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  • Amino Acid Sequence  (54)
  • Cloning, Molecular  (46)
  • ASTROPHYSICS
  • Biochemistry and Biotechnology
  • Chemistry
  • EARTH RESOURCES AND REMOTE SENSING
  • Magnetism
  • Physics
  • American Association for the Advancement of Science (AAAS)  (112)
  • 2010-2014
  • 1980-1984  (112)
  • 1925-1929
  • 1984  (71)
  • 1983  (41)
Collection
Keywords
Publisher
Years
  • 2010-2014
  • 1980-1984  (112)
  • 1925-1929
Year
  • 1
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    American Association for the Advancement of Science (AAAS)
    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    Description: Human platelet-derived growth factor (PDGF) obtained from outdated human platelets was subjected to amino-terminal amino acid sequence analysis by automated Edman degradation.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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  • 2
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    American Association for the Advancement of Science (AAAS)
    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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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-02-11
    Description: Plasmids were constructed to direct synthesis of the human interferons IFN-alpha 1, IFN-alpha 2, and IFN-gamma in the yeast Saccharomyces cerevisiae. Expression of IFN genes containing coding sequences for secretion signals resulted in the secretion of IFN activity. A large proportion of the IFN-alpha 1 and IFN-alpha 2 isolated from the yeast cell growth media had the same amino termini as the natural mature interferons, suggesting a removal of the signal sequences identical to that of human cells. These results show that a lower eukaryote, such as yeast, can utilize and process a human signal sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hitzeman, R A -- Leung, D W -- Perry, L J -- Kohr, W J -- Levine, H L -- Goeddel, D V -- New York, N.Y. -- Science. 1983 Feb 11;219(4585):620-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6186023" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; Gene Expression Regulation ; Humans ; Interferons/*genetics/secretion ; Peptides/physiology ; Plasmids ; Protein Processing, Post-Translational ; Protein Sorting Signals ; RNA Processing, Post-Transcriptional ; Saccharomyces cerevisiae/genetics
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  • 4
    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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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-05-06
    Description: Crystalline cholesterol undergoes a phase transition a few degrees below human body temperature. The high-temperature form has an unusually complex structure with 16 independent molecules. In the transition two molecules change side chain conformation, four reorient about their long axes, and ten remain unchanged. The transition mechanism implies relatively nonspecific intermolecular interactions, qualitatively consistent with the behavior of cholesterol in biomembranes. The transition preserves a remarkably closely obeyed pseudosymmetry present in the structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hsu, L Y -- Nordman, C E -- GM15259/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 May 6;220(4597):604-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6836303" target="_blank"〉PubMed〈/a〉
    Keywords: Body Temperature ; Chemical Phenomena ; Chemistry ; *Cholesterol ; Crystallization ; Humans ; Magnetic Resonance Spectroscopy ; Molecular Conformation
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  • 6
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    American Association for the Advancement of Science (AAAS)
    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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  • 7
    Publication Date: 1983-06-17
    Description: A recombinant complementary DNA clone from Plasmodium knowlesi makes a beta-lactamase fusion polypeptide in Escherichia coli that reacts with a monoclonal antibody to a Plasmodium surface antigen. An epitope of the surface antigen was localized by transposon Tn5 mutagenesis mapping of the complementary DNA clone. The Tn5 mutation having the farthest 5' insert into the complementary DNA portion of the chimeric gene, giving the shortest truncated protein that maintained the ability to bind monoclonal antibody, defined the location of the epitope.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lupski, J R -- Ozaki, L S -- Ellis, J -- Godson, G N -- New York, N.Y. -- Science. 1983 Jun 17;220(4603):1285-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6190227" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal/immunology ; Antigens, Surface/genetics/*immunology ; Cloning, Molecular ; DNA, Recombinant/immunology/*metabolism ; Epitopes/genetics/*immunology ; Escherichia coli/genetics ; Plasmodium/*genetics/immunology
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  • 8
    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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  • 9
    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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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-07-20
    Description: The iron-carbon monoxide stretching mode and the iron-carbon-oxygen bending mode in carbon monoxide-bound cytochrome oxidase have been assigned at 520 and 578 cm-1, respectively. The frequencies, widths, and intensities of these modes show that the Fe-C-O grouping in carbon monoxide-cytochrome a3 is linear but tilted from the normal to the heme plane; that the iron-histidine bond in both five- and six-coordinate cytochrome a3 is strained; and that the carbon monoxide and the proximal histidine each have characteristic, well-defined orientations in all molecules. These data can account for the binding affinities of carbon monoxide and dioxygen under physiological conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Argade, P V -- Ching, Y C -- Rousseau, D L -- New York, N.Y. -- Science. 1984 Jul 20;225(4659):329-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6330890" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carbon Monoxide/metabolism ; Cattle ; Chemical Phenomena ; Chemistry ; Electron Transport Complex IV/*metabolism ; Myoglobin/metabolism ; Oxidation-Reduction ; Oxygen/metabolism ; Spectrum Analysis, Raman
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  • 11
    Publication Date: 1984-08-31
    Description: A T lymphotropic virus found in patients with the acquired immune deficiency syndrome (AIDS) or lymphadenopathy syndrome has been postulated to be the cause of AIDS. Immunological analysis of this retrovirus and its biological properties suggest that it is a member of the family of human T-lymphotropic retroviruses known as HTLV. Accordingly, it has been named HTLV-III. In the present report it is shown by nucleic acid hybridization that sequences of the genome of HTLV-III are homologous to the structural genes (gag, pol, and env) of both HTLV-I and HTLV-II and to a potential coding region called pX located between the env gene and the long terminal repeating sequence that is unique to the HTLV family of retroviruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arya, S K -- Gallo, R C -- Hahn, B H -- Shaw, G M -- Popovic, M -- Salahuddin, S Z -- Wong-Staal, F -- New York, N.Y. -- Science. 1984 Aug 31;225(4665):927-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089333" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; Base Sequence ; Cloning, Molecular ; Dna ; DNA, Viral ; Deltaretrovirus/classification/*genetics ; Genes ; *Genes, Viral ; Humans ; *Nucleic Acid Hybridization ; RNA, Viral ; Repetitive Sequences, Nucleic Acid
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  • 12
    Publication Date: 1984-10-19
    Description: A complementary DNA probe corresponding to the beta-chain gene of Ti, the human T lymphocyte receptor, has been molecularly cloned. The chromosomal origin of the Ti beta gene was determined with the complementary DNA by screening a series of 12 cell hybrid (mouse X human) DNA's containing overlapping subsets of human chromosomes. DNA hybridization (Southern) experiments showed that the human Ti beta gene resides on chromosome 7 and is thus not linked to the immunoglobulin loci or to the major histocompatibility locus in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barker, P E -- Ruddle, F H -- Royer, H D -- Acuto, O -- Reinherz, E L -- AI 21226/AI/NIAID NIH HHS/ -- GM-09966/GM/NIGMS NIH HHS/ -- R0 1 AI 19807/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1984 Oct 19;226(4672):348-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6435246" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; *Chromosomes, Human, 6-12 and X ; Cloning, Molecular ; Dna ; *Genes ; Genetic Linkage ; Humans ; Hybrid Cells ; Immunoglobulin kappa-Chains/genetics ; Major Histocompatibility Complex ; Mice ; Nucleic Acid Hybridization ; Receptors, Antigen, T-Cell/*genetics
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  • 13
    Publication Date: 1984-02-24
    Description: The immune response genes of the mouse encode two cell-surface glycoproteins, I-A and I-E, that play critical roles in determining the animal's immune responsiveness. The I-A antigen contains two chains, alpha and beta. A cloned beta-chain gene, I-A beta k, was introduced into B-lymphoma cells that express I-Ad. The transfected gene was successfully expressed on the cell surface of the recipient cells and was functional in stimulating allospecific T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ben-Nun, A -- Glimcher, L H -- Weis, J -- Seidman, J G -- AI18436/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1984 Feb 24;223(4638):825-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6420890" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/*physiology ; Cloning, Molecular ; Gene Expression Regulation ; *Genes, MHC Class II ; Heterozygote ; Lymphocyte Cooperation ; Lymphoma ; Macromolecular Substances ; Mice ; T-Lymphocytes/physiology ; Transfection ; Transformation, Genetic
