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  • United States  (216)
  • Base Sequence  (143)
  • American Association for the Advancement of Science (AAAS)  (356)
  • Academic Press
  • American Association of Petroleum Geologists (AAPG)
  • Bonn: Institute of Labor Economics (IZA)
  • 1990-1994  (356)
  • 1992  (356)
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Publisher
  • American Association for the Advancement of Science (AAAS)  (356)
  • Academic Press
  • American Association of Petroleum Geologists (AAPG)
  • Bonn: Institute of Labor Economics (IZA)
  • Springer  (2)
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  • 1990-1994  (356)
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  • 1
    Publication Date: 1992-11-13
    Description: When glycine418 of Escherichia coli glutathione reductase, which is in a closely packed region of the dimer interface, is replaced with a bulky tryptophan residue, the enzyme becomes highly cooperative (Hill coefficient 1.76) for glutathione binding. The cooperativity is lost when the mutant subunit is hybridized with a wild-type subunit to create a heterodimer. The mutation appears to disrupt atomic packing at the dimer interface, which induces a change of kinetic mechanism. A single mutation in a region of the protein remote from the active site can thus act as a molecular switch to confer cooperativity on an enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scrutton, N S -- Deonarain, M P -- Berry, A -- Perham, R N -- New York, N.Y. -- Science. 1992 Nov 13;258(5085):1140-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Cambridge, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439821" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Escherichia coli/*enzymology/genetics ; Genes, Bacterial ; Glutathione/metabolism ; Glutathione Reductase/*chemistry/genetics/metabolism ; Glycine/chemistry ; Kinetics ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; *Mutagenesis, Site-Directed ; NADP/metabolism ; Plasmids ; Protein Multimerization ; Tryptophan/chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 1992-07-10
    Description: The technique of whole-genome polymerase chain reaction was used to study the DNA binding properties of the product of the wt1 gene. The zinc finger region of this gene is alternatively spliced such that the major transcript encodes a protein with three extra amino acids between the third and fourth fingers. The minor form of the protein binds specifically to DNA. It is now shown that the major form of wt1 messenger RNA encodes a protein that binds to DNA with a specificity that differs from that of the minor form. Therefore, alternative splicing within the DNA binding domain of a transcription factor can generate proteins with distinct DNA binding specificities and probably different physiological targets.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bickmore, W A -- Oghene, K -- Little, M H -- Seawright, A -- van Heyningen, V -- Hastie, N D -- New York, N.Y. -- Science. 1992 Jul 10;257(5067):235-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Human Genetics Unit, Western General Hospital, Edinburgh, Scotland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1321494" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites/*genetics ; Binding, Competitive ; Chromosomes, Human, Pair 11 ; DNA/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Humans ; Molecular Sequence Data ; Polymerase Chain Reaction ; *RNA Splicing ; RNA, Messenger/*metabolism ; Sequence Homology, Nucleic Acid ; Transcription, Genetic ; WT1 Proteins ; Wilms Tumor/*genetics ; Zinc Fingers/genetics
    Print ISSN: 0036-8075
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-11-06
    Description: The HM1 gene in maize controls both race-specific resistance to the fungus Cochliobolus carbonum race 1 and expression of the NADPH (reduced form of nicotinamide adenine dinucleotide phosphate)-dependent HC toxin reductase (HCTR), which inactivates HC toxin, a cyclic tetrapeptide produced by the fungus to permit infection. Several HM1 alleles were generated and cloned by transposon-induced mutagenesis. The sequence of wild-type HM1 shares homology with dihydroflavonol-4-reductase genes from maize, petunia, and snap-dragon. Sequence homology is greatest in the beta alpha beta-dinucleotide binding fold that is conserved among NADPH- and NADH (reduced form of nicotinamide adenine dinucleotide)-dependent reductases and dehydrogenases. This indicates that HM1 encodes HCTR.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johal, G S -- Briggs, S P -- New York, N.Y. -- Science. 1992 Nov 6;258(5084):985-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biotechnology Research, Pioneer Hi-Bred International, Inc., Johnston, IA 50131.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1359642" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Blotting, Southern ; Cloning, Molecular ; DNA/chemistry/genetics ; *Genes, Plant ; *Helminthosporium ; Introns ; Molecular Sequence Data ; NADP/pharmacology ; Nucleic Acid Hybridization ; Oxidoreductases/chemistry/*genetics ; Peptides, Cyclic/antagonists & inhibitors ; *Plant Diseases ; *Plant Proteins ; Polymorphism, Restriction Fragment Length ; RNA Splicing ; RNA, Messenger/genetics ; Zea mays/enzymology/*genetics
    Print ISSN: 0036-8075
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-02-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abele, L G -- DeBry, R W -- New York, N.Y. -- Science. 1992 Feb 21;255(5047):903.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1312252" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/transmission ; Centers for Disease Control and Prevention (U.S.) ; Dentistry ; Ethics ; Florida ; *HIV-1/genetics ; Humans ; Jurisprudence ; Lawyers ; Professional Misconduct ; United States
    Print ISSN: 0036-8075
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-09-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1992 Sep 11;257(5076):1472-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1523403" target="_blank"〉PubMed〈/a〉
    Keywords: *AIDS Vaccines ; Acquired Immunodeficiency Syndrome/immunology/*prevention & control ; HIV/immunology ; Humans ; National Institutes of Health (U.S.) ; Recombinant Proteins ; Safety ; United States ; Vaccines, Synthetic
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-08-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):739.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1496391" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; *Crime ; Female ; *Genetics, Medical ; Humans ; Male ; *National Institutes of Health (U.S.) ; *Research Support as Topic ; United States ; United States Dept. of Health and Human Services ; *Violence
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-08-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1992 Aug 14;257(5072):876.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1502552" target="_blank"〉PubMed〈/a〉
    Keywords: *Acquired Immunodeficiency Syndrome/prevention & control ; Emigration and Immigration ; Government Agencies ; *HIV Infections/prevention & control ; *HIV Seropositivity ; Humans ; *Politics ; Prejudice ; Travel ; United States
    Print ISSN: 0036-8075
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-08-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1992 Aug 21;257(5073):1035.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1509251" target="_blank"〉PubMed〈/a〉
    Keywords: Government Agencies/*organization & administration ; Industry ; Research Support as Topic/*economics ; United States
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-08-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):741.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1496393" target="_blank"〉PubMed〈/a〉
    Keywords: *Management Audit ; *National Institutes of Health (U.S.) ; *Research Support as Topic ; United States ; *United States Dept. of Health and Human Services
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-01-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bishop, J E -- New York, N.Y. -- Science. 1992 Jan 3;255(5040):10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553521" target="_blank"〉PubMed〈/a〉
    Keywords: Humans ; Newspapers as Topic/standards ; Periodicals as Topic/*standards ; Publishing/*standards ; Quackery ; Science/*standards ; United States
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-07-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1992 Jul 24;257(5069):476-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1636080" target="_blank"〉PubMed〈/a〉
    Keywords: Humans ; National Institutes of Health (U.S.)/*organization & administration ; Research/*standards ; *Research Support as Topic ; United States
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  • 12
    Publication Date: 1992-05-22
