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  • Gene Expression Regulation  (45)
  • American Association for the Advancement of Science (AAAS)  (45)
  • American Chemical Society
  • National Academy of Sciences
  • Oxford University Press
  • 1985-1989  (25)
  • 1980-1984  (20)
  • 1965-1969
  • 1985  (25)
  • 1983  (20)
  • 1965
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (45)
  • American Chemical Society
  • National Academy of Sciences
  • Oxford University Press
Years
  • 1985-1989  (25)
  • 1980-1984  (20)
  • 1965-1969
Year
  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fox, J L -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):828-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6138857" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*physiology ; DNA, Recombinant ; Gene Expression Regulation ; Nerve Tissue Proteins/*genetics ; Neurotransmitter Agents/*physiology ; Rats
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-02-11
    Description: Plasmids were constructed to direct synthesis of the human interferons IFN-alpha 1, IFN-alpha 2, and IFN-gamma in the yeast Saccharomyces cerevisiae. Expression of IFN genes containing coding sequences for secretion signals resulted in the secretion of IFN activity. A large proportion of the IFN-alpha 1 and IFN-alpha 2 isolated from the yeast cell growth media had the same amino termini as the natural mature interferons, suggesting a removal of the signal sequences identical to that of human cells. These results show that a lower eukaryote, such as yeast, can utilize and process a human signal sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hitzeman, R A -- Leung, D W -- Perry, L J -- Kohr, W J -- Levine, H L -- Goeddel, D V -- New York, N.Y. -- Science. 1983 Feb 11;219(4585):620-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6186023" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; Gene Expression Regulation ; Humans ; Interferons/*genetics/secretion ; Peptides/physiology ; Plasmids ; Protein Processing, Post-Translational ; Protein Sorting Signals ; RNA Processing, Post-Transcriptional ; Saccharomyces cerevisiae/genetics
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  • 3
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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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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-08-19
    Description: The structural gene for group A streptococcal M protein, the fibrillar surface molecule enabling the organism to resist phagocytosis, has been cloned into Escherichia coli. The molecule produced by Escherichia coli is slightly larger than the M protein isolated by solubilization of the streptococcal cell wall, but is similar in size to that secreted by streptococcal protoplast and L forms. Immunologically, the molecule synthesized by Escherichia coli has the same type-specific determinants as the streptococcal M protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, J R -- Fischetti, V A -- AI11822/AI/NIAID NIH HHS/ -- RR05364/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1983 Aug 19;221(4612):758-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6192499" target="_blank"〉PubMed〈/a〉
    Keywords: *Antigens, Bacterial ; *Bacterial Outer Membrane Proteins ; Bacterial Proteins/*genetics/immunology ; *Carrier Proteins ; Cloning, Molecular ; Epitopes ; Escherichia coli/*genetics ; Gene Expression Regulation ; Molecular Weight
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  • 5
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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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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-10-14
    Description: A modified cloning method designed to produce differential complementary DNA libraries permits the isolation of sequences that are present in the RNA population of any developmental stage or tissue, but are not present or are much less abundant in another stage or tissue. Selective complementary DNA cloning is especially useful when the differentially expressed RNA's are of low to moderate abundance in the cells in which they occur. A class of cytoplasmic polyadenylated RNA's differentially expressed in gastrula embryos of Xenopus laevis (DG RNA's) has been isolated. These DG RNA's occur very rarely or not at all in unfertilized eggs and blastulae, accumulate as the result of transcription before and during gastrulation, and, with some exceptions, decline in abundance as development proceeds. Many of these RNA molecules appear to be translated at the gastrula stage. Thus, DG RNA's may encode proteins that are important in the process of gastrulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sargent, T D -- Dawid, I B -- New York, N.Y. -- Science. 1983 Oct 14;222(4620):135-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6688681" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/genetics ; Gastrula/*physiology ; Gene Expression Regulation ; Nucleic Acid Hybridization ; Polyribosomes/metabolism ; Protein Biosynthesis ; Transcription, Genetic ; Xenopus laevis/*embryology/genetics
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  • 7
    Publication Date: 1983-08-19
    Description: A genomic clone consisting of the Moloney leukemia proviral genome with moderately repetitive mouse sequences was microinjected into the pronucleus of a mouse zygote. An animal was derived that carried multiple copies of proviral DNA in a tandem array. No evidence for homologous recombination was obtained. The viral genome was expressed in this animal and was transmitted as a single unit to its offspring. Subsequent breeding studies revealed that the proviral DNA had integrated on an X chromosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stewart, C -- Harbers, K -- Jahner, D -- Jaenisch, R -- New York, N.Y. -- Science. 1983 Aug 19;221(4612):760-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6683871" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/physiology ; Female ; Gene Expression Regulation ; Genes, Viral ; Mice ; Microinjections ; Moloney murine leukemia virus/*genetics ; Recombination, Genetic ; Sex Chromosomes/*physiology ; X Chromosome/*physiology
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-09-09
    Description: The structures of three proteins that regulate gene expression have been determined recently and suggest how these proteins may bind to their specific recognition sites on the DNA. One protein (Cro) is a repressor of gene expression, the second (CAP) usually stimulates gene expression, and the third (lambda repressor) can act as either a repressor or an activator. The three proteins contain a substructure consisting of two consecutive alpha helices that is virtually identical in each case. Structural and amino acid sequence comparisons suggest that this bihelical fold occurs in a number of proteins that regulate gene expression, and is an intrinsic part of the DNA-protein recognition event. The modes of repression and activation by Cro and lambda repressor are understood reasonably well, but the mode of action of CAP is still unclear.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takeda, Y -- Ohlendorf, D H -- Anderson, W F -- Matthews, B W -- GM20066/GM/NIGMS NIH HHS/ -- GM28138/GM/NIGMS NIH HHS/ -- GM30894/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Sep 9;221(4615):1020-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6308768" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chemical Phenomena ; Chemistry ; *DNA Helicases ; DNA-Binding Proteins ; Escherichia coli/genetics ; Gene Expression Regulation ; Models, Chemical ; Protein Conformation