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  • 14
    Publication Date: 1984-08-31
    Description: Bromodeoxyuridine (BrdUrd) treatment of the prolactin nonproducing subclone of GH cells (rat pituitary tumor cells) induces amplification of a 20-kilobase DNA fragment including all of the prolactin gene coding sequences. This amplified DNA segment, which is flanked by two unamplified regions, thus designates a unit of BrdUrd-induced amplified sequence. Cloned DNA segments, 10.3 kilobases long, from the 5' end of the rat prolactin gene of BrdUrd-responsive and -nonresponsive cells, were ligated to the thymidine kinase gene of herpes simplex virus type 1 (HSV1TK), and the hybrid DNA was transferred to thymidine kinase-deficient mouse fibroblast cells by transfection. The HSV1TK gene and the rat prolactin gene were amplified together in drug-treated transfectants carrying the hybrid DNA HSV1TK gene and rat prolactin gene of BrdUrd-responsive GH cells. These results suggest that the 10.3-kilobase DNA segment at the 5' end of the rat prolactin gene of BrdUrd-responsive GH cells carries the information for drug-induced gene amplification (amplicon) and that another gene, such as the HSV1TK gene, is also amplified when the latter is placed adjacent to this segment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biswas, D K -- Hartigan, J A -- Pichler, M H -- CA28218/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Aug 31;225(4665):941-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089335" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Bromodeoxyuridine/*pharmacology ; Cell Line ; Cloning, Molecular ; DNA/*genetics ; DNA, Recombinant ; *Gene Amplification ; Genes, Viral ; Mice ; Prolactin/genetics ; Rats ; Simplexvirus/genetics ; Thymidine Kinase/genetics ; Transfection
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  • 15
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    American Association for the Advancement of Science (AAAS)
    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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  • 16
    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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  • 17
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-08-19
    Description: The structural gene for group A streptococcal M protein, the fibrillar surface molecule enabling the organism to resist phagocytosis, has been cloned into Escherichia coli. The molecule produced by Escherichia coli is slightly larger than the M protein isolated by solubilization of the streptococcal cell wall, but is similar in size to that secreted by streptococcal protoplast and L forms. Immunologically, the molecule synthesized by Escherichia coli has the same type-specific determinants as the streptococcal M protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, J R -- Fischetti, V A -- AI11822/AI/NIAID NIH HHS/ -- RR05364/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1983 Aug 19;221(4612):758-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6192499" target="_blank"〉PubMed〈/a〉
    Keywords: *Antigens, Bacterial ; *Bacterial Outer Membrane Proteins ; Bacterial Proteins/*genetics/immunology ; *Carrier Proteins ; Cloning, Molecular ; Epitopes ; Escherichia coli/*genetics ; Gene Expression Regulation ; Molecular Weight
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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-12-07
    Description: The genome of the small human virus serologically associated with erythrocyte aplasia and erythema infectiosum (fifth disease) is shown to be a linear, nonpermuted, single-stranded DNA molecule with self-priming hairpin termini, properties which are characteristic of the genomes of the family Parvoviridae. This human parvovirus chromosome was molecularly cloned into bacterial plasmid vectors and the cloned DNA was used to explore its relatedness to other mammalian parvovirus serotypes by DNA:DNA hybridization. It is not related to the human adeno-associated viruses but does show a distant evolutionary relationship to genomes of the helper-independent parvoviruses of rodents. This strongly suggests that it is an autonomous parvovirus, and as such is the first example of a member of this group of common animal pathogens to cause disease in man.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cotmore, S F -- Tattersall, P -- CA29303/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Dec 7;226(4679):1161-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6095448" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular ; DNA, Single-Stranded/analysis ; DNA, Viral/*analysis ; DNA-Directed DNA Polymerase ; Dependovirus/genetics ; Escherichia coli/enzymology ; Nucleic Acid Denaturation ; Nucleic Acid Hybridization ; Parvoviridae/*genetics ; Plasmids ; Templates, Genetic
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  • 19
    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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  • 20
    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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  • 21
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-04-06
    Description: A complementary DNA clone for an alpha-tubulin has been isolated from a mouse testis complementary DNA library. The untranslated 3' end of this complementary DNA is homologous to two RNA transcripts present in postmeiotic cells of the testis but absent from meiotic cells and from several tissues including brain. The temporal expression of this alpha-tubulin complementary DNA provides evidence for the haploid expression of a mammalian structural gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Distel, R J -- Kleene, K C -- Hecht, N B -- GM 29224/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 6;224(4644):68-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6701535" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; Cloning, Molecular ; DNA/genetics ; Drosophila ; Gene Expression Regulation ; Haploidy ; Male ; Mice ; Nucleic Acid Hybridization ; Rats ; Spermatids/metabolism ; Spermatogenesis ; Spermatozoa/physiology ; Testis/*metabolism ; Tubulin/*genetics
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  • 22
    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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  • 23
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    American Association for the Advancement of Science (AAAS)
    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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  • 24
    Publication Date: 1984-12-07
    Description: A cloned fragment of the mycoplasma ribosomal RNA operon was used as a molecular probe for the detection of mycoplasmas in cell cultures. According to the conditions of hybridization, the probe can detect prokaryotes in general or mycoplasmas specifically.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gobel, U B -- Stanbridge, E J -- New York, N.Y. -- Science. 1984 Dec 7;226(4679):1211-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6505688" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; *Culture Techniques ; Genes, Bacterial ; HeLa Cells ; Humans ; Mycoplasma/*genetics/isolation & purification ; Nucleic Acid Hybridization ; RNA, Ribosomal/*genetics
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  • 25
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-10-19
    Description: Fourier transform mass spectrometry will play an important role in the future because of its unique combination of high mass resolution, high upper mass limit, and multichannel advantage. These features have already found application in gas chromatography-mass spectrometry, multiphoton ionization, laser desorption, and secondary ion mass spectrometry. However, its most notable feature is the ability to store ions. This characteristic, when combined with the others, will allow expeditious study of the interaction of gas-phase ions with both photons (photodissociation) and neutral molecules, and the convenient application of this fundamental information for chemical analysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gross, M L -- Rempel, D L -- 2-8423576/PHS HHS/ -- New York, N.Y. -- Science. 1984 Oct 19;226(4672):261-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6385250" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; *Fourier Analysis ; Ions ; Lasers ; *Mass Spectrometry/instrumentation/methods
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  • 26
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-02-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G -- New York, N.Y. -- Science. 1984 Feb 24;223(4638):805.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6695182" target="_blank"〉PubMed〈/a〉
    Keywords: Chorionic Gonadotropin/*genetics ; Cloning, Molecular ; Humans ; Luteinizing Hormone/*genetics
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  • 27
    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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  • 28
    Publication Date: 1984-05-25
    Description: In order to further define the mechanisms by which polypeptide growth factors regulate gene transcription and cellular growth, expression cloning techniques were used to select human epidermal growth factor (EGF) receptor complementary DNA clones. The EGF 3' coding domain shows striking homology to the transforming gene product of avian erythroblastosis virus (v-erbB). Over-expression of EGF receptors in A431 cell lines correlates with increased EGF receptor mRNA levels and amplification (up to 110 times) of the apparently singular EGF receptor gene. There appear to be three cytoplasmic polyadenylated RNA products of EGF receptor gene expression in A431 cells, one of which contains only 5' (EGF binding domain) sequences and is postulated to encode the secreted EGF receptor-related protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, C R -- Chen, W S -- Kruiger, W -- Stolarsky, L S -- Weber, W -- Evans, R M -- Verma, I M -- Gill, G N -- Rosenfeld, M G -- New York, N.Y. -- Science. 1984 May 25;224(4651):843-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6326261" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Line ; Cloning, Molecular ; DNA/*genetics ; Gene Amplification ; Gene Expression Regulation ; Polymorphism, Genetic ; RNA, Messenger/genetics ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/*genetics