    Description: Human immunodeficiency virus type 1 (HIV-1) transmission from infected patients to health-care workers has been well documented, but transmission from an infected health-care worker to a patient has not been reported. After identification of an acquired immunodeficiency syndrome (AIDS) patient who had no known risk factors for HIV infection but who had undergone an invasive procedure performed by a dentist with AIDS, six other patients of this dentist were found to be HIV-infected. Molecular biologic studies were conducted to complement the epidemiologic investigation. Portions of the HIV proviral envelope gene from each of the seven patients, the dentist, and 35 HIV-infected persons from the local geographic area were amplified by polymerase chain reaction and sequenced. Three separate comparative genetic analyses--genetic distance measurements, phylogenetic tree analysis, and amino acid signature pattern analysis--showed that the viruses from the dentist and five dental patients were closely related. These data, together with the epidemiologic investigation, indicated that these patients became infected with HIV while receiving care from a dentist with AIDS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ou, C Y -- Ciesielski, C A -- Myers, G -- Bandea, C I -- Luo, C C -- Korber, B T -- Mullins, J I -- Schochetman, G -- Berkelman, R L -- Economou, A N -- New York, N.Y. -- Science. 1992 May 22;256(5060):1165-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of HIV/AIDS, Centers for Disease Control, Atlanta, GA 30333.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1589796" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/blood/microbiology/*transmission ; Amino Acid Sequence ; Base Sequence ; DNA, Viral/blood/genetics/isolation & purification ; *Dentistry ; Female ; Florida ; Genetic Variation ; HIV Infections/microbiology/*transmission ; HIV-1/*genetics/isolation & purification ; Humans ; Male ; Molecular Sequence Data ; Monocytes/physiology ; Oligodeoxyribonucleotides ; *Patients ; Phylogeny ; Sequence Homology, Nucleic Acid ; Viral Envelope Proteins/*genetics
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-08-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jaron, D -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):861-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1502546" target="_blank"〉PubMed〈/a〉
    Keywords: *Government Agencies ; Humans ; *Interinstitutional Relations ; *National Institutes of Health (U.S.) ; *Research Support as Topic ; United States
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-05-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1992 May 29;256(5061):1274.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1598566" target="_blank"〉PubMed〈/a〉
    Keywords: Budgets ; Government Agencies/*economics ; *Politics ; *Research Support as Topic ; United States
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-04-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1992 Apr 24;256(5056):437-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1570504" target="_blank"〉PubMed〈/a〉
    Keywords: Child ; History, 20th Century ; Humans ; *Intelligence ; Lead/administration & dosage/*adverse effects ; Lead Poisoning/physiopathology ; *Scientific Misconduct ; United States
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  • 16
    Publication Date: 1992-04-03
    Description: Colorectal (CR) tumors are usually curable if detected before metastasis. Because genetic alterations are associated with the development of these tumors, mutant genes may be found in the stool of individuals with CR neoplasms. The stools of nine patients whose tumors contained mutations of K-ras were analyzed. In eight of the nine cases, the ras mutations were detectable in DNA purified from the stool. These patients included those with benign and malignant neoplasms from proximal and distal colonic epithelium. Thus, colorectal tumors can be detected by a noninvasive method based on the molecular pathogenesis of the disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sidransky, D -- Tokino, T -- Hamilton, S R -- Kinzler, K W -- Levin, B -- Frost, P -- Vogelstein, B -- CA06973/CA/NCI NIH HHS/ -- CA35494/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):102-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oncology, Johns Hopkins University, Baltimore, MD 21231.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1566048" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Amino Acid Sequence ; Base Sequence ; Blotting, Southern ; Carcinoma/diagnosis/*genetics/pathology ; Colonic Neoplasms/diagnosis/*genetics/pathology ; DNA, Neoplasm/genetics/*isolation & purification ; Feces/chemistry ; Female ; *Genes, ras ; Humans ; Male ; Middle Aged ; Molecular Sequence Data ; *Mutation ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction ; Prognosis ; Rectal Neoplasms/diagnosis/*genetics/pathology
    Print ISSN: 0036-8075
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  • 17
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-04-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1566053" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Child ; Female ; *Health Promotion ; Humans ; Infant ; Infant Mortality ; Male ; Middle Aged ; *Minority Groups ; National Institutes of Health (U.S.) ; *Research Support as Topic ; United States
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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-02-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abelson, P H -- New York, N.Y. -- Science. 1992 Feb 21;255(5047):901.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546282" target="_blank"〉PubMed〈/a〉
    Keywords: Government Agencies ; Hazardous Waste/*economics ; United States
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-05-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1992 May 15;256(5059):956-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1589774" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Mapping ; History, 20th Century ; Human Genome Project/economics/*organization & administration ; National Institutes of Health (U.S.) ; Research Support as Topic ; United States
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  • 20
    Publication Date: 1992-04-24
    Description: The gene that encodes the cystic fibrosis transmembrane conductance regulator (CFTR) is defective in patients with cystic fibrosis. Although the protein product of the CFTR gene has been proposed to function as a chloride ion channel, certain aspects of its function remain unclear. The role of CFTR in the adenosine 3',5'-monophosphate (cAMP)-dependent regulation of plasma membrane recycling was examined. Adenosine 3',5'-monophosphate is known to regulate endocytosis and exocytosis in chloride-secreting epithelial cells that express CFTR. However, mutant epithelial cells derived from a patient with cystic fibrosis exhibited no cAMP-dependent regulation of endocytosis and exocytosis until they were transfected with complementary DNA encoding wild-type CFTR. Thus, CFTR is critical for cAMP-dependent regulation of membrane recycling in epithelial tissues, and this function of CFTR could explain in part the pleiotropic nature of cystic fibrosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bradbury, N A -- Jilling, T -- Berta, G -- Sorscher, E J -- Bridges, R J -- Kirk, K L -- New York, N.Y. -- Science. 1992 Apr 24;256(5056):530-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Alabama, Birmingham 35294.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373908" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Membrane/*physiology ; Chlorides/metabolism ; Colforsin/pharmacology ; Cyclic AMP/pharmacology ; Cystic Fibrosis/*physiopathology ; Cystic Fibrosis Transmembrane Conductance Regulator ; DNA/genetics ; Endocytosis/drug effects/physiology ; Epithelium/secretion ; Exocytosis/drug effects/physiology ; Gene Expression ; Horseradish Peroxidase/metabolism ; Humans ; Membrane Proteins/genetics/*physiology ; Molecular Sequence Data ; Pancreatic Neoplasms ; Transfection ; Tumor Cells, Cultured ; Wheat Germ Agglutinins/metabolism
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  • 21
    Publication Date: 1992-07-31
    Description: The Wilms tumor suppressor gene wt1 encodes a zinc finger DNA binding protein, WT1, that functions as a transcriptional repressor. The fetal mitogen insulin-like growth factor II (IGF-II) is overexpressed in Wilms tumors and may have autocrine effects in tumor progression. The major fetal IGF-II promoter was defined in transient transfection assays as a region spanning from nucleotides -295 to +135, relative to the transcription start site. WT1 bound to multiple sites in this region and functioned as a potent repressor of IGF-II transcription in vivo. Maximal repression was dependent on the presence of WT1 binding sites on each side of the transcriptional initiation site. These findings provide a molecular basis for overexpression of IGF-II in Wilms tumors and suggest that WT1 negatively regulates blastemal cell proliferation by limiting the production of a fetal growth factor in the developing vertebrate kidney.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Drummond, I A -- Madden, S L -- Rohwer-Nutter, P -- Bell, G I -- Sukhatme, V P -- Rauscher, F J 3rd -- CA 10817/CA/NCI NIH HHS/ -- CA 47983/CA/NCI NIH HHS/ -- CA 52009/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 31;257(5070):674-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1323141" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Blotting, Northern ; DNA/chemistry/metabolism ; DNA-Binding Proteins/*metabolism ; Deoxyribonuclease I/metabolism ; *Gene Expression Regulation, Neoplastic ; Genes, Wilms Tumor/*physiology ; Humans ; Insulin-Like Growth Factor II/*genetics ; Kidney/embryology/metabolism ; Mice ; Molecular Sequence Data ; Promoter Regions, Genetic ; Rats ; Sequence Homology, Nucleic Acid ; Transfection ; WT1 Proteins ; Wilms Tumor/genetics/metabolism ; Zinc Fingers
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-01-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1992 Jan 31;255(5044):529-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1736355" target="_blank"〉PubMed〈/a〉
