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  • Articles  (71)
  • Gene Expression Regulation  (71)
  • American Association for the Advancement of Science (AAAS)  (71)
  • American Association for the Advancement of Science
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  • Articles  (71)
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  • American Association for the Advancement of Science (AAAS)  (71)
  • American Association for the Advancement of Science
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  • American Institute of Physics
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  • 1985-1989  (71)
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  • 1
    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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  • 2
    Publication Date: 1987-07-10
    Description: A wide variety of human tumors contain an amplified or overexpressed erbB-2 gene, which encodes a growth factor receptor-like protein. When erbB-2 complementary DNA was expressed in NIH/3T3 cells under the control of the SV40 promoter, the gene lacked transforming activity despite expression of detectable levels of the erbB-2 protein. A further five- to tenfold increase in its expression under influence of the long terminal repeat of Moloney murine leukemia virus was associated with activation of erbB-2 as a potent oncogene. The high levels of the erbB-2 product associated with malignant transformation of NIH/3T3 cells were observed in human mammary tumor cells that overexpressed this gene. These findings demonstrate a new mechanism for acquisition of oncogenic properties by genes encoding growth factor receptor-like proteins and provide a functional basis for the role of their overexpression in the development of human malignancies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Di Fiore, P P -- Pierce, J H -- Kraus, M H -- Segatto, O -- King, C R -- Aaronson, S A -- New York, N.Y. -- Science. 1987 Jul 10;237(4811):178-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2885917" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Breast Neoplasms/genetics ; Cell Line ; *Cell Transformation, Neoplastic/genetics ; DNA/genetics ; Fibroblasts/*metabolism ; Gene Expression Regulation ; Genes, Viral ; Humans ; Mice ; Moloney murine leukemia virus/genetics ; Promoter Regions, Genetic ; Proto-Oncogene Proteins/biosynthesis/genetics/*physiology ; Rats ; Receptor, Epidermal Growth Factor ; Receptor, ErbB-2 ; Receptors, Cell Surface/genetics ; Recombinant Fusion Proteins/biosynthesis/genetics/physiology ; Simian virus 40/genetics ; Tumor Stem Cell Assay
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  • 3
    Publication Date: 1987-04-03
    Description: A gene, termed gli, was identified that is amplified more than 50-fold in a malignant glioma. The gene is expressed at high levels in the original tumor and its derived cell line and is located at chromosome 12 position (q13 to q14.3). The gli gene is a member of a select group of cellular genes that are genetically altered in primary human tumors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kinzler, K W -- Bigner, S H -- Bigner, D D -- Trent, J M -- Law, M L -- O'Brien, S J -- Wong, A J -- Vogelstein, B -- CA-09243/CA/NCI NIH HHS/ -- CA-43722/CA/NCI NIH HHS/ -- NS-20023/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1987 Apr 3;236(4797):70-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3563490" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; *Chromosomes, Human, Pair 12 ; Cloning, Molecular ; DNA, Neoplasm/*genetics ; *Gene Amplification ; Gene Expression Regulation ; Glioma/*genetics ; Humans ; RNA, Messenger/genetics ; RNA, Neoplasm/genetics
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  • 4
    Publication Date: 1987-08-21
    Description: The molecular basis for the marked difference between primate and rodent cells in sensitivity to the cardiac glycoside ouabain has been established by genetic techniques. A complementary DNA encoding the entire alpha 1 subunit of the mouse Na+- and K+-dependent adenosine triphosphatase (ATPase) was inserted into the expression vector pSV2. This engineered DNA molecule confers resistance against 10(-4) M ouabain to monkey CV-1 cells. Deletion of sequences encoding the carboxyl terminus of the alpha 1 subunit abolish the activity of the complementary DNA. The ability to assay the biological activity of this ATPase in a transfection protocol permits the application of molecular genetic techniques to the analysis of structure-function relationships for the enzyme that establishes the internal Na+/K+ environment of most animal cells. The full-length alpha 1 subunit complementary DNA will also be useful as a dominant selectable marker for somatic cell genetic studies utilizing ouabain-sensitive cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kent, R B -- Emanuel, J R -- Ben Neriah, Y -- Levenson, R -- Housman, D E -- CA-07919/CA/NCI NIH HHS/ -- CA-26712/CA/NCI NIH HHS/ -- CA-38992/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Aug 21;237(4817):901-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3039660" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Cercopithecus aethiops ; DNA/genetics ; Drug Resistance ; Gene Expression Regulation ; Macromolecular Substances ; Mice ; Ouabain/*pharmacology ; Sodium-Potassium-Exchanging ATPase/antagonists & inhibitors/*genetics ; Species Specificity ; Structure-Activity Relationship ; Transfection
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-08-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1987 Aug 21;237(4817):854-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3039659" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division ; Gene Expression Regulation ; Growth Substances/pharmacology ; Proto-Oncogene Proteins/*physiology ; *Proto-Oncogenes ; Receptors, GABA-A/physiology
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-04-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1987 Apr 24;236(4800):393.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3494309" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; Gene Expression Regulation ; HIV/*genetics ; Humans ; Lymphocyte Activation ; T-Lymphocytes/cytology/*microbiology
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  • 7
    Publication Date: 1987-07-10
    Description: A dramatic and specific induction of c-fos was observed in identifiable neuronal populations in vivo after administration of the convulsant Metrazole. This effect was time- and dose-dependent and was abolished by prior treatment with the anticonvulsant drugs diazepam or pentobarbital. About 60 minutes after administration of Metrazole, c-fos messenger RNA reached a maximum and declined to basal levels after 180 minutes. A further decrease below that in normal brain was observed before a return to basal levels after 16 hours. While Metrazole still elicited seizures during this period, reinduction of c-fos was largely refractory. At 90 minutes, c-fos protein was observed in the nuclei of neurons in the dentate gyrus, and in the pyriform and cingulate cortices. Subsequently, c-fos protein appeared throughout the cortex, hippocampus, and limbic system. Thus, seizure activity results in increased c-fos gene expression in particular subsets of neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morgan, J I -- Cohen, D R -- Hempstead, J L -- Curran, T -- New York, N.Y. -- Science. 1987 Jul 10;237(4811):192-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3037702" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Brain Chemistry/drug effects ; DNA-Binding Proteins/biosynthesis/genetics ; Diazepam/pharmacology ; Fluorescent Antibody Technique ; Gene Expression Regulation ; Mice ; Mice, Inbred BALB C ; Neurons/metabolism ; Pentobarbital/pharmacology ; Pentylenetetrazole/antagonists & inhibitors/toxicity ; Proto-Oncogene Proteins/*biosynthesis/genetics ; Proto-Oncogene Proteins c-fos ; Receptors, GABA-A/drug effects ; Seizures/chemically induced/*metabolism
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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
    Publication Date: 1987-01-30
    Description: Isochromosomal, respiratory-deficient yeast strains, such as a mit-, a hypersuppressive petite, and a petite lacking mitochondrial DNA, are phenotypically identical in spite of differences in their mitochondrial genomes. Subtractive hybridizations of complementary DNA's to polyadenylated RNA isolated from derepressed cultures of these strains reveal the presence of nuclear-encoded transcripts whose abundance varies not only between them and their respiratory-competent parent, but among the respiratory-deficient strains themselves. Transcripts of some nuclear-encoded mitochondrial proteins, like cytochrome c and the alpha and beta subunits of the mitochondrial adenosine triphosphatase, whose abundance is affected by glucose or heme, do not vary. In the absence of major metabolic variables, yeast cells seem to respond to the quality and quantity of mitochondrial DNA and modulate the levels of nuclear-encoded RNA's, perhaps as a means of intergenomic regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parikh, V S -- Morgan, M M -- Scott, R -- Clements, L S -- Butow, R A -- New York, N.Y. -- Science. 1987 Jan 30;235(4788):576-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3027892" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Nucleus/physiology ; Cytochrome c Group/genetics ; DNA, Fungal/genetics ; DNA, Mitochondrial/genetics ; Electron Transport Complex IV/genetics ; Gene Expression Regulation ; Genes, Fungal ; Genotype ; Mitochondria/*physiology ; Mutation ; RNA, Fungal/genetics ; RNA, Messenger/genetics ; RNA, Ribosomal/genetics ; Saccharomyces cerevisiae/*genetics
