; Receptors, Cell Surface/physiology ; Receptors, Glutamate ; Receptors, Neurotransmitter/physiology ; Synapses/physiology ; Synaptic Membranes/physiology ; Telencephalon/physiology
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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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  • 49
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    Cerebellum: essential involvement in the classically conditioned eyelid response (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-20
    Description: Classical conditioning of the eyelid response in the rabbit was used to investigate the neuronal structures mediating basic associative learning of discrete, adaptive responses. Lesions of the ipsilateral dentate-interpositus nuclei, but not of the cerebellar cortex, abolished the learned eyeblink response. Recordings from these nuclei have revealed neuronal responses related to the learning of the response. Stimulating these recording sites produced the eyelid response. The dentate-interpositus nuclei were concluded to be critically involved in the learning and production of classically conditioned responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCormick, D A -- Thompson, R F -- 1-F31-MH08673/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1984 Jan 20;223(4633):296-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6701513" target="_blank"〉PubMed〈/a〉
    Keywords: Acoustic Stimulation ; Animals ; *Blinking ; Cerebellar Cortex/physiology ; Cerebellum/*physiology ; *Conditioning, Classical ; *Conditioning, Eyelid ; Rabbits
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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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    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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    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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    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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    Plasmodium knowlesi sporozoite antigen: expression by infectious recombinant vaccinia virus (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-04-27
    Description: The gene coding for the circumsporozoite antigen of the malaria parasite Plasmodium knowlesi was inserted into the vaccinia virus genome under the control of a defined vaccinia virus promoter. Cells infected with the recombinant virus synthesized polypeptides of 53,000 to 56,000 daltons that reacted with monoclonal antibody against the repeating epitope of the malaria protein. Furthermore, rabbits vaccinated with the recombinant virus produced antibodies that bound specifically to sporozoites. These data provide evidence for expression of a cloned malaria gene in mammalian cells and illustrate the potential of vaccinia virus recombinants as live malaria vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, G L -- Godson, G N -- Nussenzweig, V -- Nussenzweig, R S -- Barnwell, J -- Moss, B -- New York, N.Y. -- Science. 1984 Apr 27;224(4647):397-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6200932" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibody Formation ; Antigens, Surface/analysis/*genetics/immunology ; *Cloning, Molecular ; *DNA, Recombinant ; Epitopes/immunology ; Genes ; Genes, Viral ; Genetic Vectors ; Operon ; Plasmodium/*genetics/immunology ; Rabbits ; Vaccination ; Vaccinia virus/*genetics
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    Long-term potentiation of hippocampal synaptic transmission affects rate of behavioral learning (1984)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1984-05-11
    Description: Electrical stimulation techniques were used to produce a long-lasting potentiation of synaptic transmission in the hippocampus of naive rabbits. Animals were then classically conditioned. Long-term potentiation of the hippocampus before training increased the rate at which animals subsequently learned the conditioning task. This result has significance for potential cellular mechanisms of associative learning.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berger, T W -- MH 00343/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1984 May 11;224(4649):627-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6324350" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Electric Stimulation ; Hippocampus/*physiology ; Learning/*physiology ; Male ; Nictitating Membrane/physiology ; Rabbits ; Receptors, Neurotransmitter/physiology ; Synapses/physiology ; *Synaptic Transmission
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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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    Clustering of human H1 and core histone genes (1984)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1984-06-08
    Description: An H1 histone gene was isolated from a 15-kilobase human DNA genomic sequence. The presence of H2A, H2B, H3, and H4 genes in this same 15-kilobase fragment indicates that mammalian core and H1 histone genes are clustered.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carozzi, N -- Marashi, F -- Plumb, M -- Zimmerman, S -- Zimmerman, A -- Coles, L S -- Wells, J R -- Stein, G -- Stein, J -- GM 32010/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Jun 8;224(4653):1115-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6719136" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA/genetics ; *Genes ; HeLa Cells ; Histones/*genetics ; Humans ; Nucleic Acid Hybridization ; Rabbits ; Trout ; Xenopus
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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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    Major pol gene progenitors in the evolution of oncoviruses (1984)
    American Association for the Advancement of Science (AAAS)