    Keywords: National Institutes of Health (U.S.)/*organization & administration ; *Politics ; Research/*organization & administration ; United States ; United States Public Health Service/*organization & administration
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-01-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Voss, H J -- New York, N.Y. -- Science. 1992 Jan 31;255(5044):514-5; author reply 515-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1736350" target="_blank"〉PubMed〈/a〉
    Keywords: *Agriculture ; Animals ; California ; *Diptera ; Fruit ; Government Agencies ; United States ; United States Department of Agriculture
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  • 24
    Publication Date: 1992-09-25
    Description: Two major developmentally regulated isoforms of the Drosophila chorion transcription factor CF2 differ by an extra zinc finger within the DNA binding domain. The preferred DNA binding sites were determined and are distinguished by an internal duplication of TAT in the site recognized by the isoform with the extra finger. The results are consistent with modular interactions between zinc fingers and trinucleotides and also suggest rules for recognition of AT-rich DNA sites by zinc finger proteins. The results show how modular finger interactions with trinucleotides can be used, in conjunction with alternative splicing, to alter the binding specificity and increase the spectrum of sites recognized by a DNA binding domain. Thus, CF2 may potentially regulate distinct sets of target genes during development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gogos, J A -- Hsu, T -- Bolton, J -- Kafatos, F C -- New York, N.Y. -- Science. 1992 Sep 25;257(5078):1951-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Developmental Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1290524" target="_blank"〉PubMed〈/a〉
    Keywords: *Alternative Splicing ; Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; DNA-Binding Proteins/*metabolism ; *Drosophila Proteins ; Drosophila melanogaster/genetics ; Hydrogen Bonding ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry/metabolism ; Protein Binding ; *Regulatory Sequences, Nucleic Acid ; Structure-Activity Relationship ; Transcription Factors/*metabolism ; *Zinc Fingers
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-06-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pace, N R -- New York, N.Y. -- Science. 1992 Jun 5;256(5062):1402-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1376496" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Catalysis ; Chromosome Deletion ; Escherichia coli/genetics/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Biosynthesis ; Proteins/genetics ; RNA/genetics/*metabolism ; RNA, Ribosomal/genetics/*metabolism ; Ribosomes/*metabolism
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-07-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1992 Jul 31;257(5070):609.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1496368" target="_blank"〉PubMed〈/a〉
    Keywords: *Government Agencies ; Peer Review/*standards ; Surveys and Questionnaires ; United States
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  • 27
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-08-14
    Description: This article provides a historical perspective for the patenting of gene sequences and describes the fundamentals and evolution of patent law. It summarizes federal technology transfer law and policy and assesses the impacts of patenting on academic research. The patentability of gene sequences is then considered along with potential impacts that published sequence data may have on obtaining patent protection for downstream products. Industry's position on gene patenting is summarized and perspectives from the emerging public record on these issues are presented. The article discussing points at which the filing of patent applications and the licensing of patents may be appropriate. It concludes that technology transfer policies for genome research must be adopted carefully so that they remain viable in a time of rapid technological change.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adler, R G -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):908-14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1502557" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biomedical Research ; Biotechnology/*legislation & jurisprudence ; DNA/*genetics ; Federal Government ; *Genome ; Genome, Human ; Government Regulation ; Humans ; Hybridomas ; Information Dissemination ; *Patents as Topic ; *Research ; United States
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  • 28
    Publication Date: 1992-07-03
    Description: After observations that Macaca nemestrina were exceptionally susceptible to simian immunodeficiency virus and human immunodeficiency virus type-2 (HIV-2), studies of HIV-1 replication were initiated. Several strains of HIV-1, including a recent patient isolate, replicated in vitro in peripheral blood mononuclear cells (PBMCs) and in CD4-positive M. nemestrina lymphocytes in a CD4-dependent fashion. Eight animals were subsequently inoculated with either cell-associated or cell-free suspensions of HIV-1. All animals had HIV-1 isolated by cocultivation, had HIV-1 DNA in their PBMCs as shown by polymerase chain reaction, and experienced sustained seroconversion to a broad spectrum of HIV-1 proteins. Macaca nemestrina is an animal model of HIV-1 infections that provides opportunities for evaluating the pathogenesis of acute HIV-1 replication and candidate vaccines and therapies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Agy, M B -- Frumkin, L R -- Corey, L -- Coombs, R W -- Wolinsky, S M -- Koehler, J -- Morton, W R -- Katze, M G -- AI26503/AI/NIAID NIH HHS/ -- AI27757/AI/NIAID NIH HHS/ -- RR00166/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Jul 3;257(5066):103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regional Primate Research Center, University of Washington, Seattle, WA 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1621083" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/physiology ; Base Sequence ; Cysteine/metabolism ; Databases, Factual ; *Genes, gag ; HIV Infections/*physiopathology ; HIV Seropositivity ; HIV-1/isolation & purification/pathogenicity/*physiology ; Humans ; Lymphocytes/immunology/physiology ; Macaca nemestrina/*microbiology ; Methionine/metabolism ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Oligonucleotide Probes ; Viral Proteins/biosynthesis/isolation & purification ; *Virus Replication
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  • 29
    Publication Date: 1992-08-14
    Description: A pseudo--half-knot can be formed by binding an oligonucleotide asymmetrically to an RNA hairpin loop. This binding motif was used to target the human immunodeficiency virus TAR element, an important viral RNA structure that is the receptor for Tat, the major viral transactivator protein. Oligonucleotides complementary to different halves of the TAR structure bound with greater affinity than molecules designed to bind symmetrically around the hairpin. The pseudo--half-knot--forming oligonucleotides altered the TAR structure so that specific recognition and binding of a Tat-derived peptide was disrupted. This general binding motif may be used to disrupt the structure of regulatory RNA hairpins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ecker, D J -- Vickers, T A -- Bruice, T W -- Freier, S M -- Jenison, R D -- Manoharan, M -- Zounes, M -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):958-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ISIS Pharmaceuticals, Carlsbad, CA 92008.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1502560" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA, Viral/metabolism ; Gene Products, tat/metabolism ; HIV/*genetics ; Kinetics ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Oligoribonucleotides/*chemistry ; RNA, Viral/*chemistry/genetics/metabolism ; tat Gene Products, Human Immunodeficiency Virus
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-05-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1992 May 29;256(5061):1270.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1598563" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Costs and Cost Analysis ; Government Agencies/*economics ; Humans ; *Museums ; United States
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  • 31
    Publication Date: 1992-02-21
    Description: The gap genes of Drosophila are the first zygotic genes to respond to the maternal positional signals and establish the body pattern along the anterior-posterior axis. The gap gene knirps, required for patterning in the posterior region of the embryo, can be activated throughout the wild-type embryo and is normally repressed from the anterior and posterior sides. These results provide direct molecular evidence that the posterior morphogen system interacts in a fundamentally different manner than do hunchback and bicoid, which are responsible for anterior pattern formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pankratz, M J -- Busch, M -- Hoch, M -- Seifert, E -- Jackle, H -- New York, N.Y. -- Science. 1992 Feb 21;255(5047):986-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck Institut fur Biophysikalische Chemie, Abteilung Molekulare Entwicklungsbiologie, Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546296" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cloning, Molecular ; Drosophila melanogaster/embryology/*genetics ; Gene Expression Regulation ; Genes ; Molecular Sequence Data ; Morphogenesis ; Regulatory Sequences, Nucleic Acid