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  • 10
    Publication Date: 1987-06-05
    Description: Cell cycle-dependent histone genes are transcribed at a basal level throughout the cell cycle, with a three- to fivefold increase during early S phase. Protein-DNA interactions in the 5' promoter region of a cell cycle-regulated human H4 histone gene have been analyzed at single-nucleotide resolution in vivo. This region contains two sites, with four potential protein-binding domains, at which the DNA is protected from reaction with dimethyl sulfate in cells and from digestion with deoxyribonuclease I in nuclei. These protein-DNA interactions persist during all phases of the cell cycle and dissociate with 0.16 to 0.2M sodium chloride.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pauli, U -- Chrysogelos, S -- Stein, G -- Stein, J -- Nick, H -- GM32010/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jun 5;236(4806):1308-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3035717" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Cycle ; Cell Line ; Dna ; DNA Restriction Enzymes ; Deoxyribonuclease I ; Gene Expression Regulation ; Histones/*genetics ; Humans ; Nucleic Acid Hybridization ; *Promoter Regions, Genetic ; Protein Binding ; Sulfuric Acid Esters
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  • 11
    Publication Date: 1987-04-03
    Description: The primary structure of human uromodulin, a 616-amino acid, 85-kilodalton glycoprotein with in vitro immunosuppressive properties, was determined through isolation and characterization of complementary DNA and genomic clones. The amino acid sequence encoded by one of the exons of the uromodulin gene has homology to the low-density-lipoprotein receptor and the epidermal growth factor precursor. Northern hybridization analyses demonstrate that uromodulin is synthesized by the kidney. Evidence is provided that uromodulin is identical to the previously characterized Tamm-Horsfall glycoprotein, the most abundant protein in normal human urine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennica, D -- Kohr, W J -- Kuang, W J -- Glaister, D -- Aggarwal, B B -- Chen, E Y -- Goeddel, D V -- New York, N.Y. -- Science. 1987 Apr 3;236(4797):83-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3453112" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Base Sequence ; Chemistry, Physical ; Cloning, Molecular ; Cysteine ; DNA/genetics ; Gene Expression Regulation ; Genes ; Glycoproteins/*genetics ; Humans ; Mucoproteins/*analysis/*genetics ; Peptide Fragments/analysis ; Physicochemical Phenomena ; RNA, Messenger/genetics ; Uromodulin
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  • 12
    Publication Date: 1987-01-30
    Description: Increasing quantities of man-made organic chemicals are released each year into the biosphere. Some of these compounds are both toxic and relatively resistant to physical, chemical, or biological degradation, and they thus constitute an environmental burden of considerable magnitude. Genetic manipulation of microbial catabolic pathways offers a powerful means by which to accelerate evolution of biodegradative routes through which such compounds might be eliminated from the environment. In the experiments described here, a catabolic pathway for alkylbenzoates specified by the TOL plasmid of Pseudomonas was restructured to produce a pathway capable of processing a new substrate, 4-ethylbenzoate. Analysis of critical steps in the TOL pathway that prevent metabolism of 4-ethylbenzoate revealed that this compound fails to induce synthesis of the catabolic enzymes and that one of its metabolic intermediates inactivates catechol 2,3-dioxygenase (C23O), the enzyme that cleaves the aromatic ring. Consequently, the pathway was sequentially modified by recruitment of genes from mutant bacteria selected for their production of either an altered pathway operon regulator that is activated by 4-ethylbenzoate or an altered C23O that is less sensitive to metabolite inactivation. The redesigned pathway was stably expressed and enabled host bacteria to degrade 4-ethylbenzoate in addition to the normal substrates of the TOL pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ramos, J L -- Wasserfallen, A -- Rose, K -- Timmis, K N -- New York, N.Y. -- Science. 1987 Jan 30;235(4788):593-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3468623" target="_blank"〉PubMed〈/a〉
    Keywords: *Benzoates/*metabolism ; Biotransformation ; Catechol 2,3-Dioxygenase ; *Dioxygenases ; Gene Expression Regulation ; Genetic Engineering ; Oxygenases/metabolism ; *Plasmids ; Pseudomonas/enzymology/*genetics/growth & development ; Substrate Specificity
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  • 13
    Publication Date: 1987-09-25
    Description: A complementary DNA clone derived from rat brain messenger RNA has been isolated on the basis of homology to the human thyroid hormone receptor gene. Expression of this complementary DNA produces a high-affinity binding protein for thyroid hormones. Sequence analysis and the mapping of this gene to a distinct human genetic locus indicate the existence of multiple human thyroid hormone receptors. Messenger RNA from this gene is expressed in a tissue-specific fashion with highest levels in the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thompson, C C -- Weinberger, C -- Lebo, R -- Evans, R M -- GM-266444-09/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Sep 25;237(4822):1610-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3629259" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/*physiology ; DNA/genetics ; DNA-Binding Proteins/*genetics ; Gene Expression Regulation ; Genes ; Humans ; RNA, Messenger/genetics ; Rats ; Receptors, Thyroid Hormone/*genetics/metabolism ; Tissue Distribution ; Triiodothyronine/metabolism
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  • 14
    Publication Date: 1987-12-04
    Description: Genetic engineering is a powerful means of accelerating the evolution of new biological activities and has considerable potential for constructing microorganisms that can degrade environmental pollutants. Critical enzymes from five different catabolic pathways of three distinct soil bacteria have been combined in patchwork fashion into a functional ortho cleavage route for the degradation of methylphenols and methylbenzoates. The new bacterium thereby evolved was able to degrade and grow on mixtures of chloro- and methylaromatics that were toxic even for the bacteria that could degrade the individual components of the mixtures. Except for one enzymatic step, the pathway was fully regulated and its component enzymes were only synthesized in response to the presence of pathway substrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rojo, F -- Pieper, D H -- Engesser, K H -- Knackmuss, H J -- Timmis, K N -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1395-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Biochemistry, University of Geneva, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3479842" target="_blank"〉PubMed〈/a〉
    Keywords: Alcaligenes/enzymology/genetics ; Bacterial Proteins/genetics/*metabolism ; Benzoates/*metabolism ; *Biodegradation, Environmental ; Chlorobenzoates/*metabolism ; Gene Expression Regulation ; *Genes, Bacterial ; Genetic Engineering ; *Intramolecular Transferases ; Isomerases/genetics/metabolism ; Mixed Function Oxygenases/genetics/metabolism ; Oxidoreductases/genetics/metabolism ; Oxygenases/genetics/metabolism ; Pseudomonas/enzymology/genetics ; Recombinant Proteins/*metabolism
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  • 15
    Publication Date: 1987-03-20
    Description: A 4-kilobase complementary DNA (cDNA) encoding human macrophage-specific colony-stimulating factor (CSF-1) was isolated. When introduced into mammalian cells, this cDNA directs the expression of CSF-1 that is structurally and functionally indistinguishable from the natural human urinary CSF-1. Direct structural analysis of both the recombinant CSF-1 and the purified human urinary protein revealed that these species contain a sequence of at least 40 amino acids at their carboxyl termini which are not found in the coding region of a 1.6-kilobase CSF-1 cDNA that was previously described. These results demonstrate that the human CSF-1 gene can be expressed to yield at least two different messenger RNA species that encode distinct but related forms of CSF-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wong, G G -- Temple, P A -- Leary, A C -- Witek-Giannotti, J S -- Yang, Y C -- Ciarletta, A B -- Chung, M -- Murtha, P -- Kriz, R -- Kaufman, R J -- New York, N.Y. -- Science. 1987 Mar 20;235(4795):1504-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3493529" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Colony-Stimulating Factors/*genetics/urine ; DNA/genetics ; Gene Expression Regulation ; Humans ; Macrophages/physiology ; Molecular Weight ; Peptide Fragments ; Protein Processing, Post-Translational ; RNA, Messenger/genetics