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    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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    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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    Altered activity in the hippocampus is more detrimental to classical conditioning than removing the structure (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-04-15
    Description: Hippocampal ablation has no effect on the acquisition of the rabbit's classically conditioned nictitating membrane response. Systemic administration of scopolamine, which alters hippocampal neuronal activity, severely retards acquisition of the conditioned response in normal animals and those with cortical ablations. In animals with hippocampal ablations, however, scopolamine has no effect on conditioning. These findings suggest that altered neuronal activity in the hippocampus is more detrimental to conditioning than removing the structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Solomon, P R -- Solomon, S D -- Schaaf, E V -- Perry, H E -- MH33381/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1983 Apr 15;220(4594):329-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6836277" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Conditioning, Classical/drug effects/*physiology ; Female ; Hippocampus/drug effects/*physiology ; Male ; Nictitating Membrane/physiology ; Rabbits ; Scopolamine Hydrobromide/pharmacology
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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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    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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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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    Surface-active biomaterials (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-09
    Description: Since the discovery in 1969 of a man-made surface-active material that would bond to bone, a range of materials with the same ability has been developed. These include glass, glass-ceramic, and ceramic materials which have a range of reaction rates and from which it should be possible to select a surface-active material for a specific application. The available materials and their similarities, differences, and current clinical applications are reviewed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hench, L L -- Wilson, J -- New York, N.Y. -- Science. 1984 Nov 9;226(4675):630-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6093253" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biocompatible Materials/metabolism/therapeutic use ; Bone Cements/therapeutic use ; Bone and Bones/metabolism ; Ceramics ; Dogs ; Durapatite ; Glass ; Humans ; Hydroxyapatites/therapeutic use ; Male ; Orthodontics ; Rabbits ; Rats ; Rats, Inbred Strains ; Surface Properties ; Tissue Adhesives/therapeutic use
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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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    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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  • 78
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    Shiga-like toxin-converting phages from Escherichia coli strains that cause hemorrhagic colitis or infantile diarrhea (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-09
    Description: Escherichia coli K-12 acquired the ability to produce a high titer of Shiga-like toxin after lysogenization by either of two different bacteriophages isolated from a highly toxinogenic Escherichia coli O157:H7 strain that causes hemorrhagic colitis. One of these phages and another Shiga-like toxin-converting phage from an Escherichia coli O26 isolate associated with infantile diarrhea were closely related in terms of morphology, virion polypeptides, DNA restriction fragments, lysogenic immunity, and heat stability, although a difference in host range was noted. These phages are currently the best-characterized representatives from a broader family of Shiga-like toxin-converting phages.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Brien, A D -- Newland, J W -- Miller, S F -- Holmes, R K -- Smith, H W -- Formal, S B -- AI20148-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 9;226(4675):694-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6387911" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Toxins/*metabolism ; Bacteriophages/*metabolism ; Colitis, Ulcerative/*microbiology ; DNA, Viral/metabolism ; Diarrhea, Infantile/*microbiology ; Escherichia coli/*metabolism ; Humans ; Rabbits ; Shiga Toxins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 79
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    Kainic acid induces sprouting of retinal neurons (1984)
    American Association for the Advancement of Science (AAAS)
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    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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  • 80
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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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  • 81
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    DNA-binding proteins (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 82
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    Fibronectin binds to some bacteria but does not promote their uptake by phagocytic cells (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-04-08
    Description: The involvement of plasma fibronectin in phagocytosis of bacteria was investigated by testing the binding of fibronectin to several species of bacteria and by evaluating the ability of fibronectin to promote binding and endocytosis of two species of these bacteria by phagocytic cells. Fibronectin binds non-covalently to Gram-positive and Gram-negative bacteria and to yeast but did not appear to be necessary or sufficient for uptake of Staphylococcus aureus and Salmonella typhimurium by several different phagocytic cell types.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Van de Water, L -- Destree, A T -- Hynes, R O -- R01CA17007/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1983 Apr 8;220(4593):201-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6338594" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacteria/*metabolism ; Cell Line ; Cricetinae ; Endocytosis ; Fibronectins/*metabolism ; Humans ; Macrophages/physiology ; Mice ; Opsonin Proteins/physiology ; *Phagocytosis ; Rabbits ; Salmonella typhimurium/metabolism ; Sepsis/immunology ; Staphylococcus aureus/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 83
