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  • Articles  (90)
  • Latest Papers from Table of Contents or Articles in Press  (90)
  • Mutation
  • Protein Conformation
  • kinetics
  • 1980-1984  (90)
  • Computer Science  (90)
  • Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
  • Energy, Environment Protection, Nuclear Power Engineering
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  • Articles  (90)
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  • 1
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    Bioactive conformation of luteinizing hormone-releasing hormone: evidence from a conformationally constrained analog (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-11-07
    Description: An analog of luteinizing hormone-releasing hormone containing a gamma-lactam as a conformational constraint has been prepared with the use of a novel cyclization of a methionine sulfonium salt. The analog is more active as a luteinizing hormone-releasing hormone agonist that the parent hormone, and provides evidence for a bioactive conformation containing a beta-turn.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freidinger, R M -- Veber, D F -- Perlow, D S -- Brooks, J R -- Saperstein, R -- New York, N.Y. -- Science. 1980 Nov 7;210(4470):656-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001627" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Assay ; Cells, Cultured ; Female ; *Gonadotropin-Releasing Hormone/analogs & derivatives ; Hydrogen Bonding ; Lactams ; Protein Conformation ; Rats ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Collagen: molecular diversity in the body's protein scaffold (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-03-21
    Description: Intensive research in the last decade has revealed a wealth of detail on the mechanism of biosynthesis, molecular structure, and covalent cross-linking of collagen. Tissues of higher animals express a family of at least five genetically distinct types of collagen molecule, each apparently tailored for different construction work outside the cell. Within each genetic type of collagen, further chemical heterogeneity is also evident; the variations in hydroxylation, glycosylation, and cross-linking are dependent, for example, on tissue type, age, and hormonal status. The functional significance of collagen's molecular diversity and its control by different cells and tissues are not yet well understood but abnormalities of collagen in many human diseases keep this protein a focal molecule of medical research.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eyre, D R -- New York, N.Y. -- Science. 1980 Mar 21;207(4437):1315-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7355290" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcification, Physiologic ; Cartilage/ultrastructure ; *Collagen/genetics/metabolism ; Epithelium/ultrastructure ; Extracellular Space/ultrastructure ; Humans ; Hydrogen Bonding ; Polymorphism, Genetic ; Protein Biosynthesis ; Protein Conformation ; Vertebrates
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Modeling coordination sites in metallobiomolecules (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-07-11
    Description: Synthetic metal complexes can closely approach the properties of metal ions in proteins and yield useful information concerning biological structure and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ibers, J A -- Holm, R H -- New York, N.Y. -- Science. 1980 Jul 11;209(4453):223-35.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7384796" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Electron Transport ; Humans ; Iron-Sulfur Proteins ; *Metalloproteins ; *Metals ; Molecular Conformation ; Myoglobin ; Oxygen/blood ; Oxyhemoglobins ; Protein Binding ; Protein Conformation
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Altering genotype and phenotype by DNA-mediated gene transfer (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: Transformation, or DNA-mediated gene transfer, permits the introduction of new genetic information into a cell and frequently results in a change in phenotype. The transforming DNA is ultimately integrated into a recipient cell chromosome. No unique chromosomal locations are apparent, different lines contain the transforming DNA on different chromosomes. Expression of transformed genes frequently results in the synthesis of new polypeptide products which restore appropriate mutant cells to the wild-type phenotype. Thus transformation provides an in vivo assay for the functional role of DNA sequence organization about specific genes. Transforming genes coding for selectable functions, such as adenine phosphoribosyltransferase or thymidine kinase, have now been isolated by utilizing transformation in concert with molecular cloning. Finally, transformation may provide a general approach to the analysis of complex heritable phenotypes by permitting the distinction between phenotypic changes without concomitant changes in DNA and functional genetic rearrangements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pellicer, A -- Robins, D -- Wold, B -- Sweet, R -- Jackson, J -- Lowy, I -- Roberts, J M -- Sim, G K -- Silverstein, S -- Axel, R -- CA 16346/CA/NCI NIH HHS/ -- CA 17477/CA/NCI NIH HHS/ -- CA 23767/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1414-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7414320" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine Phosphoribosyltransferase/*genetics ; Cloning, Molecular/methods ; DNA/*genetics ; *DNA, Recombinant ; Genes ; Genotype ; Mutation ; Pentosyltransferases/*genetics ; Phenotype ; Recombination, Genetic ; Selection, Genetic ; Thymidine Kinase/*genetics ; *Transformation, Genetic
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Hormone binding alters the conformation of the insulin receptor (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-12-05
    Description: Fat cells or fat cell membranes were briefly subjected to mild proteolysis under conditions where insulin receptors were either free or bound to (125)I-labeled insulin. When receptors were then affinity-labeled to visualize the effects of this treatment, it was observed that receptors that had been occupied by ligand during proteolysis exhibited greater rates of degradation than unoccupied receptors. These results demonstrate that insulin-receptor interaction induces a change in receptor structure that may be related to signal transmission.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pilch, P F -- Czech, M P -- AM 06069/AM/NIADDK NIH HHS/ -- AM 17893/AM/NIADDK NIH HHS/ -- HD 11343/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1980 Dec 5;210(4474):1152-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7003712" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Animals ; Cell Membrane/metabolism ; Insulin/*metabolism ; Male ; Peptide Fragments/analysis ; Protein Binding ; Protein Conformation ; Rats ; Receptor, Insulin/*metabolism ; Trypsin/metabolism
    Print ISSN: 0036-8075
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  • 6
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    Directed deletion of a yeast transfer RNA intervening sequence (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: Many eukaryotic genes contain intevening sequences, segments of DNA that interrupt the continuity of the gene. They are removed from RNA transcripts of the gene by a process known as splicing. The intervening sequence in a yeast tyrosine transfer RNA (tRNA Tyr) suppressor gene was deleted in order to test its role in the expression of the gene. The altered gene and its parent were introduced into yeast by transformation. Both genes exhibited suppressor function, showing that the intervening sequence is not absolutely essential for the expression of this gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wallace, R B -- Johnson, P F -- Tanaka, S -- Schold, M -- Itakura, K -- Abelson, J -- CA10984/CA/NCI NIH HHS/ -- GM 26391/GM/NIGMS NIH HHS/ -- GM 35658/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1396-400.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6997991" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Deletion ; DNA, Recombinant ; Genes ; Mutation ; Nucleic Acid Precursors/genetics ; Plasmids ; RNA, Fungal/*genetics ; RNA, Transfer/*genetics ; Saccharomyces cerevisiae/genetics ; Suppression, Genetic ; Tyrosine
    Print ISSN: 0036-8075
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  • 7
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    Assembly of proteins into membranes (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-11-21
    Description: Two pathways for protein assembly into biological membranes have been proposed. The "signal hypothesis" emphasizes the role of specific membrane proteins in binding the growing polypeptide and conducting it into the bilayer during its synthesis. The "membrane-triggered folding" hypothesis emphasizes self-assembly and the role of changing protein conformation during transfer from an aqueous compartment into a membrane. These ideas provide a framework for reviewing recent data on the biogenesis of membrane proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickner, W -- New York, N.Y. -- Science. 1980 Nov 21;210(4472):861-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001628" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Transport ; Membrane Proteins/*metabolism ; Membranes/enzymology/*metabolism ; Protein Conformation ; Protein Precursors/metabolism ; Proteins/secretion ; Solubility ; Viral Proteins/metabolism
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  • 8
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    Giant polytene chromosomes from the ovaries of a Drosophila mutant (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-04-24
    Description: The chromosomes of the ovarian nurse cells of Drosophila melanogaster fall apart during their cycles of endoreduplication. However, chromosomal synapsis occurs in the pseudonurse cells produced in certain mutant females. The resulting polytene chromosomes undergo developmental changes that are strikingly different from those recorded for the giant chromosomes of the larval salivary gland cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, R C -- Riley, S F -- Cassidy, J D -- White, P E -- Paik, Y K -- New York, N.Y. -- Science. 1981 Apr 24;212(4493):441-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6782674" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromatin/ultrastructure ; Chromosome Inversion ; Chromosomes/*ultrastructure ; DNA Replication ; Drosophila melanogaster/*genetics ; Female ; Heterochromatin/ultrastructure ; Mutation ; Ovarian Neoplasms/genetics/veterinary ; Ovary/ultrastructure
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  • 9
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    Rational approaches to chemotherapy: antisickling agents (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-08-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klotz, I M -- Haney, D N -- King, L C -- New York, N.Y. -- Science. 1981 Aug 14;213(4509):724-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7256275" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Sickle Cell/*drug therapy ; Aspirin/analogs & derivatives/therapeutic use ; Chemical Phenomena ; Chemistry ; *Hemoglobin, Sickle ; Humans ; Protein Binding/drug effects ; Protein Conformation ; Salicylates/*therapeutic use ; Solubility ; Structure-Activity Relationship
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Changes in DNA during meiosis in a repair-deficient mutant (rad 52) of yeast (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-05-01
    Description: The kinetic patterns of DNA synthesis in wild-type (RAD+) and rad 52 mutants of yeast, which exhibit high levels of synchrony during meiosis, are comparable. However, RAD 52 mutants accumulate single-strand breaks in parental DNA during the DNA synthesis period. Thus, the product of the RAD 52 gene has a role in meiotic DNA metabolism, as well as in the repair of DNA damage during mitotic growth. The observed breaks may be unresolved recombination intermediates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Resnick, M A -- Kasimos, J N -- Game, J C -- Braun, R J -- Roth, R M -- 5 R01 GM17317-11/GM/NIGMS NIH HHS/ -- S07-RR07027/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1981 May 1;212(4494):543-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7010606" target="_blank"〉PubMed〈/a〉
    Keywords: *DNA Repair ; DNA, Fungal/genetics ; DNA, Single-Stranded/genetics ; Genes ; *Meiosis ; Molecular Weight ; Mutation ; *Recombination, Genetic ; Saccharomyces cerevisiae/*genetics
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  • 11
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    Diameter of the cell-to-cell junctional membrane channels as probed with neutral molecules (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-07-31
