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  • Gene Expression Regulation  (25)
  • American Association for the Advancement of Science (AAAS)  (25)
  • American Chemical Society
  • 1985-1989  (25)
  • 1980-1984
  • 1965-1969
  • 1985  (25)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (25)
  • American Chemical Society
Years
  • 1985-1989  (25)
  • 1980-1984
  • 1965-1969
Year
  • 1
    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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  • 2
    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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  • 3
    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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  • 4
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    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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  • 5
    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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  • 6
    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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  • 7
    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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  • 8
    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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  • 9
    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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  • 10
    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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  • 11
    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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  • 12
    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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  • 13
    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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  • 14
    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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  • 15
    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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  • 16
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    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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  • 17
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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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    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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    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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    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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    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 21
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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
    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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  • 22
    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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  • 23
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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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 24
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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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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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
    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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