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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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  • 84
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    C-Glucuronidation of the acetylenic moiety of ethchlorvynol in the rabbit (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-08-08
    Description: An acetylenic C-glucuronide of the sedative-hypnotic drug ethchlorvynol was isolated from rabbit urine as the major metabolite. The C-glucuronide represents a novel metabolic pathway for acetylenes and is a rare example of the formation of a carbon-glucuronide bond in mammalian systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abolin, C R -- Tozer, T N -- Craig, J C -- Gruenke, L D -- New York, N.Y. -- Science. 1980 Aug 8;209(4457):703-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7394528" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylene ; Animals ; Carbon Radioisotopes ; Ethchlorvynol/*analogs & derivatives/*metabolism/urine ; Glucuronidase ; Magnetic Resonance Spectroscopy ; Mass Spectrometry ; Rabbits ; Spectrophotometry, Infrared
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  • 85
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    Antibody to spermine: a natural biological constituent (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-06-06
    Description: A protein that binds spermine specifically was separated from normal rabbit serum by affinity chromatography. Immunoelectrophoresis, the Ouchterlony immunodiffusion test, and gradient gel electrophoresis indicated that this protein has immunoglobulin characteristics and consists of several populations of antibodies to spermine. These were sequentially released from Sepharose-spermine gel by step-wise elution with solutions ranging in pH from 4 to 1. The binding constants varied from 5.0 x 10(8) to 11.1 x 10(8) liters per mole. These globulins did not react with monoacetylputrescine, L-ornithine, L-lysine, and histamine. Negligible cross-reactivity was detected with spermidine, putrescine, N8-monoacetylspermidine, cadaverine, and diaminopropane. Since perturbations in polyamine metabolism have been identified in several diseases, the study of extracellular polyamine homeostasis may reveal an important regulatory function for this protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bartos, D -- Bartos, F -- Campbell, R A -- Grettie, D P -- Smejtek, P -- New York, N.Y. -- Science. 1980 Jun 6;208(4448):1178-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7375929" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/*isolation & purification ; Binding Sites, Antibody ; Chromatography, Affinity ; Homeostasis ; Immunoglobulin G/isolation & purification ; Kinetics ; Rabbits ; Spermine/*immunology/metabolism
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  • 86
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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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  • 87
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    Acetylcholine synthesis by displaced amacrine cells (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-10-01
    Description: The ganglion cell layer of the rabbit retina contains neurons that synthesize acetylcholine. To identify these neurons, the ganglion cells were labeled by retrograde transport of a fluorescent dye, and the acetylcholine-synthesizing cells of the same retinas were labeled by exposing the tissue to tritiated choline. Autoradiographs inspected by fluorescence microscopy showed that tritiated acetylcholine and the dye accumulated in different cells. Optic nerves of other animals were sectioned, causing degeneration of many neurons of the ganglion cell layer. This loss affected neither the retina's overall rate of acetylcholine synthesis nor the number of acetylcholine-containing cells in the ganglion cell layer. The acetylcholine-synthesizing neurons thus appear to be displaced amacrine cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hayden, S A -- Mills, J W -- Masland, R M -- EY 01075/EY/NEI NIH HHS/ -- HLO 6664/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1980 Oct;210(4468):435-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7433984" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/*biosynthesis ; Animals ; Cholinergic Fibers/metabolism ; Neurons/metabolism ; Rabbits ; Retina/cytology/*metabolism
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  • 88
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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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  • 89
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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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  • 90
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    Purified reduced nicotinamide adenine dinucleotide: responses to lactate dehydrogenase isozymes from three cell sources (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-05-01