    Description: The cell-to-cell channels in the junctions of an insect salivary gland and of insect and mammalian cells in culture were probed with fluorescent molecules-neutral linear oligosaccharides, neutral branched glycopeptides, and charged linear peptides. From the molecular dimensions of the largest permeants and smallest impermeants the permeation-limiting channel diameter was obtained: 16 to 20 angstroms for the mammalian cells and 20 to 30 angstroms for the insect cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwarzmann, G -- Wiegandt, H -- Rose, B -- Zimmerman, A -- Ben-Haim, D -- Loewenstein, W R -- CA 14464/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1981 Jul 31;213(4507):551-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7244653" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Chironomidae ; Fluorescent Dyes ; Glycopeptides/*metabolism ; Intercellular Junctions/*ultrastructure ; Mice ; Mice, Inbred BALB C ; Models, Molecular ; Oligosaccharides/*metabolism ; Protein Conformation ; Salivary Glands/*ultrastructure ; Species Specificity
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  • 12
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    Neuronal cell Thy-1 glycoprotein: homology with immunoglobulin (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-05-14
    Description: The amino acid sequences of mouse brain Thy-1 glycoproteins are shown to be homologous to those of variable-region immunoglobulin domains. There is also good homology with constant domains and beta 2-microglobulin; overall the results suggest that Thy-1 may be like the primordial immunoglobulin domain. Preliminary evidence for an invertebrate Thy-1 homolog supports this possibility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, A F -- Gagnon, J -- New York, N.Y. -- Science. 1982 May 14;216(4547):696-703.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6177036" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Surface/*immunology ; Antigens, Thy-1 ; Biological Evolution ; Epitopes ; Glycoproteins/*immunology ; Immunoglobulin Constant Regions/immunology ; Immunoglobulin Variable Region/immunology ; Immunoglobulins/*immunology ; Isoantibodies/biosynthesis ; Protein Conformation
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  • 13
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    Splice junctions: association with variation in protein structure (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 14
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    Requirement for signal peptide cleavage of Escherichia coli prolipoprotein (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 15
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    Monoclonal antibodies reveal the structural basis of antibody diversity (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-11-18
    Description: Hybridoma technology has made it possible to introduce into continuous culture normal antibody-forming cells and to obtain large amounts of the immunoglobulin produced by each of these cells. Examination of the structure of a number of monoclonal antibodies that react with a single antigen has provided new information on the structural basis of the specificity and affinity of antibodies. Comparisons of families of monoclonal antibodies derived from a single germ line gene revealed the importance of somatic mutation in generating antibody diversity. Monoclonal antibodies that react with variable regions of other monoclonals allow the further dissection and modulation of the immune response. Finally, the continued somatic instability of immunoglobulin genes in cultured antibody-forming cells makes it possible to determine the rate of somatic mutation and to generate mutant monoclonal antibodies that may be more effective serological reagents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teillaud, J L -- Desaymard, C -- Giusti, A M -- Haseltine, B -- Pollock, R R -- Yelton, D E -- Zack, D J -- Scharff, M D -- 5T32GM7288/GM/NIGMS NIH HHS/ -- AI05231/AI/NIAID NIH HHS/ -- AI10702/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):721-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356353" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/genetics/*immunology ; *Antibody Diversity ; Antibody Specificity ; Genes ; Hybridomas/immunology ; Immunoglobulin Idiotypes/immunology ; Immunoglobulin Variable Region/genetics ; Mice ; Mutation ; Protein Conformation ; Structure-Activity Relationship
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  • 16
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    Protein engineering (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-02-11
    Description: The prospects for protein engineering, including the roles of x-ray crystallography, chemical synthesis of DNA, and computer modelling of protein structure and folding, are discussed. It is now possible to attempt to modify many different properties of proteins by combining information on crystal structure and protein chemistry with artificial gene synthesis. Such techniques offer the potential for altering protein structure and function in ways not possible by any other method.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ulmer, K M -- New York, N.Y. -- Science. 1983 Feb 11;219(4585):666-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6572017" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Crystallography ; Genes ; *Genetic Engineering ; Models, Molecular ; Molecular Biology/trends ; Protein Conformation ; Proteins/*genetics ; X-Ray Diffraction
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  • 17
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    Bloom's syndrome: evidence for an increased mutation frequency in vivo (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-08-26
    Description: The incidence of lymphocytes resistant to the purine analog 6-thioguanine was studied in seven patients with Bloom's syndrome. The mean frequency was 17.3 X 10(-4). The mean incidence in age- and sex-matched controls was 2.1 X 10(-4), so approximately eight times the normal number of 6-thioguanine-resistant lymphocytes were detected in Bloom's syndrome blood. The basis for this increase is unknown, but the inherent genomic instability demonstrated in the form of chromosomal aberrations is one possible explanation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vijayalaxmi -- Evans, H J -- Ray, J H -- German, J -- HD 0413/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1983 Aug 26;221(4613):851-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6879180" target="_blank"〉PubMed〈/a〉
    Keywords: Bloom Syndrome/*genetics ; DNA Replication/drug effects ; Drug Resistance ; Humans ; Lymphocytes/physiology ; Mutation ; Thioguanine/pharmacology
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    Multiple point mutations affecting the simian virus 40 enhancer (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-02-11
    Description: Enhancers, or activators, dramatically increase the transcriptional activity of certain eukaryotic genes. A series of multiple point mutations affecting the simian virus 40 (SV40) enhancer-activator region were generated in order to define the nucleotide sequence required for this function. Three independent assays provided information leading to the identification of nucleotides essential for enhancer function. One class leads to a decrease in gene expression, while the second completely abolishes functional activity. One critical replacement appears to be the first G (guanine) in a sequence TGGAAAG (T, thymine, A, adenine) located in the 5' region of the 72 base-pair repeat of SV40. Comparison of this sequence with nucleotide sequences in other known enhancers leads to the identification of potential related core elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weiher, H -- Konig, M -- Gruss, P -- New York, N.Y. -- Science. 1983 Feb 11;219(4585):626-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6297005" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA Replication ; *Gene Expression Regulation ; Mutation ; *Operon ; Plasmids ; Repetitive Sequences, Nucleic Acid ; Simian virus 40/*genetics ; Virus Replication
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    Waterlogged molecules (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-12-09
    Description: Measurements of vapor pressures over their aqueous solutions indicate that organic compounds show profound differences in hydrophilic character. These differences are of such magnitude as to suggest an important role for changing solvation in determining free energy changes associated with metabolic transformations in water, and in governing structural equilibria of proteins and other large molecules in water. When two or more functional groups are present within the same solute molecule, their combined effects on its free energy of solvation are commonly additive. Striking departures from additivity, observed in certain cases, indicate the existence of special interactions between different parts of a solute molecule and the water that surrounds it. Similar considerations presumably apply to activated intermediates in the interconversion of biological materials.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolfenden, R -- GM 18325/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Dec 9;222(4628):1087-93.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6359416" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Organic ; Enzymes/physiology ; Kinetics ; Metabolism ; Nucleic Acid Conformation ; Nucleic Acids/physiology ; Organic Chemistry Phenomena ; Protein Conformation ; Solvents ; Water/*physiology
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  • 20
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    Regulation of a hybrid gene by glucose and temperature in hamster fibroblasts (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-10-12
    Description: A novel eukaryotic hybrid gene has been constructed from the 5' sequence of a rat gene and the bacterial neomycin-resistance gene. After transfection into hamster fibroblasts, the neo transcripts can be induced to high levels by the absence of glucose. Furthermore, this hybrid gene can be regulated by temperature when it is introduced into a temperature-sensitive mutant cell line.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Attenello, J W -- Lee, A S -- CA-27607/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Oct 12;226(4671):187-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6484570" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cricetinae ; DNA, Recombinant ; Drug Resistance, Microbial ; Fibroblasts ; *Gene Expression Regulation ; Genes, Bacterial ; *Genes, Regulator ; Glucose/*pharmacology ; *HSP70 Heat-Shock Proteins ; Membrane Proteins/biosynthesis/*genetics ; Mutation ; Neomycin/pharmacology ; Rats ; Temperature ; Transcription, Genetic ; Transfection
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  • 21
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    Studying promoters and terminators by gene fusion (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-11-18
    Description: Prokaryotic gene control signals can be isolated, compared, and characterized by precise fusion in vitro to the Escherichia coli galactokinase gene (galK), which provides both a simple assay and genetic selection. This recombinant galK fusion vector system was applied to the study of promoters and terminators recognized by the Escherichia coli RNA polymerase. Three promoters created by mutation from DNA sequences having no promoter function were characterized. Mutations that inactivate promoter function were selected, structurally defined, and functionally analyzed. Similarly, transcription termination was examined, and mutations affecting terminator function were isolated and characterized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosenberg, M -- Chepelinsky, A B -- McKenney, K -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):734-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356355" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA, Bacterial/*genetics ; DNA, Recombinant ; DNA-Directed RNA Polymerases/genetics ; Escherichia coli/genetics ; Galactokinase/genetics ; Gene Expression Regulation ; Mutation ; Nucleic Acid Conformation ; *Operon ; *Transcription, Genetic
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  • 22
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    Recombination during gene transfer into mouse cells can restore the function of deleted genes (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-01-14
    Description: Two plasmids containing nonoverlapping deletions of the herpes simplex virus thymidine kinase gene were introduced into thymidine kinase-deficient mouse L cells by DNA-mediated gene transfer. Thymidine kinase-producing transformants were generated by a mixture of the two plasmids at a frequency significantly greater than that generated by either plasmid alone. Southern blot analyses demonstrated that functional thymidine kinase genes were generated by homologous recombination between the two deletion mutants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Small, J -- Scangos, G -- New York, N.Y. -- Science. 1983 Jan 14;219(4581):174-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6294829" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cells, Cultured ; Chromosome Deletion ; *Genetic Engineering ; Mice ; Mutation ; *Plasmids ; *Recombination, Genetic ; Simplexvirus ; Thymidine Kinase/*genetics