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  • 32
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-03-20
    Description: Increased immunoglobulin A (IgA) antibodies to the Epstein-Barr virus (EBV) appear months to years before the clinical onset of nasopharyngeal carcinoma and define populations at high risk for this EBV-associated epithelial cancer common in south China. In the human HT-29 epithelial cell line, polymeric IgA (pIgA) specific for EBV promoted infection of the otherwise refractory epithelial cells. When bound to pIgA, EBV entered epithelial cells through secretory component-mediated IgA transport but no longer infected B lymphocytes. Such an immune-induced shift in EBV tissue tropism provides a paradigm for endogenous spread of EBV in the immune host that predicts infectious sequelae of epithelium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sixbey, J W -- Yao, Q Y -- CA21765/CA/NCI NIH HHS/ -- CA38877/CA/NCI NIH HHS/ -- CA52258/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Mar 20;255(5051):1578-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Infectious Diseases, St. Jude Children's Research Hospital, TN 38101-0318.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1312750" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocytes/immunology/microbiology ; Base Sequence ; Epithelium/*microbiology ; Gene Products, env ; Herpesvirus 4, Human/*pathogenicity ; Humans ; Immunoglobulin A/*immunology ; In Vitro Techniques ; Infectious Mononucleosis/immunology ; Lymphocyte Activation/immunology ; Molecular Sequence Data ; Nasopharyngeal Neoplasms/immunology ; Secretory Component/physiology
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-06-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1992 Jun 19;256(5064):1619.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1319085" target="_blank"〉PubMed〈/a〉
    Keywords: *Scientific Misconduct ; United States ; *United States Office of Research Integrity
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-09-11
    Description: The carnivorous habit in flowering plants represents a grade of structural organization. Different morphological features associated with the attraction, trapping, and digestion of prey characterize a diversity of specialized forms, including the familiar pitcher and flypaper traps. Phylogenetic analysis of nucleotide sequence data from the plastic rbcL gene indicates that both carnivory and stereotyped trap forms have arisen independently in different lineages of angiosperms. Furthermore, these results demonstrate that flypaper traps share close common ancestry with all other trap forms. Recognition of these patterns of diversification may provide ideal, naturally occurring systems for studies of developmental processes underlying macromorphological evolution in angiosperms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Albert, V A -- Williams, S E -- Chase, M W -- New York, N.Y. -- Science. 1992 Sep 11;257(5076):1491-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1523408" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Biological Evolution ; Molecular Sequence Data ; *Phylogeny ; *Plant Physiological Phenomena ; Plants/*classification/genetics ; Polymerase Chain Reaction ; Restriction Mapping
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-11-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamilton, D P -- New York, N.Y. -- Science. 1992 Nov 6;258(5084):882.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439796" target="_blank"〉PubMed〈/a〉
    Keywords: Budgets ; *National Institutes of Health (U.S.) ; Research Support as Topic/*organization & administration ; United States
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-09-25
    Description: Entry into mitosis in Schizosaccharomyces pombe is negatively regulated by the wee1+ gene, which encodes a protein kinase with serine-, theonine-, and tyrosine-phosphorylating activities. The wee1+ kinase negatively regulates mitosis by phosphorylating p34cdc2 on tyrosine 15, thereby inactivating the p34cdc2-cyclin B complex. The human homolog of the wee1+ gene (WEE1Hu) was overproduced in bacteria and assayed in an in vitro system. Unlike its fission yeast homolog, the product of the WEE1Hu gene encoded a tyrosine-specific protein kinase. The human WEE1 kinase phosphorylated the p34cdc2-cyclin B complex on tyrosine 15 but not on threonine 14 in vitro and inactivated the p34cdc2-cyclin B kinase. This inhibition was reversed by the human Cdc25C protein, which catalyzed the dephosphorylation of p34cdc2. These results indicate that the product of the WEE1Hu gene directly regulates the p34cdc2-cyclin B complex in human cells and that a kinase other than that encoded by WEE1Hu phosphorylates p34cdc2 on threonine 14.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parker, L L -- Piwnica-Worms, H -- New York, N.Y. -- Science. 1992 Sep 25;257(5078):1955-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, Tufts University School of Medicine, Boston, MA 02111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1384126" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; CDC2 Protein Kinase/antagonists & inhibitors/*metabolism ; *Cell Cycle ; *Cell Cycle Proteins ; Cyclins/antagonists & inhibitors/*metabolism ; Humans ; Macromolecular Substances ; Molecular Sequence Data ; *Nuclear Proteins ; Oligodeoxyribonucleotides/chemistry ; Phosphorylation ; Phosphotyrosine ; Protein Kinases/genetics/*metabolism ; Protein-Tyrosine Kinases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Schizosaccharomyces pombe Proteins ; Tyrosine/analogs & derivatives/metabolism
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-01-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sommer, S S -- New York, N.Y. -- Science. 1992 Jan 31;255(5044):514.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1736349" target="_blank"〉PubMed〈/a〉
    Keywords: *Alleles ; Base Sequence ; DNA/*genetics ; *Polymerase Chain Reaction ; Restriction Mapping
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  • 38
    Publication Date: 1992-07-03
    Description: Experiments were performed to determine if retroviral-mediated transfer of the human multidrug resistance 1 gene (MDR1) into murine bone marrow cells would confer drug resistance to the cells and whether the MDR1 gene could be used as a dominant selectable marker in vivo. When mice transplanted with bone marrow cells containing a transferred MDR1 gene were treated with the cytotoxic drug taxol, a substantial enrichment for transduced bone marrow cells was observed. This demonstration of positive selection establishes the ability to amplify clones of transduced hematopoietic cells in vivo and suggests possible applications in human therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sorrentino, B P -- Brandt, S J -- Bodine, D -- Gottesman, M -- Pastan, I -- Cline, A -- Nienhuis, A W -- New York, N.Y. -- Science. 1992 Jul 3;257(5066):99-103.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Clinical Hematology Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1352414" target="_blank"〉PubMed〈/a〉
    Keywords: Alkaloids/*pharmacology ; Antineoplastic Agents, Phytogenic/*pharmacology ; Base Sequence ; Bone Marrow/*physiology ; Bone Marrow Transplantation/*physiology ; DNA/genetics/isolation & purification ; Drug Resistance/*genetics ; Erythrocytes/physiology ; Genetic Vectors ; Hematopoietic Stem Cells/*cytology/drug effects ; Humans ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Paclitaxel ; Polymerase Chain Reaction/methods ; Proviruses/genetics ; Retroviridae/genetics ; *Transfection
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  • 39
    Publication Date: 1992-02-28
    Description: Multiple human immunodeficiency virus type-1 sequences from the V3 and V4-V5 regions of the envelope gene were analyzed from three mother-infant pairs. The infants' viral sequences were less diverse than those of their mothers. In two pairs, a proviral form infrequently found in the mother predominated in her infant. A conserved N-linked glycosylation site within the V3 region, present in each mother's sequence set, was absent in all of the infants' sequence sets. These findings demonstrate that a minor subset of maternal virus is transmitted to the infant.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolinsky, S M -- Wike, C M -- Korber, B T -- Hutto, C -- Parks, W P -- Rosenblum, L L -- Kunstman, K J -- Furtado, M R -- Munoz, J L -- AI-32535/AI/NIAID NIH HHS/ -- HD26619-01/HD/NICHD NIH HHS/ -- P01-25569/PHS HHS/ -- New York, N.Y. -- Science. 1992 Feb 28;255(5048):1134-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Northwestern University Medical School, Chicago, IL 60611.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546316" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/congenital/microbiology/*transmission ; Amino Acid Sequence ; Base Sequence ; Female ; Genotype ; Glycosylation ; HIV Antigens/genetics ; HIV Envelope Protein gp120/genetics/immunology ; HIV-1/*genetics/immunology ; Humans ; Infant ; Maternal-Fetal Exchange ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry ; Polymerase Chain Reaction ; Pregnancy ; Selection, Genetic ; Sequence Alignment
