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  • Genes  (24)
  • American Association for the Advancement of Science (AAAS)  (24)
  • 1980-1984  (24)
  • 1925-1929
  • 1983  (24)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (24)
  • Springer  (1)
Years
  • 1980-1984  (24)
  • 1925-1929
Year
  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-06-10
    Description: A comparison between eukaryotic gene sequences and protein sequences of homologous enzymes from bacterial and mammalian organisms shows that intron-exon junctions frequently coincide with variable surface loops of the protein structures. The altered surface structures can account for functional differences among the members of a family. Sliding of the intron-exon junctions may constitute one mechanism for generating length polymorphisms and divergent sequences found in protein families. Since intron-exon junctions map to protein surfaces, the alterations mediated by sliding of these junctions can be effected without disrupting the stability of the protein core.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Craik, C S -- Rutter, W J -- Fletterick, R -- AM21344/AM/NIADDK NIH HHS/ -- AM26081/AM/NIADDK NIH HHS/ -- GM28520/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Jun 10;220(4602):1125-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344214" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Proteins ; Base Sequence ; Biological Evolution ; DNA/genetics ; Endopeptidases/genetics ; Eukaryotic Cells/metabolism ; Genes ; Genes, Bacterial ; Protein Conformation ; Proteins/*genetics ; *Serine Endopeptidases ; Tetrahydrofolate Dehydrogenase/genetics
    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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  • 2
    Publication Date: 1983-03-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1983 Mar 18;219(4590):1312.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6828858" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Genes ; Humans ; Myoglobin/*genetics
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  • 3
    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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  • 4
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    American Association for the Advancement of Science (AAAS)
    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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  • 5
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    American Association for the Advancement of Science (AAAS)
    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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  • 6
    Publication Date: 1983-06-03
    Description: Electrophysiological analysis of the Drosophila behavioral mutants Eag and Sh and the double mutant Eag Sh indicates that the products of both genes take part in the control of potassium currents in the membranes of both nerve and muscle. In voltage-clamped larval muscle fibers, Sh affects the transient A current, whereas Eag reduces the delayed rectification and, to a lesser extent, the A current.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, C F -- Ganetzky, B -- Haugland, F N -- Liu, A X -- NS00675/NS/NINDS NIH HHS/ -- NS15797/NS/NINDS NIH HHS/ -- NS18500/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 Jun 3;220(4601):1076-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6302847" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Drosophila/genetics ; Electrophysiology ; Genes ; Ion Channels/*metabolism ; Larva ; Membrane Potentials ; Muscles/metabolism ; *Mutation ; Neuromuscular Junction/metabolism ; Potassium/*metabolism
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  • 7
    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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  • 8
    Publication Date: 1983-10-28
    Description: Burkitt lymphoma cells carrying either a rearranged or unrearranged c-myc oncogene were examined with the use of probes from the 5' exon and for the second and third exon of the oncogene. The results indicate that the normal c-myc gene on chromosome 8 and the 5' noncoding and 3' coding segments of the c-myc oncogene separated by the chromosomal translocation are under different transcriptional control in the lymphoma cells. Burkitt lymphoma cells carrying a translocated but unrearranged c-myc oncogene express normal c-myc transcripts. In contrast, lymphoma cells carrying a c-myc gene rearranged head to head with the immunoglobulin constant mu region gene express c-myc transcripts lacking the normal untranslated leader.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉ar-Rushdi, A -- Nishikura, K -- Erikson, J -- Watt, R -- Rovera, G -- Croce, C M -- CA09171/CA/NCI NIH HHS/ -- CA10815/CA/NCI NIH HHS/ -- CA16685/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 Oct 28;222(4622):390-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6414084" target="_blank"〉PubMed〈/a〉