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  • 9
    Publication Date: 1983-10-28
    Description: Burkitt lymphoma cells carrying either a rearranged or unrearranged c-myc oncogene were examined with the use of probes from the 5' exon and for the second and third exon of the oncogene. The results indicate that the normal c-myc gene on chromosome 8 and the 5' noncoding and 3' coding segments of the c-myc oncogene separated by the chromosomal translocation are under different transcriptional control in the lymphoma cells. Burkitt lymphoma cells carrying a translocated but unrearranged c-myc oncogene express normal c-myc transcripts. In contrast, lymphoma cells carrying a c-myc gene rearranged head to head with the immunoglobulin constant mu region gene express c-myc transcripts lacking the normal untranslated leader.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉ar-Rushdi, A -- Nishikura, K -- Erikson, J -- Watt, R -- Rovera, G -- Croce, C M -- CA09171/CA/NCI NIH HHS/ -- CA10815/CA/NCI NIH HHS/ -- CA16685/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 Oct 28;222(4622):390-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6414084" target="_blank"〉PubMed〈/a〉
    Keywords: Burkitt Lymphoma/*genetics ; Chromosomes, Human, 13-15 ; Chromosomes, Human, 19-20 ; Chromosomes, Human, 6-12 and X ; Gene Expression Regulation ; Genes ; Humans ; Immunoglobulin Heavy Chains/genetics ; *Oncogenes ; Operon ; Transcription, Genetic ; Translocation, Genetic
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  • 10
    Publication Date: 1983-02-25
    Description: The locus for the cellular myc (c-myc) oncogene in humans is located on the region of chromosome 8 that is translocated to chromosome 14 in cells from most undifferentiated B-cell lymphomas. It is shown in this study that the c-myc locus is rearranged in 5 out of 15 cell lines from patients with undifferentiated B-cell lymphomas, and that the rearrangement involves a region at the 5' side of an apparently intact c-myc gene. In at least three patients, this rearranged region appears to contain immunoglobulin heavy chain mu sequences that are located on chromosome 14. The data indicate that this region contains the crossover point between chromosomes 8 and 14. The break point can occur at different positions on both chromosomes among individual cell lines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dalla-Favera, R -- Martinotti, S -- Gallo, R C -- Erikson, J -- Croce, C M -- New York, N.Y. -- Science. 1983 Feb 25;219(4587):963-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6401867" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocytes/*physiology ; Cell Differentiation ; Chromosome Mapping ; Gene Expression Regulation ; Genes ; Genetic Linkage ; Humans ; Immunoglobulin Constant Regions/genetics ; Immunoglobulin Heavy Chains/genetics ; Lymphoma/*genetics ; *Oncogenes ; Recombination, Genetic
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  • 11
    Publication Date: 1983-10-28
    Description: Antiserum to a synthetic peptide corresponding to the carboxyl-terminus of the human c-myc protein immunoprecipitated a 48,000-dalton protein from a number of normal and malignant human and mouse cells. The size of the protein is consistent with the potential coding region predicted from the c-myc nucleotide sequence, and is the same for malignant cells carrying either a rearranged or an unrearranged c-myc oncogene. Because c-myc transcripts are expressed at higher levels in malignant than in normal B cells, it appears that an increased level of the c-myc protein rather than a change in the gene product is the relevant factor in determining transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Giallongo, A -- Appella, E -- Ricciardi, R -- Rovera, G -- Croce, C M -- CA10815/CA/NCI NIH HHS/ -- CA16685/CA/NCI NIH HHS/ -- CA25685/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1983 Oct 28;222(4622):430-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6604943" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocytes/*physiology ; Burkitt Lymphoma/*genetics ; Gene Expression Regulation ; Humans ; *Oncogenes ; Peptide Fragments/immunology ; Proteins/immunology/*isolation & purification ; Transformation, Genetic
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-18
    Description: Class III genes require multiple cellular factors for transcription by RNA polymerase III; these genes form stable transcription complexes, which in the case of Xenopus 5S genes are correlated with differential expression in vivo. The minimal number and identity of the factors required to form both stable and metastable complexes on three class III genes (encoding, respectively, 5S RNA, transfer RNA, and adenovirus VA RNA species) were determined. Stable complex formation requires one common factor, whose recognition site was analyzed, and either no additional factors (the VA gene), a second common factor (the transfer RNA gene), or a third gene-specific factor (the 5S gene). The mechanism of stable complex formation and its relevance to transcriptional regulation were examined in light of the various factors and the promoter sequences recognized by these factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lassar, A B -- Martin, P L -- Roeder, R G -- CA 24223/CA/NCI NIH HHS/ -- CA 24891/CA/NCI NIH HHS/ -- GM07200/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):740-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356356" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA-Directed RNA Polymerases/*genetics ; Eukaryotic Cells/physiology ; Gene Expression Regulation ; Genes ; Humans ; Operon ; RNA Polymerase III/*genetics ; RNA, Ribosomal/genetics ; RNA, Transfer/genetics ; RNA, Viral/genetics ; Transcription Factors/genetics ; *Transcription, Genetic
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-09-02