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  • 40
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-08-14
    Description: In the past year, the National Institutes of Health (NIH) has filed patent applications on more than 2750 partial complementary DNA sequences of unknown function. The rationale for the filings--that patent protection may be necessary to ensure that private firms are willing to invest in developing related products--rests on two premises: first, that NIH may obtain patent rights that will offer effective product monopolies to licensee firms, and second, that unless NIH obtains these rights now, firms will be unable to obtain a comparable degree of exclusivity by other means, such as by obtaining patents on their own subsequent innovations. Neither premise is clearly wrong, although both are subject to doubt in view of statements from industry representatives that the NIH patenting strategy will deter rather than promote product development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eisenberg, R S -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):903-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Michigan Law School, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1502556" target="_blank"〉PubMed〈/a〉
    Keywords: Biomedical Research ; Biotechnology ; DNA/*genetics ; *Federal Government ; *Genes ; Human Genome Project ; Humans ; National Institutes of Health (U.S.) ; *Patents as Topic ; United States
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-06-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1992 Jun 5;256(5062):1391.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1604312" target="_blank"〉PubMed〈/a〉
    Keywords: *Acquired Immunodeficiency Syndrome ; Ethics, Professional ; History, 20th Century ; Humans ; Jurisprudence ; National Institutes of Health (U.S.) ; Newspapers as Topic ; Paris ; Research/*standards ; Scientific Misconduct ; *Societies, Scientific ; United States
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-02-21
    Description: Ribonuclease footprinting of nascent messenger RNA within ternary complexes of vaccinia RNA polymerase revealed an RNA binding site that encompasses an 18-nucleotide RNA segment. The dimensions of the binding site did not change as the polymerase moved along the template. Capping of the 5' end of the RNA was cotranscriptional and was confined to nascent chains 31 nucleotides or greater in length. Purified capping enzyme formed a binary complex with RNA polymerase in solution in the absence of nucleic acid. These findings suggest a mechanism for cotranscriptional establishment of messenger RNA identity in eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hagler, J -- Shuman, S -- GM42498/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Feb 21;255(5047):983-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular Biology, Sloan-Kettering Institute, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546295" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell-Free System ; DNA/chemistry ; Eukaryotic Cells ; In Vitro Techniques ; Molecular Sequence Data ; *RNA Caps ; RNA Polymerase II/metabolism ; RNA, Messenger/*biosynthesis ; Templates, Genetic ; Terminator Regions, Genetic ; Transcription Factors/physiology ; *Transcription, Genetic ; Vaccinia virus
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-12-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aldhous, P -- New York, N.Y. -- Science. 1992 Dec 4;258(5088):1572-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1455243" target="_blank"〉PubMed〈/a〉
    Keywords: *DNA-Directed DNA Polymerase ; Drug Industry/*legislation & jurisprudence ; Europe ; Indicators and Reagents ; Polymerase Chain Reaction/*methods ; Taq Polymerase ; United States
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  • 44
    Publication Date: 1992-01-24
    Description: The c-Myc oncoprotein belongs to a family of proteins whose DNA binding domains contain a basic region-helix-loop-helix (bHLH) motif. Systematic mutagenesis of c-Myc revealed that dimerized bHLH motifs formed a parallel four-helix bundle with the amino termini of helices 1 and 2 directed toward the inner and outer nucleotides of the DNA binding site, respectively. Both the basic region and the carboxyl-terminal end of the loop contributed to DNA binding specificity. The DNA binding domain of c-Myc may therefore be structurally similar to that of restriction endonuclease Eco RI.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Halazonetis, T D -- Kandil, A N -- New York, N.Y. -- Science. 1992 Jan 24;255(5043):464-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Research, Merck Sharp and Dohme Research Laboratories, West Point, PA 19486.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1734524" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; DNA-Binding Proteins/*chemistry ; Deoxyribonuclease EcoRI/*chemistry ; Humans ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Conformation ; Proto-Oncogene Proteins c-myc/*chemistry ; Sequence Alignment ; Transcription Factors/chemistry
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  • 45
    Publication Date: 1992-09-04
    Description: The Autographa californica multinucleocapsid nuclear polyhedrosis virus (AcMNPV), which is used for the overexpression of eukaryotic genes and is being engineered for possible use as a viral insecticide, has a circular, supercoiled genome of approximately 128 kilobases. Despite its widespread use, little is known about the mechanism by which AcMNPV replicates. Evidence is presented in this report that AcMNPV origins of DNA replication are repeated sequences each containing several closely related imperfect palindromes that are present in six regions distributed around the genome. Although AcMNPV infection-dependent plasmid replication was initiated by a single complete palindrome, the amount of replication was substantially increased in plasmids containing six or eight palindromes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pearson, M -- Bjornson, R -- Pearson, G -- Rohrmann, G -- AI21973/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Sep 4;257(5075):1382-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Agricultural Chemistry, Oregon State University, Corvallis 97331.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1529337" target="_blank"〉PubMed〈/a〉
    Keywords: Baculoviridae/*genetics ; Base Sequence ; *DNA Replication ; DNA, Superhelical/chemistry/*genetics ; DNA, Viral/chemistry/*genetics ; Genes, Viral/*genetics ; Molecular Sequence Data ; Mutagenesis ; Nucleic Acid Hybridization ; Plasmids ; Repetitive Sequences, Nucleic Acid ; Transfection ; *Virus Replication
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  • 46
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-06-05
    Description: Knowledge of zoonotic transmission cycles is essential for the development of effective strategies for disease prevention. The enzootiology of Lyme disease in California differs fundamentally from that reported from the eastern United States. Woodrats, not mice, serve as reservoir hosts, and Ixodes neotomae, a nonhuman-biting tick, maintains the agent of Lyme disease, Borrelia burgdorferi, in enzootic cycles. The western black-legged tick, Ixodes pacificus, is the primary vector to humans, but it appears to be an inefficient maintenance vector. Isolates of B. burgdorferi from California exhibit considerable antigenic heterogeneity, and some isolates differ strikingly from isolates recovered from this and other geographic regions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, R N -- Lane, R S -- AI22501/AI/NIAID NIH HHS/ -- U50/CCU906594/PHS HHS/ -- New York, N.Y. -- Science. 1992 Jun 5;256(5062):1439-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomological Sciences, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1604318" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Bacterial Proteins/analysis ; Borrelia/isolation & purification ; Borrelia burgdorferi Group/isolation & purification/*pathogenicity ; California ; Dipodomys/parasitology ; Disease Reservoirs ; Larva ; Lyme Disease/*transmission ; Mice/parasitology ; Rodentia/*parasitology ; Ticks/*parasitology ; United States
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  • 47
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-01-10
    Description: Many specific DNA-binding proteins bind to sites with dyad symmetry, and the bound form of the protein is a dimer. For some proteins, dimers form in solution and bind to DNA. LexA repressor of Escherichia coli has been used to test an alternative binding model in which two monomers bind sequentially. This model predicts that a repressor monomer should bind with high specificity to an isolated operator half-site. Monomer binding to a half-site was observed. A second monomer bound to an intact operator far more tightly than the first monomer; this cooperativity arose from protein-protein contacts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, B -- Little, J W -- GM24178/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 10;255(5041):203-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Arizona, Tucson 85721.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553548" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*metabolism ; Base Sequence ; Binding Sites ; DNA, Bacterial/*metabolism ; DNA-Binding Proteins/*metabolism ; Deoxyribonucleases ; Escherichia coli/*metabolism ; Kinetics ; Macromolecular Substances ; Models, Structural ; Molecular Sequence Data ; Oligodeoxyribonucleotides/metabolism ; Operon ; Rec A Recombinases/genetics ; Repressor Proteins/metabolism ; *Serine Endopeptidases