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  • 29
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-08-31
    Description: High-resolution carbon-13 nuclear magnetic resonance (NMR) spectra of enzyme-inhibitor and enzyme-substrate complexes provide detailed structural and stereochemical information on the mechanism of enzyme action. The proteases trypsin and papain are shown to form tetrahedrally coordinated complexes and acyl derivatives with a variety of compounds artificially enriched at the site or sites of interest. These results are compared with the structural information derived from x-ray diffraction. Detailed NMR studies have provided a clearer picture of the ionization state of the residues participating in enzyme-catalyzed processes than other more classical techniques. The dynamics of enzymic catalysis can be observed at sub-zero temperatures by a combination of cryoenzymology and carbon-13 NMR spectroscopy. With these powerful techniques, transient, covalently bound intermediates in enzyme-catalyzed reactions can be detected and their structures rigorously assigned.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mackenzie, N E -- Malthouse, J P -- Scott, A I -- New York, N.Y. -- Science. 1984 Aug 31;225(4665):883-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6433481" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Carbon Isotopes ; Carboxypeptidases/metabolism ; Carboxypeptidases A ; Catalysis ; Chemical Phenomena ; Chemistry ; Coenzymes/*metabolism ; Endopeptidases/metabolism ; Enzymes/*metabolism ; Freezing ; Fructose-Bisphosphate Aldolase/metabolism ; Magnetic Resonance Spectroscopy ; Papain/metabolism ; Pepsin A/metabolism ; Peptide Hydrolases/*metabolism ; Protease Inhibitors ; Pterins/metabolism ; Pyridoxal Phosphate/metabolism ; Serine Endopeptidases
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  • 30
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    American Association for the Advancement of Science (AAAS)
    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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  • 31
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-01-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1984 Jan 13;223(4632):152-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6318316" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Hemolytic/blood/*complications ; Anemia, Sickle Cell/blood/*complications ; Child ; Cloning, Molecular ; Erythema/*etiology ; Erythrocytes/microbiology ; Erythropoiesis ; Humans ; Parvoviridae/genetics/immunology/physiology ; Parvoviridae Infections/*complications ; Viral Vaccines ; Virus Replication
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  • 32
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-03-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maugh, T H 2nd -- New York, N.Y. -- Science. 1984 Mar 9;223(4640):1051-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6695193" target="_blank"〉PubMed〈/a〉
    Keywords: *Air Pollutants ; *Atmosphere ; Carbon Tetrachloride ; Chemical Phenomena ; Chemistry ; *Chlorofluorocarbons, Methane ; Free Radicals ; Nitrogen Dioxide ; Nitrous Oxide ; Oxygen ; *Ozone ; Photochemistry ; Risk ; Singlet Oxygen ; Trichloroethanes ; Ultraviolet Rays
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  • 33
    Publication Date: 1984-10-19
    Description: Pyrolysis mass spectrometry in combination with computerized multivariate statistical analysis enables qualitative and quantitative analysis of nonvolatile organic materials containing molecular assemblies of a complexity and size far beyond the capabilities of direct mass spectrometry. The state of the art in pyrolysis mass spectrometry techniques is illustrated through specific applications, including structural determination and quality control of synthetic polymers, quantitative analysis of polymer mixtures, classification and structural characterization of fossil organic matter, and nonsupervised numerical extraction of component patterns from complex biological samples.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meuzelaar, H L -- Windig, W -- Harper, A M -- Huff, S M -- McClennen, W H -- Richards, J M -- New York, N.Y. -- Science. 1984 Oct 19;226(4672):268-74.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6484572" target="_blank"〉PubMed〈/a〉
    Keywords: Biochemical Phenomena ; Biochemistry ; Chemical Phenomena ; Chemistry ; Coal ; Enterobacteriaceae/analysis/isolation & purification ; Hot Temperature ; Mass Spectrometry/*methods ; Polymers
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  • 34
    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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  • 35
    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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  • 36
    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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  • 37
    Publication Date: 1984-08-31
    Description: The splicing of messenger RNA precursors in vitro proceeds through an intermediate that has the 5' end of the intervening sequence joined to a site near the 3' splice site. This lariat structure, which has been characterized for an adenovirus 2 major late transcript, has a branch point, with 2'-5' and 3'-5' phosphodiester bonds emanating from a single adenosine residue. The excised intervening sequence retains the branch site and terminates in a guanosine residue with a 3' hydroxyl group. The phosphate group at the splice junction between the two exons originates from the 3' splice site at the precursor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Padgett, R A -- Konarska, M M -- Grabowski, P J -- Hardy, S F -- Sharp, P A -- P01-CA14051/CA/NCI NIH HHS/ -- P01-CA26717/CA/NCI NIH HHS/ -- R01-GM32467/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Aug 31;225(4665):898-903.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6206566" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviruses, Human/metabolism ; Base Sequence ; Chemical Phenomena ; Chemistry ; Nucleic Acid Conformation ; Nucleic Acid Precursors/analysis/*metabolism ; Oligoribonucleotides/metabolism ; Phosphates/metabolism ; RNA/analysis/*metabolism ; RNA Precursors ; *RNA Splicing ; RNA, Messenger/analysis/*metabolism ; RNA, Viral/analysis/*metabolism
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  • 38
    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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  • 39
    Publication Date: 1984-03-23
    Description: Interferon-beta 1 (IFN-beta 1) complementary DNA was used as a hybridization probe to isolate human genomic DNA clones lambda B3 and lambda B4 from a human genomic DNA library. Blot-hybridization procedures and partial nucleotide sequencing revealed that lambda B3 is related to IFN-beta 1 (and more distantly to IFN-alpha 1). Analyses of DNA obtained from a panel of human-rodent somatic cell hybrids that were probed with DNA derived from lambda B3 showed that lambda B3 is on human chromosome 2. Similar experiments indicated that lambda B4 is not on human chromosomes 2, 5, or 9. The finding that DNA related to the IFN-beta 1 gene (and IFN-alpha 1 gene) is dispersed in the human genome raises new questions about the origins of the interferon genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sagar, A D -- Sehgal, P B -- May, L T -- Inouye, M -- Slate, D L -- Shulman, L -- Ruddle, F H -- AI-16262/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1984 Mar 23;223(4642):1312-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6546621" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human/*analysis ; Chromosomes, Human, 1-3 ; Chromosomes, Human, 4-5 ; Chromosomes, Human, 6-12 and X ; Cloning, Molecular ; Cricetinae ; DNA/*analysis ; *Genes ; Humans ; Hybrid Cells ; Interferon Type I/*genetics ; Mice ; Nucleic Acid Hybridization
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  • 40
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-09-21
    Description: On the basis of an analysis of the human and rat calcitonin genes and of a related gene, alternative RNA processing represents a developmental strategy of the brain to dictate tissue-specific patterns of polypeptide synthesis. This regulation allows the calcitonin gene to generate two messenger RNA's, one encoding the precursor of a novel neuropeptide, referred to as CGRP, which predominates in the brain, and the second encoding the precursor to the hormone calcitonin which predominates in thyroid C cells. The distribution of CGRP in the central and peripheral nervous system and in endocrine and other organ systems suggests potential functions in nociception, ingestive behavior, cardiovascular homeostasis, and mineral metabolism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosenfeld, M G -- Amara, S G -- Evans, R M -- New York, N.Y. -- Science. 1984 Sep 21;225(4668):1315-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089345" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Calcitonin/*genetics ; Calcitonin Gene-Related Peptide ; Cloning, Molecular ; DNA/analysis ; DNA Restriction Enzymes ; *Genes ; Nerve Tissue Proteins/*genetics ; Neurons/*metabolism ; Phenotype ; *RNA Processing, Post-Transcriptional ; RNA, Messenger/*genetics ; Rats
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  • 41
    Publication Date: 1984-12-07
    Description: Mouse and human atrial natriuretic factor (ANF) genes have been cloned and their nucleotide sequences determined. Each ANF gene consists of three coding blocks separated by two intervening sequences. The 5' flanking sequences and those encoding proANF are highly conserved between the two species, while the intervening sequences and 3' untranslated regions are not. The conserved sequences 5' of the gene may play an important role in the regulation of ANF gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seidman, C E -- Bloch, K D -- Klein, K A -- Smith, J A -- Seidman, J G -- AI-18436/AI/NIAID NIH HHS/ -- HL-070208/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1984 Dec 7;226(4679):1206-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6542248" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Atrial Natriuretic Factor ; Base Sequence ; Cloning, Molecular ; Gene Expression Regulation ; Genes ; Heart Atria/metabolism ; Humans ; Mice ; Natriuretic Agents ; Protein Precursors/genetics ; Proteins/*genetics ; Receptors, Glucocorticoid/metabolism