    Keywords: Burkitt Lymphoma/*genetics ; Chromosomes, Human, 13-15 ; Chromosomes, Human, 19-20 ; Chromosomes, Human, 6-12 and X ; Gene Expression Regulation ; Genes ; Humans ; Immunoglobulin Heavy Chains/genetics ; *Oncogenes ; Operon ; Transcription, Genetic ; Translocation, Genetic
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-07-01
    Description: Sea urchin histone genes contained in a recombinant plasmid pSp102 were microinjected into the cytoplasm of fertilized eggs of Xenopus laevis. By the late blastula stage, plasmid DNA sequences were detected comigrating with the high molecular weight cellular DNA (greater than 48 kilobases). Analysis of the DNA from injected embryos digested with various restriction endonuclease demonstrated that the injected DNA was integrated into the frog genome. Clones of embryos containing the pSp102 DNA sequences were produced by means of nuclear transplantation. Individuals of the same clone contain the pSp102 sequences integrated into similar chromosomal locations. These sites vary between different clones.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Etkin, L D -- Roberts, M -- GM31479-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 1;221(4605):67-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6857265" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Clone Cells ; DNA, Recombinant/metabolism ; Genes ; Histones/*genetics ; *Nuclear Transfer Techniques ; Plasmids ; Sea Urchins/genetics ; Xenopus laevis/genetics
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  • 10
    Publication Date: 1983-02-25
    Description: The locus for the cellular myc (c-myc) oncogene in humans is located on the region of chromosome 8 that is translocated to chromosome 14 in cells from most undifferentiated B-cell lymphomas. It is shown in this study that the c-myc locus is rearranged in 5 out of 15 cell lines from patients with undifferentiated B-cell lymphomas, and that the rearrangement involves a region at the 5' side of an apparently intact c-myc gene. In at least three patients, this rearranged region appears to contain immunoglobulin heavy chain mu sequences that are located on chromosome 14. The data indicate that this region contains the crossover point between chromosomes 8 and 14. The break point can occur at different positions on both chromosomes among individual cell lines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dalla-Favera, R -- Martinotti, S -- Gallo, R C -- Erikson, J -- Croce, C M -- New York, N.Y. -- Science. 1983 Feb 25;219(4587):963-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6401867" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocytes/*physiology ; Cell Differentiation ; Chromosome Mapping ; Gene Expression Regulation ; Genes ; Genetic Linkage ; Humans ; Immunoglobulin Constant Regions/genetics ; Immunoglobulin Heavy Chains/genetics ; Lymphoma/*genetics ; *Oncogenes ; Recombination, Genetic
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-05-27
    Description: The utility of somatic cell genetic analysis for the chromosomal localization of genes in mammals is well established. With the development of recombinant DNA probes and efficient blotting techniques that allow visualization of single-copy cellular genes, somatic cell genetics has been extended from the level of phenotypes expressed by whole cells to the level of the cellular genome itself. This extension has proved invaluable for the analysis of genes not readily expressed in somatic cell hybrids and for the study of multigene families, especially pseudogenes dispersed in different chromosomes throughout the genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉D'Eustachio, P -- Ruddle, F H -- GM-09966/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 May 27;220(4600):919-24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6573776" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Chromosome Mapping ; Chromosomes, Human ; Cricetinae ; Cricetulus ; DNA, Recombinant/metabolism ; Genes ; Genetic Markers ; Genetics ; Humans ; Hybrid Cells/metabolism ; Mice ; Polymorphism, Genetic ; RNA, Messenger/metabolism
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-18