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  • 48
    Publication Date: 1992-04-10
    Description: The myoD family of DNA binding proteins has been implicated in the control of myogenesis in a variety of organisms. Searches for homologs in the nematode Caenorhabditis elegans yielded only one gene, designated hlh-1, expressed in body-wall muscle cells and their precursors. To assess the role of hlh-1 in C. elegans myogenesis, genetic deficiencies spanning the hlh-1 locus were isolated after gamma irradiation. Embryos homozygous for these deficiencies exhibited extensive body-wall muscle differentiation, including expression of several characteristic myofilament proteins and weak contracile behavior. Thus, zygotic hlh-1 expression was not required for body-wall muscle precursors to adopt muscle cell fates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, L -- Krause, M -- Draper, B -- Weintraub, H -- Fire, A -- R01 GM037706/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 10;256(5054):240-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Carnegie Institution of Washington, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1314423" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Caenorhabditis/embryology/genetics/*physiology ; Cell Differentiation ; *Chromosome Deletion ; Chromosome Mapping ; Crosses, Genetic ; DNA/genetics/isolation & purification ; DNA-Binding Proteins/*genetics ; Embryo, Nonmammalian/cytology/physiology/radiation effects ; Gamma Rays ; Homozygote ; Molecular Sequence Data ; Multigene Family ; Muscle Proteins/*genetics ; Muscles/*embryology/physiology/radiation effects ; MyoD Protein ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction ; Sequence Homology, Nucleic Acid
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  • 49
    Publication Date: 1992-12-07
    Description: An adeno-associated virus vector encoding an antisense RNA was used to transduce stable intracellular resistance to human immunodeficiency virus-1 (HIV-1) in human hemopoietic and non-hemopoietic cell lines. The antisense targets are present in all HIV-1 transcripts and include the TAR sequence, which is critical for transcription and virus replication, and the polyadenylation signal. Cell lines expressing antisense RNA showed up to 95 percent inhibition of gene expression directed by the HIV-1 long terminal repeat and greater than 99 percent reduction in infectious HIV-1 production, with no detectable cellular toxicity. Because of their efficient transcription and inability to recombine with HIV-1, adeno-associated virus vectors represent a promising form of anti-retroviral gene therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chatterjee, S -- Johnson, P R -- Wong, K K Jr -- New York, N.Y. -- Science. 1992 Nov 27;258(5087):1485-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health, Rockville, MD 20852.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1359646" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; CD4-Positive T-Lymphocytes/microbiology ; Cell Line ; Chloramphenicol O-Acetyltransferase/genetics ; Dependovirus/*genetics ; Drug Resistance, Microbial/genetics ; Gene Products, tat/genetics ; Genetic Vectors/*genetics ; HIV Long Terminal Repeat/genetics ; HIV-1/*genetics/physiology ; Humans ; Molecular Sequence Data ; Neomycin/pharmacology ; RNA, Antisense/*genetics ; RNA, Messenger/genetics ; RNA, Viral/genetics ; Transfection ; Virus Replication/genetics ; tat Gene Products, Human Immunodeficiency Virus
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  • 50
    Publication Date: 1992-11-27
    Description: The cystic fibrosis gene product (CFTR) is a complex protein that functions as an adenosine 3,5-monophosphate (cAMP)-stimulated ion channel and possibly as a regulator of intracellular processes. In order to determine whether the CFTR molecule contains a functional aqueous pathway, anion, water, and urea transport were measured in Xenopus oocytes expressing CFTR. Cyclic AMP agonists induced a Cl- conductance of 94 microsiemens and an increase in water permeability of 4 x 10(-4) centimeter per second that was inhibited by a Cl- channel blocker and was dependent on anion composition. CFTR has a calculated single channel water conductance of 9 x 10(-13) cubic centimeter per second, suggesting a pore-like aqueous pathway. Oocytes expressing CFTR also showed cAMP-stimulated transport of urea but not the larger solute sucrose. Thus CFTR contains a cAMP-stimulated aqueous pore that can transport anions, water, and small solutes. The results also provide functional evidence for water movement through an ion channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hasegawa, H -- Skach, W -- Baker, O -- Calayag, M C -- Lingappa, V -- Verkman, A S -- DK35124/DK/NIDDK NIH HHS/ -- DK43840/DK/NIDDK NIH HHS/ -- HL42368/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Nov 27;258(5087):1477-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco 94143-0532.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1279809" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Transport/physiology ; Chlorides/metabolism ; Cyclic AMP/physiology ; Cystic Fibrosis Transmembrane Conductance Regulator ; Female ; Humans ; In Vitro Techniques ; Ion Channels/*physiology ; Membrane Proteins/*physiology ; Molecular Sequence Data ; Oocytes ; Urea/metabolism ; Water/metabolism ; Xenopus
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  • 51
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-10-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, R -- New York, N.Y. -- Science. 1992 Oct 23;258(5082):540.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1329204" target="_blank"〉PubMed〈/a〉
    Keywords: Centers for Disease Control and Prevention (U.S.) ; *Communicable Disease Control ; *Institute of Medicine (U.S.) ; Population Surveillance ; United States
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  • 52
    Publication Date: 1992-12-11
    Description: Angiogenic factors produced by monocytes-macrophages are involved in the pathogenesis of chronic inflammatory disorders characterized by persistent angiogenesis. The possibility was tested that interleukin-8 (IL-8), which is a cytokine that is chemotactic for lymphocytes and neutrophils, is also angiogenic. Human recombinant IL-8 was potently angiogenic when implanted in the rat cornea and induced proliferation and chemotaxis of human umbilical vein endothelial cells. Angiogenic activity present in the conditioned media of inflamed human rheumatoid synovial tissue macrophages or lipopolysaccharide-stimulated blood monocytes was equally blocked by antibodies to either IL-8 or tumor necrosis factor-alpha. An IL-8 antisense oligonucleotide specifically blocked the production of monocyte-induced angiogenic activity. These data suggest a function for macrophage-derived IL-8 in angiogenesis-dependent disorders such as rheumatoid arthritis, tumor growth, and wound repair.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koch, A E -- Polverini, P J -- Kunkel, S L -- Harlow, L A -- DiPietro, L A -- Elner, V M -- Elner, S G -- Strieter, R M -- AR30692/AR/NIAMS NIH HHS/ -- AR41492/AR/NIAMS NIH HHS/ -- HL39926/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Dec 11;258(5089):1798-801.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Northwestern University Medical School, Chicago, IL 60611.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1281554" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arthritis, Rheumatoid/physiopathology ; Base Sequence ; Cell Division/drug effects ; Cells, Cultured ; Chemotaxis/*drug effects ; Cornea/*drug effects/physiology ; Dose-Response Relationship, Drug ; Endothelium, Vascular/drug effects/*physiology ; Fibroblast Growth Factor 2/pharmacology ; Humans ; Interleukin-8/genetics/*pharmacology ; Macrophages/*physiology ; Mice ; Molecular Sequence Data ; Monocytes/physiology ; *Neovascularization, Pathologic ; Oligonucleotides, Antisense/*pharmacology ; Rabbits ; Rats ; Recombinant Proteins/pharmacology ; Synovial Fluid/physiology ; Tumor Necrosis Factor-alpha/genetics ; Umbilical Veins
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  • 53
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-11-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1992 Nov 13;258(5085):1176-237.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439828" target="_blank"〉PubMed〈/a〉
    Keywords: *Minority Groups ; *Science ; United States
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  • 54
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-09-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, R -- New York, N.Y. -- Science. 1992 Sep 18;257(5077):1619.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1529346" target="_blank"〉PubMed〈/a〉
    Keywords: Budgets/*legislation & jurisprudence ; Financing, Government/legislation & jurisprudence ; National Institutes of Health (U.S.)/*economics ; United States
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  • 55
    Publication Date: 1992-02-07