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  • 42
    Publication Date: 1984-09-21
    Description: The Aplysia neuroendocrine system is a particularly advantageous model for cellular and molecular studies because of the relatively small number and large size of its component neurons. Recombinant DNA techniques have been used to isolate the genes that encode the precursors of peptides expressed in identified neurons of known function. The organization and developmental expression of these genes have been examined in detail. Several of the genes encode precursors of multiple biologically active peptides that are expressed in cells which also contain classical transmitters. These studies, as well as immunohistochemical studies and the use of intracellular recording and voltage clamp techniques are the first steps toward revealing the mechanisms by which neuropeptides govern simple behaviors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scheller, R H -- Kaldany, R R -- Kreiner, T -- Mahon, A C -- Nambu, J R -- Schaefer, M -- Taussig, R -- New York, N.Y. -- Science. 1984 Sep 21;225(4668):1300-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6474178" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aplysia/*physiology ; Behavior, Animal ; Cloning, Molecular ; DNA, Recombinant/metabolism ; Female ; Ganglia/physiology ; Genes ; Male ; Nerve Tissue Proteins/genetics/*physiology ; *Nervous System Physiological Phenomena ; Neurons/physiology ; Protein Biosynthesis ; Reproduction
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  • 43
    Publication Date: 1984-12-07
    Description: The human T-cell leukemia (lymphotropic) virus type III (HTLV-III) appears to be central to the causation of the acquired immune deficiency syndrome (AIDS). Two full-length integrated proviral DNA forms of HTLV-III have now been cloned and analyzed, and DNA sequences of the virus in cell lines and fresh tissues from patients with AIDS or AIDS-related complex (ARC) have been characterized. The results revealed that (i) HTLV-III is an exogenous human retrovirus, approximately 10 kilobases in length, that lacks nucleic acid sequences derived from normal human DNA; (ii) HTLV-III, unlike HTLV types I and II, shows substantial diversity in its genomic restriction enzyme cleavage pattern; (iii) HTLV-III persists in substantial amounts in cells as unintegrated linear DNA, an uncommon property that has been linked to the cytopathic effects of certain animal retroviruses; and (iv) HTLV-III viral DNA can be detected in low levels in fresh (primary) lymphoid tissue of a minority of patients with AIDS or ARC but appears not to be present in Kaposi's sarcoma tissue. These findings have important implications concerning the biological properties of HTLV-III and the pathophysiology of AIDS and Kaposi's sarcoma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shaw, G M -- Hahn, B H -- Arya, S K -- Groopman, J E -- Gallo, R C -- Wong-Staal, F -- New York, N.Y. -- Science. 1984 Dec 7;226(4679):1165-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6095449" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; Base Sequence ; Cell Line ; Child ; Cloning, Molecular ; Cytopathogenic Effect, Viral ; DNA Restriction Enzymes/metabolism ; DNA, Viral/*analysis ; Deltaretrovirus/*genetics ; Humans ; Male ; Nucleic Acid Hybridization
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  • 44
    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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  • 45
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-10-14
    Description: A modified cloning method designed to produce differential complementary DNA libraries permits the isolation of sequences that are present in the RNA population of any developmental stage or tissue, but are not present or are much less abundant in another stage or tissue. Selective complementary DNA cloning is especially useful when the differentially expressed RNA's are of low to moderate abundance in the cells in which they occur. A class of cytoplasmic polyadenylated RNA's differentially expressed in gastrula embryos of Xenopus laevis (DG RNA's) has been isolated. These DG RNA's occur very rarely or not at all in unfertilized eggs and blastulae, accumulate as the result of transcription before and during gastrulation, and, with some exceptions, decline in abundance as development proceeds. Many of these RNA molecules appear to be translated at the gastrula stage. Thus, DG RNA's may encode proteins that are important in the process of gastrulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sargent, T D -- Dawid, I B -- New York, N.Y. -- Science. 1983 Oct 14;222(4620):135-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6688681" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/genetics ; Gastrula/*physiology ; Gene Expression Regulation ; Nucleic Acid Hybridization ; Polyribosomes/metabolism ; Protein Biosynthesis ; Transcription, Genetic ; Xenopus laevis/*embryology/genetics
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  • 46
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-05-11
    Description: The mechanism of lipid peroxidation and the manner in which antioxidants function is reviewed. beta-Carotene is a purported anticancer agent, which is believed by some to have antioxidant action of a radical-trapping type. However, definitive experimental support for such action has been lacking. New experiments in vitro show that beta-carotene belongs to a previously unknown class of biological antioxidants. Specifically, it exhibits good radical-trapping antioxidant behavior only at partial pressures of oxygen significantly less than 150 torr, the pressure of oxygen in normal air. Such low oxygen partial pressures are found in most tissues under physiological conditions. At higher oxygen pressures, beta-carotene loses its antioxidant activity and shows an autocatalytic, prooxidant effect, particularly at relatively high concentrations. Similar oxygen-pressure-dependent behavior may be shown by other compounds containing many conjugated double bonds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burton, G W -- Ingold, K U -- New York, N.Y. -- Science. 1984 May 11;224(4649):569-73.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6710156" target="_blank"〉PubMed〈/a〉
    Keywords: Antioxidants/*metabolism ; Carotenoids/*metabolism ; Chemical Phenomena ; Chemistry ; Free Radicals ; Humans ; Linoleic Acids/metabolism ; *Lipid Metabolism ; Oxidation-Reduction ; Oxygen/metabolism ; Partial Pressure ; Peroxides/metabolism ; Tetrahydronaphthalenes/metabolism ; beta Carotene
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  • 47
    Publication Date: 1983-12-16
    Description: Aplysiatoxin and debromoaplysiatoxin, which are isolated from the seaweed, Lyngbya gracilis, differ in their chemical structure only by the presence or absence of a bromine residue in the hydrophilic region. The function and the structure-activity relation of the hydrophilic region are not known. Aplysiatoxin increased malignant transformation, stimulated DNA synthesis, and inhibited the binding of phorbol-12,13-dibutyrate and epidermal growth factor to cell receptors. Debromoaplysiatoxin inhibited the binding of these two substances as strongly as aplysiatoxin but did not increase malignant transformation or stimulate DNA synthesis. These results indicate that a slight change in the chemical structure of the hydrophilic region of aplysiatoxin affects its abilities to increase cell transformation and stimulate DNA synthesis and that the abilities of the tumor promoters to inhibit the binding of phorbol-12,13-dibutyrate and epidermal growth factor are dissociable from their abilities to increase cell transformation and stimulate DNA synthesis under some circumstances.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shimomura, K -- Mullinix, M G -- Kakunaga, T -- Fujiki, H -- Sugimura, T -- New York, N.Y. -- Science. 1983 Dec 16;222(4629):1242-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6316505" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Caenorhabditis elegans Proteins ; Carcinogens/*pharmacology ; Carrier Proteins ; Cell Line ; Cell Transformation, Neoplastic/*drug effects ; Chemical Phenomena ; Chemistry ; DNA/biosynthesis ; Epidermal Growth Factor/metabolism ; Lactones/analysis/*pharmacology ; *Lyngbya Toxins ; Mice ; Phorbol 12,13-Dibutyrate ; Phorbol Esters/metabolism ; *Protein Kinase C ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/metabolism ; *Receptors, Drug ; Structure-Activity Relationship
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  • 48
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    Unknown
    American Association for the Advancement of Science (AAAS)
    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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  • 49
    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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  • 50
    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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  • 51
    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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  • 52
    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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  • 53
    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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  • 54
    Publication Date: 1984-09-07