    Description: Class III genes require multiple cellular factors for transcription by RNA polymerase III; these genes form stable transcription complexes, which in the case of Xenopus 5S genes are correlated with differential expression in vivo. The minimal number and identity of the factors required to form both stable and metastable complexes on three class III genes (encoding, respectively, 5S RNA, transfer RNA, and adenovirus VA RNA species) were determined. Stable complex formation requires one common factor, whose recognition site was analyzed, and either no additional factors (the VA gene), a second common factor (the transfer RNA gene), or a third gene-specific factor (the 5S gene). The mechanism of stable complex formation and its relevance to transcriptional regulation were examined in light of the various factors and the promoter sequences recognized by these factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lassar, A B -- Martin, P L -- Roeder, R G -- CA 24223/CA/NCI NIH HHS/ -- CA 24891/CA/NCI NIH HHS/ -- GM07200/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):740-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356356" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA-Directed RNA Polymerases/*genetics ; Eukaryotic Cells/physiology ; Gene Expression Regulation ; Genes ; Humans ; Operon ; RNA Polymerase III/*genetics ; RNA, Ribosomal/genetics ; RNA, Transfer/genetics ; RNA, Viral/genetics ; Transcription Factors/genetics ; *Transcription, Genetic
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  • 13
    Publication Date: 1983-08-19
    Description: Cloned myosin heavy chain DNA probes from rat and human were hybridized to restriction endonuclease digests of genomic DNA from somatic cell hybrids and their parental cells. The mouse myosin heavy chain genes detectable by this assay were located on chromosome 11, and three different human sarcomeric myosin heavy chain genes were mapped to the short arm of chromosome 17. A synteny between myosin heavy chain and two unrelated markers, thymidine kinase and galactokinase, was found to be preserved in the rodent and human genomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leinwand, L A -- Fournier, R E -- Nadal-Ginard, B -- Shows, T B -- GM26449/GM/NIGMS NIH HHS/ -- GM29090/GM/NIGMS NIH HHS/ -- GM31281/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 Aug 19;221(4612):766-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6879174" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Chromosome Mapping ; Chromosomes, Human, 16-18 ; Genes ; Genetic Linkage ; Humans ; Mice ; Myosins/*genetics
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-08-19
    Description: Ia (I region-associated) antigens are cell-surface glycoproteins involved in the regulation of immune responsiveness. They are composed of one heavy (alpha) and one light (beta) polypeptide chain. We have sequenced the gene encoding the A beta d chain of the BALB/c mouse. The presence of six exons is predicted by comparison with the complementary DNA sequences of human beta chains and with partial protein sequence data for the A beta d polypeptide. Sequence comparisons have been made to other proteins involved in immune responses and the consequent implications for the evolutionary relationships of these genes are discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malissen, M -- Hunkapiller, T -- Hood, L -- New York, N.Y. -- Science. 1983 Aug 19;221(4612):750-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6410508" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Evolution ; Codon ; Genes ; *Genes, MHC Class II ; Macromolecular Substances ; Major Histocompatibility Complex ; Mice ; beta 2-Microglobulin/genetics
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  • 15
    Publication Date: 1983-08-26
    Description: The complete nucleotide sequence of the diphtheria tox228 gene encoding the nontoxic serologically related protein CRM228 has been determined. A comparison of the predicted amino acid sequence with the available amino acid sequences from the wild-type toxin made it possible to deduce essentially the entire nucleotide sequence of the wild-type tox gene. The signal peptide of pro-diphtheria toxin and the putative tox promoter have been identified, a highly symmetrical nucleotide sequence downstream of the toxin gene has been detected; this region may be the corynebacteriophage beta attachment site (attP). The cloned toxin gene was expressed at a low level in Escherichia coli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaczorek, M -- Delpeyroux, F -- Chenciner, N -- Streeck, R E -- Murphy, J R -- Boquet, P -- Tiollais, P -- New York, N.Y. -- Science. 1983 Aug 26;221(4613):855-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6348945" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular ; Diphtheria Toxin/*genetics ; Escherichia coli/genetics ; Gene Expression Regulation ; Genes ; Genes, Bacterial ; Nucleic Acid Conformation ; Operon
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-09-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1983 Sep 23;221(4617):1278-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6612341" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; Genes ; Receptors, Antigen, T-Cell/*genetics
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  • 17
    Publication Date: 1983-07-15
