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  • Base Sequence  (56)
  • American Association for the Advancement of Science (AAAS)  (56)
  • American Geophysical Union
  • Elsevier
  • Institute of Physics
  • Periodicals Archive Online (PAO)
  • 1980-1984  (56)
  • 1925-1929
  • 1983  (33)
  • 1982  (23)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (56)
  • American Geophysical Union
  • Elsevier
  • Institute of Physics
  • Periodicals Archive Online (PAO)
Years
  • 1980-1984  (56)
  • 1925-1929
Year
  • 1
    Publication Date: 1982-02-19
    Description: The 14S messenger RNA (1300 to 1500 nucleotides) for the alpha A chain of alpha-crystallin of the mammalian lens is nearly three times larger than required to code for the polypeptide that contains 173 amino acids. As a means of accounting for this anomaly, a complementary DNA clone for the mouse alpha A-crystallin messenger RNA was constructed in pBR322 and sequenced. Derivation of the protein sequence from the nucleic acid sequence showed that mouse alpha A-crystallin is similar to that of other organisms. The messenger RNA contains 536 nucleotides located on the 3' side of the coding region, excluding the polyadenylate stretch. This 3' sequence does not encode any other crystallin and has multiple termination codons in the three possible reading frames.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, C R -- Shinohara, T -- Piatigorsky, J -- New York, N.Y. -- Science. 1982 Feb 19;215(4535):985-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7156978" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; Crystallins/*genetics ; Mice ; RNA, Messenger/*genetics
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-08-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1982 Aug 27;217(4562):817-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7100925" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *DNA/*analysis ; *Information Systems
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-08-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1982 Aug 13;217(4560):621-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6283639" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA/*genetics ; DNA Transposable Elements ; DNA, Satellite/genetics ; *Repetitive Sequences, Nucleic Acid ; Species Specificity
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  • 4
    Publication Date: 1982-06-25
    Description: Avian myeloblastosis virus is defective in reproductive capacity, requiring a helper virus to provide the viral proteins essential for synthesis of new infectious virus. This virus arose by recombination of the nondefective helper virus and host cellular sequences present within the normal avian genome. These latter sequences are essential for leukemogenic activity. The complete nucleotide sequence of this region is reported. Within the acquired cellular sequences there is an open reading frame of 795 nucleotides starting with the initiation codon ATG (adenine, thymine, guanine) and terminating with the triplet TAG. This open reading frame could code for the putative transforming protein of 265 amino acids with a molecular weight of approximately 30,000.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rushlow, K E -- Lautenberger, J A -- Papas, T S -- Baluda, M A -- Perbal, B -- Chirikjian, J G -- Reddy, E P -- New York, N.Y. -- Science. 1982 Jun 25;216(4553):1421-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6283631" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avian Leukosis Virus/*genetics ; Avian Myeloblastosis Virus/*genetics ; Avian Sarcoma Viruses/genetics ; Base Sequence ; Cell Transformation, Viral ; Chickens/genetics ; DNA Restriction Enzymes ; Gene Expression Regulation ; *Genes, Viral ; RNA, Viral/analysis ; Viral Proteins/biosynthesis
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  • 5
    Publication Date: 1982-12-10
    Description: Simian sarcoma virus (SSV) deletion mutants were constructed from a molecular clone containing the entire infectious provirus. Transfection analysis of these mutants localized the SSV transforming gene to a small region of the viral genome encompassing its cell-derived sequence (v-sis). Antiserum to a peptide synthesized on the basis of the predicted amino acid sequence of the SSV transforming gene detected a 28,000-dalton protein that was specifically expressed in SSV transformed cells and that corresponded in size to that predicted from the v-sis coding sequence. The v-sis gene product designated p28sis was not a phosphoprotein, nor did it possess detectable protein kinase activity. These findings distinguish p28sis from a number of other retroviral onc proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Robbins, K C -- Devare, S G -- Reddy, E P -- Aaronson, S A -- New York, N.Y. -- Science. 1982 Dec 10;218(4577):1131-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6293053" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Viral ; Base Sequence ; *Cell Transformation, Viral ; *Genes, Viral ; Mice ; Molecular Weight ; *Oncogenes ; Phosphoproteins/genetics ; Protein Kinases/genetics ; Retroviridae/*genetics ; Sarcoma Virus, Woolly Monkey/*genetics ; Viral Proteins/*genetics/immunology
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-06-04
    Description: A family of related sequences that includes approximately 500,000 members is the most prominent short dispersed repeat family in primate and rodent DNA's. The primate sequence is approximately 300 base pairs in length and is composed of two imperfectly repeated monomer units, whereas the rodent repeat consists of only a single monomer. Properties of this repeat sequence, its flanking sequences in chromosomal DNA, and RNA's transcribed from it suggest that it may be a mobile DNA element inserted at hundreds of thousands of different chromosomal locations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schmid, C W -- Jelinek, W R -- New York, N.Y. -- Science. 1982 Jun 4;216(4550):1065-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6281889" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Evolution ; DNA/*genetics ; *DNA Transposable Elements ; Genetic Linkage ; Muridae/genetics ; Primates/genetics ; RNA Polymerase III/metabolism ; RNA, Heterogeneous Nuclear/genetics ; *Repetitive Sequences, Nucleic Acid ; Transcription, Genetic