    Description: Treatment of mice with the carcinogen N-methylnitrosourea results in the development of thymic lymphomas with frequent involvement of the N-ras oncogene. The activated mouse N-ras gene was isolated from one of these lymphomas and, by transformation in concert with restriction digestion, a map of the gene was prepared and its approximate boundaries were determined. By means of somatic cell hybrids the normal N-ras gene was found to be unlinked to other members of the ras gene family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guerrero, I -- Villasante, A -- D'Eustachio, P -- Pellicer, A -- CA-16239/CA/NCI NIH HHS/ -- GM-32105/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Sep 7;225(4666):1041-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089339" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Transformation, Neoplastic ; Chromosome Mapping ; Cloning, Molecular ; Cricetinae ; DNA Restriction Enzymes ; Deoxyribonuclease EcoRI ; Genetic Linkage ; Hybrid Cells ; Lymphoma/chemically induced/*genetics ; Methylnitrosourea ; Mice ; Mice, Inbred Strains ; *Oncogenes ; Thymus Neoplasms/chemically induced/*genetics
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  • 55
    Publication Date: 1984-09-14
    Description: Mouse tumors induced by gamma radiation are a useful model system for oncogenesis. DNA from such tumors contains an activated K-ras oncogene that can transform NIH 3T3 cells. This report describes the cloning of a fragment of the mouse K-ras oncogene containing the first exon from both a transformant in rat-2 cells and the brain of the same mouse that developed the tumor. Hybrid constructs containing one of the two pieces were made and only the plasmid including the first exon from the transformant gave rise to foci in NIH 3T3 cells. There was only a single base difference (G----A) in the exonic sequence, which changed glycine to aspartic acid in the transformant. By use of a synthetic oligonucleotide the presence of the mutation was demonstrated in the original tumor, ruling out modifications during DNA-mediated gene transfer and indicating that the alteration was present in the thymic lymphoma but absent from other nonmalignant tissue. The results are compatible with gamma radiation being a source of point mutations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guerrero, I -- Villasante, A -- Corces, V -- Pellicer, A -- CA-36327/CA/NCI NIH HHS/ -- GM-32036/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Sep 14;225(4667):1159-62.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6474169" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Transformation, Neoplastic ; Cells, Cultured ; Cloning, Molecular ; Gamma Rays ; Lymphoma/*genetics ; Mice ; Mutation ; Neoplasms, Radiation-Induced/*genetics ; Nucleic Acid Hybridization ; *Oncogenes ; Rats
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  • 56
    Publication Date: 1984-09-21
    Description: Recombinant DNA technology has provided a vast new source of DNA markers displaying heritable sequence variation in humans. These markers can be used in family studies to identify the chromosomal location of defective genes causing nervous system disorders. The discovery of a DNA marker linked to Huntington's disease has opened new avenues of research into this disorder and may ultimately permit cloning and characterization of the defective gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gusella, J F -- Tanzi, R E -- Anderson, M A -- Hobbs, W -- Gibbons, K -- Raschtchian, R -- Gilliam, T C -- Wallace, M R -- Wexler, N S -- Conneally, P M -- NS16367/NS/NINDS NIH HHS/ -- NS20012/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1984 Sep 21;225(4668):1320-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089346" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Chromosome Mapping ; Cloning, Molecular ; DNA/*genetics ; DNA Restriction Enzymes ; *DNA, Recombinant ; Female ; *Genes ; *Genetic Linkage ; *Genetic Markers ; Genetic Vectors ; Humans ; Huntington Disease/*genetics ; Male ; Mutation ; Pedigree ; Phenotype ; Polymorphism, Genetic
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  • 57
    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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  • 58
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-03-16
    Description: Yeast phenylalanine transfer RNA was subjected to a 12-picosecond molecular dynamics simulation. The principal features of the x-ray crystallographic analysis are reproduced, and the amplitudes of atomic displacements appear to be determined by the degree of exposure of the atoms. An analysis of the hydrogen bonds shows a correlation between the average length of a bond and the fluctuation in that length and reveals a rocking motion of bases in Watson-Crick guanine X cytosine base pairs. The in-plane motions of the bases are generally of larger amplitude than the out-of-plane motions, and there are correlations in the motions of adjacent bases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harvey, S C -- Prabhakaran, M -- Mao, B -- McCammon, J A -- New York, N.Y. -- Science. 1984 Mar 16;223(4641):1189-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6560785" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; Computers ; Cytosine ; Guanine ; Hydrogen Bonding ; Nucleic Acid Conformation ; *RNA, Fungal ; *RNA, Transfer, Amino Acyl ; Yeasts/analysis
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  • 59
    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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  • 60
    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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  • 61
    Publication Date: 1984-11-16
    Description: Sequence-dependent variations in DNA revealed by x-ray crystallographic studies have suggested that certain DNA-reactive drugs may react preferentially with defined sequences in DNA. Drugs that wind around the helix and reside within one of the grooves of DNA have perhaps the greatest chance of recognizing sequence-dependent features of DNA. The antitumor antibiotic CC-1065 covalently binds through N-3 of adenine and resides within the minor groove of DNA. This drug overlaps with five base pairs for which a high sequence specificity exists.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hurley, L H -- Reynolds, V L -- Swenson, D H -- Petzold, G L -- Scahill, T A -- New York, N.Y. -- Science. 1984 Nov 16;226(4676):843-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6494915" target="_blank"〉PubMed〈/a〉
    Keywords: Antibiotics, Antineoplastic/*metabolism ; *Base Sequence ; Binding Sites ; Chemical Phenomena ; Chemistry ; DNA/*metabolism ; *Indoles ; Leucomycins/*metabolism ; Molecular Conformation ; X-Ray Diffraction
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  • 62
    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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  • 63
    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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  • 64
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    American Association for the Advancement of Science (AAAS)
    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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  • 65
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    American Association for the Advancement of Science (AAAS)
    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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  • 66
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    American Association for the Advancement of Science (AAAS)
    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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  • 67
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    American Association for the Advancement of Science (AAAS)
    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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  • 68
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    American Association for the Advancement of Science (AAAS)
    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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  • 69
    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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  • 70
    Publication Date: 1984-06-15
    Description: A new class of synthetic antifungal agents, the allylamines , has been developed by modification of naftifine , a topical antimycotic. SF 86-327, the most effective of these compounds so far, is highly active in vitro against a wide range of fungi and exceeds clinical standards in the oral and topical treatment of guinea pig dermatophytoses. SF 86-327 is a powerful specific inhibitor of fungal squalene epoxidase, a key enzyme in sterol biosynthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Petranyi, G -- Ryder, N S -- Stutz, A -- New York, N.Y. -- Science. 1984 Jun 15;224(4654):1239-41.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6547247" target="_blank"〉PubMed〈/a〉
    Keywords: Allylamine/analogs & derivatives/*chemical synthesis/pharmacology ; Amines/*chemical synthesis ; Animals ; Antifungal Agents/*chemical synthesis/pharmacology ; Chemical Phenomena ; Chemistry ; Dermatomycoses/drug therapy ; Fungi/*drug effects/enzymology ; Guinea Pigs ; Naphthalenes/chemical synthesis/pharmacology ; Oxygenases/*antagonists & inhibitors ; Squalene Monooxygenase
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  • 71
    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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  • 72
    Publication Date: 1984-11-02
    Description: By recombinant DNA techniques, a disulfide bond was introduced at a specific site in T4 lysozyme, a disulfide-free enzyme. This derivative retained full enzymatic activity and was more stable toward thermal inactivation than the wild-type protein. The derivative, T4 lysozyme (Ile3----Cys), was prepared by substituting a Cys codon for an Ile codon at position 3 in the cloned lysozyme gene by means of oligonucleotide-dependent, site-directed mutagenesis. The new gene was expressed in Escherichia coli under control of the (trp-lac) hybrid tac promoter, and the protein was purified. Mild oxidation generated a disulfide bond between the new Cys3 and Cys97, one of the two unpaired cysteines of the native molecule. Oxidized T4 lysozyme (Ile3----Cys) exhibited specific activity identical to that of the wild-type enzyme when measured at 20 degrees C in a cell-clearing assay. The cross-linked protein was more stable than the wild type during incubation at elevated temperatures as determined by recovered enzymatic activity at 20 degrees C.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perry, L J -- Wetzel, R -- New York, N.Y. -- Science. 1984 Nov 2;226(4674):555-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6387910" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; DNA, Recombinant/metabolism ; Escherichia coli/enzymology ; *Genetic Engineering ; Kinetics ; Muramidase/*genetics/metabolism ; Protein Denaturation