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    Genes of the major histocompatibility complex in mouse and man (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-11-18
    Description: The genes of the major histocompatibility complex code for cell-surface molecules that play an important role in the generation of the immune response. These genes and molecules have been studied intensively over the last five decades by geneticists, biochemists, and immunologists, but only recently has the isolation of the genes by molecular biologists facilitated their precise characterization. Many surprising findings have been made concerning their structure, multiplicity, organization, function, and evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steinmetz, M -- Hood, L -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):727-33.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356354" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Chromosome Mapping ; Genes ; H-2 Antigens/*genetics ; HLA Antigens/*genetics ; Histocompatibility Antigens/genetics ; Humans ; *Major Histocompatibility Complex ; Mice ; Polymorphism, Genetic ; Protein Conformation
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  • 24
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    Cyclic AMP receptor protein: role in transcription activation (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-05-25
    Description: The structure of this pleiotropic activator of gene transcription in bacteria and its interaction sites at promoter DNA's as well as the role of this protein in the RNA polymerase-promoter interactions are reviewed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Crombrugghe, B -- Busby, S -- Buc, H -- New York, N.Y. -- Science. 1984 May 25;224(4651):831-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6372090" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Crystallography ; DNA, Bacterial/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Galactose/genetics ; *Gene Expression Regulation ; Lac Operon ; Operon ; Protein Conformation ; Receptors, Cyclic AMP/*physiology ; *Transcription, Genetic
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  • 25
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    Amphiphilic secondary structure: design of peptide hormones (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-20
    Description: Peptide synthesis can be used for elucidating the roles of secondary structures in the specificity of hormones, antigens, and toxins. Intermediate sized peptides with these activities assume amphiphilic secondary structures in the presence of membranes. When models are designed to optimize the amphiphilicity of the secondary structure, stronger interactions can be observed with the synthetic peptides than with the naturally occurring analogs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, E T -- Kezdy, F J -- HL-18577/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1984 Jan 20;223(4633):249-55.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6322295" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apolipoprotein A-I ; Apolipoproteins ; Binding Sites ; Calcitonin ; Chemical Phenomena ; Chemistry ; Corticotropin-Releasing Hormone ; Endorphins ; Glucagon ; Growth Hormone-Releasing Hormone ; *Hormones/pharmacology ; Lipoproteins, HDL ; Melitten ; Models, Structural ; *Peptides/chemical synthesis/metabolism/pharmacology ; Protein Conformation ; Structure-Activity Relationship ; beta-Endorphin
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  • 26
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    Reversal of knob formation on Plasmodium falciparum-infected erythrocytes (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-10-05
    Description: The human malarial parasite Plasmodium falciparum can produce surface protrusions (knobs) on infected erythrocytes; however, long-term culturing of the parasite results in the appearance of knobless cells. In this study it was found that a knob-producing clone lost the ability to produce knobs in vitro. Furthermore, a clone not producing knobs derived from the knob-producing clone regained the capacity to produce knobby cells in vitro. Certain parasite proteins were associated with the knobby phenotype but not with the knobless type. These results indicate that the parasites change in vitro in a spontaneous and reversible manner independent of immunological selection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gritzmacher, C A -- Reese, R T -- AI 18695/AI/NIAID NIH HHS/ -- DRR 00833/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1984 Oct 5;226(4670):65-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6382613" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Clone Cells ; Erythrocytes/*parasitology/ultrastructure ; Humans ; Mutation ; Phenotype ; Plasmodium falciparum/analysis/genetics/growth & development/*physiology ; Proteins/analysis
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  • 27
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    Nucleosome reconstruction via phosphorus mapping (1984)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1984-11-23
    Description: Electron spectroscopic imaging was combined with reconstruction algorithms to derive the three-dimensional structure of the nucleosome core particle to a resolution of 1.5 nanometers. Images of phosphorus distributions within individual nucleosomes were interpreted as projections of a supercoil of DNA. These were used to orient the corresponding individual nucleosome images, making it possible to reconstruct the entire nucleosome in three dimensions. The structure is consistent with known biochemical and biophysical data and explains site-specific nuclease sensitivity, although differing in part with other nucleosome models.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harauz, G -- Ottensmeyer, F P -- New York, N.Y. -- Science. 1984 Nov 23;226(4677):936-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6505674" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/analysis ; Deoxyribonucleoproteins/analysis ; Histones/analysis ; Microscopy, Electron/methods ; Models, Structural ; Nucleic Acid Conformation ; Nucleosomes/*ultrastructure ; Protein Conformation ; Spectrum Analysis/methods
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  • 28
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    Time-varying magnetic fields: effect on DNA synthesis (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-02-24
    Description: Human fibroblasts have exhibited enhanced DNA synthesis when exposed to sinusoidally varying magnetic fields for a wide range of frequencies (15 hertz to 4 kilohertz) and amplitudes (2.3 X 10(-6) to 5.6 X 10(-4) tesla). This effect, which is at maximum during the middle of the S phase of the cell cycle, appears to be independent of the time derivative of the magnetic field, suggesting an underlying mechanism other than Faraday's law. The threshold is estimated to be between 0.5 X 10(-5) and 2.5 X 10(-5) tesla per second. These results bring into question the allegedly specific magnetic wave shapes now used in therapeutic devices for bone nonunion. The range of magnetic field amplitudes tested encompass the geomagnetic field, suggesting the possibility of mutagenic interactions directly arising from short-term changes in the earth's field.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liboff, A R -- Williams, T Jr -- Strong, D M -- Wistar, R Jr -- New York, N.Y. -- Science. 1984 Feb 24;223(4638):818-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6695183" target="_blank"〉PubMed〈/a〉
    Keywords: Cells, Cultured ; DNA/*biosynthesis ; Humans ; *Magnetics ; Mutation ; Periodicity
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    Inhibition of collagen fibril formation in vitro and subsequent cross-linking by glucose (1984)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1984-09-28
    Description: Glucose inhibits collagen fibril formation in vitro. A linear dose response was observed, with half-maximum inhibition of fibril formation occurring at 50 mM glucose. Nonfibrillar collagen cannot be cross-linked by lysyl oxidase, an enzyme that catalyzes the initial cross-linking reaction. The degree of decreased fibril formation correlated with the loss of ability of the collagen to serve as a substrate for lysyl oxidase. Collagen that is not cross-linked is unstable and more susceptible to collagenolytic attack. Interference with collagen cross-linking and more rapid degradation may explain the decreased amounts of interstitial collagen and the poor healing of wounds associated with diabetes mellitus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lien, Y H -- Stern, R -- Fu, J C -- Siegel, R C -- New York, N.Y. -- Science. 1984 Sep 28;225(4669):1489-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6147899" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Collagen/*metabolism ; Diabetes Mellitus/metabolism ; Diabetes Mellitus, Experimental/metabolism ; Elastin/metabolism ; Glucose/*pharmacology ; Humans ; In Vitro Techniques ; Macromolecular Substances ; Protein Conformation ; Protein-Lysine 6-Oxidase/metabolism ; Rats
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    Transfection of the DNA polymerase-alpha gene (1984)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1984-11-16
    Description: DNA polymerase-alpha is the major replicative DNA polymerase in animal cells. The gene coding for a mutant DNA polymerase-alpha was transferred from one cell to another by transfection of DNA from mutant cells. The DNA was isolated from a mutant hamster cell line resistant to aphidicolin, a specific inhibitor of DNA polymerase-alpha, and transferred into an aphidicolin-sensitive cell line. The resulting transfectants exhibited increased survival in the presence of aphidicolin and contained an aphidicolin-resistant DNA polymerase-alpha.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, P K -- Loeb, L A -- CA07418/CA/NCI NIH HHS/ -- CA24845/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 16;226(4676):833-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6436977" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aphidicolin ; Cell Line ; Clone Cells ; Cricetinae ; Cricetulus/genetics ; DNA Polymerase II/*genetics ; Diterpenes/pharmacology ; Escherichia coli/genetics ; Humans ; Mice ; Mutation ; Salmon/genetics ; *Transfection
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    Message transmission: receptor controlled adenylate cyclase system (1984)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1984-09-21
    Description: The adenylate cyclase system is composed of an activating hormone or neurotransmitter (H), its receptor (R), the guanosine triphosphate (GTP) binding protein (Gs), and the catalytic unit (C). The activation of the receptor R involves a transient change in conformation, from a loose binding of the neurotransmitter H to an extremely tight interaction, termed locking. The system is regulated in the activation steps and also by three deactivation processes. A guanosine triphosphatase activity is built into the Gs protein so that the active GsGTP has only a limited lifetime during which it is able to activate C. In addition, the continued occupation of R by H causes desensitization of R. Finally, there are inhibitory receptors, such as alpha-adrenergic and opiate receptors, which inhibit the adenylate cyclase by way of a specific GTP binding protein (Gi). Yet to be determined are the conformational transformations of pure R on binding of an agonist or a partial agonist; the genes that code for the many different receptors that activate the adenylate cyclase, and the possibility that the G components interact with systems in the cell other than the adenylate cyclase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schramm, M -- Selinger, Z -- AM10451/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Sep 21;225(4668):1350-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6147897" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/*metabolism ; Animals ; Cyclic AMP/*physiology ; Enzyme Activation ; GTP Phosphohydrolases/metabolism ; GTP-Binding Proteins ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Guanylyl Imidodiphosphate/metabolism ; Membrane Lipids/physiology ; Neurotransmitter Agents/physiology ; Protein Conformation ; Receptors, Cell Surface/metabolism ; *Synaptic Transmission
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  • 32
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    Biogenesis of ornithine transcarbamylase in spfash mutant mice: two cytoplasmic precursors, one mitochondrial enzyme (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-10-28