    Description: Lactate dehydrogenase (LDH, E.C. 1.1.1.27) isozymes from three single-cell sources reacted differently with reduced nicotinamide adenine dinucleotide (NADH) purified to published chromatographic and spectrophotometric specifications and free of inhibitors of LDH, when compared with a commercial preparation of NADH. The activity of LDH-1, purified from rabbit erythrocytes, increased the most with inhibitor-free NADH; the next most stimulated were the LDH isozymes from a control hepatocyte line; but hardly responsive at all were the same isozymes from chemically transformed cells. Thus isozyme composition alone did not account for the range of responses to purified NADH. The commercial preparation of NADH used in these studies contains the Strandjord-Clayson inhibitors, the most potent group identified in NADH preparations relative to LDH activity. The results suggest that specific molecular differences in individual isozymes contribute to the differential response to the Strandjord-Clayson inhibitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaplan, A E -- Weiss, E R -- Byrne, S T -- El-Torkey, N M -- Margolis, S A -- New York, N.Y. -- Science. 1981 May 1;212(4494):553-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7209551" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Transformation, Neoplastic/metabolism ; Erythrocytes/enzymology ; Isoenzymes ; L-Lactate Dehydrogenase/antagonists & inhibitors/*metabolism ; Liver Neoplasms, Experimental/enzymology ; NAD/analysis/*metabolism ; Rabbits ; Rats
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  • 91
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    Specific and sensitive radioimmunoassay for 3-methoxy-4-hydroxyphenylethyleneglycol (MOPEG) (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-02-06
    Description: Antibodies that specifically bind the norepinephrine metabolite 3-methoxy-4-hydroxyphenylethyleneglycol (MOPEG) were produced in rabbits after injection of a derivative of MOPEG conjugated with bovine thyroglobulin. A sensitive radioimmunoassay was devised with this antiserum, in which as little as 0.5 nanogram of MOPEG can be accurately measured with a final antibody dilution of 1:180. The antibody appears to be specific for MOPEG, since tritiated MOPEG was not displaced from the antibodies by norepinephrine, epinephrine, dopamine, serotonin, or their major metabolites including MOPEG-sulfate (333 nanograms each).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keeton, T K -- Krutzsch, H -- Lovenberg, W -- New York, N.Y. -- Science. 1981 Feb 6;211(4482):586-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7455697" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibody Specificity ; Brain/*metabolism ; Brain Mapping ; Glycols/*analysis ; Methoxyhydroxyphenylglycol/*analysis/metabolism ; Rabbits ; *Radioimmunoassay/methods ; Rats ; Thyroglobulin
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  • 92
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    Serum albumin beads: an injectable, biodegradable system for the sustained release of drugs (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-07-10
    Description: Biologically active compounds were entrapped in cross-linked serum albumin microbeads. Injection of these drug-impregnated beads into rabbits produced no adverse immunological reactions. Sustained release (20 days) of progesterone was demonstrated in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, T K -- Sokoloski, T D -- Royer, G P -- New York, N.Y. -- Science. 1981 Jul 10;213(4504):233-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6787705" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Delayed-Action Preparations ; Glutaral ; Injections, Intramuscular ; Injections, Subcutaneous ; Kinetics ; Male ; Microscopy, Electron, Scanning ; Norgestrel/administration & dosage ; Progesterone/*administration & dosage/blood ; Rabbits ; Serum Albumin, Bovine/*administration & dosage
    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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  • 93
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    Assessment of pharmacological treatment of myocardial infarction by phosphorus-31 NMR with surface coils (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-01-09
    Description: Phosphorus-31 nuclear magnetic resonance (NMR) measurements with small surface coils have been used to observe phosphorus metabolism of perfused hearts within localized regions. The method allows for direct, noninvasive, sequential assessment of the altered regional metabolism resulting from myocardial infarction and its response to drug treatment, which cannot be observed by conventional techniques.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nunnally, R L -- Bottomley, P A -- GM 17172/GM/NIGMS NIH HHS/ -- HL 17655-06/HL/NHLBI NIH HHS/ -- HL 22080/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1981 Jan 9;211(4478):177-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7444460" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chlorpromazine/therapeutic use ; Coronary Circulation/drug effects ; Disease Models, Animal ; Magnetic Resonance Spectroscopy/*methods ; Myocardial Infarction/*diagnosis/drug therapy/metabolism ; Phosphorus/*metabolism ; Phosphorus Isotopes ; Rabbits ; Verapamil/therapeutic use
    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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  • 94
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    Hyperkeratosis induced by sunlight degradation products of the major polybrominated biphenyl in Firemaster (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-08-21
    Description: Sunlight photodegradation of 2,2', 4,4', 5,5' -hexabromobiphenyl, the major component of Firemaster, gave a mixture that produces severe hyperkeratosis of the rabbit ear. This component in its pure state does not cause hyperkeratosis. One or more of the four major photolysis products must be responsible for this activity. A similar photodegradation pattern was observed for 2,2', 3,4,4', 5,5' -heptabromobiphenyl, the second largest component of Firemaster.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Patterson, D G -- Hill, R H -- Needham, L L -- Orti, D L -- Kimbrough, R D -- Liddle, J A -- New York, N.Y. -- Science. 1981 Aug 21;213(4510):901-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6266016" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biphenyl Compounds/radiation effects ; Chemical Industry ; Disease Models, Animal ; Environmental Exposure ; Keratosis/*chemically induced ; Michigan ; Photochemistry ; *Polybrominated Biphenyls/radiation effects ; Rabbits ; Sunlight