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-11-12
    Description: Transfer RNA's are probably very strongly selected for translational efficiency. In this article, the argument is presented that the coding performance of the triplet anticodon is enhanced by selection of a matching anticodon loop and stem sequence. the anticodon plus these nearby sequence features (the extended anticodon) therefore contains more coding information than the anticodon alone and can perform more efficiently and accurately at the ribosome. This idea successfully accounts for the relative efficiencies of many transfer RNA's.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yarus, M -- New York, N.Y. -- Science. 1982 Nov 12;218(4573):646-52.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6753149" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Escherichia coli/genetics ; Kinetics ; Nucleic Acid Conformation ; *Protein Biosynthesis ; RNA, Transfer/*genetics ; Ribosomes/metabolism ; Structure-Activity Relationship ; Suppression, Genetic
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-06-10
    Description: A comparison between eukaryotic gene sequences and protein sequences of homologous enzymes from bacterial and mammalian organisms shows that intron-exon junctions frequently coincide with variable surface loops of the protein structures. The altered surface structures can account for functional differences among the members of a family. Sliding of the intron-exon junctions may constitute one mechanism for generating length polymorphisms and divergent sequences found in protein families. Since intron-exon junctions map to protein surfaces, the alterations mediated by sliding of these junctions can be effected without disrupting the stability of the protein core.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Craik, C S -- Rutter, W J -- Fletterick, R -- AM21344/AM/NIADDK NIH HHS/ -- AM26081/AM/NIADDK NIH HHS/ -- GM28520/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Jun 10;220(4602):1125-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344214" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Proteins ; Base Sequence ; Biological Evolution ; DNA/genetics ; Endopeptidases/genetics ; Eukaryotic Cells/metabolism ; Genes ; Genes, Bacterial ; Protein Conformation ; Proteins/*genetics ; *Serine Endopeptidases ; Tetrahydrofolate Dehydrogenase/genetics
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-06-10
    Description: An important question concerning the mechanism of somatic mutation of immunoglobulin variable (V) genes is whether it involves all of the numerous V genes in a differentiated B cell, independent of location, or if it is restricted to a particular chromosomal site. Comparison of the sequence of two alleles of a given V gene shows that the mutations are limited to the rearranged V gene, while the same V gene on the other chromosome has not undergone mutation. This indicates that a V gene sequence alone is not sufficient for somatic mutation to take place. The mutation is therefore restricted to the rearranged V gene and consequently does not occur before rearrangement.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gorski, J -- Rollini, P -- Mach, B -- New York, N.Y. -- Science. 1983 Jun 10;220(4602):1179-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6857243" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites, Antibody/*genetics ; Chromosomes/physiology ; DNA/genetics ; *Genes ; Immunoglobulin Constant Regions/genetics ; Immunoglobulin Variable Region/*genetics ; Immunoglobulins/genetics ; Lymphocytes/metabolism ; Mice ; *Mutation
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  • 10
    Publication Date: 1983-06-24
    Description: The size of the Epstein-Barr virus (EBV) nuclear antigen (EBNA) in cells infected with different EBV isolates varies directly with the size of the EBV triplet repeat array, IR3. The isolate with the largest IR3 fragment has approximately 170 more codons than the isolates with the smallest IR3 fragment; it encodes an EBNA which is approximately 17,000 daltons larger than the smallest EBNA. The EBV IR3 encodes part of a 2-kilobase exon of a latently infected cell messenger RNA which must be translated into a repetitive amino acid domain of EBNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hennessy, K -- Heller, M -- van Santen, V -- Kieff, E -- CA 17281/CA/NCI NIH HHS/ -- CA 19264/CA/NCI NIH HHS/ -- GM 07183/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 Jun 24;220(4604):1396-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6304878" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Viral/*genetics ; Base Sequence ; Cell Nucleus/immunology ; DNA, Viral/*genetics ; Epstein-Barr Virus Nuclear Antigens ; Herpesvirus 4, Human/*genetics/immunology ; Humans ; Mice ; RNA, Viral/genetics
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-02-18
    Description: Polynucleotide templates containing C (cytidine) as the major component facilitate the synthesis of oligonucleotides from mixtures of the activated mononucleotide derivatives (as indicated by structure 1 in the text). A nucleotide is incorporated into oligomeric products if and only if its complement is present in the template. The reaction has a high fidelity and produces products with mean chain lengths of six to ten nucleotides. Bases other than guanosine are incorporated within oligomers or at their 3' termini, but rarely at their 5' termini.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inoue, T -- Orgel, L E -- GM-13435/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Feb 18;219(4586):859-62.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6186026" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA-Directed RNA Polymerases/*metabolism ; Hydrogen Bonding ; Models, Chemical ; RNA/*chemical synthesis ; Templates, Genetic
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-07-01