    Description: The transforming protein of a primate sarcoma virus and a platelet-derived growth factor are derived from the same or closely related cellular genes. This conclusion is based on the demonstration of extensive sequence similarity between the transforming protein derived from the simian sarcoma virus onc gene, v-sis, and a human platelet-derived growth factor. The mechanism by which v-sis transforms cells could involve the constitutive expression of a protein with functions similar or identical to those of a factor active transiently during normal cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doolittle, R F -- Hunkapiller, M W -- Hood, L E -- Devare, S G -- Robbins, K C -- Aaronson, S A -- Antoniades, H N -- CA30101/CA/NCI NIH HHS/ -- RR00757/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 15;221(4607):275-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6304883" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cebidae ; Cell Transformation, Neoplastic/metabolism ; Genes ; Growth Substances/*genetics/physiology ; Humans ; *Oncogenes ; Peptides/*genetics/physiology ; Platelet-Derived Growth Factor ; Retroviridae/*genetics ; Sarcoma Virus, Woolly Monkey/*genetics
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  • 18
    Publication Date: 1983-11-18
    Description: The characteristic chromosomal translocations that occur in certain human malignancies offer opportunities to understand how two gene systems can affect one another when they are accidentally juxtaposed. In the case of Burkitt lymphoma, such a translocation joins the cellular oncogene, c-myc, to a region encoding one of the immunoglobulin genes. In at least one example, the coding sequence of the rearranged c-myc gene is identical to that of the normal gene, implying that the gene must be quantitatively, rather than qualitatively, altered in its expression if it is to play a role in transformation. One might expect to find the rearranged c-myc gene in a configuration that would allow it to take advantage of one of the known immunoglobulin promoters or enhancer elements. However, the rearranged c-myc gene is often placed so that it can utilize neither of these structures. Since the level of c-myc messenger RNA is often elevated in Burkitt cells, the translocation may lead to a deregulation of the c-myc gene. Further, since the normal allele in a Burkitt cell is often transcriptionally silent in the presence of a rearranged allele, a model for c-myc regulation is suggested that involves a trans-acting negative control element that might use as its target a highly conserved portion of the c-myc gene encoding two discrete transcriptional promoters.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leder, P -- Battey, J -- Lenoir, G -- Moulding, C -- Murphy, W -- Potter, H -- Stewart, T -- Taub, R -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):765-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356357" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Burkitt Lymphoma/*genetics ; Cell Transformation, Neoplastic/etiology ; Chromosome Aberrations/*genetics ; Chromosome Disorders ; Chromosome Mapping ; Gene Expression Regulation ; Genes ; Humans ; Immunoglobulins/genetics ; Models, Biological ; Neoplasms/*genetics ; *Oncogenes ; *Translocation, Genetic
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-07-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1983 Jul 15;221(4607):251-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344222" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Drosophila/metabolism ; Escherichia coli/metabolism ; Genes ; Heat-Shock Proteins ; Hot Temperature/*adverse effects ; Humans ; Proteins/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-03-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1983 Mar 4;219(4588):1055-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6823566" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; Genes ; Receptors, Cholinergic/*genetics ; Torpedo
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 21
    Publication Date: 1983-11-18
    Description: Egg-laying behavior in Aplysia is mediated by a set of peptides, including egg-laying hormone (ELH), which are released by a cluster of identified neurons, the bag cells. A family of neuropeptide genes which includes the gene encoding ELH along with two additional genes encoding the A and B peptides thought to initiate the egg-laying process has been isolated and their nucleotide sequence has been determined. In situ hybridization and immunofluorescence was used to explore the origin and distribution of the neurons that express this family of genes. The ELH genes are expressed, not only in the bag cells, but in an extensive system of neurons distributed in four of the five ganglia of the central nervous system. The genes for ELH are expressed in these cells early in the animal's life cycle. As a result, it was possible to use in situ hybridization to trace the cells expressing ELH to their site of origin. The cells originate outside the central nervous system in the ectoderm of the body wall and appear to migrate to their final locations within the central nervous system by crawling along strands of connective tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McAllister, L B -- Scheller, R H -- Kandel, E R -- Axel, R -- 5 PO1 CA-23767/CA/NCI NIH HHS/ -- GM-32099/GM/NIGMS NIH HHS/ -- NCL-5RO1 CA-16346/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):800-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356362" target="_blank"〉PubMed〈/a〉