    Description: Development proceeds by way of a discrete yet overlapping series of biosynthetic and restructuring events that result in the continued molding of tissues and organs into highly restricted and specialized states required for adult function. Individual molecules and cells are replaced by molecular and cellular variants, called isoforms; these arise and function during embryonic development or later life. Isoforms, whether molecular or cellular, have been identified by their structural differences, which allow separation and characterization of each variant. These isoforms play a central and controlling role in the continued and dynamic remodeling that takes place during development. Descriptions of the individual phases of the orderly replacement of one isoform for another provides an experimental context in which the process of development can be better understood.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Caplan, A I -- Fiszman, M Y -- Eppenberger, H M -- New York, N.Y. -- Science. 1983 Sep 2;221(4614):921-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6348946" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/physiology ; Animals ; Bone Development ; Cartilage/*embryology ; Cell Differentiation ; Creatine Kinase/physiology ; Extracellular Space/physiology ; Gene Expression Regulation ; Humans ; Muscle Contraction ; Muscles/cytology/*embryology ; Myosins/physiology ; Phosphoproteins/physiology ; Proteoglycans/physiology
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  • 14
    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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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-18
    Description: Two dozen cellular proto-oncogenes have been discovered to date through the study of retroviruses and the use of gene transfer. They form a structurally and functionally heterogeneous group. At least five distinct mechanisms are responsible for their conversion to active oncogenes. Recent work provides experimental strategies by which many of these oncogenes, as well as oncogenes of DNA tumor viruses, may be placed into functional categories. These procedures may lead to definition of a small number of common pathways through which the various oncogenes act to transform cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Land, H -- Parada, L F -- Weinberg, R A -- CA14051/CA/NCI NIH HHS/ -- CA26717/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):771-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356358" target="_blank"〉PubMed〈/a〉
    Keywords: Gene Expression Regulation ; Genes, Viral ; Humans ; Neoplasms/*etiology/genetics ; *Oncogenes ; Retroviridae/*genetics ; Tissue Distribution ; Transfection
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  • 16
    Publication Date: 1983-08-26
    Description: The gene for the Harvey murine sarcoma virus (Ha-MuSV) p21ras protein was fused to the amino-terminal portion of the bacteriophage lambda cII gene on the expression vector pJL6. The fusion was such that transcription was controlled by the well-regulated phage lambda pL promoter, and translation initiated in the cII gene continued in frame into the ras gene sequences that code for p21. When the pL promoter was derepressed, the Escherichia coli cells harboring the fusion plasmid synthesized 23,000-dalton protein, which represented more than 10 percent of the total cellular protein. This protein was chimeric and contained 14 residues, which were specified by the vector; these residues were followed by all of the amino acids that make up Ha-MuSV p21ras except for four residues at the amino-terminal end. The protein appears similar to Ha-MuSV p21ras in that it undergoes immunoprecipitation by monoclonal antibodies directed toward that protein, binds guanosine diphosphate, and is capable of autophosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lautenberger, J A -- Ulsh, L -- Shih, T Y -- Papas, T S -- New York, N.Y. -- Science. 1983 Aug 26;221(4613):858-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6308763" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Transformation, Viral ; Escherichia coli/genetics ; Gene Expression Regulation ; Molecular Weight ; *Oncogenes ; Plasmids ; Sarcoma Viruses, Murine/enzymology/*genetics ; Viral Proteins/*genetics
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  • 17
    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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  • 18
    Publication Date: 1983-11-18
    Description: Synapses between neuroblastoma-hybrid cells and myotubes exhibit a high degree of plasticity. Increase of cyclic adenosine monophosphate (AMP) levels of the hybrid cells for several days results in the appearance of functional voltage-sensitive Ca2+ channels, which are required for evoked secretion of acetylcholine. The results show that cyclic AMP regulates synaptogenesis by regulating the expression of voltage-sensitive Ca2+ channels, and suggest that cyclic AMP affects posttranslational modifications of some glycoproteins and cellular levels of certain proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nirenberg, M -- Wilson, S -- Higashida, H -- Rotter, A -- Krueger, K -- Busis, N -- Ray, R -- Kenimer, J G -- Adler, M -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):794-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6314503" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Calcium/physiology ; Cell Adhesion ; Cells, Cultured ; Cyclic AMP/*physiology ; Gene Expression Regulation ; Humans ; Membrane Potentials ; Nerve Tissue Proteins/physiology ; Neuromuscular Junction/*physiology ; Neuronal Plasticity ; Receptors, Cell Surface/physiology ; Retina/*physiology ; Synapses/*physiology
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  • 19
    Publication Date: 1985-09-13
    Description: As a consequence of alternative RNA processing events, a single rat gene can generate messenger RNA's (mRNA's) encoding either calcitonin or a neuropeptide referred to as alpha-type calcitonin gene-related peptide (alpha-CGRP). An mRNA product of a related gene has been identified in rat brain and thyroid encoding the protein precursor of a peptide differing from alpha-CGRP by only a single amino acid. The RNA encoding this peptide, which is referred to as beta-CGRP, appears to be the only mature transcript of the beta-CGRP gene. Hybridization histochemistry reveals a similar distribution of alpha- and beta-CGRP mRNA's, but their relative levels of expression vary in different cranial nerve nuclei. Thus beta-CGRP is a new member of a family of related genes with potential functions in regulating the transduction of sensory and motor information.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amara, S G -- Arriza, J L -- Leff, S E -- Swanson, L W -- Evans, R M -- Rosenfeld, M G -- New York, N.Y. -- Science. 1985 Sep 13;229(4718):1094-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994212" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Brain Chemistry ; Calcitonin Gene-Related Peptide ; DNA/analysis ; DNA Restriction Enzymes/metabolism ; Gene Expression Regulation ; Nerve Tissue Proteins/*genetics ; RNA, Messenger/*analysis ; Rats
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  • 20
    Publication Date: 1985-07-05