    Description: Oligonucleotide-directed site-specific mutagenesis was applied to alter the cleavage site in the signal peptide of the major outer membrane lipoprotein of Escherichia coli. Replacing the glycine residue at the cleavage site with an alanine residue did not affect the processing of the signal peptide. However, when the same cleavage site was constructed by the deletion of the glycine residue, the signal peptide was no longer cleaved. These results indicate that stringent structural integrity at the cleavage site in the lipoprotein signal sequence is required for correct processing of prolipoprotein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inouye, S -- Hsu, C P -- Itakura, K -- Inouye, M -- GM19043/GM/NIGMS NIH HHS/ -- GM30395/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 1;221(4605):59-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344218" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Bacterial Outer Membrane Proteins ; Base Sequence ; DNA, Bacterial/metabolism ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/*metabolism ; *Escherichia coli Proteins ; Lipoproteins/*biosynthesis ; Membrane Proteins/biosynthesis ; Mutation ; Protein Precursors/*biosynthesis
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-01-07
    Description: The illustration that accompanied the review by C. C. Albritton, Jr., of W. H. Goetzmann and K. Sloan's Looking Far North (Viking, New York, 1982) in the issue of 10 December, page 1109, should have been credited to the Bancroft Library, University of California, Berkeley, as well as to the book under review.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lerman, L S -- New York, N.Y. -- Science. 1983 Jan 7;219(4580):10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6184778" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; RNA/*physiology ; RNA, Small Nuclear
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  • 14
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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〉Lewin, R -- New York, N.Y. -- Science. 1983 Mar 4;219(4588):1052-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6186029" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Nucleus/physiology ; DNA/*genetics ; Humans ; Poly A/genetics ; RNA/*genetics ; Repetitive Sequences, Nucleic Acid ; Transcription, Genetic
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  • 15
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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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  • 16
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    American Association for the Advancement of Science (AAAS)
    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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  • 17
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    American Association for the Advancement of Science (AAAS)
    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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  • 18
    Publication Date: 1983-07-15
    Description: The structure of the messenger RNA (mRNA) encoding the precursor to mouse submaxillary epidermal growth factor (EGF) was determined from the sequence of a set of overlapping complementary DNA's (cDNA). The mRNA is unexpectedly large, about 4750 nucleotide bases, and predicts the sequence of preproEGF, a protein of 1217 amino acids (133,000 molecular weight). The EGF moiety (53 amino acids) is flanked by polypeptide segments of 976 and 188 amino acids at its amino and carboyxl termini, respectively. The amino terminal segment of the precursor contains seven peptides with sequences that are similar but not identical to EGF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, J -- Urdea, M -- Quiroga, M -- Sanchez-Pescador, R -- Fong, N -- Selby, M -- Rutter, W J -- Bell, G I -- 21344/PHS HHS/ -- New York, N.Y. -- Science. 1983 Jul 15;221(4607):236-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6602382" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Epidermal Growth Factor/biosynthesis/*genetics ; Humans ; Male ; Mice ; RNA, Messenger/*genetics ; Submandibular Gland/metabolism
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  • 19
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    American Association for the Advancement of Science (AAAS)
    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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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-18
    Description: Comparison of two closely related primate papovaviruses, simian virus 40 (SV40) and human BK virus (BKV), reveals that the only region of extensive divergence, the tandem sequences adjacent to the origins of DNA replication, is responsible in SV40 for enhancing early gene expression. This study demonstrates a similar enhancer function for the analogous repeated region in BKV. The dissimilarity in sequence of the BKV and SV40 enhancer elements suggests that they may have been acquired since SV40 and BKV diverged. A locus cloned from the human genome homologous to the BKV tandem repeats has been shown to function as low level enhancer element in mammalian cells. These data support the hypothesis that viral enhancer sequences may be evolutionarily related to host cell sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosenthal, N -- Kress, M -- Gruss, P -- Khoury, G -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):749-55.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6314501" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; BK Virus/*genetics ; Base Sequence ; Biological Evolution ; DNA, Viral/*genetics ; Gene Expression Regulation ; *Genes, Regulator ; Humans ; Plasmids ; Polyomavirus/*genetics ; Repetitive Sequences, Nucleic Acid ; Species Specificity
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  • 21
    Publication Date: 1983-06-03