    Description: In retroviral integration, the viral integration protein (integrase) mediates a concerted DNA cleavage-ligation reaction in which the target DNA is cleaved and the resulting 5' ends of target DNA are joined to the 3' ends of viral DNA. Through an oligonucleotide substrate that mimics the recombination intermediate formed by this initial cleavage-ligation reaction, the purified integrase of human immunodeficiency virus was shown to promote the same reaction in reverse, a process called disintegration. Analysis of a set of structurally related substrates showed that integrase could promote a range of DNA cleavage-ligation reactions. When the viral DNA component of the disintegration substrate was single-stranded, integrase could mediate a DNA splicing reaction analogous to RNA splicing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chow, S A -- Vincent, K A -- Ellison, V -- Brown, P O -- AI27205/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Feb 7;255(5045):723-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Stanford University Medical Center, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1738845" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/chemistry/*metabolism ; DNA Nucleotidyltransferases/*metabolism ; DNA, Viral/chemistry/*metabolism ; Esterification ; HIV-1/*enzymology/genetics ; Integrases ; Molecular Sequence Data ; RNA Splicing
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  • 56
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-03-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Healy, B -- New York, N.Y. -- Science. 1992 Mar 13;255(5050):1333.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1542782" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; Humans ; Research Personnel/*statistics & numerical data ; Science/*manpower ; United States ; Women, Working/*statistics & numerical data
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 57
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-02-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hedges, S B -- Kumar, S -- Tamura, K -- Stoneking, M -- GM 20293-20/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Feb 7;255(5045):737-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1738849" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Base Sequence ; *Biological Evolution ; DNA, Mitochondrial/*chemistry ; Humans ; Phylogeny
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  • 58
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-03-06
    Description: Trypsin (Tr) and chymotrypsin (Ch) have similar tertiary structures, yet Tr cleaves peptides at arginine and lysine residues and Ch prefers large hydrophobic residues. Although replacement of the S1 binding site of Tr with the analogous residues of Ch is sufficient to transfer Ch specificity for ester hydrolysis, specificity for amide hydrolysis is not transferred. Trypsin is converted to a Ch-like protease when the binding pocket alterations are further modified by exchange of the Ch surface loops 185 through 188 and 221 through 225 for the analogous Tr loops. These loops are not structural components of either the S1 binding site or the extended substrate binding sites. This mutant enzyme is equivalent to Ch in its catalytic rate, but its substrate binding is impaired. Like Ch, this mutant utilizes extended substrate binding to accelerate catalysis, and substrate discrimination occurs during the acylation step rather than in substrate binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hedstrom, L -- Szilagyi, L -- Rutter, W J -- DK21344/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1992 Mar 6;255(5049):1249-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hormone Research Institute, University of California, San Francisco 94143-0534.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546324" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; Chymotrypsin/*chemistry/metabolism ; Hydrolysis ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Mutagenesis, Site-Directed ; Protein Conformation ; Substrate Specificity ; Trypsin/*chemistry/genetics/metabolism
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  • 59
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-08-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, R -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):739.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1496390" target="_blank"〉PubMed〈/a〉
    Keywords: Bioethics ; Body Height ; Child ; Growth Disorders/*drug therapy ; Growth Hormone/adverse effects/*therapeutic use ; Humans ; National Institutes of Health (U.S.) ; United States
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  • 60
    Publication Date: 1992-04-03
    Description: Interleukin-1 beta (IL-1 beta) mediates a wide range of immune and inflammatory responses. The active cytokine is generated by proteolytic cleavage of an inactive precursor. A complementary DNA encoding a protease that carries out this cleavage has been cloned. Recombinant expression in COS-7 cells enabled the cells to process precursor IL-1 beta to the mature form. Sequence analysis indicated that the enzyme itself may undergo proteolytic processing. The gene encoding the protease was mapped to chromosomal band 11q23, a site frequently involved in rearrangement in human cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cerretti, D P -- Kozlosky, C J -- Mosley, B -- Nelson, N -- Van Ness, K -- Greenstreet, T A -- March, C J -- Kronheim, S R -- Druck, T -- Cannizzaro, L A -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):97-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Corporation, Seattle, WA 98101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373520" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Caspase 1 ; Cell Line ; Chromosome Banding ; *Chromosomes, Human, Pair 11 ; Cloning, Molecular ; Enzyme Precursors/biosynthesis/*genetics/isolation & purification ; Humans ; Metalloendopeptidases/biosynthesis/*genetics/isolation & purification ; Molecular Sequence Data ; Neutrophils/enzymology ; Oligodeoxyribonucleotides ; Poly A/genetics/isolation & purification ; Polymerase Chain Reaction/methods ; RNA/genetics/isolation & purification ; RNA, Messenger/genetics ; Recombinant Proteins/biosynthesis/isolation & purification ; Transfection
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  • 61
    Publication Date: 1992-11-27
    Description: Peptide nucleic acids (PNAs) are polyamide oligomers that can strand invade duplex DNA, causing displacement of one DNA strand and formation of a D-loop. Binding of either a T10 PNA or a mixed sequence 15-mer PNA to the transcribed strand of a G-free transcription cassette caused 90 to 100 percent site-specific termination of pol II transcription elongation. When a T10 PNA was bound on the nontranscribed strand, site-specific inhibition never exceeded 50 percent. Binding of PNAs to RNA resulted in site-specific termination of both reverse transcription and in vitro translation, precisely at the position of the PNA.RNA heteroduplex. Nuclear microinjection of cells constitutively expressing SV40 large T antigen (T Ag) with either a 15-mer or 20-mer PNA targeted to the T Ag messenger RNA suppressed T Ag expression. This effect was specific in that there was no reduction in beta-galactosidase expression from a coinjected expression vector and no inhibition of T Ag expression after microinjection of a 10-mer PNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hanvey, J C -- Peffer, N J -- Bisi, J E -- Thomson, S A -- Cadilla, R -- Josey, J A -- Ricca, D J -- Hassman, C F -- Bonham, M A -- Au, K G -- New York, N.Y. -- Science. 1992 Nov 27;258(5087):1481-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Glaxo Inc. Research Institute, Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1279811" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Polyomavirus Transforming/genetics ; Base Sequence ; DNA/*metabolism ; Deoxyribonuclease HindIII/antagonists & inhibitors ; Gene Expression/drug effects ; HeLa Cells ; Humans ; In Vitro Techniques ; Molecular Sequence Data ; Oligodeoxyribonucleotides/*metabolism/pharmacology ; Oligonucleotides, Antisense/*metabolism/pharmacology ; *Peptide Nucleic Acids ; Plasmids ; Protein Biosynthesis/drug effects ; RNA/metabolism ; Rabbits ; Rats ; Transcription, Genetic/drug effects
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 62
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-06-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koshland, D E Jr -- New York, N.Y. -- Science. 1992 Jun 5;256(5062):1373.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1604307" target="_blank"〉PubMed〈/a〉
    Keywords: Animal Husbandry ; Cost-Benefit Analysis ; *Costs and Cost Analysis ; Economics, Hospital ; *Legislation as Topic ; United States ; Universities/economics
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  • 63
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-02-28
    Description: The transcription factor E2F controls the expression of several proliferation-related genes and is a target of the adenovirus E1A oncogene. In human cells, both cyclin A and the cdk2 protein kinase were found in complexes with E2F. Although the total amounts of cdk2 were constant in the cell cycle, binding to E2F was detected only when cells entered S phase, a time when the cdk2 kinase is activated. These data suggest that the interaction between cdk2 and E2F requires an active kinase that has cyclin A as a targeting component.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pagano, M -- Draetta, G -- Jansen-Durr, P -- New York, N.Y. -- Science. 1992 Feb 28;255(5048):1144-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1312258" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus Early Proteins ; Base Sequence ; *CDC2-CDC28 Kinases ; *Carrier Proteins ; Cell Cycle ; *Cell Cycle Proteins ; Cyclin-Dependent Kinase 2 ; *Cyclin-Dependent Kinases ; Cyclins/*metabolism ; *DNA-Binding Proteins ; E2F Transcription Factors ; HeLa Cells ; Humans ; Macromolecular Substances ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry ; Oncogene Proteins, Viral/genetics ; Protamine Kinase/metabolism ; Protein Kinases/*metabolism ; *Protein-Serine-Threonine Kinases ; Retinoblastoma-Binding Protein 1 ; *S Phase ; Transcription Factor DP1 ; Transcription Factors/*metabolism