    Description: Human T-lymphotropic virus type III (HTLV-III) encodes a trans-acting factor that activates the expression of genes linked to the HTLV-III long terminal repeat. By functional mapping of complementary DNA transcripts of viral messenger RNA's the major functional domain of the gene encoding this factor was localized to a region immediately before the env gene of the virus, a region previously thought to be noncoding. This newly identified gene consists of three exons, and its transcription into messenger RNA involves two splicing events bringing together sequences from the 5' part (287 base pairs), middle (268 base pairs), and 3'part (1258 base pairs) of the HTLV-III genome. A similar messenger RNA with a truncated second exon (70 base pairs) does not encode a trans-acting function. It is proposed that this second messenger RNA is the transcript of a gene (3'-orf) located after the env gene. Messenger RNA's were also identified for the env and gag-pol genes of HTLV-III.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arya, S K -- Guo, C -- Josephs, S F -- Wong-Staal, F -- New York, N.Y. -- Science. 1985 Jul 5;229(4708):69-73.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990040" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Deltaretrovirus/*genetics ; Gene Expression Regulation ; Genes, Regulator ; *Genes, Viral ; Humans ; RNA Splicing ; RNA, Messenger/genetics ; RNA, Viral/genetics ; Repetitive Sequences, Nucleic Acid ; Transcription Factors/*genetics ; Viral Proteins/genetics
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  • 21
    Publication Date: 1985-05-31
    Description: The carcinogenic process is extremely complex and is affected by diverse environmental and host factors. The mechanism for the gradual development of the transformed phenotype (a process termed "progression") was studied in type 5 adenovirus (Ad5)-transformed rat embryo cells. Progression was not correlated with major changes in the pattern of integration of viral DNA sequences. Instead, it was associated with an increased methylation of integrated viral sequences other than those corresponding to the E1 transforming genes of Ad5. A single exposure of progressed cells to the demethylating agent 5-azacytidine (Aza) resulted in a stable reversion to the unprogressed state of the original parental clone. A further selection of cells after growth in agar allowed the isolation of Aza-treated clones that had regained the progressed phenotype. These observations indicate that progression is a reversible process and suggest that progression may be associated with changes in the state of methylation of one or more specific genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Babiss, L E -- Zimmer, S G -- Fisher, P B -- CA-33434/CA/NCI NIH HHS/ -- CA-35675/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 31;228(4703):1099-101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2581317" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviruses, Human/*genetics ; Animals ; Azacitidine/*pharmacology ; Cell Division ; Cell Transformation, Viral/*drug effects ; Cells, Cultured ; DNA, Neoplasm/genetics ; DNA, Viral/genetics ; Gene Expression Regulation ; Genes, Viral ; *Methylation ; Mice ; Neoplasms, Experimental/*pathology ; Rats ; Rats, Inbred Strains/embryology ; Transcription, Genetic
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  • 22
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-02-15
    Description: The expression of myosin heavy chain isoforms was examined in normal and dystrophic chicken muscle with a monoclonal antibody specific for neonatal myosin. Adult dystrophic muscle continued to contain neonatal myosin long after it disappeared from adult normal muscle. A new technique involving western blotting and peptide mapping demonstrated that the immunoreactive myosin in adult dystrophic muscle was identical to that found in neonatal normal muscle. Immunocytochemistry revealed that all fibers in the dystrophic muscle failed to repress neonatal myosin heavy chain. These studies suggest that muscular dystrophy inhibits the myosin gene switching that normally occurs during muscle maturation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bandman, E -- AM31731/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1985 Feb 15;227(4688):780-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3969567" target="_blank"〉PubMed〈/a〉
    Keywords: Age Factors ; Animals ; Animals, Newborn/physiology ; Antibodies, Monoclonal ; Cell Differentiation ; Chickens ; Gene Expression Regulation ; Muscles/*cytology ; Muscular Dystrophy, Animal/*metabolism ; Myosins/genetics/immunology/*metabolism
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  • 23
    Publication Date: 1985-08-09
    Description: The T-cell receptor beta-chain gene has a nuclease hypersensitive site in several kinds of T cells, which does not appear in B cells expressing immunoglobulins. Conversely, the kappa immunoglobulin gene shows a known hypersensitive site at its enhancer element in B cells, as expected, but this site is absent in T cells. As is the case with immunoglobulin genes, the T-cell receptor site lies within the gene, in the intron separating joining and constant region segments. These nuclease hypersensitive DNA configurations in the introns of active T-cell receptor and immunoglobulin genes may arise from control elements that share ancestry but have diverged to the extent that each normally acts only in lymphoid cells which use the proximal gene product.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bier, E -- Hashimoto, Y -- Greene, M I -- Maxam, A M -- AI 19901/AI/NIAID NIH HHS/ -- CA 22427/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 9;229(4713):528-34.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3927483" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/metabolism ; Base Sequence ; Binding Sites ; Cell Line ; Chromosome Mapping ; Collodion ; Deoxyribonuclease I/*metabolism ; Enhancer Elements, Genetic ; Gene Expression Regulation ; Humans ; Hybridomas ; Immunochemistry ; Immunoglobulin Fragments/*genetics ; Immunoglobulin Heavy Chains/genetics ; Immunoglobulin kappa-Chains/genetics ; Mice ; Receptors, Antigen, T-Cell/*genetics ; T-Lymphocytes/*metabolism ; Transcription, Genetic
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  • 24
    Publication Date: 1985-11-15
    Description: Heterokaryons provide a model system in which to examine how tissue-specific phenotypes arise and are maintained. When muscle cells are fused with nonmuscle cells, muscle gene expression is activated in the nonmuscle cell type. Gene expression was studied either at a single cell level with monoclonal antibodies or in mass cultures at a biochemical and molecular level. In all of the nonmuscle cell types tested, including representatives of different embryonic lineages, phenotypes, and developmental stages, muscle gene expression was induced. Differences among cell types in the kinetics, frequency, and gene dosage requirements for gene expression provide clues to the underlying regulatory mechanisms. These results show that the expression of genes in the nuclei of differentiated cells is remarkably plastic and susceptible to modulation by the cytoplasm. The isolation of the genes encoding the tissue-specific trans-acting regulators responsible for muscle gene activation should now be possible.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blau, H M -- Pavlath, G K -- Hardeman, E C -- Chiu, C P -- Silberstein, L -- Webster, S G -- Miller, S C -- Webster, C -- GM07149/GM/NIGMS NIH HHS/ -- GM26717/GM/NIGMS NIH HHS/ -- HD18179/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Nov 15;230(4727):758-66.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2414846" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Animals ; Antibodies, Monoclonal ; *Cell Differentiation ; Cell Fusion ; Cell Nucleus/ultrastructure ; Epidermis/cytology ; Fetus/metabolism ; Fibroblasts/cytology ; Gene Expression Regulation ; Genes ; HeLa Cells/metabolism ; Humans ; Hybrid Cells/metabolism ; Keratins/physiology ; Kinetics ; Liver/cytology ; Mice ; Muscle Development ; Muscles/cytology ; Myosins/genetics ; Phenotype ; Transcription, Genetic ; Transcriptional Activation