    Description: In order to investigate the functions of stimulus recognition, signal transduction, and adaptation, the aspartate receptor gene for bacterial chemotaxis in Salmonella typhimurium has been sequenced and modified. A carboxyl-terminal truncated receptor was shown to bind aspartate and to transmit a signal to change motility behavior. However, the truncated receptor showed greatly reduced methyl-accepting capacity, and did not allow adaptation to the sensory stimulation. The separation of receptor functions by alteration of primary structure emphasizes that the receptor is directly involved in adaptation and is not solely a device for transmitting a signal across a membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russo, A F -- Koshland, D E Jr -- New York, N.Y. -- Science. 1983 Jun 3;220(4601):1016-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6302843" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Amino Acid Sequence ; Aspartic Acid ; *Bacterial Physiological Phenomena ; Base Sequence ; *Chemotaxis ; Escherichia coli/physiology ; Methylation ; *Receptors, Amino Acid ; Receptors, Cell Surface/genetics/*physiology ; Salmonella typhimurium/physiology ; Serine
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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-18
    Description: Insertion sequences (IS) are discrete segments of DNA that can transpose from one genomic site to another and promote genetic rearrangements. A question that is central to understanding the mechanism of transpositional recombination is whether genetic rearrangements are accompanied by duplication of the IS that promotes them. Analysis of adjacent deletions mediated by IS903 provides the strongest evidence to date than any IS-mediated transpositional recombination can occur by an efficient replicative mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weinert, T A -- Schaus, N A -- Grindley, N D -- GM28470/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):755-65.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6314502" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Deletion ; *DNA Transposable Elements ; DNA, Bacterial/*genetics ; Plasmids ; *Recombination, Genetic ; Repetitive Sequences, Nucleic Acid
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  • 23
    Publication Date: 1982-12-17
    Description: A 311-base pair fragment containing the SV40 origin of replication was linked to the chicken thymidine kinase gene on a recombinant plasmid. This molecule was transfected into human 143 thymidine kinase-deficient (TK-) cells, and colonies positive for thymidine kinase were selected. When cell lines derived from these colonies were fused to permissive simian cells that produce SV40 T antigen, the recombinant plasmid excised itself from the human cellular genome and replicated with a high copy number per cell. These results show that this segment of the viral genome is the only sequence required in cis to mediate SV40 excision and replication upon fusion to permissive cells. In addition, we have shown that excised plasmids apparently identical to the input DNA can be efficiently rescued in Escherichia coli. SV40 excision and replication may therefore be useful for the recovery of cloned genes from eukaryotic cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Conrad, S E -- Liu, C P -- Botchan, M R -- CA 30490/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1982 Dec 17;218(4578):1223-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6293055" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cells, Cultured ; Chickens ; *DNA Replication ; DNA, Viral/*genetics ; Gene Expression Regulation ; Genes, Viral ; Humans ; Recombination, Genetic ; Simian virus 40/*genetics ; *Virus Replication
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  • 24
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-08-27
    Description: Cellular genes potentially capable of inducing oncogenic transformation have been identified by homology to the transforming genes of retroviruses and by the biological activity of cellular DNA's in transfection assays. DNA's of various tumors induce transformation with high efficiencies, indicating that oncogenesis can involve dominant genetic alterations resulting in activation of cellular transforming genes. The identification and characterization of cellular transforming genes and their possible involvement in naturally occurring cancers, is discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cooper, G M -- New York, N.Y. -- Science. 1982 Aug 27;217(4562):801-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6285471" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Cell Transformation, Neoplastic ; Cells, Cultured ; Chick Embryo ; DNA/genetics ; DNA Restriction Enzymes ; DNA, Viral/genetics ; Gene Expression Regulation ; *Genes ; Genes, Viral ; Humans ; Mice ; Neoplasms/*genetics ; Oncogene Protein pp60(v-src) ; Rats ; Retroviridae/*genetics ; Transfection ; Viral Proteins/genetics
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  • 25
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-07-02
    Description: Research on the early development of the sea urchin offers new insights into the process of embryogenesis. Maternal messenger RNA stored in the unfertilized egg supports most of the protein synthesis in the early embryo, but the structure of maternal transcripts suggests that additional functions are also possible. The overall developmental patterns of transcription and protein synthesis are known, and current measurements describe the expression of specific genes, including the histone genes, the ribosomal genes, and the actin genes. Possible mechanisms of developmental commitment are explored for regions of the early embryo that give rise to specified cell lineages, such as the micromere-mesenchyme cell lineage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davidson, E H -- Hough-Evans, B R -- Britten, R J -- GM20927/GM/NIGMS NIH HHS/ -- HD05753/HD/NICHD NIH HHS/ -- RR00986/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1982 Jul 2;217(4554):17-26.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6178156" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/genetics ; Animals ; Base Sequence ; Blastocyst/physiology ; Embryo, Nonmammalian/*physiology ; Female ; Fertilization ; Gastrula/physiology ; Histones/genetics ; Kinetics ; Larva/physiology ; Polyribosomes/metabolism ; RNA/genetics ; RNA, Messenger/genetics ; Ribosomal Proteins/genetics ; Sea Urchins/*physiology ; Transcription, Genetic