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  • 16
    Publication Date: 1987-03-20
    Description: A human B-cell growth factor (BCGF) (12 kilodaltons) supports the clonal proliferation of B lymphocytes. A clone was isolated that contained the proper structural sequence to encode biologically active, 12-kilodalton BCGF in Escherichia coli and to hybridize to a specific messenger RNA, identified by in vitro translation in Xenopus laevis oocytes. A relatively hydrophobic region of 18 amino acids was found at the amino terminal of the 124-amino acid-long polypeptide. The carboxyl terminal is composed of at least 32 amino acids that are derived from nucleotide sequences bearing significant homology to the Alu repeat family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharma, S -- Mehta, S -- Morgan, J -- Maizel, A -- 16672/PHS HHS/ -- CA38499/CA/NCI NIH HHS/ -- CA39798/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 20;235(4795):1489-92.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3547651" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; B-Lymphocytes/*physiology ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Escherichia coli ; Gene Expression Regulation ; Growth Substances/*genetics ; Interleukin-4 ; Lymphokines/*genetics ; Repetitive Sequences, Nucleic Acid ; Sequence Homology, Nucleic Acid
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  • 17
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-01-30
    Description: The messenger RNA (mRNA) that encodes alpha subunit of the guanosine triphosphate-binding protein transducin (T alpha) and T alpha immunoreactivity were localized and measured in the rat retina during the light-dark cycle with in situ hybridization and immunohistochemistry. Both T alpha mRNA and T alpha immunoreactivity were observed only in photoreceptors. Within the photoreceptor T alpha mRNA was present primarily in the inner segments and to a lesser extent in the outer nuclear layer at all times during the day and night. However, the distribution of T alpha immunoreactivity varied profoundly with the light-dark cycle; during the day, T alpha immunoreactivity was highest in the inner segments, and at night the outer segments were more immunoreactive. The amounts of T alpha mRNA and T alpha immunoreactivity also depended on the light-dark cycle. Levels of T alpha mRNA were high immediately before and after lights on; levels were low for the rest of the light-dark cycle. During the day, T alpha immunoreactivity increased in the inner segments following the increase in T alpha mRNA. After the lights were turned off, T alpha immunoreactivity decreased in the inner segments and increased in the outer segments. Thus, it appears that T alpha is synthesized in the inner segments after a morning increase in T alpha mRNA. Newly synthesized T alpha remains in the inner segments until it is transported to the outer segments at night, where it may be involved in the increase in the sensitivity of photoreceptor rods at night.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brann, M R -- Cohen, L V -- New York, N.Y. -- Science. 1987 Jan 30;235(4788):585-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3101175" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport ; Circadian Rhythm ; GTP-Binding Proteins/*genetics/immunology/metabolism ; Gene Expression Regulation ; Immunoenzyme Techniques ; Male ; Membrane Proteins/*genetics/immunology/metabolism ; Photoreceptor Cells/*physiology/ultrastructure ; RNA, Messenger/genetics ; Rats ; Transducin
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  • 18
    Publication Date: 1987-03-20
    Description: An accelerated rate of glucose transport is among the most characteristic biochemical markers of cellular transformation. To study the molecular mechanism by which transporter activity is altered, cultured rodent fibroblasts transfected with activated myc, ras, or src oncogenes were used. In myc-transfected cells, the rate of 2-deoxy-D-glucose uptake was unchanged. However, in cells transfected with activated ras and src oncogenes, the rate of glucose uptake was markedly increased. The increased transport rate in ras- and src-transfected cells was paralleled by a marked increase in the amount of glucose transporter protein, as assessed by immunoblots, as well as by a markedly increased abundance of glucose transporter messenger RNA. Exposure of control cells to the tumor-promoting phorbol ester 12-O-tetradecanoyl phorbol-13-acetate (TPA) for 18 hours had a similar effect of increasing the rate of glucose transport and the abundance of transporter messenger RNA. For ras, src, and TPA, the predominant mechanism responsible for activation of the transport system is increased expression of the structural gene encoding the glucose transport protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flier, J S -- Mueckler, M M -- Usher, P -- Lodish, H F -- AM00856/AM/NIADDK NIH HHS/ -- AM28082/AM/NIADDK NIH HHS/ -- GM35012/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 20;235(4795):1492-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3103217" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division ; Cell Membrane/physiology ; Cell Transformation, Neoplastic/*physiopathology ; Deoxyglucose/metabolism ; GTP-Binding Proteins/physiology ; Gene Expression Regulation ; Glucose/*metabolism ; Monosaccharide Transport Proteins/*genetics ; *Oncogenes ; Protein-Tyrosine Kinases/physiology ; RNA, Messenger/genetics ; Rats ; Tetradecanoylphorbol Acetate/pharmacology ; Transfection
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  • 19
    Publication Date: 1987-01-02
    Description: The 5' flanking region of the mouse alpha-fetoprotein (AFP) gene contains a tissue-specific promoter and three upstream regulatory elements that behave as classical enhancers. At least one of these enhancers is now shown to be required for the tissue-specific expression of the AFP gene when it is introduced into the mouse genome by microinjection of cloned DNA fragments into fertilized eggs. Each enhancer can direct expression in the appropriate tissues, the visceral endoderm of the yolk sac, the fetal liver, and the gastrointestinal tract, but each exerts different influence in these three tissues. These differences may explain the tissue-specific diversity in the levels of expression characteristic of the AFP gene. The postnatal repression of transcription of the AFP gene in both liver and gut, as well as the reinitiation of its transcription during liver regeneration, is mimicked by the introduced gene when it is linked to the enhancer domains together or singly. Thus, the DNA sequence elements responsible for directing the activation of AFP transcription, its repression, and reinduction are contained in a limited segment of DNA within or 5' to the gene (or both) and are operative in the absence of the closely linked albumin gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hammer, R E -- Krumlauf, R -- Camper, S A -- Brinster, R L -- Tilghman, S M -- CA06927/CA/NCI NIH HHS/ -- CA28050/CA/NCI NIH HHS/ -- HD17321/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1987 Jan 2;235(4784):53-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2432657" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; *Enhancer Elements, Genetic ; Gene Expression Regulation ; Genes ; *Genes, Regulator ; Intestines/physiology ; Liver/physiology ; Mice ; Promoter Regions, Genetic ; RNA, Messenger/genetics ; Tissue Distribution ; Transcription, Genetic ; Transfection ; Yolk Sac/physiology ; alpha-Fetoproteins/*genetics
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  • 20
    Publication Date: 1987-05-01
    Description: GAP-43 is one of a small subset of cellular proteins selectively transported by a neuron to its terminals. Its enrichment in growth cones and its increased levels in developing or regenerating neurons suggest that it has an important role in neurite growth. A complementary DNA (cDNA) that encodes rat GAP-43 has been isolated to study its structural characteristics and regulation. The predicted molecular size is 24 kilodaltons, although its migration in SDS-polyacrylamide gels is anomalously retarded. Expression of GAP-43 is limited to the nervous system, where its levels are highest during periods of neurite outgrowth. Nerve growth factor or adenosine 3',5'-monophosphate induction of neurites from PC12 cells is accompanied by increased GAP-43 expression. GAP-43 RNA is easily detectable, although at diminished levels, in the adult rat nervous system. This regulation of GAP-43 is concordant with a role in growth-related processes of the neuron, processes that may continue in the mature animal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karns, L R -- Ng, S C -- Freeman, J A -- Fishman, M C -- New York, N.Y. -- Science. 1987 May 1;236(4801):597-600.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2437653" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Axons/physiology ; Bacteriophage lambda/genetics ; Base Sequence ; *Cloning, Molecular ; DNA/*genetics ; Electrophoresis, Polyacrylamide Gel ; GAP-43 Protein ; Ganglia, Spinal/analysis/embryology ; Gene Expression Regulation ; Growth Substances/genetics ; Immunosorbent Techniques ; Membrane Proteins/*genetics ; Nerve Tissue Proteins/*genetics ; Protein Biosynthesis ; RNA/genetics ; RNA, Messenger/genetics ; Rats