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  • 25
    Publication Date: 1985-11-29
    Description: The transfer of the human gene for hypoxanthine phosphoribosyltransferase (HPRT) into human bone marrow cells was accomplished by use of a retroviral vector. The cells were infected in vitro with a replication-incompetent murine retroviral vector that carried and expressed a mutant HPRT complementary DNA. The infected cells were superinfected with a helper virus and maintained in long-term culture. The production of progeny HPRT virus by the bone marrow cells was demonstrated with a colony formation assay on cultured HPRT-deficient, ouabain-resistant murine fibroblasts. Hematopoietic progenitor cells able to form colonies of granulocytes or macrophages (or both) in semisolid medium in the presence of colony stimulating factor were present in the nonadherent cell population. Colony forming units cloned in agar and subsequently cultured in liquid medium produced progeny HPRT virus, indicating infection of this class of hematopoietic progenitor cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gruber, H E -- Finley, K D -- Hershberg, R M -- Katzman, S S -- Laikind, P K -- Seegmiller, J E -- Friedmann, T -- Yee, J K -- Jolly, D J -- AM 13622/AM/NIADDK NIH HHS/ -- GM 28223/GM/NIGMS NIH HHS/ -- HD20034/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Nov 29;230(4729):1057-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3864246" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Gene Expression Regulation ; *Genetic Engineering ; Genetic Vectors ; Hematopoietic Stem Cells/*physiology ; Humans ; Hypoxanthine Phosphoribosyltransferase/*genetics ; Mice ; Retroviridae/*genetics ; Transfection
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  • 26
    Publication Date: 1985-11-01
    Description: The 21-base pair repeat elements of the SV40 promoter contain six tandem copies of the GGGCGG hexanucleotide (GC-box), each of which can bind, with varying affinity, to the cellular transcription factor, Sp1. In vitro SV40 early RNA synthesis is mediated by interaction of Sp1 with GC-boxes I, II, and III, whereas transcription in the late direction is mediated by binding to GC-boxes III, V, and VI.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gidoni, D -- Kadonaga, J T -- Barrera-Saldana, H -- Takahashi, K -- Chambon, P -- Tjian, R -- New York, N.Y. -- Science. 1985 Nov 1;230(4725):511-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996137" target="_blank"〉PubMed〈/a〉
    Keywords: Autoradiography ; Base Sequence ; Binding Sites ; DNA-Binding Proteins/*metabolism ; Deoxyribonuclease I/metabolism ; Electrophoresis, Polyacrylamide Gel ; Gene Expression Regulation ; Mutation ; Pregnancy Proteins/*metabolism ; RNA, Messenger/analysis ; RNA, Viral/biosynthesis ; Simian virus 40/*genetics ; Sp1 Transcription Factor ; Templates, Genetic ; Transcription Factors/*metabolism ; *Transcription, Genetic
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  • 27
    Publication Date: 1985-11-29
    Description: Phototransduction is the process by which light-stimulated photoreceptor cells of the visual system send electrical signals to the nervous system. Many of the steps that follow the initial event in phototransduction, absorption of light by rhodopsin, are ill-defined. The fruitfly, Drosophila melanogaster, provides a means to dissect phototransduction genetically. Mutations such as transient receptor potential (trp) affect intermediate steps in phototransduction. In order to facilitate molecular studies of phototransduction, the trp gene was isolated and its identity was confirmed by complementing the mutant trpCM allele of the trp gene by P-element mediated germline transformation of a 7.1-kilobase DNA fragment. Expression of the trp gene begins late in pupal development and appears to be limited to the eyes and ocelli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Montell, C -- Jones, K -- Hafen, E -- Rubin, G -- New York, N.Y. -- Science. 1985 Nov 29;230(4729):1040-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3933112" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA/genetics ; Drosophila melanogaster/*genetics/physiology ; Gene Expression Regulation ; Genes ; Mutation ; Ocular Physiological Phenomena ; RNA, Messenger/genetics ; *Vision, Ocular
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  • 28
    Publication Date: 1985-06-07
    Description: Measles virus generally produces acute illness. Rarely, however, persistent infection of brain cells occurs, resulting in a chronic and fatal neurological disease, subacute sclerosing panencephalitis (SSPE). Evidence indicates that expression of the measles virus matrix protein is selectively restricted in this persistent infection, but the mechanism underlying this restriction has not been identified. Defective translation of matrix messenger RNA has been described in one SSPE cell line. This report presents evidence that in a different SSPE tissue culture cell line IP-3-Ca, the matrix protein is synthesized but fails to accumulate. A general scheme is proposed to reconcile the different levels at which restriction of matrix protein has been observed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sheppard, R D -- Raine, C S -- Bornstein, M B -- Udem, S A -- CA13330-12/CA/NCI NIH HHS/ -- NS 08952/NS/NINDS NIH HHS/ -- NS 11920/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1219-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4001938" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Gene Expression Regulation ; Humans ; Hydrolysis ; Measles virus/genetics/growth & development/*metabolism ; Molecular Weight ; Mutation ; Protein Processing, Post-Translational ; Subacute Sclerosing Panencephalitis/*microbiology ; Viral Matrix Proteins ; Viral Proteins/*biosynthesis/genetics ; Virus Replication
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  • 29
    Publication Date: 1985-07-05
    Description: The retrovirus involved in acquired immune deficiency syndrome (HTLV-III/LAV) contains a region that is necessary for stimulation of gene expression directed by the viral long terminal repeat. This region is located between nucleotides 5365 and 5607, immediately 5' to the envelope gene. A doubly-spliced message containing this region could encode an 86-amino acid protein with structural features similar to those of nucleic acid-binding proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sodroski, J -- Patarca, R -- Rosen, C -- Wong-Staal, F -- Haseltine, W -- CA07094/CA/NCI NIH HHS/ -- CAA07580/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jul 5;229(4708):74-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990041" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Deletion ; Chromosome Mapping ; Deltaretrovirus/*genetics ; Gene Expression Regulation ; *Genes, Viral ; Humans ; Promoter Regions, Genetic ; RNA Splicing ; RNA, Messenger/genetics ; RNA, Viral/genetics ; Repetitive Sequences, Nucleic Acid ; Transcription Factors/*genetics ; Viral Proteins/*genetics