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  • 26
    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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  • 27
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-08-20
    Description: An extensive computer-assisted analysis of known pre-proinsulin coding sequences has shown correlations that can be interpreted as evidence for an intron-mediated juxtaposition of exons in the evolution of these genes. The evidence includes the discovery that the regions of the pre-proinsulin genes that code for the signal peptide consist of nearly tandem repeating units of nine base pairs. This pattern reappears in the C region of the genes after a large intron that occurs in three of the four genes analyzed. A model is proposed in which primordial insulin was coded for by two separate minigenes arising from a gene duplication, each with identical or nearly identical signal peptide coding regions. The minigenes fused into one transcriptional unit mediated by the large intron, and the signal peptide coding region of one of the putative minigenes evolved into the latter portion of the C peptide coding region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Douthart, R J -- Norris, F H -- New York, N.Y. -- Science. 1982 Aug 20;217(4561):729-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7100918" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Biological Evolution ; Computers ; Cricetinae ; Disulfides ; Genes ; Humans ; Insulin ; Models, Genetic ; Proinsulin/*genetics ; Protein Precursors/*genetics ; Rats ; Repetitive Sequences, Nucleic Acid
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-07-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1982 Jul 30;217(4558):434-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6283636" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA, Recombinant ; *Gene Expression Regulation ; Genes ; Genes, Regulator ; *Mutation ; RNA, Messenger ; Simplexvirus/genetics ; Thymidine Kinase/genetics ; *Transcription, Genetic
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  • 29
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-07-23
    Description: Transcriptional control signals of a model eukaryotic protein-coding gene have been identified by a new procedure of in vitro mutagenesis. This method allows small clusters of nucleotide residues to be substituted in a site-directed manner without causing the addition or deletion of other sequences. Transcription assays of a systematic series of these clustered point mutants have led to the identification of three distinct control signals located within the 105-nucleotide residues immediately upstream from the point where transcription begins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McKnight, S L -- Kingsbury, R -- New York, N.Y. -- Science. 1982 Jul 23;217(4557):316-24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6283634" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA, Recombinant ; *Gene Expression Regulation ; Genes ; Genes, Regulator ; *Mutation ; RNA, Messenger/analysis ; Simplexvirus/genetics ; Thymidine Kinase/genetics ; *Transcription, Genetic
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  • 30
    Publication Date: 1982-12-17
    Description: A 3.4-kilobase DNA fragment containing the gene coding for the E alpha chain of an Ia (I region-associated) antigen from the BALB/c mouse has been sequenced. It contains at least three exons, which correlate with the major structural domains of the E alpha chain-the two external domains alpha 1 and alpha 2, and the transmembrane-cytoplasmic domain. The coding sequence of the mouse E alpha gene shows striking homology to its counterpart at the DNA and protein levels. The translated alpha 2 exon demonstrates significant similarity to beta 2-microglobulin, to immunoglobulin constant region domains, and to certain domains of transplantation antigens. These observations and those of others suggest that the Ia antigen, transplantation antigen, and immunoglobulin gene families share a common ancestor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McNicholas, J -- Steinmetz, M -- Hunkapiller, T -- Jones, P -- Hood, L -- New York, N.Y. -- Science. 1982 Dec 17;218(4578):1229-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6815800" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Evolution ; Genes ; *Genes, MHC Class II ; Macromolecular Substances ; Mice ; Mice, Inbred BALB C/*genetics ; beta 2-Microglobulin/genetics
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  • 31
    Publication Date: 1982-02-05
    Description: The sequence of a gene, denoted 27.5, encoding a transplantation antigen for the BALB/c mouse has been determined. Gene transfer studies and comparison of the translated sequence with the partial amino acid sequence of the Ld transplantation antigen establish that gene 27.5 encodes an Ld polypeptide. A comparison of the gene 27.5 sequence with several complementary DNA sequences suggests that the BALB/c mouse may contain a number of closely related L-like genes. Gene 27.5 has eight exons that correlate with the structural domains of the transplantation antigen.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, K W -- Sher, B T -- Sun, Y H -- Eakle, K A -- Hood, L -- 1 T32 GM07616/GM/NIGMS NIH HHS/ -- GM 06965/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 Feb 5;215(4533):679-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7058332" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular/methods ; Genes ; H-2 Antigens/*genetics ; *Major Histocompatibility Complex ; Mice ; Mice, Inbred BALB C/*genetics ; Plasmids ; Repetitive Sequences, Nucleic Acid
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  • 32
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-05-07