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  • 21
    Publication Date: 1987-02-20
    Description: Human T-cell leukemia virus (HTLV) types I and II are unusual among replication-competent retroviruses in that they contain a fourth gene (chi) necessary for replication. The chi gene product, p chi, transcriptionally transactivates the viral long repeat (LTR), and is thus a positive regulator. To investigate p chi transactivation, sequences from the U3 regions of the LTRs of HTLV-I and -II were inserted into the Moloney murine leukemia virus (M-MuLV) LTR by recombinant DNA techniques. Transient expression assays of the chimeric LTRs indicated that the HTLV sequences conferred to the M-MuLV LTR responsiveness to HTLV p chi protein. M-MuLV enhancers were not required for function of the chimeric LTRs. Infectious recombinant M-MuLVs containing chimeric LTRs were also generated. These viruses showed higher infectivity when assayed in mouse cells expressing HTLV-II p chi protein compared to normal mouse cells. Thus the HTLV sequences were able to confer p chi responsiveness to infectious M-MuLV. The generation of a virus dependent on a transactivating protein for its replication has implications for the evolution of the human T-cell leukemia viruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kitado, H -- Chen, I S -- Shah, N P -- Cann, A J -- Shimotohno, K -- Fan, H -- CA32454/CA/NCI NIH HHS/ -- CA32455/CA/NCI NIH HHS/ -- CA38597/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Feb 20;235(4791):901-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3027896" target="_blank"〉PubMed〈/a〉
    Keywords: DNA, Viral/*genetics ; Deltaretrovirus/*genetics ; Enhancer Elements, Genetic ; Gene Expression Regulation ; Moloney murine leukemia virus/*genetics ; Promoter Regions, Genetic ; Repetitive Sequences, Nucleic Acid ; Retroviridae Proteins/*genetics ; Trans-Activators ; Transcription Factors/*genetics ; Transcription, Genetic ; *Virus Replication
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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-08-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1987 Aug 7;237(4815):602-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3603042" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Transformation, Neoplastic ; Colonic Neoplasms/genetics ; Fibroblast Growth Factors/genetics ; Gene Expression Regulation ; Humans ; Mutation ; *Oncogenes ; Proto-Oncogenes ; Sarcoma, Kaposi/genetics
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  • 23
    Publication Date: 1987-02-06
    Description: The human T-cell leukemia viruses, HTLV-I and HTLV-II, contain a gene, termed x, with transcriptional regulatory function. The properties of the x proteins were analyzed by constructing mutant genes containing site-directed deletions and point mutations. The results demonstrate that the amino terminal 17 amino acids of the x protein constitute part of a functional domain that is critical for the transcriptional activating properties of the protein. Within this region, substitution of a leucine residue for a proline residue results in major changes in the trans-activation phenotype of the protein. The mutant HTLV-II x protein, though incapable of activating the HTLV-II long terminal repeat, will block trans-activation of the HTLV-II long terminal repeat by the wild-type protein. The altered phenotype of this mutant suggests a potential negative regulatory function of the x protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wachsman, W -- Cann, A J -- Williams, J L -- Slamon, D J -- Souza, L -- Shah, N P -- Chen, I S -- CA 30388/CA/NCI NIH HHS/ -- CA 32727/CA/NCI NIH HHS/ -- CA 38597/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1987 Feb 6;235(4789):674-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3027894" target="_blank"〉PubMed〈/a〉
    Keywords: Deltaretrovirus/*genetics ; Gene Expression Regulation ; *Genes, Viral ; Mutation ; Transcription Factors/*genetics ; Transcription, Genetic
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  • 24
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-11-20
    Description: The ability to generate a diverse immune response depends on the somatic assembly of genes that encode the antigen-binding portions of immunoglobulin molecules. In this article, we discuss the mechanism and control of these genomic rearrangement events and how aspects of this process are involved in generating the primary antibody repertoire.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alt, F W -- Blackwell, T K -- Yancopoulos, G D -- AI-20047/AI/NIAID NIH HHS/ -- CA-40427/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 20;238(4830):1079-87.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, College of Physicians and Surgeons of Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3317825" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/*genetics ; *Antibody Diversity ; B-Lymphocytes/*physiology ; Gene Expression Regulation ; *Genes, Immunoglobulin ; Humans ; Immunoglobulin Variable Region/*genetics
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  • 25
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-01-23
    Description: The glucocorticoid receptor from mouse AtT-20 cells exists in three forms: the untransformed receptor (9.1S; Mr of 319,000), a large oligomeric molecule that does not bind to DNA; the transformed receptor (4S; Mr of 96,000), which is formed by dissociation of untransformed receptor after steroid binding and which binds to DNA to modulate gene expression; and an intermediate size receptor (6S; Mr of 132,000), which also binds to DNA and contains a bound small RNA molecule. This RNA species has now been purified and identified as transfer RNA (tRNA). The three tRNA's for the basic amino acids accounted for about 78% of the total amino acid-accepting activity [arginine (52%), lysine (17%), and histidine (9%)], while the remaining 22% was represented by six other tRNA species. This tRNA-binding activity of the glucocorticoid receptor may reflect post-transcriptional mechanisms of regulating gene expression, such as alterations in the translational efficiency of or the modulation of the stability of hormone-induced proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ali, M -- Vedeckis, W V -- AM-36086/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1987 Jan 23;235(4787):467-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3798121" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation ; Mice ; Molecular Weight ; RNA, Transfer/classification/*metabolism ; Receptors, Glucocorticoid/*metabolism
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  • 26
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-08-21
    Description: Gene expression is dependent on the interaction of DNA binding factors with distinct promoter control elements to activate RNA synthesis. The expression of the HIS4 gene in yeast is under two different control systems. One of these, general amino acid control, involves a DNA binding protein, GCN4, that stimulates transcription in response to amino acid starvation by binding to 5'-TGACTC-3' sequences in the HIS4 promoter region. A second system, the basal level control, stimulates HIS4 transcription in the absence of amino acid starvation. The basal level transcription of the HIS4 gene is under the control of two genes, BAS1 and BAS2, which are also required for the control of purine biosynthesis. In addition, BAS2 is required for the utilization of organic phosphates in the growth medium. Genetic mapping and DNA sequence analysis show that BAS2 is PHO2, a gene previously identified as a regulator of phosphate metabolism. Direct biochemical analysis shows that the BAS2 gene encodes a protein that binds to both the HIS4 and PHO5 promoters. The involvement of a single DNA binding protein in the regulation of histidine, adenine, and phosphate metabolism suggests that yeast may use a few key DNA binding proteins to coordinate the regulation of diverse metabolic pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arndt, K T -- Styles, C -- Fink, G R -- GM 35010-04/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Aug 21;237(4817):874-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3303332" target="_blank"〉PubMed〈/a〉
    Keywords: Acid Phosphatase/*genetics ; Chromosome Mapping ; Gene Expression Regulation ; Genes, Fungal ; Histidine/*genetics ; Mutation ; Phosphates/physiology ; Promoter Regions, Genetic ; Saccharomyces cerevisiae/*genetics ; Transcription Factors/physiology ; Transcription, Genetic