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  • 30
    Publication Date: 1985-06-21
    Description: Human T-cell leukemia viruses type I and II (HTLV-I and -II) exhibit several features characteristic of this retroviral family: the presence of an x-lor gene encoding a nuclear protein, transformation properties suggesting the involvement of a virus-associated trans-acting factor, and transcriptional trans-activation of the long terminal repeat (LTR) in infected cells. In the study described here the HTL x-lor products, in the absence of other viral proteins, were able to activate gene expression in trans directed by HTLV LTR. The regulation of the expression of particular genes in trans by HTLV x-lor products suggests that they play a role in viral replication and possibly in transformation of T lymphocytes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sodroski, J -- Rosen, C -- Goh, W C -- Haseltine, W -- CA07094/CA/NCI NIH HHS/ -- CA07580/CA/NCI NIH HHS/ -- CA36974/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 21;228(4706):1430-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990028" target="_blank"〉PubMed〈/a〉
    Keywords: Deltaretrovirus/*genetics ; Gene Expression Regulation ; Genes, Viral ; Humans ; Plasmids ; Viral Proteins/*genetics
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  • 31
    Publication Date: 1985-06-28
    Description: DNA from a replication-defective spleen focus-forming virus (SFFV) was reconstructed and transfected into psi-2 cells containing a packaging-defective mutant of Moloney murine leukemia virus. Replication-incompetent retrovirus particles (helper virus-free containing genomes that express the transforming envelope gene of SFFV (gp52) transformed bone marrow cells in vitro and, after direct intravenous introduction of the vector, induced malignant erythroid disease in vivo. Disease induction was dependent on prior treatment of mice with phenylhydrazine, which probably increased the availability of erythroid target cells. Since there was no evidence of virus particle expression in mice with malignant disease, this study demonstrates the acute oncogenic potential of a limited number of erythroid cells expressing SFFV gp52. Direct inoculation of animals with nonreplicating retroviral vectors containing transforming genes may be useful in study the oncogenic effects of such genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolff, L -- Ruscetti, S -- New York, N.Y. -- Science. 1985 Jun 28;228(4707):1549-52.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990034" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Marrow/analysis ; *Cell Transformation, Neoplastic ; DNA Restriction Enzymes/metabolism ; DNA, Viral/metabolism ; Erythroblasts/*cytology ; Gene Expression Regulation ; Mice ; Oncogenes ; Phenotype ; Retroviridae/*genetics ; Spleen/microbiology ; Transfection ; Viral Envelope Proteins/genetics ; Virion/metabolism
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  • 32
    Publication Date: 1985-08-23
    Description: Mouse lymphoma cells were hybridized with two human acute T-cell leukemias with a t(11;14) (p13;q11) translocation and the segregated hybrids were examined for the presence of the DNA segments coding for the constant (C) and the variable (V) regions of the alpha chain (C alpha and V alpha) of the T-cell receptor. The C alpha segment was translocated to the involved chromosome 11 (11p+) while the V alpha segment remained on the involved chromosome 14 (14q-). The data indicate that the locus for the alpha chain of the T-cell receptor is split by the chromosomal breakpoint between the V alpha and the C alpha gene segments, and that the V alpha segments are proximal to the C alpha segment within chromosome band 14q11.2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erikson, J -- Williams, D L -- Finan, J -- Nowell, P C -- Croce, C M -- CA16685/CA/NCI NIH HHS/ -- CA36521/CA/NCI NIH HHS/ -- CA39860/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Aug 23;229(4715):784-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3875152" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; *Chromosomes, Human, 13-15 ; *Chromosomes, Human, 6-12 and X ; Gene Expression Regulation ; Genes ; Humans ; Leukemia/*genetics ; Oncogenes ; Receptors, Antigen, T-Cell/*genetics ; T-Lymphocytes/physiology ; *Translocation, Genetic
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  • 33
    Publication Date: 1985-08-16
    Description: Expression of the pX protein of human T-cell leukemia virus type I (HTLV-I) in animal cells demonstrates that this protein is a specific transcriptional activator of the long terminal repeats (LTR) of HTLV-I. Several other promoters are not affected by pX. No lymphocyte-specific factors are required for this activation. pX can be detected in the nucleus of transfected monkey kidney cells (line CV1) by indirect immunofluorescence. These results indicate that the pX protein is essential for the replication cycle of the virus and that it may be directly involved in the immortalization of human lymphocytes by HTLV-I.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Felber, B K -- Paskalis, H -- Kleinman-Ewing, C -- Wong-Staal, F -- Pavlakis, G N -- N01-C0-23909/PHS HHS/ -- New York, N.Y. -- Science. 1985 Aug 16;229(4714):675-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2992082" target="_blank"〉PubMed〈/a〉
    Keywords: DNA, Recombinant ; DNA-Directed RNA Polymerases/genetics ; Deltaretrovirus/*genetics ; Gene Expression Regulation ; Peptides/genetics ; Plasmids ; Promoter Regions, Genetic ; Repetitive Sequences, Nucleic Acid ; Transcription Factors/*genetics ; Transcription, Genetic ; Transforming Growth Factors ; Viral Proteins/*genetics
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  • 34
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-09-06
    Description: The cellular gene encoding the receptor for epidermal growth factor (EGF) has considerable homology to the oncogene of avian erythroblastosis virus. In a human mammary carcinoma, a DNA sequence was identified that is related to v-erbB but amplified in a manner that appeared to distinguish it from the gene for the EGF receptor. Molecular cloning of this DNA segment and nucleotide sequence analysis revealed the presence of two putative exons in a DNA segment whose predicted amino acid sequence was closely related to, but different from, the corresponding sequence of the erbB/EGF receptor. Moreover, this DNA segment identified a 5-kilobase transcript distinct from the transcripts of the EGF receptor gene. Thus, a new member of the tyrosine kinase proto-oncogene family has been identified on the basis of its amplification in a human mammary carcinoma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, C R -- Kraus, M H -- Aaronson, S A -- New York, N.Y. -- Science. 1985 Sep 6;229(4717):974-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2992089" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Breast Neoplasms/*genetics ; Cell Line ; Cloning, Molecular ; DNA, Neoplasm/*genetics ; Female ; *Gene Amplification ; Gene Expression Regulation ; Humans ; *Oncogenes ; Protein Kinases/*genetics ; Protein-Tyrosine Kinases ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 35