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  • 73
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    American Association for the Advancement of Science (AAAS)
    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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  • 74
    Publication Date: 1984-01-13
    Description: T-cell growth factor (TCGF) or interleukin-2 (IL-2), an immunoregulatory lymphokine, is produced by lectin- or antigen-activated mature T lymphocytes and in a constitutive manner by certain T-cell lymphoma cell lines. By means of a molecular clone of human TCGF and DNA extracted from a panel of somatic cell hybrids (rodent cells X normal human lymphocytes), the TCGF structural gene was identified on human chromosome 4. In situ hybridization of the TCGF clone to human chromosomes resulted in significant labeling of the midportion of the long arm of chromosome 4, indicating that the TCGF gene was located at band q26-28. Genomic DNA from a panel of hybrids prepared with HUT-102 B2 cells was examined with the same molecular clone. In this clone of cells, which produces human T-cell leukemia virus, the TCGF gene was also located on chromosome 4 and was apparently not rearranged. The homologous TCGF locus in the domestic cat was assigned to chromosome B1 by using a somatic cell hybrid panel that segregates cat chromosomes. Linkage studies as well as high-resolution G-trypsin banding indicate that this feline chromosome is partially homologous to human chromosome 4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seigel, L J -- Harper, M E -- Wong-Staal, F -- Gallo, R C -- Nash, W G -- O'Brien, S J -- New York, N.Y. -- Science. 1984 Jan 13;223(4632):175-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6318318" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cats/*genetics ; Chromosome Banding ; Chromosome Mapping ; *Chromosomes ; *Chromosomes, Human, 4-5 ; Cloning, Molecular ; Deltaretrovirus ; *Genes ; Genetic Linkage ; Humans ; Hybrid Cells ; Interleukin-2/*genetics ; Nucleic Acid Hybridization
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  • 75
    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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  • 76
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-06-08
    Description: The effect of a partial pressure of nitrogen of 50 atmospheres (5065 kilopascals ) on the hydrogen evolution reaction of nitrogenase has been investigated. Evolution of hydrogen was not blocked completely by 50 atmospheres of nitrogen in any of four experiments; rather, 27.3 +/- 2.4 percent of the total electron flux through nitrogenase was directed toward production of hydrogen. The ratio of hydrogen evolved to nitrogen fixed was close to 1:1, which implies that hydrogen evolution is obligatory in the fixation of molecular nitrogen by nitrogenase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simpson, F B -- Burris, R H -- AI-00848/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1984 Jun 8;224(4653):1095-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6585956" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; *Hydrogen ; *Nitrogen ; Nitrogen Fixation ; *Nitrogenase ; Partial Pressure
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  • 77
    Publication Date: 1983-09-23
    Description: A peptide that accumulated as the major product during the proteolysis of arginine vasopressin by rat brain synaptic membranes was isolated and its structure was shown to be the hexapeptide pGlu-Asn-Cys(Cys)-Pro-Arg-Gly-NH2. When administered intracerebroventricularly in extremely low doses, this vasopressin fragment and its desglycinamide derivative facilitated memory consolidation in a passive avoidance situation. These vasopressin metabolites, which are devoid of pressor activity, constitute highly potent neuropeptides with selective effects on memory and related processes; they are activated via proteolytic processing of vasopressin by brain peptidases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burbach, J P -- Kovacs, G L -- de Wied, D -- van Nispen, J W -- Greven, H M -- New York, N.Y. -- Science. 1983 Sep 23;221(4617):1310-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6351252" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arginine Vasopressin/*metabolism/physiology ; Avoidance Learning/physiology ; Brain/*metabolism ; Dose-Response Relationship, Drug ; Male ; Memory/*physiology ; Oligopeptides/metabolism ; Peptide Hydrolases/metabolism ; Rats ; Structure-Activity Relationship
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  • 78
    Publication Date: 1983-07-15
    Description: The polymorphism of immune response genes plays a critical role in determining the immune capabilities of a particular individual. The molecular nature of this polymorphism was studied by examining the structure of the coding portions of three alleles of the I-A beta chain gene, an immune response gene whose protein product constitutes a subunit of the I-A molecule. Comparison of the I-A beta chains encoded by these alleles revealed an amino acid sequence divergence of 5 to 8 percent. The differences were found to be a series of short alterations clustered in the amino terminal half of the polypeptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Choi, E -- McIntyre, K -- Germain, R N -- Seidman, J G -- AI18436/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 15;221(4607):283-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6407114" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; *Genes, MHC Class II ; Histocompatibility Antigens Class II/immunology ; Humans ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; *Polymorphism, Genetic
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  • 79
    Publication Date: 1983-09-30
    Description: The near identity of the partial amino acid sequence of human platelet-derived growth factor (PDGF) and that predicted for p28sis, the putative transforming protein of the simian sarcoma virus (SSV), suggests expression of a growth factor activity may be central for transformation by SSV. It is now reported that SSV-transformed cells but not control cells contain a growth factor activity that is identical to PDGF in immunoassay, in mitogenic dose response, and in specific mitogenic activity. The protein immunoprecipitated by antiserum to human PDGF has an apparent molecular weight of 20,000, identical to that of p20sis, the putative intracellular degradation product of p28sis. The results support the concept that expression of a PDGF-like molecule, which appears to be the product of the viral-sis gene, is responsible for the abnormal regulation of growth is SSV-transformed cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deuel, T F -- Huang, J S -- Huang, S S -- Stroobant, P -- Waterfield, M D -- New York, N.Y. -- Science. 1983 Sep 30;221(4618):1348-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6310754" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Cell Transformation, Viral ; Cross Reactions ; DNA Replication/drug effects ; *Genes, Viral ; Growth Substances/*genetics/immunology ; Mice ; Molecular Weight ; Peptides/*genetics/immunology ; Platelet-Derived Growth Factor ; Retroviridae/*genetics ; Sarcoma Virus, Woolly Monkey/*genetics ; Sarcoma, Experimental/*physiopathology
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  • 80
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-10-28
    Description: The recently reported amino acid sequence of rat angiotensinogen was subjected to a computer-assisted search for homology with known sequences stored in a data bank and found to be significantly related to that of plasma alpha 1-antitrypsin, itself a member of a family that includes antithrombin III and ovalbumin. An alignment of the four sequences shows indisputably the common ancestry of all four proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doolittle, R F -- RR 00757/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1983 Oct 28;222(4622):417-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6604942" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Angiotensinogen/*genetics ; Angiotensins/*genetics ; Animals ; Antithrombins/genetics ; *Biological Evolution ; Macromolecular Substances ; Ovalbumin/genetics ; Rats ; alpha 1-Antitrypsin/genetics
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  • 81
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-02-11
    Description: Human insulin produced by recombinant DNA technology is the first commercial health care product derived from this technology. Work on this product was initiated before there were federal guidelines for large-scale recombinant DNA work or commercial development of recombinant DNA products. The steps taken to facilitate acceptance of large-scale work and proof of the identity and safety of such a product are described. While basic studies in recombinant DNA technology will continue to have a profound impact on research in the life sciences, commercial applications may well be controlled by economic conditions and the availability of investment capital.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, I S -- New York, N.Y. -- Science. 1983 Feb 11;219(4585):632-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6337396" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; DNA, Recombinant ; *Drug Industry ; Genetic Engineering ; Humans ; Insulin/*genetics
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  • 82
    Publication Date: 1983-05-20
