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  • Articles  (37)
  • Transcription, Genetic  (37)
  • American Association for the Advancement of Science (AAAS)  (37)
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  • Articles  (37)
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  • American Association for the Advancement of Science (AAAS)  (37)
  • American Geophysical Union
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  • 1
    Publication Date: 1987-06-05
    Description: The use of molecular biological approaches has defined new mechanisms that store information in the mammalian nervous system. Environmental stimuli alter steady-state levels of messenger RNA species encoding neurotransmitters, thereby altering synaptic, neuronal, and network function over time. External or internal stimuli alter impulse activity, which alters membrane depolarization and selectively changes the expression of specific transmitter genes. These processes occur in diverse peripheral and central neurons, suggesting that information storage is widespread in the neuraxis. The temporal profile of any particular molecular mnemonic process is determined by specific kinetics of turnover and by the geometry of the neuron resulting in axonal transport of molecules to different synaptic arrays at different times. Generally, transmitters, the agents of millisecond-to-millisecond communication, are subject to relatively long-lasting changes in expression, ensuring that ongoing physiological function is translated into information storage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Black, I B -- Adler, J E -- Dreyfus, C F -- Friedman, W F -- LaGamma, E F -- Roach, A H -- HD 12108/HD/NICHD NIH HHS/ -- NS 10259/NS/NINDS NIH HHS/ -- NS 20788/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jun 5;236(4806):1263-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2884727" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Medulla/metabolism ; Animals ; Brain/physiology ; Memory/*physiology ; Nervous System/anatomy & histology/metabolism ; *Nervous System Physiological Phenomena ; Neurons/physiology ; Neurotransmitter Agents/metabolism/*physiology ; Sympathetic Nervous System/metabolism/physiology ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 1987-03-20
    Description: Elevation of glucose transport is an alteration common to most virally induced tumors. Rat fibroblasts transformed with wild-type or a temperature-sensitive Fujinami sarcoma virus (FSV) were studied in order to determine the mechanisms underlying the increased transport. Five- to tenfold increases in total cellular glucose transporter protein in response to transformation were accompanied by similar increases in transporter messenger RNA levels. This, in turn, was preceded by an absolute increase in the rate of glucose transporter gene transcription within 30 minutes after shift of the temperature-sensitive FSV-transformed cells to the permissive temperature. The transporter messenger RNA levels in transformed fibroblasts were higher than those found in proliferating cells maintained at the nonpermissive temperature. The activation of transporter gene transcription by transformation represents one of the earliest known effects of oncogenesis on the expression of a gene encoding a protein of well-defined function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Birnbaum, M J -- Haspel, H C -- Rosen, O M -- AM35430-01/AM/NIADDK NIH HHS/ -- DK 35158/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 20;235(4795):1495-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3029870" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avian Sarcoma Viruses ; Cell Division ; Cell Line ; *Cell Transformation, Viral ; Fibroblasts ; Gene Expression Regulation ; Kinetics ; Monosaccharide Transport Proteins/*genetics ; RNA, Messenger/genetics ; Rats ; Transcription, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-11-06
    Description: The c-erbA gene belongs to a multigene family that encodes transcriptional regulatory proteins including the v-erbA oncogene product, steroid hormone receptors, and the vitamin D3 receptor. A v-erbA DNA probe encoding the DNA-binding region of the v-erbA protein was used to screen a human complementary DNA testis library. One of the clones isolated, erbA-T-1, was found to encode a 490-amino acid protein (erbA-T). The erbA-T polypeptide shows high homology with the proteins encoded by both the chicken c-erbA and the human c-erbA-beta genes but is most closely related to the chicken gene. The chicken c-erbA and the human c-erbA-beta genes encode high-affinity receptors for thyroid hormone, and here it is shown that the erbA-T protein binds specifically to 3,5,3'-triiodo-L-thyronine with a dissociation constant of 3.8 +/- 0.2 x 10(-10) M. These data imply that more than one thyroid hormone receptor exists in humans and that these receptors might have different tissue- and gene-activating specificities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benbrook, D -- Pfahl, M -- DK-35083/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 6;238(4828):788-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research Center, La Jolla Cancer Research Foundation, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3672126" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Cloning, Molecular ; DNA/*metabolism ; *Genes ; Humans ; Kinetics ; Male ; Protein Biosynthesis ; *Proto-Oncogenes ; Receptors, Thyroid Hormone/*genetics/metabolism ; Testis/*metabolism ; Transcription, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 1987-10-30