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  • 27
    Publication Date: 1987-07-03
    Description: The distribution of cells containing messenger RNA that encodes amyloid beta protein was determined in hippocampi and in various cortical regions from cynomolgus monkeys, normal humans, and patients with Alzheimer's disease by in situ hybridization. Both 35S-labeled RNA antisense and sense probes to amyloid beta protein messenger RNA were used to ensure specific hybridization. Messenger RNA for amyloid beta protein was expressed in a subset of neurons in the prefrontal cortex from monkeys, normal humans, and patients with Alzheimer's disease. This messenger RNA was also present in the neurons of all the hippocampal fields from monkeys, normal humans and, although to a lesser extent in cornu ammonis 1, patients with Alzheimer's disease. The distribution of amyloid beta protein messenger RNA was similar to that of the neurofibrillary tangles of Alzheimer's disease in some regions, but the messenger RNA was also expressed in other neurons that are not usually involved in the pathology of Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bahmanyar, S -- Higgins, G A -- Goldgaber, D -- Lewis, D A -- Morrison, J H -- Wilson, M C -- Shankar, S K -- Gajdusek, D C -- AG05131/AG/NIA NIH HHS/ -- MH00519/MH/NIMH NIH HHS/ -- NS23038/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jul 3;237(4810):77-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3299701" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics ; Amyloid/*genetics ; Amyloid beta-Peptides ; Animals ; Brain/*physiopathology ; Cerebral Cortex/physiology ; Gene Expression Regulation ; Hippocampus/physiology ; Humans ; Macaca fascicularis ; Nucleic Acid Hybridization ; RNA, Messenger/genetics
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-06-05
    Description: The complementary DNAs and genes encoding the four major human myeloid growth factors--granulocyte colony-stimulating factor, macrophage colony-stimulating factor, granulocyte-macrophage colony-stimulating factor, and interleukin-3--have all been molecularly cloned. These DNA clones have proved valuable for studying the molecular biology of these important regulatory molecules as well as for the large-scale production of the recombinant growth factor proteins. These advances have led to a much better understanding of the role of the myeloid growth factors in regulating hematopoiesis in vivo that should soon find practical application in clinical medicine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clark, S C -- Kamen, R -- New York, N.Y. -- Science. 1987 Jun 5;236(4806):1229-37.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3296190" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; Gene Expression Regulation ; Granulocytes/cytology ; Humans ; *Interleukin-3/genetics/physiology/therapeutic use ; Macrophages/cytology ; Recombinant Proteins
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  • 29
    Publication Date: 1987-01-23
    Description: Transgenic mice carrying the gamma 2-crystallin promoter fused to the coding region of the bacterial lacZ gene were generated. The offspring of three founder mice expressed high levels of the enzyme solely in the central nuclear fiber cells of the lens as measured by an in situ assay for the detection of beta-galactosidase activity. These results suggest that gamma 2-crystallin sequences between -759 to +45 contain essential information required for appropriate tissue-specific and temporal regulation of the mouse gamma 2-crystallin gene. In a broader context, this study also demonstrates the utility of beta-galactosidase hybrid gene constructs for monitoring the activity of gene regulatory elements in transgenic mice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goring, D R -- Rossant, J -- Clapoff, S -- Breitman, M L -- Tsui, L C -- New York, N.Y. -- Science. 1987 Jan 23;235(4787):456-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3099390" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cataract/enzymology ; Crystallins/*genetics ; Galactosidases/*genetics ; Gene Expression Regulation ; *Lac Operon ; Lens, Crystalline/*physiology ; Mice ; Promoter Regions, Genetic ; Recombinant Fusion Proteins/*genetics ; Recombinant Proteins/*genetics ; Tissue Distribution ; Transfection ; beta-Galactosidase/*genetics/metabolism
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  • 30
    Publication Date: 1987-07-17
    Description: New blood vessel growth occurs during normal fetal development and in diseases such as cancer and diabetes. The polypeptide angiogenin induces new blood vessel growth in two biological assays and may play a role in the vascular development of the fetus and in the neovascularization that accompanies diseases and wound healing. A complementary DNA probe for human angiogenin was used to examine the tissue distribution of angiogenin messenger RNA (mRNA) in the developing rat and in selected transformed cell lines. Angiogenin mRNA was detected predominantly in adult liver but was also detectable at low levels in other tissues. The expression of the angiogenin gene in rat liver was found to be developmentally regulated; mRNA levels were low in the developing fetus, increased in the neonate, and maximal in the adult. The amount of angiogenin mRNA in human HT-29 colon carcinoma and SK-HEP hepatoma cells was not greater than that in normal rat liver. These results demonstrate that angiogenin is predominantly expressed in adult liver, that the pattern of angiogenin gene expression is not temporally related to vascular development in the rat, and that the transformed cells studied do not contain more angiogenin mRNA than does normal liver. If angiogenin activity is controlled at the transcriptional level, the results of this study suggest that the primary function of angiogenin in vivo may be in processes other than the regulation of vascular growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weiner, H L -- Weiner, L H -- Swain, J L -- HL26831/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1987 Jul 17;237(4812):280-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2440105" target="_blank"〉PubMed〈/a〉
    Keywords: Age Factors ; Animals ; Cell Line ; Gene Expression Regulation ; Humans ; Liver/physiology ; Neoplasm Proteins/*genetics ; Neovascularization, Pathologic ; RNA, Messenger/genetics ; Rats ; *Ribonuclease, Pancreatic ; Tissue Distribution
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  • 31
    Publication Date: 1987-08-14
    Description: The deduced amino acid sequence of a Drosophila gene isolated with a vertebrate sodium channel complementary DNA probe revealed an organization virtually identical to the vertebrate sodium channel protein; four homologous domains containing all putative membrane-spanning regions are repeated in tandem with connecting linkers of various sizes. All areas of the protein presumed to be critical for channel function show high evolutionary conservation. These include those proposed to function in voltage-sensitive gating, inactivation, and ion selectivity. All 24 putative gating charges of the vertebrate protein are in identical positions in the Drosophila gene. Ten introns interrupt the coding regions of the four homology units; introns with positions conserved among homology units bracket a region hypothesized to be the selectivity filter for the channel. The Drosophila gene maps to the right arm of the second chromosome in region 60D-E. This position does not coincide with any known mutations that confer behavioral phenotypes, but is close to the seizure locus (60A-B), which has been hypothesized to code for a voltage-sensitive sodium channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Salkoff, L -- Butler, A -- Wei, A -- Scavarda, N -- Giffen, K -- Ifune, C -- Goodman, R -- Mandel, G -- 1 R01 NS24785-01/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Aug 14;237(4816):744-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2441469" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Evolution ; DNA/genetics ; DNA Restriction Enzymes ; Drosophila/*genetics ; Drosophila melanogaster/genetics ; Electrophorus/genetics ; Exons ; Gene Expression Regulation ; Introns ; *Ion Channels ; Membrane Proteins/*genetics ; RNA, Messenger/genetics ; Sequence Homology, Nucleic Acid ; Sodium/*metabolism
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  • 32
    Publication Date: 1987-10-02