    Description: Three types of tumors termed plasmacytomas (ABPC's), lymphosarcomas (ABLS's), and plasmacytoid lymphosarcomas (ABPL's) arise in BALB/c mice treated with pristane and Abelson murine leukemia virus (A-MuLV). While most ABPC's and BLS's contain integrated A-MuLV proviral genome and synthesize the v-abl RNA, most ABPL's do not. The ABPL tumors were examined for the expression of other oncogenes that may be associated with their transformed state, in the absence of transforming virus. These tumors expressed abundant c-myb RNA of unusually large size and showed DNA rearrangements of the c-myb locus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mushinski, J F -- Potter, M -- Bauer, S R -- Reddy, E P -- New York, N.Y. -- Science. 1983 May 20;220(4599):795-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6687762" target="_blank"〉PubMed〈/a〉
    Keywords: Abelson murine leukemia virus/genetics ; Animals ; Cell Transformation, Neoplastic/metabolism ; Cloning, Molecular ; DNA, Neoplasm/*genetics ; *Gene Expression Regulation ; Humans ; Lymphoma, Non-Hodgkin/*genetics ; Mice ; Mice, Inbred BALB C ; *Oncogenes ; Plasmacytoma/genetics ; RNA, Neoplasm/genetics
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  • 83
    Publication Date: 1983-08-26
    Description: The complete nucleotide sequence of the diphtheria tox228 gene encoding the nontoxic serologically related protein CRM228 has been determined. A comparison of the predicted amino acid sequence with the available amino acid sequences from the wild-type toxin made it possible to deduce essentially the entire nucleotide sequence of the wild-type tox gene. The signal peptide of pro-diphtheria toxin and the putative tox promoter have been identified, a highly symmetrical nucleotide sequence downstream of the toxin gene has been detected; this region may be the corynebacteriophage beta attachment site (attP). The cloned toxin gene was expressed at a low level in Escherichia coli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaczorek, M -- Delpeyroux, F -- Chenciner, N -- Streeck, R E -- Murphy, J R -- Boquet, P -- Tiollais, P -- New York, N.Y. -- Science. 1983 Aug 26;221(4613):855-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6348945" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular ; Diphtheria Toxin/*genetics ; Escherichia coli/genetics ; Gene Expression Regulation ; Genes ; Genes, Bacterial ; Nucleic Acid Conformation ; Operon
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  • 84
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-09-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1983 Sep 23;221(4617):1278-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6612341" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; Genes ; Receptors, Antigen, T-Cell/*genetics
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  • 85
    Publication Date: 1983-08-12
    Description: Two regions in the immunoglobulin heavy chain locus were tested for their ability to enhance transcription of the SV40 early promoter. A portion of the intervening sequence between the heavy chain joining region (Jh) and the constant region of the mu chain (Cmu) can enhance transcription when it is cloned either 5' or 3' to the SV40 early promoter. The region between C alpha and the alpha switch site, which occurs 5' to the translocated c-myc oncogene in many murine plasmacytomas, does not show transcriptional enhancer activity in this assay.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mercola, M -- Wang, X F -- Olsen, J -- Calame, K -- GM 29361/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Aug 12;221(4611):663-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6306772" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; *Gene Expression Regulation ; Genetic Vectors ; Immunoglobulin Heavy Chains/*genetics ; Mice ; Operon ; Simian virus 40/genetics ; *Transcription, Genetic ; Transfection
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  • 86
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-06-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krenitsky, T A -- Beauchamp, L -- New York, N.Y. -- Science. 1983 Jun 10;220(4602):1106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6857236" target="_blank"〉PubMed〈/a〉
    Keywords: Acyclovir/metabolism ; *Antiviral Agents/metabolism ; Chemical Phenomena ; Chemistry ; Humans ; Vidarabine/metabolism
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  • 87
    Publication Date: 1983-05-06
    Description: Resonance Raman spectra of photolyzed carbonmonoxyhemoglobin obtained with 10-nanosecond pulses are compared with the spectra of photolyzed carbonmonoxyhemoglobin stabilized at 80 K. In comparing the deoxy with the photodissociated species, the changes in the Raman spectra are the same for these two experimental regimes. These results show that at ambient and cryogenic temperatures the heme pocket in liganded hemoglobin is significantly different from that of deoxyhemoglobin. It is concluded that measurements of the properties of intermediate species from photodissociated hemoglobin stabilized at low temperatures can be used to probe the short-lived metastable forms of hemoglobin present after photodissociation under biologically relevant solution conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ondrias, M R -- Friedman, J M -- Rousseau, D L -- New York, N.Y. -- Science. 1983 May 6;220(4597):615-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6836305" target="_blank"〉PubMed〈/a〉
    Keywords: Carboxyhemoglobin ; Chemical Phenomena ; Chemistry ; Freezing ; *Hemoglobins ; Humans ; Ligands ; Spectrum Analysis, Raman ; Temperature
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  • 88
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-07-08
    Description: The nucleotide sequence of the oncogene of the Rasheed strain of rat sarcoma virus was determined. The oncogene (Ra-v-ras) encodes a 29,000-dalton (p29) transforming protein. This protein is distinct from the immunologically related 21,000-dalton protein (p21) of the Harvey murine sarcoma virus in its amino terminus and in having additional mutations in its carboxyl terminus. Although the functional significance of these changes is unknown, they appear to occur only in rat sarcoma virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rasheed, S -- Norman, G L -- Heidecker, G -- CA 27246/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 8;221(4606):155-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344220" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Mice ; Neoplasm Proteins/genetics ; *Oncogenes ; Proto-Oncogene Proteins p21(ras) ; Rats ; Retroviridae/*genetics
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  • 89
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-06-03
    Description: The nucleotide sequence of the T24 human bladder carcinoma oncogene was determined, and the coding and noncoding sequences of the genome were identified. The amino acid sequence of p21, the translational product of the T24 oncogene, was predicted from the nucleotide sequence of the oncogene. Comparison of this sequence with that of the normal cellular homolog showed that a single point mutation in the coding sequences of the T24 oncogene resulted in the acquisition of transforming properties. Other differences between the T24 oncogene and its normal cellular homolog were found in the 5' noncoding and 3' noncoding sequences, but these differences appear to be due to polymorphism and do not play a significant role in the transformation process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reddy, E P -- New York, N.Y. -- Science. 1983 Jun 3;220(4601):1061-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6844927" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carcinoma/*genetics ; Cell Transformation, Neoplastic/metabolism ; Humans ; Mice ; Neoplasm Proteins/genetics ; *Oncogenes ; Oncogenic Viruses/genetics ; Rats ; Urinary Bladder Neoplasms/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 90
    Publication Date: 1983-04-15
    Description: Alkylating agents that display strong selectivity for opiate receptor types delta or mu were prepared by appropriate modification of the structures of the strong analgesics fentanyl, etonitazene, and endoethenotetrahydrooripavine. The availability of these substances should facilitate studies of the structural basis of receptor specificity and of the physiologic roles of these receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rice, K C -- Jacobson, A E -- Burke, T R Jr -- Bajwa, B S -- Streaty, R A -- Klee, W A -- New York, N.Y. -- Science. 1983 Apr 15;220(4594):314-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6132444" target="_blank"〉PubMed〈/a〉
    Keywords: Alkylation ; Animals ; Benzimidazoles/analogs & derivatives/metabolism ; Brain/physiology ; Cells, Cultured ; Chemical Phenomena ; Chemistry ; Enkephalin, Methionine/analogs & derivatives/metabolism ; Fentanyl/analogs & derivatives/metabolism ; *Isothiocyanates ; Ligands ; Rats ; Receptors, Opioid/*metabolism/physiology ; Thebaine/analogs & derivatives/pharmacology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 91
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-05-27
    Description: The adult mouse brain contains complex populations of polyadenylated [poly(A)+] and nonpolyadenylated [poly(A)-] messenger RNA's (mRNA's). These mRNA's are separate sequence populations, similar in complexity, and in combination are equivalent to approximately 150,000 different mRNA sequences, of average length. Essentially all of the "adult" poly(A)+ mRNA's are present in the brain at birth. In contrast, most of the poly(A)- mRNA's are absent. Brain poly(A)- mRNA's begin to appear soon after birth, but the full adult complement is not reached until young adulthood. This suggests that these poly(A)- mRNA's specify proteins required for the biological capabilities of the brain that emerge during the course of postnatal development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chaudhari, N -- Hahn, W E -- NS10813/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1983 May 27;220(4600):924-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6189184" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*growth & development ; Cell Differentiation ; Cloning, Molecular ; DNA/physiology ; Fetus/physiology ; *Gene Expression Regulation ; Guinea Pigs ; Kidney/metabolism ; Liver/metabolism ; Mice ; Organ Specificity ; Poly A/physiology ; RNA/physiology ; RNA, Messenger/physiology ; RNA, Ribosomal/physiology ; Rats
