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  • Base Sequence  (23)
  • American Association for the Advancement of Science (AAAS)  (23)
  • 1980-1984  (23)
  • 1925-1929
  • 1982  (23)
Collection
Keywords
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  • American Association for the Advancement of Science (AAAS)  (23)
Years
  • 1980-1984  (23)
  • 1925-1929
Year
  • 1
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    alpha A-crystallin messenger RNA of the mouse lens: more noncoding than coding sequences (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-02-19
    Description: The 14S messenger RNA (1300 to 1500 nucleotides) for the alpha A chain of alpha-crystallin of the mammalian lens is nearly three times larger than required to code for the polypeptide that contains 173 amino acids. As a means of accounting for this anomaly, a complementary DNA clone for the mouse alpha A-crystallin messenger RNA was constructed in pBR322 and sequenced. Derivation of the protein sequence from the nucleic acid sequence showed that mouse alpha A-crystallin is similar to that of other organisms. The messenger RNA contains 536 nucleotides located on the 3' side of the coding region, excluding the polyadenylate stretch. This 3' sequence does not encode any other crystallin and has multiple termination codons in the three possible reading frames.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, C R -- Shinohara, T -- Piatigorsky, J -- New York, N.Y. -- Science. 1982 Feb 19;215(4535):985-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7156978" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; Crystallins/*genetics ; Mice ; RNA, Messenger/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Long-awaited decision on DNA database (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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  • 3
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    Repeated DNA still in search of a function (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 4
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    Nucleotide sequence of the transforming gene of avian myeloblastosis virus (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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  • 5
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    In vivo identification of the transforming gene product of simian sarcoma virus (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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  • 6
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    The Alu family of dispersed repetitive sequences (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Translational efficiency of transfer RNA's: uses of an extended anticodon (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Fragment spanning the SV40 replication origin is the only DNA sequence required in cis for viral excision (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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  • 9
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    Cellular transforming genes (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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  • 10
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    Molecular biology of the sea urchin embryo (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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  • 11
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    Nucleotide sequence of the p21 transforming protein of Harvey murine sarcoma virus (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 12
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    Events in the evolution of pre-proinsulin (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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  • 13
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    Gene scanning with block mutations (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 14
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    Transcriptional control signals of a eukaryotic protein-coding gene (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 15
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    DNA sequence of the gene encoding the E alpha Ia polypeptide of the BALB/c mouse (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 16
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    DNA sequence of a gene encoding a BALB/c mouse Ld transplantation antigen (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 17
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    DNA conformation, dynamics, and interactions in solution (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 18
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    Herpes simplex virus type-1 glycoprotein D gene: nucleotide sequence and expression in Escherichia coli (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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  • 19
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    Diverse mechanisms in the generation of human beta-tubulin pseudogenes (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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  • 20
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    Human beta-globin gene sequences injected into mouse eggs, retained in adults, and transmitted to progeny (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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  • 21
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    Transposition of cloned P elements into Drosophila germ line chromosomes (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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  • 22
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    Form and function of retroviral proviruses (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-05-21
    Description: Retroviruses have proved to be useful reagents for studying genetic and epigenetic (such as regulatory) changes in eukaryotic cells, for assessing functional and structural relationships between transposable genetic elements, for inducing insertional mutations, including some important in oncogenesis, and for transporting genes into eukaryotic cells, either after natural transduction of putative cellular oncogenes or after experimental construction of recombinant viruses. Many of these properties of retroviruses depend on their capacity to establish a DNA (proviral) form of their RNA genomes as a stable component of host chromosomes, in either somatic or germinal cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Varmus, H E -- New York, N.Y. -- Science. 1982 May 21;216(4548):812-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6177038" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA Transposable Elements ; DNA, Viral/biosynthesis/genetics ; Gene Expression Regulation ; Genes, Viral ; Genetic Vectors ; Mutation ; RNA-Directed DNA Polymerase/metabolism ; Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; Retroviridae/*physiology ; Transcription, Genetic ; Virus Replication
    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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  • 23
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    Nucleotide sequence of the oncogene encoding the p21 transforming protein of Kirsten murine sarcoma virus (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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