    Description: Extracts of liver from hemizygous affected mice with the X-linked spfash mutation have 5 to 10 percent of normal ornithine transcarbamylase (OTC) activity, yet the homogeneous enzyme isolated from these extracts is identical to that in controls. The OTC messenger RNA from mutant livers programs the synthesis of two distinct OTC precursor polypeptides--one normal in size, the other distinctly elongated. Both precursors are imported and proteolytically processed by mitochondria, but only the normal one is assembled into active trimer. This novel phenotype may result from a mutation in the structural gene for OTC leading, primarily, to aberrant splicing of OTC messenger RNA and, secondarily, to formation of a structurally altered precursor whose posttranslational pathway is ultimately futile because its mature mitochondrial form is not capable of assembly and functional expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosenberg, L E -- Kalousek, F -- Orsulak, M D -- AM 09527/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1983 Oct 28;222(4622):426-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6623083" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Genes ; Liver/enzymology ; Macromolecular Substances ; Mice ; Mice, Mutant Strains/genetics/physiology ; Mitochondria, Liver/enzymology ; Mutation ; Ornithine Carbamoyltransferase/*genetics ; Protein Precursors/genetics ; Protein Processing, Post-Translational ; RNA, Messenger/genetics
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    Fourier transform infrared difference spectra of intermediates in rhodopsin bleaching (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-03-18
    Description: The membrane protein rhodopsin is the primary light receptor in vision. Fourier transform infrared difference spectroscopy is sensitive to conformational changes in both the protein and the retinylidene chromophore of rhodopsin. By blocking rhodopsin bleaching at specific intermediates, it is possible to elucidate some of the primary molecular events of vision.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rothschild, K J -- Cantore, W A -- Marrero, H -- New York, N.Y. -- Science. 1983 Mar 18;219(4590):1333-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6828860" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Fourier Analysis ; Protein Conformation ; *Retinal Pigments ; *Rhodopsin ; Spectrophotometry, Infrared ; *Vision, Ocular
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    Acetylcholine receptor: an allosteric protein (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-09-21
    Description: The nicotine receptor for the neurotransmitter acetylcholine is an allosteric protein composed of four different subunits assembled in a transmembrane pentamer alpha 2 beta gamma delta. The protein carries two acetylcholine sites at the level of the alpha subunits and contains the ion channel. The complete sequence of the four subunits is known. The membrane-bound protein undergoes conformational transitions that regulate the opening of the ion channel and are affected by various categories of pharmacologically active ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Changeux, J P -- Devillers-Thiery, A -- Chemouilli, P -- New York, N.Y. -- Science. 1984 Sep 21;225(4668):1335-45.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6382611" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Sequence ; Animals ; Binding Sites ; Cell Membrane/ultrastructure ; Cloning, Molecular ; DNA/analysis ; Electric Organ/metabolism ; Electrophorus ; Macromolecular Substances ; Protein Conformation ; *Receptors, Nicotinic/genetics/metabolism ; Torpedo
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    Homologous recombination catalyzed by mammalian cell extracts in vitro (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-12-07
    Description: An assay was developed to detect recombination events taking place in an in vitro reaction. Extracts of cultured mouse preB lymphocytes were found to catalyze homologous recombination between substrate DNA molecules but not site-specific recombination between cloned mouse immunoglobulin D and J genes. Addition of deoxyribonucleoside triphosphates increased the frequency of homologous recombination. This recombination activity was not observed in two differentiated lymphocyte cell lines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Darby, V -- Blattner, F -- AI19325/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1984 Dec 7;226(4679):1213-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6334360" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes ; Cells, Cultured ; Crossing Over, Genetic ; DNA, Viral ; Immunoglobulin Variable Region/genetics ; Mice ; Mutation ; Nucleoproteins/genetics ; *Recombination, Genetic
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    A trans-acting product needed for P factor transposition in Drosophila (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-12-07
    Description: A transposable genetic element of the P family in Drosophila melanogaster was found to be unstable in the presence of other P elements but stable in their absence. A sensitive assay for P transpositional activity is provided by the snw allele, a defective P insert in the singed bristle locus which becomes hypermutable only in the presence of complete elements. This measure of activity was highly correlated with a type of female sterility normally associated with P activity. There was no cross-reactivity with transposase from another hybrid dysgenesis-causing element (the I factor).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Engels, W R -- GM30948/GM/NIGMS NIH HHS/ -- PCM8104332/PC/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Dec 7;226(4679):1194-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6095450" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cross Reactions ; *DNA Transposable Elements ; Drosophila melanogaster/*genetics ; Female ; Gonadal Dysgenesis/genetics ; Infertility, Female/genetics ; Male ; Mutation
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    Activation of a c-K-ras oncogene by somatic mutation in mouse lymphomas induced by gamma radiation (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    DNA markers for nervous system diseases (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Requirement for a signal sequence in biological expression of the v-sis oncogene (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-12-07
    Description: The protein encoded by the simian sarcoma virus oncogene (v-sis) contains a signal sequence, derived from the envelope gene of the parental retrovirus, which is required for transformation. Removal of the proposed signal sequence was correlated with loss of biological activity. This activity was restored to inactive deletion mutants by fusion with the coding region for a heterologous signal sequence. Biological activity of v-sis was also abolished by either a small deletion within the coding region of the signal sequence or by a point mutation introduced by site-directed mutagenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hannink, M -- Donoghue, D J -- CA34456/CA/NCI NIH HHS/ -- GM07313/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Dec 7;226(4679):1197-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6095451" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Transformation, Viral ; *Gene Expression Regulation ; Mutation ; *Oncogenes ; *Protein Biosynthesis ; Retroviridae/*genetics ; Sarcoma Virus, Woolly Monkey/*genetics ; Viral Proteins/biosynthesis
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    Homologies between signal transducing G proteins and ras gene products (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-16
    Description: The guanosine triphosphate-binding proteins (G proteins) found in a variety of tissues transduce signals generated by ligand binding to cell surface receptors into changes in intracellular metabolism. Amino acid sequences of peptides prepared by partial proteolysis of the alpha subunit of a bovine brain G protein and the alpha subunit of rod outer-segment transducin were determined. The two proteins show regions of sequence identity as well as regions of diversity. A portion of the amino-terminal peptide sequence of each protein is highly homologous with the corresponding region in the ras protein (a protooncogene product). These similarities suggest that G proteins and ras proteins may have analogous functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hurley, J B -- Simon, M I -- Teplow, D B -- Robishaw, J D -- Gilman, A G -- GM 09731-02/GM/NIGMS NIH HHS/ -- NS 18153/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 16;226(4676):860-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6436980" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cattle ; GTP-Binding Proteins/*metabolism ; Neoplasm Proteins/*metabolism ; Oncogenes ; Protein Conformation ; Proto-Oncogene Proteins p21(ras) ; Transduction, Genetic
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    Pigment gene scrutinized (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-10-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1984 Oct 5;226(4670):35.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6236555" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cattle ; Eye Proteins/genetics ; *Genes ; Humans ; Photoreceptor Cells/analysis ; Protein Conformation ; Retinal Pigments/*genetics ; Rhodopsin/analysis/*genetics ; Rod Opsins
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    The continuing tale of a small worm (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-07-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1984 Jul 13;225(4658):153-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6729473" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis/*anatomy & histology/genetics/growth & development ; Mutation ; Nervous System/anatomy & histology/growth & development
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    Caenorhabditis elegans: getting to know you (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-07-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1984 Jul 6;225(4657):40-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6729468" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis/genetics/*growth & development ; Cell Differentiation ; Cell Survival ; Female ; Male ; Mutation
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    Need a catalyst? Design an enzyme (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maugh, T H 2nd -- New York, N.Y. -- Science. 1984 Jan 20;223(4633):269-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6608147" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Biochemistry/*methods ; Catalysis ; *Cloning, Molecular ; Enzymes/genetics/*metabolism ; Mutation ; Structure-Activity Relationship ; Substrate Specificity ; Tetrahydrofolate Dehydrogenase/metabolism ; Tyrosine-tRNA Ligase/metabolism ; beta-Lactamases/metabolism
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    The significance of responses of the genome to challenge (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McClintock, B -- New York, N.Y. -- Science. 1984 Nov 16;226(4676):792-801.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15739260" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/metabolism ; Chromosome Breakage ; Chromosomes, Plant/physiology/radiation effects ; *DNA Transposable Elements ; Gene Expression Regulation ; *Gene Expression Regulation, Plant ; Genetics/history ; *Genome, Plant ; History, 20th Century ; Hybridization, Genetic ; Meiosis ; Mitosis ; Mutation ; Plant Viruses/physiology ; Telophase ; Zea mays/*genetics/physiology/virology
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    Retinoblastoma: clues to human oncogenesis (1984)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1984-03-09
    Description: The retinoblastoma gene can be considered a model for a class of recessive human cancer genes that have a "suppressor" or "regulatory" function. The loss or inactivation of both alleles of this gene appears to be a primary mechanism in the development of retinoblastoma. Such a mechanism is in direct contrast to that of putative human oncogenes which are thought to induce tumorigenesis following activation or alteration. The high incidence of second primary tumors among patients who inherit one inactive retinoblastoma allele also suggests that this cancer gene plays a key role in the etiology of several other primary malignancies. Finally, the observation that extra nonrandom copies of specific chromosomal regions occur in some of these tumors provides circumstantial evidence that an "expressor" gene (possibly an oncogene) may be involved in retinoblastoma development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murphree, A L -- Benedict, W F -- EY-02715/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1984 Mar 9;223(4640):1028-33.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6320372" target="_blank"〉PubMed〈/a〉
    Keywords: Adenocarcinoma/genetics ; Alleles ; Child ; Chromosome Deletion ; Chromosome Mapping ; Chromosomes, Human, 13-15 ; Chromosomes, Human, 6-12 and X ; Eye Neoplasms/*genetics ; Genes, Recessive ; Genotype ; Humans ; Kidney Neoplasms/genetics ; Mutation ; Neuroblastoma/genetics ; *Oncogenes ; Polymorphism, Genetic ; Retinoblastoma/*genetics ; *Suppression, Genetic ; Translocation, Genetic ; Wilms Tumor/genetics
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    Evolution of proteolytic enzymes (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-04-27