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 92
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-02-11
    Description: Microbial secondary metabolites are now being used for applications other than as antibacterial, antifungal, and antitumor agents. These applications include use against parasites (coccidia, helminths) and insects as well as for animal and plant growth stimulation, immunosuppression, uterocontraction, and other pharmacological activities. Further applications are possible in various areas of pharmacology and agriculture, a development catalyzed by the use of simple enzyme assays for screening prior to testing in intact animals or in the field.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Demain, A L -- New York, N.Y. -- Science. 1983 Feb 11;219(4585):709-14.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6337397" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; Enzyme Inhibitors/*genetics ; *Genetic Engineering ; Humans ; Insecticides ; Parasitic Diseases/*drug therapy
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 93
    Publication Date: 1983-05-13
    Description: A recombinant bacterial plasmid, pMS1, was constructed that contains 318 nucleotides complementary to a portion of pro-opiolipomelanocortin (proOLMC) messenger RNA from an ectopic adrenocorticotropin-producing tumor. The cloned complementary DNA insert, which contains the sequence that codes for all of the beta-melanocyte-stimulating hormone and beta-endorphin portions of proOLMC, as well as the 3' nontranslated section, is identical to the genomic sequence. Hybridization of tumor proOLMC complementary DNA to RNA subjected to electrophoresis and transferred to a nitrocellulose filter revealed two proOLMC messenger RNA species in the tumor polyadenylated RNA, but only one in pituitary polyadenylated RNA. At least one of the tumor proOLMC messenger RNA's is similar, if not identical, to human pituitary proOLMC messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeBold, C R -- Schworer, M E -- Connor, T B -- Bird, R E -- Orth, D N -- 2-R01-GM25526/GM/NIGMS NIH HHS/ -- 5-R01-CA11685/CA/NCI NIH HHS/ -- 5-R25-CA19429/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 May 13;220(4598):721-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6301015" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Carcinoid Tumor/physiopathology ; Cloning, Molecular ; DNA, Neoplasm/genetics ; DNA, Recombinant/*metabolism ; Endorphins/*genetics ; Hormones, Ectopic/*genetics ; Humans ; Male ; Melanocyte-Stimulating Hormones/*genetics ; Middle Aged ; Pancreatic Neoplasms/physiopathology ; Pituitary Hormones, Anterior/*genetics ; Pro-Opiomelanocortin ; Protein Precursors/*genetics ; RNA, Messenger/genetics ; beta-Endorphin
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 94
    Publication Date: 1983-07-15
    Description: The transforming protein of a primate sarcoma virus and a platelet-derived growth factor are derived from the same or closely related cellular genes. This conclusion is based on the demonstration of extensive sequence similarity between the transforming protein derived from the simian sarcoma virus onc gene, v-sis, and a human platelet-derived growth factor. The mechanism by which v-sis transforms cells could involve the constitutive expression of a protein with functions similar or identical to those of a factor active transiently during normal cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doolittle, R F -- Hunkapiller, M W -- Hood, L E -- Devare, S G -- Robbins, K C -- Aaronson, S A -- Antoniades, H N -- CA30101/CA/NCI NIH HHS/ -- RR00757/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 15;221(4607):275-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6304883" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cebidae ; Cell Transformation, Neoplastic/metabolism ; Genes ; Growth Substances/*genetics/physiology ; Humans ; *Oncogenes ; Peptides/*genetics/physiology ; Platelet-Derived Growth Factor ; Retroviridae/*genetics ; Sarcoma Virus, Woolly Monkey/*genetics
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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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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-03-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1983 Mar 4;219(4588):1055-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6823566" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; Genes ; Receptors, Cholinergic/*genetics ; Torpedo
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  • 96
    Publication Date: 1983-12-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1983 Dec 2;222(4627):1001-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6417788" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Female ; *Gene Expression Regulation ; *Genetic Engineering ; Immunoglobulin Light Chains/*genetics ; Immunoglobulin kappa-Chains/biosynthesis/*genetics ; Liver/metabolism ; Male ; Mice ; Organ Specificity ; Spleen/metabolism ; Transferrin/biosynthesis/*genetics
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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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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-05-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1983 May 27;220(4600):937-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6844920" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; *Genes ; Humans ; *Major Histocompatibility Complex ; Mice ; Transplantation Immunology
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  • 98
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-05-06
    Description: DNA-mediated gene transfer (transfection) is used to introduce specific genes into vertebrate cells. Events soon after transfection were quantitatively analyzed by determining the infectivity of the DNA from an avian retrovirus and of mixtures of subgenomic fragments of this DNA. The limiting step of transfection with two DNA molecules is the uptake by a single cell of both DNA's in a biologically active state. Transfected cells mediate ligation and recombination of physically unlinked DNA's at nearly 100 percent efficiency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, C K -- Temin, H M -- CA-07175/CA/NCI NIH HHS/ -- CA-09135/CA/NCI NIH HHS/ -- CA-22443/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1983 May 6;220(4597):606-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6301012" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chick Embryo ; Cloning, Molecular ; DNA Restriction Enzymes ; DNA, Recombinant/*metabolism ; DNA, Viral/genetics ; Fibroblasts/metabolism ; Helper Viruses/genetics ; Reticuloendotheliosis virus/genetics ; Retroviridae/genetics
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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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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-04-20
    Description: Human epidermoid carcinoma A431 cells in culture produce a soluble 105-kilodalton protein which, by the criteria of epidermal growth factor (EGF) binding, recognition by monoclonal and polyclonal antibodies to the EGF receptor, amino-terminal sequence analysis and carbohydrate content, is related to the cell surface domain of the EGF receptor. The high rate of production and the finding that with biosynthetic labeling the specific activity of this 105-kilodalton protein exceeds that of the intact receptor indicate that it is not derived from membrane-bound mature receptor but is separately produced by the cell. These cells thus separately synthesize an EGF receptor that is inserted into the membrane and an EGF receptor-related protein that is secreted.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weber, W -- Gill, G N -- Spiess, J -- AM13149/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 20;224(4646):294-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6324343" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal/immunology ; Carbohydrates/analysis ; Carcinoma, Squamous Cell/*metabolism ; Cell Line ; Epidermal Growth Factor/metabolism ; Glycoproteins/analysis/*biosynthesis ; Humans ; Kinetics ; Molecular Weight ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/analysis/immunology/metabolism
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  • 100
    Publication Date: 1984-06-29
    Description: The gene encoding human interleukin-2 (IL-2) has been cloned from human spleen cells, peripheral blood lymphocytes, and the Jurkat cell line. Nucleotide sequence analysis of the gene revealed that the encoded IL-2 protein has three cysteines located at amino acid residues 58, 105, and 125 of the mature protein. Site-specific mutagenesis procedures were used to modify the IL-2 gene by changing each of the cysteine codons individually to serine codons. Substitution of serine for cysteine residues at either position 58 or 105 of the IL-2 protein substantially reduced biological activity, indicating that the cysteines at these positions are necessary for maintenance of the biologically active conformation and may therefore be linked by a disulfide bridge. The modified IL-2 protein containing a substitution at position 125 retained full biological activity, suggesting that the cysteine at this position is not involved in a disulfide bond and that a free sulfhydryl group at that position is not necessary for receptor binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, A -- Lu, S D -- Mark, D F -- New York, N.Y. -- Science. 1984 Jun 29;224(4656):1431-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6427925" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; Cysteine/metabolism ; DNA, Recombinant/metabolism ; Escherichia coli/genetics ; Genes ; Humans ; Interleukin-2/*genetics ; *Mutation ; Receptors, Immunologic/metabolism ; Receptors, Interleukin-2 ; Serine/metabolism ; Structure-Activity Relationship
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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