    Description: Thyroid hormone is important in the regulation of synthesis and secretion of thyroid-stimulating hormone (TSH) in the anterior pituitary, but its role in the control of hypothalamic thyrotropin-releasing hormone (TRH) is controversial. To determine whether thyroid hormone regulates the function of TRH in the hypothalamic tuberoinfundibular system, a study was made of the effect of hypothyroidism on thyrotropin-releasing hormone messenger RNA (proTRH mRNA) and TRH prohormone in the rat paraventricular nucleus. Extracts of rat hypothalamic paraventricular nucleus were examined by quantitative Northern blot analysis, and coronal sections of rat brain were examined by in situ hybridization histochemistry and immunocytochemistry. A nearly twofold increase in proTRH mRNA was observed in hypothyroid animals; this increase could be obliterated by levothyroxine treatment, suggesting an inverse relation between circulating thyroid hormone and proTRH mRNA. In situ hybridization showed that this response occurred exclusively in medial parvocellular neurons of the paraventricular nucleus. A simultaneous increase in proTRH mRNA and immunoreactive TRH prohormone in this region suggests that hypothyroidism induces both transcription and translation of the TRH prohormone in the paraventricular nucleus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Segerson, T P -- Kauer, J -- Wolfe, H C -- Mobtaker, H -- Wu, P -- Jackson, I M -- Lechan, R M -- DK 07900/DK/NIDDK NIH HHS/ -- DK 34540/DK/NIDDK NIH HHS/ -- DK 37021/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 2;238(4823):78-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, New England Medical Center Hospitals, Boston, MA 02111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3116669" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain Mapping ; Gene Expression Regulation ; Hypothyroidism/*physiopathology ; Immunoenzyme Techniques ; Paraventricular Hypothalamic Nucleus/*physiology ; RNA, Messenger/genetics ; Rats ; Thyroid Hormones/*physiology ; Thyrotropin-Releasing Hormone/*biosynthesis
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  • 33
    Publication Date: 1987-01-16
    Description: The autocrine model postulates that constitutive release of a mitogenic growth factor can lead to uncontrolled proliferation and cell transformation. A synthetic polynucleotide encoding epidermal growth factor conferred a tumorigenic phenotype on cells. These cells were transformed through the action of an autocrine circuit having an extracellular component.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stern, D F -- Hare, D L -- Cecchini, M A -- Weinberg, R A -- CA07285-03/CA/NCI NIH HHS/ -- R01CA39964/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Jan 16;235(4786):321-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3492043" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Cell Division ; *Cell Transformation, Neoplastic/pathology ; DNA, Recombinant ; Epidermal Growth Factor/antagonists & inhibitors/*genetics/immunology ; Gene Expression Regulation ; Mice ; Neoplasms, Experimental/genetics/pathology ; *Oncogenes ; Rats ; Transfection
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  • 34
    Publication Date: 1987-08-21
    Description: Humoral hypercalcemia of malignancy is a common complication of lung and certain other cancers. The hypercalcemia results from the actions of tumor factors on bone and kidney. We report here the isolation of full-length complementary DNA clones of a putative hypercalcemia factor, and the expression from the cloned DNA of the active protein in mammalian cells. The clones encode a prepro peptide of 36 amino acids and a mature protein of 141 amino acids that has significant homology with parathyroid hormone in the amino-terminal region. This previously unrecognized hormone may be important in normal as well as abnormal calcium metabolism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Suva, L J -- Winslow, G A -- Wettenhall, R E -- Hammonds, R G -- Moseley, J M -- Diefenbach-Jagger, H -- Rodda, C P -- Kemp, B E -- Rodriguez, H -- Chen, E Y -- New York, N.Y. -- Science. 1987 Aug 21;237(4817):893-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3616618" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Line ; Cloning, Molecular ; DNA/genetics ; Gene Expression Regulation ; Humans ; Hypercalcemia/*genetics ; Lung Neoplasms/complications/*genetics ; Neoplasm Proteins/*genetics ; Parathyroid Hormone/genetics ; Parathyroid Hormone-Related Protein
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  • 35
    Publication Date: 1987-12-04
    Description: Nuclear oncogene products have the potential to induce alterations in gene regulation leading to the genesis of cancer. The biochemical mechanisms by which nuclear oncoproteins act remain unknown. Recently, an oncogene, v-jun, was found to share homology with the DNA binding domain of a yeast transcription factor, GCN4. Furthermore, GCN4 and the phorbol ester-inducible enhancer binding protein, AP-1, recognize very similar DNA sequences. The human proto-oncogene c-jun has now been isolated, and the deduced amino acid sequence indicates more than 80 percent identity with v-jun. Expression of cloned c-jun in bacteria produced a protein with sequence-specific DNA binding properties identical to AP-1. Antibodies raised against two distinct peptides derived from v-jun reacted specifically with human AP-1. In addition, partial amino acid sequence of purified AP-1 revealed tryptic peptides in common with the c-jun protein. The structural and functional similarities between the c-jun product and the enhancer binding protein suggest that AP-1 may be encoded by c-jun. These findings demonstrate that the proto-oncogene product of c-jun interacts directly with specific target DNA sequences to regulate gene expression, and therefore it may now be possible to identify genes under the control of c-jun that affect cell growth and neoplasia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bohmann, D -- Bos, T J -- Admon, A -- Nishimura, T -- Vogt, P K -- Tjian, R -- CA25417/CA/NCI NIH HHS/ -- CA42564/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1386-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry, University of California, Berkeley, CA 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2825349" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies/immunology ; Avian Sarcoma Viruses/genetics ; Base Sequence ; Cross Reactions ; DNA/genetics ; DNA-Binding Proteins/genetics/immunology/*physiology ; Enhancer Elements, Genetic ; Fungal Proteins/genetics ; Gene Expression Regulation ; Genes, Viral ; Humans ; Molecular Sequence Data ; Oncogene Protein p65(gag-jun) ; Oncogenes ; *Protein Kinases ; Proto-Oncogene Proteins/genetics/immunology/*physiology ; Proto-Oncogene Proteins c-jun ; *Proto-Oncogenes ; Recombinant Proteins/genetics ; Retroviridae Proteins/genetics ; Saccharomyces cerevisiae/genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Homology, Nucleic Acid ; Transcription Factors/genetics/immunology/*physiology ; Transcription, Genetic
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  • 36
    Publication Date: 1987-10-30
    Description: To investigate whether a particular receptor subtype can be coupled to multiple effector systems, recombinant M2 muscarinic receptors were expressed in cells lacking endogenous receptor. The muscarinic agonist carbachol both inhibited adenylyl cyclase and stimulated phosphoinositide hydrolysis. The stimulation of phosphoinositide hydrolysis was significantly less efficient and more dependent on receptor levels than the inhibition of adenylyl cyclase. Both responses were mediated by guanine nucleotide binding proteins, as evidenced by their inhibition by pertussis toxin; the more efficiently coupled adenylyl cyclase response was significantly more sensitive. Thus, individual subtypes of a given receptor are capable of regulating multiple effector pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ashkenazi, A -- Winslow, J W -- Peralta, E G -- Peterson, G L -- Schimerlik, M I -- Capon, D J -- Ramachandran, J -- CA16417/CA/NCI NIH HHS/ -- HL23632/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):672-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology, Genentech, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2823384" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylate Cyclase Toxin ; Adenylyl Cyclases/*metabolism ; Animals ; Carbachol/pharmacology ; Cell Line ; Cricetinae ; Cyclic AMP/biosynthesis ; GTP-Binding Proteins/*metabolism ; Gene Expression Regulation ; Guanosine 5'-O-(3-Thiotriphosphate) ; Guanosine Triphosphate/analogs & derivatives/metabolism ; Oxotremorine/pharmacology ; Pertussis Toxin ; Phosphatidylinositols/*metabolism ; Receptors, Muscarinic/*metabolism ; Recombinant Proteins ; Thionucleotides/metabolism ; Virulence Factors, Bordetella/metabolism
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  • 37
    Publication Date: 1987-04-03
    Description: The determination of cell fates during the assembly of the ommatidia in the compound eye of Drosophila appears to be controlled by cell-cell interactions. In this process, the sevenless gene is essential for the development of a single type of photoreceptor cell. In the absence of proper sevenless function the cells that would normally become the R7 photoreceptors instead become nonneuronal cells. Previous morphological and genetic analysis has indicated that the product of the sevenless gene is involved in reading or interpreting the positional information that specifies this particular developmental pathway. The sevenless gene has now been isolated and characterized. The data indicate that sevenless encodes a transmembrane protein with a tyrosine kinase domain. This structural similarity between sevenless and certain hormone receptors suggests that similar mechanisms are involved in developmental decisions based on cell-cell interaction and physiological or developmental changes induced by diffusible factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hafen, E -- Basler, K -- Edstroem, J E -- Rubin, G M -- GM32795/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Apr 3;236(4797):55-63.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2882603" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; Cloning, Molecular ; DNA Restriction Enzymes ; Drosophila melanogaster/*embryology/genetics ; Eye/cytology/embryology ; Gene Expression Regulation ; Genes ; *Genes, Homeobox ; Growth Substances/physiology ; Membrane Proteins/genetics ; Phenotype ; Protein-Tyrosine Kinases/*genetics/physiology ; Receptors, Cell Surface/*genetics/physiology ; Transcription, Genetic