    Description: The conformation and dynamics of the d(CGCGAATTCGCG) duplex, its analogs containing mismatched base pairs and helix interruptions, and its complexes with actinomycin and Netropsin, bound separately and simultaneously, have been investigated by nuclear magnetic resonance spectroscopy in aqueous solution. Structural information has been deduced from chemical shift and nuclear Overhauser effect parameters, while the kinetics have been probed from line width and saturation recovery experiments on proton and phosphorus markers at the individual base pair level. These studies lead to an improved understanding of the role of nucleic acid sequence on the structure, flexibility, and conformational interconversions in the duplex state. The nuclear magnetic resonance measurements readily identify helix modification and antibiotic binding sites on the nucleic acid and estimate the extent to which the observed conformational and dynamic perturbations are transmitted to adjacent base pair regions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Patel, D J -- Pardi, A -- Itakura, K -- New York, N.Y. -- Science. 1982 May 7;216(4546):581-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6280281" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Dna ; Dactinomycin ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Motion ; Netropsin ; *Nucleic Acid Conformation ; Oligodeoxyribonucleotides ; Protons ; Structure-Activity Relationship ; Temperature
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  • 33
    Publication Date: 1982-10-22
    Description: The protein coding region of the herpes simplex virus type-1 glycoprotein D (gD) gene was mapped, and the nucleotide sequence was determined. The predicted amino acid sequence of the gD polypeptide was found to contain a number of features in common with other virus glycoproteins. Insertion of this protein coding region into a bacterial expressor plasmid enabled synthesis in Escherichia coli of an immunoreactive gD-related polypeptide. The potential of this system for preparation of a type-common herpes simplex virus vaccine is discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watson, R J -- Weis, J H -- Salstrom, J S -- Enquist, L W -- New York, N.Y. -- Science. 1982 Oct 22;218(4570):381-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6289440" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/genetics ; Base Sequence ; Escherichia coli/genetics ; Gene Expression Regulation ; Genes ; Genes, Viral ; Glycoproteins/*genetics ; Peptides/genetics ; Protein Sorting Signals ; Simplexvirus/*genetics ; Viral Proteins/*genetics/immunology ; Viral Vaccines
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  • 34
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-08-26
    Description: One variant of a complex satellite DNA of the Bermuda land crab is significantly longer than the average repeat unit of the satellite. The extra DNA in the variant is accounted for by a fivefold tandem amplification of a 0.142-kilobase sequence. The amplified sequence is bounded by a tetranucleotide inverted repeat; the upstream arm of the inverted repeat is missing from two other variants of the satellite. The latter variants contain only one copy of a sequence that is closely related to the amplified sequence. By contrast, in several satellite DNA's of other organisms, extra DNA is inserted.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonnewell, V -- Fowler, R F -- Skinner, D M -- New York, N.Y. -- Science. 1983 Aug 26;221(4613):862-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6879182" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Brachyura/genetics ; Chromosome Inversion ; DNA, Satellite/*genetics ; *Gene Amplification ; Nucleic Acid Conformation
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  • 35
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-08-06
    Description: The sequence of two human beta-tubulin pseudogenes is described. One contains an intervening sequence but lacks sequences encoding the 55 N-terminal amino acids of the polypeptide chain. A second has no introns but has a polyadenylate signal and an oligoadenylate tract at its 3' end, and it is flanked by a short direct repeat. These sequences have arisen by different mechanisms, including one that probably involves reverse transcription of a processed messenger RNA and reintegration of the complementary DNA copy into the genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilde, C D -- Crowther, C E -- Cowan, N J -- GM26456/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 Aug 6;217(4559):549.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6178164" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/analysis ; DNA Restriction Enzymes ; DNA Transposable Elements ; DNA, Recombinant ; *Gene Expression Regulation ; Humans ; Nucleic Acid Hybridization ; Poly A/genetics ; RNA Splicing ; RNA-Directed DNA Polymerase/metabolism ; Recombination, Genetic ; Tubulin/*genetics
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  • 36
    Publication Date: 1983-07-15
    Description: The polymorphism of immune response genes plays a critical role in determining the immune capabilities of a particular individual. The molecular nature of this polymorphism was studied by examining the structure of the coding portions of three alleles of the I-A beta chain gene, an immune response gene whose protein product constitutes a subunit of the I-A molecule. Comparison of the I-A beta chains encoded by these alleles revealed an amino acid sequence divergence of 5 to 8 percent. The differences were found to be a series of short alterations clustered in the amino terminal half of the polypeptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Choi, E -- McIntyre, K -- Germain, R N -- Seidman, J G -- AI18436/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 15;221(4607):283-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6407114" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; *Genes, MHC Class II ; Histocompatibility Antigens Class II/immunology ; Humans ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; *Polymorphism, Genetic
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  • 37
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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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  • 38