    Keywords: Age Factors ; Animals ; Aplysia/*physiology ; Behavior, Animal/*physiology ; Cell Differentiation ; Female ; *Gene Expression Regulation ; Genes ; Invertebrate Hormones/genetics ; Nerve Tissue Proteins/*genetics ; Neurons/*physiology ; Nucleic Acid Hybridization ; Oviposition ; RNA, Messenger/genetics
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 22
    Publication Date: 1983-01-28
    Description: Restriction endonucleases cut and partially removed DNA throughout fixed air-dried human metaphase chromosomes. Some enzymes produced a G-banding pattern; some revealed the presence of multiple chromosome-specific classes of highly repetitive DNA in C-band heterochromatin. Enzymes that produced the informative C-band patterns had recognition sequences that were four or five, but not six, base pairs long and did not contain a cytosine-guanine doublet. In both rat and human chromosomes, regions containing amplified ribosomal RNA genes were specifically removed by the restriction endonuclease Msp I.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, D A -- Choi, Y C -- Miller, O J -- CA27655/CA/NCI NIH HHS/ -- GM25193/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Jan 28;219(4583):395-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6294832" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Banding ; Chromosome Mapping ; DNA Restriction Enzymes ; Gene Amplification ; Genes ; Humans ; RNA, Ribosomal/*genetics ; *Repetitive Sequences, Nucleic Acid
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 23
    Publication Date: 1983-07-01
    Description: With a synthetic oligonucleotide mixture as probe, complementary DNA clones of C-reactive protein were isolated from an adult human liver complementary DNA library. The clones ranged in size from 700 to 1100 base pairs and were identified by partial DNA sequence analysis. One complementary DNA clone was used as a probe for hybridization with human-rodent DNA's isolated from somatic cell hybrids and bound to nitrocellulose filters (Southern blot analysis) to assign the human C-reactive protein gene to chromosome 1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whitehead, A S -- Bruns, G A -- Markham, A F -- Colten, H R -- Woods, D E -- AI15033/AI/NIAID NIH HHS/ -- HD4807/HD/NICHD NIH HHS/ -- HL22487/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 Jul 1;221(4605):69-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6857266" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; C-Reactive Protein/*genetics ; *Chromosome Mapping ; *Chromosomes, Human, 1-3 ; Cloning, Molecular ; Cricetinae ; DNA/*genetics/isolation & purification ; Genes ; Humans ; Hybrid Cells/metabolism ; Mice
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 24
    Publication Date: 1983-11-18
    Description: Three mutations of the enzyme dihydrofolate reductase were constructed by oligonucleotide-directed mutagenesis of the cloned Escherichia coli gene. The mutations--at residue 27, aspartic acid replaced with asparagine; at residue 39, proline replaced with cysteine; and at residue 95, glycine replaced with alanine--were designed to answer questions about the relations between molecular structure and function that were raised by the x-ray crystal structures. Properties of the mutant proteins show that Asp-27 is important for catalysis and that perturbation of the local structure at a conserved cis peptide bond following Gly-95 abolishes activity. Substitution of cysteine for proline at residue 39 results in the appearance of new forms of the enzyme that correspond to various oxidation states of the cysteine. One of these forms probably represents a species cross-linked by an intrachain disulfide bridge between the cysteine at position 85 and the new cysteine at position 39.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Villafranca, J E -- Howell, E E -- Voet, D H -- Strobel, M S -- Ogden, R C -- Abelson, J N -- Kraut, J -- CA17374/CA/NCI NIH HHS/ -- F32 GM09375/GM/NIGMS NIH HHS/ -- GM10928/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):782-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356360" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Disulfides ; Escherichia coli/genetics ; Gene Expression Regulation ; Genes ; Genes, Bacterial ; *Mutation ; Structure-Activity Relationship ; Tetrahydrofolate Dehydrogenase/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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