    Description: The major late transcription factor (MLTF) is a 46-kilodalton polypeptide that specifically binds to and activates transcription from the major late promoter of adenovirus. The presence of this promoter-specific transcription factor in uninfected HeLa cell extracts suggests that MLTF is also involved in the transcription of cellular genes. This report demonstrates that MLTF specifically stimulates transcription of the rat gamma-fibrinogen gene through a high-affinity binding site. Stimulation of transcription by MLTF was not dependent on the exact position of the MLTF binding site with respect either to the transcription initiation site or to adjacent promoter elements. These results suggest that one of the cellular functions of MLTF is to control gamma-fibrinogen gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chodosh, L A -- Carthew, R W -- Morgan, J G -- Crabtree, G R -- Sharp, P A -- P01-CA42063/CA/NCI NIH HHS/ -- P30-CA14051/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):684-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3672119" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviruses, Human/*genetics ; Animals ; DNA-Binding Proteins/*genetics ; Fibrinogen/*genetics ; *Gene Expression Regulation ; *Promoter Regions, Genetic ; RNA Polymerase II/metabolism ; Rats ; Regulatory Sequences, Nucleic Acid ; Transcription Factors/*genetics ; Transcription, Genetic ; Viral Proteins/genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 1987-02-20
    Description: Four clones were isolated from an adult human brain complementary DNA library with an oligonucleotide probe corresponding to the first 20 amino acids of the beta peptide of brain amyloid from Alzheimer's disease. The open reading frame of the sequenced clone coded for 97 amino acids, including the known amino acid sequence of this polypeptide. The 3.5-kilobase messenger RNA was detected in mammalian brains and human thymus. The gene is highly conserved in evolution and has been mapped to human chromosome 21.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldgaber, D -- Lerman, M I -- McBride, O W -- Saffiotti, U -- Gajdusek, D C -- New York, N.Y. -- Science. 1987 Feb 20;235(4791):877-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3810169" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics ; Amino Acid Sequence ; Amyloid/*genetics ; *Chromosomes, Human, Pair 21 ; Cloning, Molecular ; DNA/genetics ; Humans ; Protein Conformation ; RNA, Messenger/genetics ; Solubility ; Transcription, Genetic
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  • 6
    Publication Date: 1987-12-18
    Description: Growth factors and their receptors are involved in the regulation of cell proliferation and also play a key role in oncogenesis. In this study, a novel putative kinase receptor gene, termed eph, has been identified and characterized by molecular cloning. Its primary structure is similar to that of tyrosine kinase receptors thus far cloned and includes a cysteine-rich region in the extracellular domain. However, other features of the sequence distinguish the eph gene product from known receptors with tyrosine kinase activity. Thus the eph protein may define a new class of these molecules. The eph gene is overexpressed in several human carcinomas, suggesting that this gene may be involved in the neoplastic process of some tumors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hirai, H -- Maru, Y -- Hagiwara, K -- Nishida, J -- Takaku, F -- New York, N.Y. -- Science. 1987 Dec 18;238(4834):1717-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2825356" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA Restriction Enzymes ; *Genes ; Humans ; Molecular Sequence Data ; Neoplasms/metabolism ; Oncogenes ; Protein-Tyrosine Kinases/metabolism ; Receptor, Epidermal Growth Factor/*genetics ; Transcription, Genetic
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  • 7
    Publication Date: 1987-07-24
    Description: Abnormal accumulation of connective tissue in blood vessels contributes to alterations in vascular physiology associated with disease states such as hypertension and atherosclerosis. Elastin synthesis was studied in blood vessels from newborn calves with severe pulmonary hypertension induced by alveolar hypoxia in order to investigate the cellular stimuli that elicit changes in pulmonary arterial connective tissue production. A two- to fourfold increase in elastin production was observed in pulmonary artery tissue and medial smooth muscle cells from hypertensive calves. This stimulation of elastin production was accompanied by a corresponding increase in elastin messenger RNA consistent with regulation at the transcriptional level. Conditioned serum harvested from cultures of pulmonary artery smooth muscle cells isolated from hypertensive animals contained one or more low molecular weight elastogenic factors that stimulated the production of elastin in both fibroblasts and smooth muscle cells and altered the chemotactic responsiveness of fibroblasts to elastin peptides. These results suggest that connective tissue changes in the pulmonary vasculature in response to pulmonary hypertension are orchestrated by the medial smooth muscle cell through the generation of specific differentiation factors that alter both the secretory phenotype and responsive properties of surrounding cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mecham, R P -- Whitehouse, L A -- Wrenn, D S -- Parks, W C -- Griffin, G L -- Senior, R M -- Crouch, E C -- Stenmark, K R -- Voelkel, N F -- CA31777/CA/NCI NIH HHS/ -- HD20521/HD/NICHD NIH HHS/ -- HL14985/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1987 Jul 24;237(4813):423-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3603030" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anoxia ; Cattle ; Connective Tissue/pathology/*physiopathology ; Disease Models, Animal ; Elastin/genetics/physiology ; Humans ; Hypertension, Pulmonary/pathology/*physiopathology ; Muscle, Smooth, Vascular/pathology/*physiopathology ; RNA, Messenger/genetics ; Transcription, Genetic