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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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  • 39
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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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  • 40
    Publication Date: 1982-09-10
    Description: Foreign gene sequences were retained in two adult mice (out of 62 analyzed) from fertilized eggs injected with a recombinant plasmid containing the human beta-globin genomic region and the herpes simplex viral thymidine kinase gene. The intact human and viral genes were found in DNA of one of the animals and, in the other, at least part of the human globin gene was present. The latter individual transmitted these sequences to its progeny in a Mendelian ration. Thus, human DNA may be incorporated into the germ line of mice for in vivo studies of regulation of gene expression in development, genetic diseases, and malignancy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steward, T A -- Wagner, E F -- Mintz, B -- CA-60927/CA/NCI NIH HHS/ -- HD-01646/HD/NICHD NIH HHS/ -- RR-05539/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1982 Sep 10;217(4564):1046-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6287575" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA/genetics ; DNA Restriction Enzymes ; DNA, Recombinant ; Female ; Genes ; Genes, Viral ; Germ Cells ; Globins/*genetics ; Humans ; Mice ; Microinjections ; Nucleic Acid Hybridization ; *Recombination, Genetic ; Simplexvirus/enzymology ; Thymidine Kinase/genetics ; Zygote
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-10-22
    Description: Recombinant DNA carrying the 3-kilobase transposable element was injected into Drosophila embryos of a strain that lacked such elements. Under optimum conditions, half of the surviving embryos showed evidence of P element-induced mutations in a fraction of their progeny. Direct analysis of the DNA of strains derived from such flies showed them to contain from one to five intact 3-kilobase P elements located at a wide variety of chromosomal sites. DNA sequences located outside the P element on the injected DNA were not transferred. Thus P elements can efficiently and selectively transpose from extrachromosomal DNA to the DNA of germ line chromosomes in Drosophila embryos. These observations provide the basis for efficient DNA-mediated gene transfer in Drosophila.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Spradling, A C -- Rubin, G M -- New York, N.Y. -- Science. 1982 Oct 22;218(4570):341-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6289435" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosome Mapping ; *DNA Transposable Elements ; Drosophila melanogaster/*genetics ; Female ; Genes ; Genetic Linkage ; Hybridization, Genetic ; Male ; *Mutation ; Nucleic Acid Hybridization ; Recombination, Genetic
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  • 42
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    American Association for the Advancement of Science (AAAS)
    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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  • 43
    Publication Date: 1983-11-04
    Description: The gene for glycoprotein D of herpes simplex virus type 1 (HSV-1) was expressed in stable mammalian cell lines. Glycoprotein D produced in these cells has a number of antigenic determinants in common with the native glycoprotein. Cell lines expressing glycoprotein D were used in an enzyme-linked immunosorbent assay to detect human antibodies to glycoprotein D. This strategy should prove useful in determining the extent to which the immune response to HSV-1 is directed toward glycoprotein D.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berman, P W -- Dowbenko, D -- Lasky, L A -- Simonsen, C C -- New York, N.Y. -- Science. 1983 Nov 4;222(4623):524-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6312563" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Viral/*analysis ; Base Sequence ; Cell Line ; Clone Cells ; DNA Restriction Enzymes ; DNA, Viral/genetics ; Enzyme-Linked Immunosorbent Assay ; *Genes ; *Genes, Viral ; Humans ; Plasmids ; Simplexvirus/genetics/*immunology ; Tetrahydrofolate Dehydrogenase/genetics ; *Viral Envelope Proteins ; Viral Proteins/*genetics/immunology
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1983 Nov 25;222(4626):915.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6314505" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *DNA Transposable Elements ; Viroids/*genetics
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  • 45
    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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  • 46
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-06-24
    Description: Human G gamma-globin genes containing tandem duplications of the donor (5') or acceptor (3') RNA splice sites of the second intervening sequence were constructed in order to ascertain the directionality of RNA splice site selection. These genes were introduced into cultured monkey cells, and their transcripts were analyzed. Transcripts of these duplication variants were spliced only at the proximal copy of the duplicated splice sites. These data are consistent with a 5' leads to 3' model of splice site selection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lang, K M -- Spritz, R A -- AM28598/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1983 Jun 24;220(4604):1351-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6304877" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cells, Cultured ; Globins/genetics ; Haplorhini ; Humans ; Plasmids ; *RNA Splicing ; RNA, Messenger/genetics/physiology ; Simian virus 40/genetics ; Transcription, Genetic
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  • 47
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-07-08