    Description: Proteolytic enzymes have many physiological functions, ranging from generalized protein digestion to more specific regulated processes such as the activation of zymogens, blood coagulation and the lysis of fibrin clots, the release of hormones and pharmacologically active peptides from precursor proteins, and the transport of secretory proteins across membranes. They are present in all forms of living organisms. Comparisons of amino acid sequences, three-dimensional structures, and enzymatic reaction mechanisms of proteases indicate that there are distinct families of these proteins. Changes in molecular structure and function have accompanied the evolution of proteolytic enzymes and their inhibitors, each having relatively simple roles in primitive organisms and more diverse and more complex functions in higher organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neurath, H -- GM-15731/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 27;224(4647):350-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6369538" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; *Biological Evolution ; Blood Coagulation ; Chemistry, Physical ; Enzyme Activation ; Enzyme Precursors/metabolism ; Genes ; Humans ; Mutation ; *Peptide Hydrolases/analysis/genetics/metabolism ; Peptides/metabolism ; Physicochemical Phenomena ; Protease Inhibitors/analysis/metabolism ; Protein Conformation ; Protein Sorting Signals ; Substrate Specificity
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    Sindbis virus mutants selected for rapid growth in cell culture display attenuated virulence in animals (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-07-27
    Description: Mutants of Sindbis virus were selected for rapid growth in baby hamster kidney (BHK) cell cultures and screened for attenuation of virulence in suckling mice. Comparisons among independently isolated virulent and attenuated strains, as well as a classical reversion analysis, showed that accelerated penetration of BHK cells was correlated with attenuation in vivo. Both phenotypic changes resulted from a reorganization of virion structure as detected by monoclonal antibodies. These results suggest that mutants selected for rapid growth in cell culture may be useful as attenuated vaccines and for studies of the molecular basis of virus pathogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olmsted, R A -- Baric, R S -- Sawyer, B A -- Johnston, R E -- AI19433/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1984 Jul 27;225(4660):424-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6204381" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology ; Antibodies, Viral/immunology ; Cells, Cultured ; Cricetinae ; Kidney/cytology ; Mice ; Mutation ; Neutralization Tests ; RNA/biosynthesis ; Sindbis Virus/genetics/growth & development/immunology/*pathogenicity ; Togaviridae Infections/microbiology
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    Spectrographic representation of globular protein breathing motions (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-13
    Description: Two useful ways of describing the frequency composition of the breathing motions of globular proteins are the spectrogram and three-dimensional power spectrum, representations similar to those frequently used in speech analysis. In this report "low-frequency" vibrations of globular proteins, corresponding to the collective oscillations of atoms from many different residues, are considered. Radii of gyration fluctuations provide a sensitive way to characterize such concerted motions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pickover, C A -- New York, N.Y. -- Science. 1984 Jan 13;223(4632):181-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6691144" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Physicochemical Phenomena ; Protein Conformation ; Spectrum Analysis ; *Trypsin Inhibitors
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    DNA-binding proteins (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-09-09
    Description: The structures of three proteins that regulate gene expression have been determined recently and suggest how these proteins may bind to their specific recognition sites on the DNA. One protein (Cro) is a repressor of gene expression, the second (CAP) usually stimulates gene expression, and the third (lambda repressor) can act as either a repressor or an activator. The three proteins contain a substructure consisting of two consecutive alpha helices that is virtually identical in each case. Structural and amino acid sequence comparisons suggest that this bihelical fold occurs in a number of proteins that regulate gene expression, and is an intrinsic part of the DNA-protein recognition event. The modes of repression and activation by Cro and lambda repressor are understood reasonably well, but the mode of action of CAP is still unclear.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takeda, Y -- Ohlendorf, D H -- Anderson, W F -- Matthews, B W -- GM20066/GM/NIGMS NIH HHS/ -- GM28138/GM/NIGMS NIH HHS/ -- GM30894/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Sep 9;221(4615):1020-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6308768" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chemical Phenomena ; Chemistry ; *DNA Helicases ; DNA-Binding Proteins ; Escherichia coli/genetics ; Gene Expression Regulation ; Models, Chemical ; Protein Conformation
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    A revolution in biology (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abelson, J -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1319-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6251541" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular/methods ; DNA Transposable Elements ; *DNA, Recombinant ; Drug Industry ; Eukaryotic Cells/physiology ; Forecasting ; Genes ; Immunoglobulins/genetics ; Molecular Biology/*trends ; Mutation ; Transformation, Genetic
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    Hybrid dysgenesis in Drosophila melanogaster (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-02-08
    Description: Several dysgenic traits may occur within the Drosophila melanogaster species as a result of crosses between different strains. Crossing two mutually interacting categories, named inducer and reactive, may lead, among other abnormalities, to a specific kind of female sterility that has proved useful for investigating the genetic factors involved in the interaction. The reactive state appears to result from a cytoplasmic state ultimately controlled by a chromosomal polygenic system. The inducer character is determined by a chromosomal factor that exhibits all characteristics of a transposable element. Overall, the data contribute to clarification of mutator activities in D. melanogaster and open new opportunities to investigate unusual genetic mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bregliano, J C -- Picard, G -- Bucheton, A -- Pelisson, A -- Lavige, J M -- L'Heritier, P -- New York, N.Y. -- Science. 1980 Feb 8;207(4431):606-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6766221" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Animals ; Animals, Laboratory/genetics ; Animals, Wild/genetics ; Cytoplasm/physiology ; Drosophila melanogaster/*genetics ; Ecology ; Female ; Genes, Regulator ; Hot Temperature ; Hybridization, Genetic ; Infertility, Female/genetics ; Mutation ; Oocytes/physiology
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    Circadian rhythms in Neurospora crassa: oligomycin-resistant mutations affect periodicity (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-02-22
    Description: Nuclear mutations conferring resistance to oligomycin, a mitochondrial inhibitor, shorten the period of the circadian conidiation rhythm of Neurospora crassa from the normal 21.5 hours to 18 to 19 hours and slow the linear growth rate by 30 percent. These olir mutations map very close to frq, a locus at which mutations affecting periodicity have been previously obtained. The possibilities are discussed that mitochondria are involved in circadian rhythm generation and that certain period-length mutations affect mitochondrial functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diekmann, C -- Brody, S -- New York, N.Y. -- Science. 1980 Feb 22;207(4433):896-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6444467" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Transport ; Circadian Rhythm/*drug effects ; Drug Resistance, Microbial ; Genetic Linkage ; Mitochondria/drug effects/physiology ; Mutation ; Neurospora/*physiology ; Neurospora crassa/genetics/*physiology ; Oligomycins/*pharmacology ; Protons
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    Chemical DNA synthesis and recombinant DNA studies (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-09-19
    Description: Chemically synthesized DNA has been used in many recombinant DNA studies. These uses have included the total synthesis and cloning of functional genes, the cloning and expression of natural genes, and editing of changing genes by directed mutation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Itakura, K -- Riggs, A D -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1401-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6106285" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular/*methods ; DNA/*chemical synthesis ; DNA Restriction Enzymes ; *DNA, Recombinant ; *Genes ; *Genes, Synthetic ; Insulin/genetics ; Mutation ; Nucleic Acid Hybridization ; Oligodeoxyribonucleotides/chemical synthesis ; Somatostatin/genetics
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    Folic acid: crystal structure and implications for enzyme binding (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-10-17
    Description: The crystal and molecular structure of folic acid dihydrate has been determined by x-ray diffraction. Folic acid is in an extended conformation with the pteridine ring in the keto form. The C(4) oxygen and N(10) atoms are on the same side of the molecule, hydrogen-bonded to the same water. This conformation has the pteridine rotated approximately 180 degrees away from the orientation of the pteridine ring of methotrexate bound to dihydrofolate reductase. The folic acid pteridine and phenyl rings interact in a stacking manner which is suggestive of the type of associations these groups could form in a complex of folate, dihydrofolate reductase, and reduced nicotinamide adenine dinucleotide phosphate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mastropaolo, D -- Camerman, A -- Camerman, N -- CA-15879/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1980 Oct 17;210(4467):334-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7423195" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallography ; *Folic Acid ; Molecular Conformation ; Protein Conformation ; Tetrahydrofolate Dehydrogenase ; X-Ray Diffraction
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    Cyclophosphamide-induced spermatogenic effects detected in the F1 generation by behavioral testing (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-01-02
    Description: Fischer 344 male rats were treated with cyclophosphamide (10 milligrams per kilogram of body weight) for 5 weeks and subsequently mated to females previously treated with saline or cyclophosphamide. The F1 progeny of the cyclophosphamide-treated males exhibited behavior deficits when compared to controls. These data could indicate a chemically induced genetic effect manifested by behavioral alterations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adams, P M -- Fabricant, J D -- Legator, M S -- New York, N.Y. -- Science. 1981 Jan 2;211(4477):80-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7444453" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avoidance Learning ; Behavior, Animal/*physiology ; Cyclophosphamide/*pharmacology ; Female ; Locomotion ; Male ; Motor Activity ; Mutation ; Rats ; Spermatogenesis/*drug effects
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    Cross-linked fibrinogen dimers demonstrate a feature of the molecular packing in fibrin fibers (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-01-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fowler, W E -- Erickson, H P -- Hantgan, R R -- McDonagh, J -- Hermans, J -- HL 20319/HL/NHLBI NIH HHS/ -- HL 23454/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1981 Jan 16;211(4479):287-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6108612" target="_blank"〉PubMed〈/a〉
    Keywords: Factor XIII/metabolism ; *Fibrin/metabolism ; *Fibrinogen/metabolism ; Humans ; Macromolecular Substances ; Microscopy, Electron ; Protein Conformation ; gamma-Glutamyltransferase/metabolism
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    A new understanding of sickle cell emerges (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-01-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maugh, T H 2nd -- New York, N.Y. -- Science. 1981 Jan 16;211(4479):265-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7444466" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Sickle Cell/*blood ; Erythrocytes, Abnormal/pathology ; *Hemoglobin, Sickle ; Humans ; Protein Binding ; Protein Conformation ; Temperature