    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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  • 95
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    Hemoglobin Parchman: double crossover within a single human gene (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 96
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    Destruction of noradrenergic neurons in rabbit brainstem elevates plasma vasopressin, causing hypertension (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-08-13
    Description: When A1 noradrenergic neurons in the caudal ventrolateral medulla of rabbits are destroyed electrolytically or by local injection of the neurotoxin kainic acid, the concentration of vasopressin in plasma increases, causing hypertension. The A1 neurons may tonically inhibit the activity of vasopressin-secreting neuroendocrine cells through a direct hypothalamic projection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blessing, W W -- Sved, A F -- Reis, D J -- HL 1894/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1982 Aug 13;217(4560):661-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6124043" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic Fibers/*physiology ; Animals ; Arginine Vasopressin/*blood ; Blood Pressure ; Brain Stem/*physiology ; Glutamates/pharmacology ; Glutamic Acid ; Hypertension/*etiology ; Hypothalamus/physiology ; Kainic Acid/pharmacology ; Male ; Neurosecretion ; Norepinephrine/physiology ; Rabbits
    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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  • 97
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    Lyme disease-a tick-borne spirochetosis? (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-06-18
    Description: A treponema-like spirochete was detected in and isolated from adult Ixodes dammini, the incriminated tick vector of Lyme disease. Causally related to the spirochetes may be long-lasting cutaneous lesions that appeared on New Zealand White rabbits 10 to 12 weeks after infected ticks fed on them. Samples of serum from patients with Lyme disease were shown by indirect immunofluorescence to contain antibodies to this agent. It is suggested that the newly discovered spirochete is involved in the etiology of Lyme disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burgdorfer, W -- Barbour, A G -- Hayes, S F -- Benach, J L -- Grunwaldt, E -- Davis, J P -- New York, N.Y. -- Science. 1982 Jun 18;216(4552):1317-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7043737" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arachnid Vectors/*microbiology ; Arthritis, Infectious/*microbiology ; Digestive System/microbiology ; Fluorescent Antibody Technique ; Humans ; Microscopy, Electron ; Microvilli/microbiology/ultrastructure ; Rabbits ; Seasons ; Spirochaetales/ultrastructure ; Spirochaetales Infections/*microbiology ; Ticks/*microbiology
    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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    Naloxone reverses neonatal depression caused by fetal asphyxia (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-06-11
    Description: Pregnant near-term rabbits were given an intravenous dose of saline or the opiate antagonist naloxone and then asphyxiated. The fetuses were delivered by cesarean section and evaluated for respiration, color, muscle tone, response to stimulation, and general activity at 1, 3, 5, 10, 15, and 30 minutes of age. The naloxone-treated pups had significantly better scores during the first 15 minutes after birth than the saline-treated pups. Naloxone did not adversely affect the scores of nonasphyxiated pups. These data suggest that endogenous opiates worsen the neonatal depression caused by intrauterine asphyxia and that this effect can be reversed by naloxone.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chernick, V -- Craig, R J -- New York, N.Y. -- Science. 1982 Jun 11;216(4551):1252-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7200636" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn/*physiology ; Asphyxia Neonatorum/complications/*physiopathology ; Depression/prevention & control ; Disease Models, Animal ; Humans ; Infant, Newborn ; Naloxone/*pharmacology ; Rabbits
    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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  • 99
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    Phagocyte impotence caused by an invasive bacterial adenylate cyclase (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-09-03
    Description: For unknown reasons, humans infected with the bacterium Bordetella pertussis are exceptionally vulnerable to secondary infections. Bordetella species elaborate a soluble, heat-stable, and highly active adenylate cyclase. This enzyme is internalized by phagocytic cells and catalyzes the unregulated formation of adenosine 3',5'-monophosphate (cyclic AMP), thereby disrupting normal cellular function. This unusual phenomenon may explain Bordetella-induced aphylaxis and may prove to be useful for investigating a variety of cyclic AMP-governed processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Confer, D L -- Eaton, J W -- 5T32H- L07062/PHS HHS/ -- New York, N.Y. -- Science. 1982 Sep 3;217(4563):948-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6287574" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/*metabolism ; Animals ; Bordetella pertussis/*enzymology ; Cells, Cultured ; Cyclic AMP/biosynthesis ; Humans ; Macrophages/physiology ; Neutrophils/physiology ; Phagocytes/*physiology ; Rabbits ; Superoxides/metabolism ; Temperature
    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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  • 100
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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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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