    Description: The nucleotide sequence of the oncogene of the Rasheed strain of rat sarcoma virus was determined. The oncogene (Ra-v-ras) encodes a 29,000-dalton (p29) transforming protein. This protein is distinct from the immunologically related 21,000-dalton protein (p21) of the Harvey murine sarcoma virus in its amino terminus and in having additional mutations in its carboxyl terminus. Although the functional significance of these changes is unknown, they appear to occur only in rat sarcoma virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rasheed, S -- Norman, G L -- Heidecker, G -- CA 27246/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 8;221(4606):155-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344220" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Mice ; Neoplasm Proteins/genetics ; *Oncogenes ; Proto-Oncogene Proteins p21(ras) ; Rats ; Retroviridae/*genetics
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  • 48
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-06-03
    Description: The nucleotide sequence of the T24 human bladder carcinoma oncogene was determined, and the coding and noncoding sequences of the genome were identified. The amino acid sequence of p21, the translational product of the T24 oncogene, was predicted from the nucleotide sequence of the oncogene. Comparison of this sequence with that of the normal cellular homolog showed that a single point mutation in the coding sequences of the T24 oncogene resulted in the acquisition of transforming properties. Other differences between the T24 oncogene and its normal cellular homolog were found in the 5' noncoding and 3' noncoding sequences, but these differences appear to be due to polymorphism and do not play a significant role in the transformation process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reddy, E P -- New York, N.Y. -- Science. 1983 Jun 3;220(4601):1061-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6844927" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carcinoma/*genetics ; Cell Transformation, Neoplastic/metabolism ; Humans ; Mice ; Neoplasm Proteins/genetics ; *Oncogenes ; Oncogenic Viruses/genetics ; Rats ; Urinary Bladder Neoplasms/*genetics
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  • 49
    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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  • 50
    Publication Date: 1983-05-13
    Description: A recombinant bacterial plasmid, pMS1, was constructed that contains 318 nucleotides complementary to a portion of pro-opiolipomelanocortin (proOLMC) messenger RNA from an ectopic adrenocorticotropin-producing tumor. The cloned complementary DNA insert, which contains the sequence that codes for all of the beta-melanocyte-stimulating hormone and beta-endorphin portions of proOLMC, as well as the 3' nontranslated section, is identical to the genomic sequence. Hybridization of tumor proOLMC complementary DNA to RNA subjected to electrophoresis and transferred to a nitrocellulose filter revealed two proOLMC messenger RNA species in the tumor polyadenylated RNA, but only one in pituitary polyadenylated RNA. At least one of the tumor proOLMC messenger RNA's is similar, if not identical, to human pituitary proOLMC messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeBold, C R -- Schworer, M E -- Connor, T B -- Bird, R E -- Orth, D N -- 2-R01-GM25526/GM/NIGMS NIH HHS/ -- 5-R01-CA11685/CA/NCI NIH HHS/ -- 5-R25-CA19429/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 May 13;220(4598):721-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6301015" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Carcinoid Tumor/physiopathology ; Cloning, Molecular ; DNA, Neoplasm/genetics ; DNA, Recombinant/*metabolism ; Endorphins/*genetics ; Hormones, Ectopic/*genetics ; Humans ; Male ; Melanocyte-Stimulating Hormones/*genetics ; Middle Aged ; Pancreatic Neoplasms/physiopathology ; Pituitary Hormones, Anterior/*genetics ; Pro-Opiomelanocortin ; Protein Precursors/*genetics ; RNA, Messenger/genetics ; beta-Endorphin
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  • 51
    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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  • 52
    Publication Date: 1983-02-04
    Description: The 5' nucleotide sequences of the transforming gene of simian sarcoma virus (v-sis) and its human cellular homolog (c-sis) were compared. A short homology was found between helper virus and cellular DNA sequences at the junction of v-sis and c-sis, which may have had a role in the original recombination event leading to the generation of simian sarcoma virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Josephs, S F -- Dalla-Favera, R -- Gelmann, E P -- Gallo, R C -- Wong-Staal, F -- New York, N.Y. -- Science. 1983 Feb 4;219(4584):503-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6297002" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Genes, Viral ; Helper Viruses/genetics ; Humans ; *Oncogenes ; Recombination, Genetic ; Retroviridae/*genetics ; Sarcoma Virus, Woolly Monkey/*genetics
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  • 53
    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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  • 54
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-07-22
    Description: Nucleotide sequences of translated regions of the trp operon in 12 wild strains of Escherichia coli reveal striking uniformity among eight strains (suggesting recent common ancestry and supporting the importance of periodic selection in natural populations) and clustered substitutions in four strains (implicating events affecting runs of nucleotides).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milkman, R -- Crawford, I P -- New York, N.Y. -- Science. 1983 Jul 22;221(4608):378-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6346486" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA, Bacterial/genetics ; Escherichia coli/*genetics ; Genes, Bacterial
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  • 55
    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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  • 56
    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
    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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