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-11-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1985 Nov 15;230(4727):794-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2997919" target="_blank"〉PubMed〈/a〉
    Keywords: Bovine papillomavirus 1/genetics ; DNA/*genetics ; Drosophila melanogaster/genetics ; Gene Expression Regulation ; Simian virus 40/genetics ; Transcription, Genetic ; Ustilago/genetics
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  • 36
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-01-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1985 Jan 11;227(4683):156-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2981426" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/microbiology ; Base Sequence ; Cell Transformation, Viral ; Deltaretrovirus/*classification/genetics ; Gene Expression Regulation ; RNA, Viral ; T-Lymphocytes/microbiology
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-05-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1985 May 24;228(4702):975-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4001932" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Cloning, Molecular ; Cytochrome P-450 Enzyme System/biosynthesis/*genetics ; Disease Susceptibility ; Enzyme Induction ; Gene Conversion ; Gene Expression Regulation ; Genes ; Humans ; Neoplasms/etiology
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  • 38
    Publication Date: 1985-06-07
    Description: The concentration in plasma of the female protein (FP) of the golden Syrian hamster is regulated by sex steroids and by mediators of the acute-phase response to tissue injury or inflammation. A complementary DNA (cDNA) clone corresponding to FP was isolated from a hamster liver cDNA library and used to determine the nucleotide sequence and derived amino acid sequence of native FP. The primary sequence of FP is 69 percent identical to human serum amyloid P component and 50 percent identical to human C-reactive protein. Evidence showed that sex-limited and acute-phase control of the FP gene is pretranslational. The FP protein is thus a useful model for investigating dual regulation of expression of a single gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dowton, S B -- Woods, D E -- Mantzouranis, E C -- Colten, H R -- AI20959/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1206-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2408337" target="_blank"〉PubMed〈/a〉
    Keywords: Acute-Phase Proteins ; Alpha-Globulins/*genetics ; Amino Acid Sequence ; Animals ; Base Sequence ; Blood Proteins/genetics ; *C-Reactive Protein ; Cricetinae/*physiology ; DNA/genetics ; Female ; Gene Expression Regulation ; Genes ; Liver/physiology ; Male ; Mesocricetus/*physiology ; RNA, Messenger/genetics
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  • 39
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-07-26
    Description: Nerve growth factor (NGF) is essential for the development and differentiation of sympathetic or sensory neurons. A complementary DNA was cloned that corresponds to a gene sequence induced more than 50-fold in a cultured target cell line of pheochromocytoma cells (PC12 cells) 5 hours after the addition of NGF. The induced messenger RNA encodes a 90,000-dalton polypeptide that may represent one of the primary events in NGF-induced differentiation of neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levi, A -- Eldridge, J D -- Paterson, B M -- New York, N.Y. -- Science. 1985 Jul 26;229(4711):393-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3839317" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/genetics ; Adrenal Gland Neoplasms/genetics ; Animals ; Base Sequence ; Cell Line ; Chickens ; *Cloning, Molecular ; DNA/genetics ; Gene Expression Regulation ; *Genes ; Nerve Growth Factors/*physiology ; Nucleic Acid Hybridization ; Pheochromocytoma/genetics ; RNA, Messenger/genetics ; Rabbits ; Rats
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  • 40
    Publication Date: 1985-08-23
    Description: The sequence of the entire RNA genome of the type flavivirus, yellow fever virus, has been obtained. Inspection of this sequence reveals a single long open reading frame of 10,233 nucleotides, which could encode a polypeptide of 3411 amino acids. The structural proteins are found within the amino-terminal 780 residues of this polyprotein; the remainder of the open reading frame consists of nonstructural viral polypeptides. This genome organization implies that mature viral proteins are produced by posttranslational cleavage of a polyprotein precursor and has implications for flavivirus RNA replication and for the evolutionary relation of this virus family to other RNA viruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rice, C M -- Lenches, E M -- Eddy, S R -- Shin, S J -- Sheets, R L -- Strauss, J H -- AI 10793/AI/NIAID NIH HHS/ -- AI 20612/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 23;229(4715):726-33.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4023707" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Biological Evolution ; Gene Expression Regulation ; Genes ; Glycoproteins/genetics ; Nucleic Acid Conformation ; Protein Biosynthesis ; Protein Conformation ; Protein Processing, Post-Translational ; RNA, Viral/*genetics ; Viral Proteins/*genetics ; *Virus Replication ; Yellow fever virus/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-01-25