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  • 8
    Publication Date: 1987-05-15
    Description: Antibody-producing cells display a special form of regulation whereby each cell produces immunoglobulin from only one of its two sets of antibody genes. This phenomenon, called allelic exclusion, is thought to be mediated by the product of one heavy chain allele restricting the expression of the other. Heavy chains are synthesized in two molecular forms, secreted and membrane bound. In order to determine whether it is specifically the membrane-bound form of the immunoglobulin M (IgM) heavy chain (mu) that mediates this regulation, transgenic mice were created that carry a human mu chain gene altered so that it can only direct the synthesis of the membrane-bound protein. The membrane-bound form of the human mu chain was made by most of the B cells in these animals as measured by assays of messenger RNA and surface immunoglobulins. Further, the many B cells that express the human gene do not express endogenous mouse IgM, and the few B cells that express endogenous mouse mu do not express the transgene. Thus, the membrane-bound form of the mu chain is sufficient to mediate allelic exclusion. In addition, the molecular structures recognized for this purpose are conserved between human and mouse systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nussenzweig, M C -- Shaw, A C -- Sinn, E -- Danner, D B -- Holmes, K L -- Morse, H C 3rd -- Leder, P -- New York, N.Y. -- Science. 1987 May 15;236(4803):816-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3107126" target="_blank"〉PubMed〈/a〉
    Keywords: *Alleles ; Animals ; Antibody-Producing Cells/*immunology ; Gene Expression Regulation ; *Genes ; Humans ; Immunoglobulin M/genetics ; Immunoglobulin mu-Chains/*genetics ; Mice ; Mice, Inbred Strains ; RNA, Messenger/genetics ; Transcription, Genetic
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  • 9
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-01-09
    Description: The MerR protein mediates the induction of the mercury resistance phenotype in bacteria; it has been isolated in order to study the effects of metal-ion induced changes in the metabolism of prokaryotic cells at the molecular level. After DNA sequences responsible for negative autoregulation were removed, the 16-kilodalton protein was overproduced and purified to more than 90 percent homogeneity by a salt extraction procedure that yields about 5 milligrams of protein per gram of cells. Complementation data, amino terminal analysis, gel filtration, and deoxyribonuclease I protection studies demonstrate that the purified merR gene product is a dimer under nondenaturing conditions and that it binds specifically to DNA, in the presence and absence of mercury, at a palindromic site which is directly between the -10 and -35 regions of the structural genes and adjacent to its own promoter. These initial results indicate that MerR is a DNA-binding metalloregulatory protein that plays a central role in this heavy metal responsive system and they delineate an operator site in the mer operon.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Halloran, T -- Walsh, C -- AI07256/AI/NIAID NIH HHS/ -- GM20011/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jan 9;235(4785):211-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3798107" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/genetics/*isolation & purification ; Base Sequence ; Chromatography, Gel ; DNA/metabolism ; DNA-Binding Proteins/genetics/*isolation & purification ; Macromolecular Substances ; *Mercury ; Operator Regions, Genetic ; R Factors/*genetics ; Transcription, Genetic
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  • 10
    Publication Date: 1987-08-14
    Description: On the basis of electrophysiological analysis of Shaker mutants, the Shaker locus of Drosophila melanogaster has been proposed to encode a structural component of a voltage-dependent potassium channel, the A channel. Unlike sodium channels, acetylcholine receptors, and calcium channels, K+ channels have not been purified biochemically. To facilitate biochemical studies of a K+ channel, genomic DNA from the Shaker locus has been cloned. Rearrangements in five Shaker mutants have been mapped to a 60-kilobase segment of the genome. Four complementary DNA clones have been analyzed. These clones indicate that the Shaker gene contains multiple exons distributed over at least 65 kilobases of genomic DNA in the region where the mutations mapped. Furthermore, the gene may produce several classes of alternatively spliced transcripts. Two of the complementary DNA clones have been sequenced and their sequences support the hypothesis that Shaker encodes a component of a K+ channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Papazian, D M -- Schwarz, T L -- Tempel, B L -- Jan, Y N -- Jan, L Y -- NS15963/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Aug 14;237(4816):749-53.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2441470" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cloning, Molecular ; DNA/*genetics/isolation & purification ; Drosophila melanogaster/*genetics ; Exons ; *Ion Channels ; Membrane Proteins/*genetics ; Mutation ; Nucleic Acid Hybridization ; Potassium/*metabolism ; RNA Splicing ; Transcription, Genetic ; Translocation, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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