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    Coupling of histone and DNA synthesis in the somatic cell cycle (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-01-01
    Description: The coupling of histone and DNA synthesis was examined in the temperature-sensitive hamster fibroblast cell line K12. By monitoring total cellular histone synthesis at various times after quiescent cells were stimulated to proliferate at permissive and nonpermissive temperatures, a direct correlation was found between the rates of DNA and histone synthesis. Furthermore, when DNA synthesis was blocked by the K12 mutation, histone synthesis was reduced to the basal rate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Delegeane, A M -- Lee, A S -- 2S07RR05356/RR/NCRR NIH HHS/ -- CA27607/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1982 Jan 1;215(4528):79-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7053561" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Cycle ; Cell Line ; Cricetinae ; DNA/biosynthesis ; *DNA Replication ; Histones/*biosynthesis ; Mutation
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    Nucleotide sequence of the p21 transforming protein of Harvey murine sarcoma virus (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-09-03
    Description: Harvey murine sarcoma virus is a retrovirus which transforms cells by means of a single virally encoded protein called p21 has. We have determined the nucleotide sequence of 1.0 kilobase in the 5' half of the viral genome which encompasses the has coding sequences and its associated regulatory signals. The nucleotide sequence has identified the amino acid sequence of two additional overlapping polypeptides which share their reading frames and the carboxyl termini with p21 but which contain additional NH2-terminal amino acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dhar, R -- Ellis, R W -- Shih, T Y -- Oroszlan, S -- Shapiro, B -- Maizel, J -- Lowy, D -- Scolnick, E -- New York, N.Y. -- Science. 1982 Sep 3;217(4563):934-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6287572" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Transformation, Viral ; Cells, Cultured ; Defective Viruses/*genetics ; Genes, Viral ; Oncogene Protein p21(ras) ; Peptide Fragments ; Protein Biosynthesis ; Protein Conformation ; RNA, Viral/genetics ; Sarcoma Viruses, Murine/*genetics ; Viral Proteins/analysis/*genetics
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    Biological diversity in metastatic neoplasms: origins and implications (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-09-10
    Description: Whether neoplasms are unicellular or multicellular in their origin, the process of tumor evolution and progression can rapidly generate biological diversity. Metastases result from the survival and proliferation of specialized subpopulations of cells within the parent tumor. Metastases may have a clonal origin and different metastases may develop from different progenitor cells. However, as with the primary tumor, the origin of metastases is unimportant since the process of tumor evolution and progression can generate biological diversity within and among different metastatic foci.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fidler, I J -- Hart, I R -- N01-CO-75380/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1982 Sep 10;217(4564):998-1003.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7112116" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Transformation, Neoplastic/pathology ; Clone Cells ; Humans ; Immunity ; Melanoma/genetics/pathology ; Mice ; Mice, Inbred Strains ; Mutation ; Neoplasm Metastasis/*pathology ; Neoplasms, Experimental/pathology ; Phenotype ; Skin Neoplasms/genetics/pathology
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    Crystallization of the tetramer of histones H3 and H4 (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-05-28
    Description: Crystals of the histone tetramer (H3-H4)2 from calf thymus have been grown. The crystals yield x-ray diffraction patterns with Bragg spacings as small as 3.5 angstroms. Crystals grown from two types of preparations have the symmetry of the space group P61 (or P65). The best crystals were grown from histones that had the amino terminal arms removed by mild trypsinization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lattman, E -- Burlingame, R -- Hatch, C -- Moudrianakis, E N -- New York, N.Y. -- Science. 1982 May 28;216(4549):1016-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7079748" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallization ; *Histones ; Nucleosomes/ultrastructure ; Protein Binding ; Protein Conformation
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    Rapid evolution of RNA genomes (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-03-26
    Description: RNA viruses show high mutation frequencies partly because of a lack of the proofreading enzymes that assure fidelity of DNA replication. This high mutation frequency is coupled with high rates of replication reflected in rates of RNA genome evolution which can be more than a millionfold greater than the rates of the DNA chromosome evolution of their hosts. There are some disease implications for the DNA-based biosphere of this rapidly evolving RNA biosphere.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holland, J -- Spindler, K -- Horodyski, F -- Grabau, E -- Nichol, S -- VandePol, S -- AI 14627/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1982 Mar 26;215(4540):1577-85.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7041255" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Defective Viruses/genetics ; Humans ; Mutation ; RNA Viruses/*genetics ; RNA, Viral/*genetics ; Recombination, Genetic ; Virus Diseases/genetics ; Virus Replication
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    Light-induced modification of Drosophila retinal polypeptides in vivo (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-08-27
    Description: The effect of light on the polypeptide map profile of the Drosophila eye preparation was examined by two-dimensional polyacrylamide gel electrophoresis. The results show (i) that illuminating the living fly reversibly changes the isoelectric points of three classes of polypeptides specific for the photoreceptor layer and (ii) that the norpA mutation, which prevents the generation of the receptor potential, blocks the modifications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsumoto, H -- O'Tousa, J E -- Pak, W L -- EY 00033/EY/NEI NIH HHS/ -- EY 07008/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1982 Aug 27;217(4562):839-41.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7100927" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Drosophila/*metabolism ; Electrophoresis, Polyacrylamide Gel ; Eye Proteins/*metabolism ; Isoelectric Point ; Kinetics ; *Light ; Mutation ; Peptides/*metabolism ; Photoreceptor Cells/metabolism ; Retina/*metabolism
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    Variation of influenza A, B, and C viruses (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-03-19
    Description: Influenza is caused by highly variable RNA viruses belonging to the orthomyxovirus group. These viruses are capable of constantly changing the genes coding for their surface proteins as well as for their nonsurface proteins. The mechanisms responsible for these changes in type A influenza viruses include recombination (reassortment) of genes among strains, deletions and insertions in genes, and, frequently, point mutations. In addition, old strains may reappear in the population. Influenza viruses of types B and C appear to vary to a lesser degree. The mechanisms responsible for changes in these viruses are not well characterized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palese, P -- Young, J F -- New York, N.Y. -- Science. 1982 Mar 19;215(4539):1468-74.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7038875" target="_blank"〉PubMed〈/a〉
    Keywords: Genetic Variation ; Hemagglutinins, Viral/genetics ; Mutation ; Neuraminidase/genetics ; Orthomyxoviridae/*genetics ; Viral Proteins/genetics
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    Synthesis and secretion of the plasmid-coded heat-labile enterotoxin of Escherichia coli in Vibrio cholerae (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-07-15
    Description: Both cholera toxin and heat-labile enterotoxin were made and secreted into culture supernatants by Vibrio cholerae containing the enterotoxin plasmid pCG86. Several regulatory mutations in V. cholerae that increased or decreased the synthesis of cholera toxin did not affect production of heat-labile enterotoxin. In contrast, a mutation in V. cholerae that interfered with the secretion of cholera toxin also decreased the secretion of heat-labile enterotoxin, indicating that they are processed by a common secretory pathway. Vibrio cholerae should be useful as a model system for analyzing the secretion of true extracellular proteins by Gram-negative bacteria.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neill, R J -- Ivins, B E -- Holmes, R K -- 5 R22 AI14107/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 15;221(4607):289-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6857285" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacterial Toxins ; Cholera Toxin/metabolism ; Enterotoxins/*biosynthesis/genetics/secretion ; *Escherichia coli Proteins ; Mutation ; *Plasmids ; Vibrio cholerae/*genetics/metabolism
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    Suppressible four-base glycine and proline codons in yeast (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-04-24
    Description: Five ICR-170--induced mutations at the His4 locus in yeast are +1 G.C (G, guanine; C, cytosine) additions in DNA regions that contain multiple G.C base pairs. These mutations represents both nonsuppressible and suppressible alleles. All externally, suppressible frameshift mutations occur in glycine and proline codons to produce the four-base codons GGGU (U, uracil), GGGG, and CCCU. This implies that suppression of these four-base codons in yeast, as in bacteria, involves a four-base anticodon or its functional equivalent. Two identical four-base codons (CCCU) at widely separate regions with His4 are not suppressed equally.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Donahue, T F -- Farabaugh, P J -- Fink, G R -- New York, N.Y. -- Science. 1981 Apr 24;212(4493):455-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7010605" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Codon ; DNA, Fungal/genetics ; Glycine/*genetics ; Histidine/genetics ; Mutation ; Proline/*genetics ; *RNA, Messenger ; Saccharomyces cerevisiae/*genetics ; *Suppression, Genetic
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    Real-time color graphics in studies of molecular interactions (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-02-13
    Description: Studies of the structures and interactions of large biological molecules require both coordinate data and three-dimensional visualization. Orthodox molecular models often bear a tenuous relationship to the coordinate data. In contrast, computer graphics requires that the display directly and accurately represent the data, and storage of modified configurations and recovery of original structures are simple. Software has been developed that allows real-time display of color line and surface displays of several interacting molecules, while quantitatively monitoring the stereochemistry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Langridge, R -- Ferrin, T E -- Kuntz, I D -- Connolly, M L -- GM 19267/GM/NIGMS NIH HHS/ -- RR-1081-03/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1981 Feb 13;211(4483):661-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7455704" target="_blank"〉PubMed〈/a〉
    Keywords: Carboxypeptidases/antagonists & inhibitors ; Color ; *Computers ; Macromolecular Substances ; *Models, Molecular ; *Models, Structural ; Nucleic Acid Conformation ; Protein Conformation ; Trypsin ; Trypsin Inhibitors ; Water
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    Penicillin target enzyme and the antibiotic binding site (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-10-29
    Description: The three-dimensional structure of a penicillin-sensitive D-alanyl-carboxypeptidase-transpeptidase has been determined by x-ray crystallography to a resolution of 2.8 angstroms. The site of binding of the beta-lactam antibiotics penicillin and cephalosporin has been located. These findings constitute direct observation of the interaction of beta-lactams with a transpeptidase enzyme and establish the feasibility of defining the molecular stereochemistry of this interaction for purposes of drug design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kelly, J A -- Moews, P C -- Knox, J R -- Frere, J M -- Ghuysen, J M -- AI-13364-05/AI/NIAID NIH HHS/ -- AI-16702/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1982 Oct 29;218(4571):479-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7123246" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; *Carboxypeptidases ; *Cephalosporins ; Crystallography ; Models, Molecular ; *Muramoylpentapeptide Carboxypeptidase ; *Penicillins ; Protein Conformation ; X-Ray Diffraction