    Description: There is convincing evidence that cellular prooxidant states--that is, increased concentrations of active oxygen and organic peroxides and radicals--can promote initiated cells to neoplastic growth. Prooxidant states can be caused by different classes of agents, including hyperbaric oxygen, radiation, xenobiotic metabolites and Fenton-type reagents, modulators of the cytochrome P-450 electron-transport chain, peroxisome proliferators, inhibitors of the antioxidant defense, and membrane-active agents. Many of these agents are promoters or complete carcinogens. They cause chromosomal damage by indirect action, but the role of this damage in carcinogenesis remains unclear. Prooxidant states can be prevented or suppressed by the enzymes of the cellular antioxidant defense and low molecular weight scavenger molecules, and many antioxidants are antipromoters and anticarcinogens. Finally, prooxidant states may modulate the expression of a family of prooxidant genes, which are related to cell growth and differentiation, by inducing alterations in DNA structure or by epigenetic mechanisms, for example, by polyadenosine diphosphate-ribosylation of chromosomal proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cerutti, P A -- New York, N.Y. -- Science. 1985 Jan 25;227(4685):375-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2981433" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antioxidants/pharmacology ; *Carcinogens/metabolism/pharmacology ; Cations/metabolism ; Cell Differentiation ; Cell Division ; Cell Line ; Cell Membrane/physiology ; *Cell Transformation, Neoplastic ; Chromosome Aberrations ; Chromosomes/drug effects ; Cytochrome P-450 Enzyme System/metabolism ; DNA/metabolism ; Electron Transport ; Gene Expression Regulation ; Humans ; Hydrogen Peroxide/metabolism ; Hydroxides/metabolism ; Hydroxyl Radical ; Lipid Peroxides/metabolism ; Microbodies/metabolism ; Mutation ; Neoplasms/*chemically induced ; Oxidation-Reduction ; Oxygen/*metabolism/physiology ; Poly Adenosine Diphosphate Ribose/metabolism ; Singlet Oxygen ; Sulfhydryl Compounds/physiology ; Superoxides/metabolism ; Ultraviolet Rays
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-09-20
    Description: Methods have been developed to transfect immunoglobulin genes into lymphoid cells. The transfected genes are faithfully expressed, and assembly can occur both between the transfected and endogenous chains and between two transfected chains. Gene transfection can be used to reconstitute immunoglobulin molecules and to produce novel immunoglobulin molecules. These novel molecules can represent unique combinations of heavy and light chains; alternatively, by means of recombinant DNA technology, genes can be assembled in vitro, transfected, and expressed. The end products of such manipulations include chimeric molecules with variable regions joined to different isotypic constant regions; this is possible both within and between species. It is also possible to synthesize altered immunoglobulin molecules, as well as molecules having immunoglobulin sequences fused with nonimmunoglobulin sequences (for example, enzyme sequences).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morrison, S L -- CA 13696/CA/NCI NIH HHS/ -- CA 16858/CA/NCI NIH HHS/ -- CA 22736/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Sep 20;229(4719):1202-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3929380" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Chimera ; DNA, Recombinant ; Gene Expression Regulation ; Genes, Bacterial ; Humans ; Hybridomas/*metabolism ; Immunoglobulin Constant Regions/biosynthesis/genetics ; Immunoglobulin Heavy Chains/biosynthesis/genetics ; Immunoglobulin Light Chains/biosynthesis/genetics ; Immunoglobulin Variable Region/biosynthesis/genetics ; Immunoglobulins/biosynthesis/*genetics/physiology ; Lymphocytes/immunology ; Mice ; Structure-Activity Relationship ; *Transfection
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-09-20
    Description: Analyses of the function of specific genes and sequences of large DNA viruses such as herpesviruses and poxviruses present special problems because of the size of their genomes (120 to 250 kilobase pairs). Various methods for engineering site-specific insertions or deletions based on the use of selectable markers have been developed and applied for the elucidation of the function of specific DNA sequences, the identification of genes nonessential for virus growth in cell culture, and the expression of foreign genes. These methods should also make possible the construction of viral vectors capable of delivering genes specifying antigens for the prevention of infectious diseases in humans and animals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roizman, B -- Jenkins, F J -- CA08494/CA/NCI NIH HHS/ -- CA09241/CA/NCI NIH HHS/ -- CA19264/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Sep 20;229(4719):1208-14.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994215" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA, Recombinant ; DNA, Viral ; Gene Expression Regulation ; *Genes ; *Genes, Viral ; Genetic Engineering/*methods ; Poxviridae/genetics ; Simplexvirus/analysis/enzymology/*genetics ; Thymidine Kinase/genetics ; Virology/methods ; Virus Replication
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  • 44
    Publication Date: 1983-09-02
    Description: Human fetal muscles at ages 110, 125, and 132 days contain a fetal-specific myosin light chain. This light chain is absent in adult human muscle, copurifies with myosin, and is identified as a slow light chain because it reacts with purified antibody to chicken slow muscle light chains and does not react strongly with antibody to fast myosin light chains. This light chain is synthesized in cultures of fetal muscle along with normal myosin light chains. The presence of a fetal light chain in culture provides a marker for studies of human muscle disease in which it is important to know when or if the muscle makes a transition from embryonic or fetal expression to true adult phenotype.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strohman, R C -- Micou-Eastwood, J -- Glass, C A -- Matsuda, R -- New York, N.Y. -- Science. 1983 Sep 2;221(4614):955-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6879193" target="_blank"〉PubMed〈/a〉
    Keywords: Fetus/physiology ; Gene Expression Regulation ; Humans ; Muscles/*embryology ; Myosins/*biosynthesis/genetics/immunology
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  • 45
    Publication Date: 1983-11-18
    Description: Three mutations of the enzyme dihydrofolate reductase were constructed by oligonucleotide-directed mutagenesis of the cloned Escherichia coli gene. The mutations--at residue 27, aspartic acid replaced with asparagine; at residue 39, proline replaced with cysteine; and at residue 95, glycine replaced with alanine--were designed to answer questions about the relations between molecular structure and function that were raised by the x-ray crystal structures. Properties of the mutant proteins show that Asp-27 is important for catalysis and that perturbation of the local structure at a conserved cis peptide bond following Gly-95 abolishes activity. Substitution of cysteine for proline at residue 39 results in the appearance of new forms of the enzyme that correspond to various oxidation states of the cysteine. One of these forms probably represents a species cross-linked by an intrachain disulfide bridge between the cysteine at position 85 and the new cysteine at position 39.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Villafranca, J E -- Howell, E E -- Voet, D H -- Strobel, M S -- Ogden, R C -- Abelson, J N -- Kraut, J -- CA17374/CA/NCI NIH HHS/ -- F32 GM09375/GM/NIGMS NIH HHS/ -- GM10928/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):782-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356360" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Disulfides ; Escherichia coli/genetics ; Gene Expression Regulation ; Genes ; Genes, Bacterial ; *Mutation ; Structure-Activity Relationship ; Tetrahydrofolate Dehydrogenase/*genetics
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