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  • 38
    Publication Date: 1987-04-10
    Description: The somatomedins or insulin-like growth factors (IGFs) are synthesized in many organs and tissues, but the specific cells that synthesize them in vivo have not been defined. By in situ hybridization histochemistry, IGF I (somatomedin C) and IGF II messenger RNAs were localized to connective tissues or cells of mesenchymal origin in 14 organs and tissues from human fetuses. IGF messenger RNAs were localized to perisinusoidal cells of liver, to perichondrium of cartilage, to sclera of eye, and to connective tissue layers, sheaths, septa, and capsules of each organ and tissue. All of the hybridizing regions are comprised predominantly of fibroblasts or other cells of mesenchymal origin. Because these cells are widely distributed and anatomically integrated into tissues and organs, they are ideally located for production of IGFs, which may exert paracrine effects on nearby target cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Han, V K -- D'Ercole, A J -- Lund, P K -- HD00435/HD/NICHD NIH HHS/ -- R01-HD08299/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1987 Apr 10;236(4798):193-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3563497" target="_blank"〉PubMed〈/a〉
    Keywords: Fetus/*physiology ; Gene Expression Regulation ; Humans ; Insulin-Like Growth Factor I/*physiology ; Insulin-Like Growth Factor II/*physiology ; Nucleic Acid Hybridization ; RNA, Messenger/metabolism ; Somatomedins/*physiology ; Tissue Distribution
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  • 39
    Publication Date: 1987-10-30
    Description: The gene for the human platelet alpha 2-adrenergic receptor has been cloned with oligonucleotides corresponding to the partial amino acid sequence of the purified receptor. The identity of this gene has been confirmed by the binding of alpha 2-adrenergic ligands to the cloned receptor expressed in Xenopus laevis oocytes. The deduced amino acid sequence is most similar to the recently cloned human beta 2- and beta 1-adrenergic receptors; however, similarities to the muscarinic cholinergic receptors are also evident. Two related genes have been identified by low stringency Southern blot analysis. These genes may represent additional alpha 2-adrenergic receptor subtypes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kobilka, B K -- Matsui, H -- Kobilka, T S -- Yang-Feng, T L -- Francke, U -- Caron, M G -- Lefkowitz, R J -- Regan, J W -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):650-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2823383" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Blood Platelets/*physiology ; Cloning, Molecular ; GTP-Binding Proteins/metabolism ; Gene Expression Regulation ; Genes ; Humans ; Infant, Newborn ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Multigene Family ; Oligodeoxyribonucleotides ; Phosphoproteins/genetics ; Receptors, Adrenergic, alpha/*genetics
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  • 40
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-09-18
    Description: A sea urchin DNA clone complementary to an embryonic messenger RNA whose protein product bears striking homology to the epidermal growth factor family of proteins has been identified and characterized. The structure of the protein is similar to that of previously identified regulatory genes in Drosophila and Caenorhabditis. RNA gel blot hybridization showed a unique temporal pattern of expression of this gene during embryogenesis and transcript enrichment in the embryonic ectoderm. These results suggest that this member of the epidermal growth factor gene family plays a role in early development decisions in sea urchin embryos.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hursh, D A -- Andrews, M E -- Raff, R A -- R01 HD21986/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1987 Sep 18;237(4821):1487-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3498216" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cysteine/analysis ; DNA/analysis ; Epidermal Growth Factor/*genetics ; Gene Expression Regulation ; Humans ; Mice ; Nucleic Acid Hybridization ; Peptides/*genetics ; RNA, Messenger/metabolism ; Repetitive Sequences, Nucleic Acid ; Sea Urchins/genetics
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  • 41
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-07-17
    Description: Cell fusion experiments have implicated positive or negative regulatory factors in the cell type--specific expression of specialized endogenous genes. The inability to readily manipulate such genes has prevented characterization of the cis-acting DNA sequences that interact with these factors. A transfection-fusion technique, which combined stable gene transfer and formation of transient heterokaryons, was used to study this class of factors and their DNA binding sites. Messenger RNA directed by a quiescent, rat prolactin promoter region stably transferred into mouse fibroblasts was detected only after fusion to rat pituitary cells, implying that pituitary cells contain a positive cell type--specific factor or factors. Nuclear run-on assays showed that fusion activation is transcriptional. Fusion did not activate either a stably transferred rat growth hormone gene promoter or expression of the endogenous silent fibroblast prolactin or growth hormone genes. Analysis by 5'-deletion mutation identified a 30-base pair DNA sequence required for cell fusion activation of the rat prolactin promoter region. Comparison with previous results from direct cellular transfer of this region implies that transfection-fusion identifies novel regulatory DNA sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lufkin, T -- Bancroft, C -- GM36847/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jul 17;237(4812):283-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3474782" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/genetics ; Animals ; Cell Fusion ; Chloramphenicol O-Acetyltransferase ; Gene Expression Regulation ; Growth Hormone/genetics ; Pituitary Gland/*physiology ; Prolactin/*genetics ; *Promoter Regions, Genetic ; Rats ; Transcription Factors/*genetics ; Transcription, Genetic ; Transfection
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  • 42
    Publication Date: 1987-03-20
    Description: Expression of the class I transplantation antigens of the major histocompatibility complex (MHC) is suppressed in cells transformed by the oncogenic human adenovirus 12 (Ad12). This suppression of class I antigen expression, which contributes to the tumorigenic phenotype of the transformed cells, has also been observed in some naturally occurring cancers. In the present study, the rate of transcription initiation of class I genes was measured by a nuclear run-on assay in Ad5- and Ad12-transformed cells of three different types. The rate of transcription was the same in all three. The stability of the class I messenger RNA was also examined and found to be the same in all three cell types. The results indicate that in Ad12-transformed cells the suppression is caused by an inhibition of the post-transcriptional processing of class I MHC messenger RNA in the nucleus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vaessen, R T -- Houweling, A -- van der Eb, A J -- New York, N.Y. -- Science. 1987 Mar 20;235(4795):1486-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3823900" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviruses, Human ; Cell Nucleus/metabolism ; *Cell Transformation, Viral ; Gene Expression Regulation ; HLA Antigens/*genetics ; Humans ; RNA Processing, Post-Transcriptional ; RNA, Messenger/genetics ; Transcription, Genetic
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  • 43
    Publication Date: 1987-04-17