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    Infrared spectrum of the purple membrane: clue to a proton conduction mechanism? (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-04-23
    Description: The infrared spectrum of the purple membrane of Halobacterium halobium has amide I and amide A frequencies that are anomalously high for standard alpha-helical structures. Normal mode calculations indicate that these and other unusual features of the spectrum can be attributed to alpha 11-helices. Such structures suggest that the helix backbone may provide the framework through which proton transport takes place.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krimm, S -- Dwivedi, A M -- New York, N.Y. -- Science. 1982 Apr 23;216(4544):407-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6280277" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacteriorhodopsins ; Biological Transport, Active ; *Carotenoids ; Halobacterium/*ultrastructure ; Hydrogen Bonding ; Ion Channels ; Protein Conformation ; Protons ; Spectrophotometry, Infrared
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    Genetic transformation of Drosophila with transposable element vectors (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-10-22
    Description: Exogenous DNA sequences were introduced into the Drosophila germ line. A rosy transposon (ry1), constructed by inserting a chromosomal DNA fragment containing the wild-type rosy gene into a P transposable element, transformed germ line cells in 20 to 50 percent of the injected rosy mutant embryos. Transformants contained one or two copies of chromosomally integrated, intact ry1 that were stably inherited in subsequent generations. These transformed flies had wild-type eye color indicating that the visible genetic defect in the host strain could be fully and permanently corrected by the transferred gene. To demonstrate the generality of this approach, a DNA segment that does not confer a recognizable phenotype on recipients was also transferred into germ line chromosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rubin, G M -- Spradling, A C -- New York, N.Y. -- Science. 1982 Oct 22;218(4570):348-53.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6289436" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; *DNA Transposable Elements ; Drosophila/embryology/*genetics ; Genes ; Genetic Engineering/*methods ; Mutation ; Nucleic Acid Hybridization ; Plasmids ; *Transformation, Genetic ; Xanthine Dehydrogenase/genetics
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    Form and function of retroviral proviruses (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-05-21
    Description: Retroviruses have proved to be useful reagents for studying genetic and epigenetic (such as regulatory) changes in eukaryotic cells, for assessing functional and structural relationships between transposable genetic elements, for inducing insertional mutations, including some important in oncogenesis, and for transporting genes into eukaryotic cells, either after natural transduction of putative cellular oncogenes or after experimental construction of recombinant viruses. Many of these properties of retroviruses depend on their capacity to establish a DNA (proviral) form of their RNA genomes as a stable component of host chromosomes, in either somatic or germinal cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Varmus, H E -- New York, N.Y. -- Science. 1982 May 21;216(4548):812-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6177038" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA Transposable Elements ; DNA, Viral/biosynthesis/genetics ; Gene Expression Regulation ; Genes, Viral ; Genetic Vectors ; Mutation ; RNA-Directed DNA Polymerase/metabolism ; Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; Retroviridae/*physiology ; Transcription, Genetic ; Virus Replication
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    Blood cell surface changes in Drosophila mutants with melanotic tumors (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-04-01
    Description: When wheat germ agglutinin conjugated to fluorescein isothiocyanate is bound to hemocytes from larvae of Drosophila melanogaster, two populations of hemocytes are distinguished. One shows a fluorescent speckled surface (spk+) and the other lacks this characteristic (spk-). In mutant larvae with melanotic tumors and in larval hosts with heterospecific implants, most of the lamellocytes (a hemocyte variant involved in capsule formation and tissue rejection) are spk+, whereas the lamellocytes in nontumorous larvae are spk-. This suggests that spk+ lamellocytes are necessary for encapsulation of aberrant tissues in the mutant larvae and are responsible for rejection of foreign tissue implants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rizki, T M -- Rizki, R M -- AG-01945/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1983 Apr 1;220(4592):73-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6402819" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Cells/*immunology ; Drosophila melanogaster/*immunology ; Graft Rejection ; Hemocytes/drug effects/*immunology ; Larva ; Lectins/pharmacology ; Mutation ; Neoplasms, Experimental/blood/*immunology
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    Structural changes at the heme induced by freezing hemoglobin (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-08-07
    Description: A dramatic change occurs in the vibrational properties of the iron-histidine bond, trans to the oxygen binding site, on freezing deoxyhemoglobin. The large, quaternary structure-dependent differences in the shape and frequency of the iron-histidine mode observed in resonance Raman scattering measurements above freezing ae significantly diminished by the freezing event and the scattering intensity increases substantially. On further reduction in temperature to 10 K this broad line becomes narrow and shifts to a higher frequency. These data implicate dynamical processes and protein interaction with water as contributors to the quaternary structure dependence of the iron-histidine bond and thus reflect on the role of that bond in the energetics of cooperative ligand binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ondrias, M R -- Rousseau, D L -- Simon, S R -- New York, N.Y. -- Science. 1981 Aug 7;213(4508):657-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7256263" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; *Freezing ; *Heme ; *Hemoglobin A ; Histidine ; Humans ; Motion ; Protein Conformation ; Spectrum Analysis, Raman ; Water
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    Germplasm conservation (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-12-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russell, E S -- New York, N.Y. -- Science. 1981 Dec 4;214(4525):1074, 1076.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6946561" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cats ; Disease Models, Animal ; Dogs ; *Genetic Engineering ; *Genetics, Medical ; Humans ; Mice ; Mutation ; Rats
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    Cadmium-113 nuclear magnetic resonance studies of bovine insulin: two-zinc insulin hexamer specifically binds calcium (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-05-01
    Description: By use of cadmium-113 nuclear magnetic resonance spectroscopy, a specific calcium ion binding site has been identified in the bovine two-zinc insulin hexamer. This site is composed of six glutamyl carboxylate groups clustered in the center of the hexamer, and is distinct from the normal zinc ion binding sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sudmeier, J L -- Bell, S J -- Storm, M C -- Dunn, M F -- 5S05RR 07010-09/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1981 May 1;212(4494):560-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7010607" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cadmium ; Calcium/*metabolism ; Cattle ; *Insulin/metabolism ; Isotopes ; Ligands ; Macromolecular Substances ; Magnetic Resonance Spectroscopy ; Protein Conformation ; Zinc/*metabolism
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    Nucleotide sequence of the oncogene encoding the p21 transforming protein of Kirsten murine sarcoma virus (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-09-03
    Description: The transforming protein of Kirsten murine sarcoma virus (Ki-MuSV) is a virally encoded 21-kilodalton protein called p21 kis. The sequences encoding p21 kis were genetically localized to a 1.3-kilobase segment near the 5' end of the viral genome by assaying the capacity of a series of defined deletion mutants of molecularly cloned Ki-MuSV DNA to induce focal transformation of mouse cells. Nucleotide sequencing of a portion of this region has led to the identification of an open reading frame of 567 nucleotides coding for p21 kis protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsuchida, N -- Ryder, T -- Ohtsubo, E -- CA-22701/CA/NCI NIH HHS/ -- CA21124/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1982 Sep 3;217(4563):937-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6287573" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Transformation, Viral ; Cells, Cultured ; DNA Restriction Enzymes ; DNA, Recombinant ; DNA, Viral/genetics ; Genes, Viral ; Kirsten murine sarcoma virus/*genetics ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Mutation ; Oncogene Protein p21(ras) ; RNA, Viral/genetics ; Sarcoma Viruses, Murine/*genetics ; Viral Proteins/*genetics
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    A gene controlling condensation of heterochromatin in Drosophila melanogaster (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-07-01
    Description: A temperature-sensitive lethal mutant of Drosophila melanogaster was used to identify an essential cell cycle function that is necessary for the mitotic condensation of heterochromatic but not of euchromatic portions of the genome. This mutant is an allele at a locus (mus-101) identified earlier by the use of mutagen-sensitive mutants. The data suggest that the mutagen-sensitive and repair-defective phenotypes of viable mus-101 mutants result from a disruption in chromosome organization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gatti, M -- Smith, D A -- Baker, B S -- GM23345/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 1;221(4605):83-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6407113" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Cycle ; Chromosomes/ultrastructure ; Drosophila melanogaster ; Female ; *Genes ; Heterochromatin/*genetics/physiology ; Male ; Mutation
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    The human c-ras1H oncogene: a mutation in normal and neoplastic tissue from the same patient (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-02-18
    Description: The c-ras1H oncogene can be distinguished from its normal cellular counterpart by the loss of a restriction endonuclease site. This sequence alteration is the basis of a rapid screening method for the presence of this oncogene. DNA's from 34 individuals were screened by this method, and all were homozygous for the normal allele. In contrast, DNA from a patient's bladder tumor, as well as DNA from his normal bladder and leukocytes, were heterozygous at that restriction endonuclease site. Further restriction enzyme mapping pinpointed the change in the mutant allele as being one of two nucleotides, either of which would change the 12th amino acid (glycine) in the normal c-ras1H gene product. Point mutations in the codon for this amino acid have previously been described in a bladder tumor cell line and in the viral oncogene v-rasH. These results indicate that the patient carried a c-ras1H oncogene in his germ line, raising the possibility that the c-ras1H oncogene confers a predisposition to neoplasia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muschel, R J -- Khoury, G -- Lebowitz, P -- Koller, R -- Dhar, R -- New York, N.Y. -- Science. 1983 Feb 18;219(4586):853-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6337398" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Transformation, Neoplastic/pathology ; Humans ; Mutation ; *Oncogenes ; Urinary Bladder Neoplasms/*genetics
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  • 80
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    Catecholamine-induced alteration in sedimentation behavior of membrane bound beta-adrenergic receptors (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-10-01
    Description: Incubation of astrocytoma cells with catecholamines results in a decrease in catecholamine-stimulated adenylate cyclase activity and a concomitant alteration in the sedimentation properties of particulate beta-adrenergic receptors. The altered receptors exhibit agonist binding properties similar to those of receptors that are "uncoupled" from adenylate cyclase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harden, T K -- Cotton, C U -- Waldo, G L -- Lutton, J K -- Perkins, J P -- GM 25163/GM/NIGMS NIH HHS/ -- HL 22490/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1980 Oct;210(4468):441-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6254143" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Astrocytoma ; Cell Line ; Centrifugation, Density Gradient ; Concanavalin A/pharmacology ; Endocytosis ; Humans ; Isoproterenol/*metabolism ; Protein Conformation ; Receptors, Adrenergic/*metabolism ; Receptors, Adrenergic, beta/*metabolism ; Time Factors
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    Testing for cancer risk (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-02-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G B -- New York, N.Y. -- Science. 1980 Feb 29;207(4434):967-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6243421" target="_blank"〉PubMed〈/a〉
    Keywords: Aryl Hydrocarbon Hydroxylases/metabolism ; Ataxia Telangiectasia/genetics ; Chromosome Aberrations ; Chromosome Disorders ; Fanconi Anemia/genetics ; Genetic Counseling ; Humans ; Mutation ; Neoplasms/etiology/*genetics ; Polycyclic Compounds/metabolism ; Risk ; Wilms Tumor/genetics ; Xeroderma Pigmentosum/genetics
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    Monte Carlo simulation of water behavior around the dipeptide N-acetylalanyl-N-methylamide (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-05-09
    Description: Applications of Monte Carlo and molecular dynamics computer simulation techniques indicate that they are potentially powerful tools for understanding biological systems at the molecular level. The Monte Carlo technique can be used to study the solvent structure around a small peptide and the effect of the aqueous environment on the conformational equilibria of the peptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hagler, A T -- Osguthorpe, D J -- Robson, B -- New York, N.Y. -- Science. 1980 May 9;208(4444):599-601.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7367882" target="_blank"〉PubMed〈/a〉
    Keywords: *Alanine/*analogs & derivatives ; *Dipeptides ; Models, Chemical ; Monte Carlo Method ; Protein Conformation ; Solvents ; *Water
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    Silent nucleotide substitutions and the molecular evolutionary clock (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-11-28
    Description: Half of the nucleotide substitutions during the evolutionary divergence of genes in animals, bacteria, and viruses are silent changes. These result from an inherent biochemical property of DNA and are fixed by genetic drift. Evolution may be viewed as a device for protecting DNA molecules from extinction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jukes, T H -- New York, N.Y. -- Science. 1980 Nov 28;210(4473):973-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7434017" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Biological Evolution ; Codon ; DNA/*genetics ; DNA, Viral/genetics ; *Genes ; Genetic Code ; Globins/genetics ; Histones/genetics ; Mutation ; RNA, Messenger/genetics
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    Evolutionary theory under fire (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-11-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1980 Nov 21;210(4472):883-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6107993" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; *Biological Evolution ; Chicago ; Congresses as Topic ; Fossils ; Gene Frequency ; Models, Theoretical ; Mutation ; Time Factors
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    Acetylcholine receptor: complex of homologous subunits (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-06-27
    Description: The acetylcholine receptor from the electric ray Torpedo californica is composed of five subunits; two are identical and the other three are structurally related to them. Microsequence analysis of the four polypeptides demonstrates amino acid homology among the subunits. Further sequence analysis of both membrane-bound and Triton-solubilized, chromatographically purified receptor gave the stoichiometry of the four subunits (40,000:50,000:60,000:65,000 daltons) as 2:1:1:1, indicating that this protein is a pentameric complex with a molecular weight of 255,000 daltons. Genealogical analysis suggests that divergence from a common ancestral gene occurred early in the evolution of the receptor. This shared ancestry argues that each of the four subunits plays a functional role in the receptor's physiological action.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raftery, M A -- Hunkapiller, M W -- Strader, C D -- Hood, L E -- New York, N.Y. -- Science. 1980 Jun 27;208(4451):1454-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7384786" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/metabolism ; Amino Acid Sequence ; Animals ; Electric Organ/*analysis ; Fishes ; Macromolecular Substances ; Molecular Weight ; Protein Conformation ; *Receptors, Cholinergic
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  • 86
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    The molecular structure of a DNA-triostin A complex (1984)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1984-09-14
    Description: The molecular structure of triostin A, a cyclic octadepsipeptide antibiotic, has been solved complexed to a DNA double helical fragment with the sequence CGTACG (C, cytosine; G, guanine; T, thymine; A, adenine). The two planar quinoxaline rings of triostin A bis intercalate on the minor groove of the DNA double helix surrounding the CG base pairs at either end. The alanine residues form hydrogen bonds to the guanines. Base stacking in the DNA is perturbed, and the major binding interaction involves a large number of van der Waals contacts between the peptides and the nucleic acid. The adenine residues in the center are in the syn conformation and are paired to thymine through Hoogsteen base pairing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, A H -- Ughetto, G -- Quigley, G J -- Hakoshima, T -- van der Marel, G A -- van Boom, J H -- Rich, A -- New York, N.Y. -- Science. 1984 Sep 14;225(4667):1115-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6474168" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallization ; DNA/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; Protein Conformation ; Quinoxalines/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 87
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    Expression of cellular oncogenes in human malignancies (1984)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1984-04-20
    Description: Cellular oncogenes have been implicated in the induction of malignant transformation in some model systems in vitro and may be related to malignancies in vivo in some vertebrate species. This article describes a study of the expression of 15 cellular oncogenes in fresh human tumors from 54 patients, representing 20 different tumor types. More than one cellular oncogene was transcriptionally active in all of the tumors examined. In 14 patients it was possible to study normal and malignant tissue from the same organ. In many of these patients, the transcriptional activity of certain oncogenes was greater in the malignant than the normal tissue. The cellular fes (feline sarcoma) oncogene, not previously known to be transcribed in mammalian tissue, was found to be active in lung and hematopoietic malignancies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Slamon, D J -- deKernion, J B -- Verma, I M -- Cline, M J -- AM 18058/AM/NIADDK NIH HHS/ -- CA 15619/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 20;224(4646):256-62.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6538699" target="_blank"〉PubMed〈/a〉
    Keywords: Adenocarcinoma/genetics ; Breast Neoplasms/genetics ; Carcinogens/pharmacology ; Cell Differentiation ; Cell Division ; Cell Transformation, Neoplastic ; Female ; Gastrointestinal Neoplasms/genetics ; Gene Amplification ; Genes, Viral ; Genital Neoplasms, Female/genetics ; Humans ; Kidney Neoplasms/genetics ; Leukemia/genetics ; Lymphoma/genetics ; Methylation ; Mutation ; Neoplasms/*genetics ; Nucleic Acid Hybridization ; *Oncogenes ; RNA, Messenger/genetics ; RNA, Neoplasm/genetics ; Sarcoma/genetics ; *Transcription, Genetic ; Translocation, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 88
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    Molecular dissection of transcriptional control elements within the long terminal repeat of the retrovirus (1984)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1984-01-20
    Description: The retroviral long terminal repeat (LTR) contains transcriptional control elements that affect viral gene expression. By deletion mutagenesis of the genome of the cloned Abelson murine leukemia virus, regulatory signals could be mapped to at least three domains within the LTR. A defective 5' LTR that did not sustain transforming gene function was complemented by an intact LTR positioned at the 3' end of the genome. This versatility of the retroviral genome with respect to its transcriptional control elements appears to provide a strong selective advantage for viral gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Srinivasan, A -- Reddy, E P -- Dunn, C Y -- Aaronson, S A -- New York, N.Y. -- Science. 1984 Jan 20;223(4633):286-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6322296" target="_blank"〉PubMed〈/a〉
    Keywords: Abelson murine leukemia virus/*genetics ; Animals ; Cell Line ; Cell Transformation, Viral ; Cloning, Molecular ; *Gene Expression Regulation ; *Genes, Viral ; Leukemia Virus, Murine/*genetics ; Mice ; Mutation ; *Repetitive Sequences, Nucleic Acid ; *Transcription, Genetic ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 89
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    Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase (1984)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1984-12-14
    Description: Few and limited amino acid sequence homologies have been found among eight bacterial aminoacyl transfer RNA (tRNA) synthetases whose primary structures are known. The entire 939-amino acid primary structure of Escherichia coli isoleucyl-tRNA synthetase is now reported. In a sequence of 11 consecutive amino acids matching a sequence in E. coli methionyl-tRNA synthetase, there are ten identical residues and one conservative change. This is the strongest homology recorded between any two aminoacyl tRNA synthetases. This part of the methionine enzyme's three-dimensional structure has been determined, and it occurs in a mononucleotide binding fold; a close three-dimensional structural homology of this part of the enzyme with Bacillus stearothermophilus tyrosyl-tRNA synthetase has also been reported. The three synthetases probably fold identically in this region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Webster, T -- Tsai, H -- Kula, M -- Mackie, G A -- Schimmel, P -- GM15539/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Dec 14;226(4680):1315-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6390679" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Amino Acyl-tRNA Synthetases ; Escherichia coli/enzymology ; Geobacillus stearothermophilus/enzymology ; Isoleucine-tRNA Ligase ; Methionine-tRNA Ligase ; Protein Conformation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 90
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    Malignant activation of a K-ras oncogene in lung carcinoma but not in normal tissue of the same patient (1984)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1984-02-17
    Description: A single genetic alteration, a guanine-to-cytosine transversion, is responsible for the acquisition of malignant properties by K-ras genes of two human tumor cell lines established from carcinomas of the bladder (A1698) and lung (A2182). As a consequence, arginine instead of the normal glycine is incorporated into the K-ras-coded p21 proteins at amino acid position 12. This mutation creates a restriction enzyme polymorphism that can be used to screen human cells for transforming K-ras genes. This approach was used to identify the mutational event responsible for the malignant activation of a K-ras oncogene in a squamous cell lung carcinoma of a 66-year-old man; this point mutation was not present in either the normal bronchial or parenchymal tissue or in the blood lymphocytes. Hence, malignant activation of a ras oncogene appears to be specifically associated with the development of a human neoplasm.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Santos, E -- Martin-Zanca, D -- Reddy, E P -- Pierotti, M A -- Della Porta, G -- Barbacid, M -- New York, N.Y. -- Science. 1984 Feb 17;223(4637):661-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6695174" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Cell Transformation, Neoplastic ; DNA, Neoplasm/genetics ; Genes, Dominant ; Humans ; Lung Neoplasms/*genetics ; Mutation ; *Oncogenes ; Organ Specificity ; Polymorphism, Genetic
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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