    Description: Genetic analysis provides an approach for identifying regulatory loci that govern the expression of specific genes within the context of the entire organism. Such analyses have defined two unlinked regulatory loci, termed raf and Rif, that modulate the levels of alpha-fetoprotein in liver. Of primary importance for the isolation and characterization of the raf product is to determine whether it is produced by the hepatocyte or whether it is produced by a different cell type. By means of analysis of alpha-fetoprotein expression in livers of embryo aggregation chimeras derived from mice of different raf genotypes it was possible to conclude that the product of the raf locus is expressed as a hepatocyte autonomous function that acts in trans to regulate the level of alpha-fetoprotein messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogt, T F -- Solter, D -- Tilghman, S M -- CA06927/CA/NCI NIH HHS/ -- CA28050/CA/NCI NIH HHS/ -- HD17720/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1987 Apr 17;236(4799):301-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2436297" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chimera ; Crosses, Genetic ; Gene Expression Regulation ; *Genes ; *Genes, Regulator ; Genotype ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mosaicism ; Polymorphism, Restriction Fragment Length ; RNA, Messenger/genetics ; Species Specificity ; alpha-Fetoproteins/*genetics
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  • 44
    Publication Date: 1987-04-10
    Description: The development of Wilms' tumor, a pediatric nephroblastoma, has been associated with a deletion in the p13 region of chromosome 11. The structure and function or functions of this deleted genetic material are unknown. The role of this deletion in the process of malignant transformation was investigated by introducing a normal human chromosome 11 into a Wilms' tumor cell line by means of the microcell transfer technique. These variant cells, derived by microcell hybridization, expressed similar transformed traits in culture as the parental cell line. Furthermore, expression of several proto-oncogenes by the parental cells was unaffected by the introduction of this chromosome. However, the ability of these cells to form tumors in nude mice was completely suppressed. Transfer of other chromosomes, namely X and 13, had no effect on the tumorigenicity of the Wilms' tumor cells. These studies provide support for the existence of genetic information on chromosome 11 which can control the malignant expression of Wilms' tumor cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weissman, B E -- Saxon, P J -- Pasquale, S R -- Jones, G R -- Geiser, A G -- Stanbridge, E J -- CA 19401/CA/NCI NIH HHS/ -- SO7RR05469-23/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1987 Apr 10;236(4798):175-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3031816" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Transformation, Neoplastic/genetics ; Cells, Cultured ; *Chromosomes, Human, Pair 11 ; Gene Expression Regulation ; Humans ; Hybrid Cells ; Karyotyping ; Mice ; Mice, Nude ; Oncogenes ; Suppression, Genetic ; Wilms Tumor/*genetics/pathology
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  • 45
    Publication Date: 1987-10-02
    Description: Methylation of cytosine residues in eukaryotic DNA is common, but poorly understood. Typically several percent of the cytosines are methylated; however, it is unclear what governs which sequences eventually become modified. Neurospora crassa DNA containing the "zeta-eta" (zeta-eta) region, which is a region of unusually heavy methylation, was tested for its ability to direct DNA methylation de novo. DNA stripped of its methylation by propagation in Escherichia coli was reintroduced into Neurospora crassa by transformation. The zeta-eta region reproducibly became "properly" methylated whether inserted at its native chromosomal position or at ectopic sites. Adjacent Neurospora and bacterial sequences in the transforming DNA rarely became methylated. A model is presented that accounts for position-independent faithful methylation as observed in the zeta-eta region, as well as position-dependent methylation, as occasionally observed, especially with sequences not native to Neurospora.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Selker, E U -- Jensen, B C -- Richardson, G A -- GM 35690/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 2;238(4823):48-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2958937" target="_blank"〉PubMed〈/a〉
    Keywords: DNA, Fungal/*genetics ; Gene Expression Regulation ; Genes, Fungal ; *Methylation ; Neurospora/*genetics ; Neurospora crassa/*genetics ; RNA, Ribosomal, 5S/genetics ; Transformation, Genetic
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  • 46
    Publication Date: 1987-02-20
    Description: The amyloid beta protein has been identified as an important component of both cerebrovascular amyloid and amyloid plaques of Alzheimer's disease and Down syndrome. A complementary DNA for the beta protein suggests that it derives from a larger protein expressed in a variety of tissues. Overexpression of the gene in brain tissue from fetuses with Down syndrome (trisomy 21) can be explained by dosage since the locus encoding the beta protein maps to chromosome 21. Regional localization of this gene by both physical and genetic mapping places it in the vicinity of the genetic defect causing the inherited form of Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanzi, R E -- Gusella, J F -- Watkins, P C -- Bruns, G A -- St George-Hyslop, P -- Van Keuren, M L -- Patterson, D -- Pagan, S -- Kurnit, D M -- Neve, R L -- AG00029/AG/NIA NIH HHS/ -- HD10658/HD/NICHD NIH HHS/ -- HD20118/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1987 Feb 20;235(4791):880-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2949367" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics ; Amino Acid Sequence ; Amyloid/*genetics ; Amyloidosis/genetics ; Brain/physiopathology ; Chromosome Mapping ; *Chromosomes, Human, Pair 21 ; DNA/genetics ; Down Syndrome/genetics ; Gene Expression Regulation ; Genetic Linkage ; Humans ; RNA, Messenger/genetics ; Tissue Distribution ; Transcription, Genetic
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  • 47
    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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  • 48
    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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  • 49
    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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  • 50
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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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  • 51
    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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  • 52
    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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  • 53
    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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  • 54
    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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  • 55
    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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  • 56
    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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  • 57
    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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  • 58
    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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  • 59
    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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  • 60
    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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  • 61
    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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  • 62
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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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  • 63
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    Unknown
    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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  • 64
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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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  • 65
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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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  • 66
    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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  • 67
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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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  • 68
    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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  • 69
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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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  • 70
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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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  • 71
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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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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