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  • 64
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-11-20
    Description: A synthetic RNA-DNA bubble duplex construct intended to mimic the nucleic acid framework of a functional transcription elongation complex was designed and assembled. The construct consisted of a double-stranded DNA duplex of variable length (the template and nontemplate strands) containing an internal noncomplementary DNA "bubble" sequence. The 3' end of an RNA oligonucleotide that is partially complementary to the template DNA strand was hybridized within the DNA bubble to form an RNA-DNA duplex with a non-complementary 5'-terminal RNA tail. The addition of either Escherichia coli or T7 RNA polymerase to this construct formed a complex that synthesized RNA with good efficiency from the hybridized RNA primer in a template-directed and processive manner, and displayed other features of a normal promoter-initiated transcription elongation complex. Other such constructs can be designed to examine many of the functional and regulatory properties of transcription systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Daube, S S -- von Hippel, P H -- GM-15792/GM/NIGMS NIH HHS/ -- GM-29158/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Nov 20;258(5086):1320-4.〈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/1280856" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/genetics ; DNA-Directed RNA Polymerases/*metabolism ; Escherichia coli/enzymology/genetics ; In Vitro Techniques ; Molecular Sequence Data ; Nucleic Acid Hybridization ; *Promoter Regions, Genetic ; RNA/genetics ; Structure-Activity Relationship ; Templates, Genetic ; *Transcription, Genetic
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  • 65
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-10-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malacinski, G M -- Doniach, S -- New York, N.Y. -- Science. 1992 Oct 23;258(5082):531.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411557" target="_blank"〉PubMed〈/a〉
    Keywords: *Career Mobility ; *Financing, Government ; National Institutes of Health (U.S.)/*economics ; *Research Support as Topic ; United States ; Universities/*economics
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  • 66
    Publication Date: 1992-09-04
    Description: Yeast RNA polymerase II initiation factor b copurifies with three polypeptides of 85, 73, and 50 kilodaltons and with a protein kinase that phosphorylates the carboxyl-terminal repeat domain (CTD) of the largest polymerase subunit. The gene that encodes the 73-kilodalton polypeptide, designated TFB1, was cloned and found to be essential for cell growth. The deduced protein sequence exhibits no similarity to those of protein kinases. However, the sequence is similar to that of the 62-kilodalton subunit of the HeLa transcription factor BFT2, suggesting that this factor is the human counterpart of yeast factor b. Immunoprecipitation experiments using antibodies to the TFB1 gene product demonstrate that the transcriptional and CTD kinase activities of factor b are closely associated with an oligomer of the three polypeptides. Photoaffinity labeling with 3'-O-(4-benzoyl)benzoyl-ATP (adenosine triphosphate) identified an ATP-binding site in the 85-kilodalton polypeptide, suggesting that the 85-kilodalton subunit contains the catalytic domain of the kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gileadi, O -- Feaver, W J -- Kornberg, R D -- GM-36659/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Sep 4;257(5075):1389-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Sherman Fairchild Center, Stanford University Medical School, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1445600" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Affinity Labels ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; *Cloning, Molecular ; Immunosorbent Techniques ; Molecular Sequence Data ; Phosphorylation ; Protein Kinases/chemistry/*genetics/metabolism ; RNA Polymerase II/metabolism ; Saccharomyces cerevisiae/*enzymology/genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Homology, Nucleic Acid ; Transcription Factors/chemistry/*genetics ; *Transcription Factors, General ; *Transcription Factors, TFII ; *Transcriptional Elongation Factors
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  • 67
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-08-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, I S -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):860.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1489402" target="_blank"〉PubMed〈/a〉
    Keywords: Antineoplastic Agents/*isolation & purification/therapeutic use ; Developing Countries ; *Drug Industry ; Humans ; Madagascar ; Neoplasms/drug therapy ; *Plants, Medicinal ; United States ; Vinblastine/isolation & purification/therapeutic use ; Vincristine/isolation & purification/therapeutic use
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  • 68
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-04-24
    Description: A cleavage reagent directed to the active site of the Tetrahymena catalytic RNA was synthesized by derivatization of the guanosine substrate with a metal chelator. When complexed with iron(II), this reagent cleaved the RNA in five regions. Cleavage at adenosine 207, which is far from the guanosine-binding site in the primary and secondary structure, provides a constraint for the higher order folding of the RNA. This cleavage site constitutes physical evidence for a key feature of the Michel-Westhof model. Targeting a reactive entity to a specific site should be generally useful for determining proximity within folded RNA molecules or ribonucleoprotein complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, J F -- Cech, T R -- New York, N.Y. -- Science. 1992 Apr 24;256(5056):526-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1315076" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Edetic Acid/metabolism ; Free Radicals ; Guanosine/*metabolism ; Guanosine Monophosphate/metabolism ; Iron/metabolism ; Iron Chelating Agents/metabolism ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Nucleic Acid Conformation ; Pentetic Acid/metabolism ; RNA, Catalytic/*chemistry/metabolism ; Tetrahymena/*chemistry
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  • 69
    Publication Date: 1992-01-10
    Description: Matrix attachment regions (MARs) are thought to separate chromatin into topologically constrained loop domains. A MAR located 5' of the human beta-interferon gene becomes stably base-unpaired under superhelical strain, as do the MARs flanking the immunoglobulin heavy chain gene enhancer; in both cases a nucleation site exists for DNA unwinding. Concatemerized oligonucleotides containing the unwinding nucleation site exhibited a strong affinity for the nuclear scaffold and augmented SV40 promoter activity in stable transformants. Mutated concatemerized oligonucleotides resisted unwinding, showed weak affinity for the nuclear scaffold, and did not enhance promoter activity. These results suggest that the DNA feature capable of relieving superhelical strain is important for MAR functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bode, J -- Kohwi, Y -- Dickinson, L -- Joh, T -- Klehr, D -- Mielke, C -- Kohwi-Shigematsu, T -- R0I CA39681/CA/NCI NIH HHS/ -- R0I CA51377/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 10;255(5041):195-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gesellschaft fur Biotechnologische Forschung, mbH, Genetik von Eukaryoten, Mascheroder Weg 1, Braunschweig-Stockheim, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553545" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/drug effects/*genetics/isolation & purification ; Electrophoresis, Polyacrylamide Gel ; *Enhancer Elements, Genetic ; Humans ; Hydrazines/pharmacology ; Immunoglobulin Heavy Chains/*genetics ; Interferon-beta/*genetics ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Nuclear Matrix/physiology ; Oligodeoxyribonucleotides ; Plasmids ; Restriction Mapping ; Sulfuric Acid Esters ; Transcription, Genetic
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  • 70
    Publication Date: 1992-11-20
    Description: The amount of the heterotrimeric G protein subunit G alpha i2 decreases after the induction of F9 teratocarcinoma cells to become primitive endoderm in the presence of retinoic acid (RA). The reduction of the G alpha i2 protein in F9 cells by antisense RNA expression was associated with (i) loss of receptor-mediated inhibition of adenylyl cyclase; (ii) decreased cell doubling time; (iii) induction of a primitive, endoderm-like phenotype in the absence of RA; and (iv) production of the differentiation marker tissue-type plasminogen activator. Expression of a constitutively active, mutant G alpha i2 blocked RA-induced differentiation. These data suggest the involvement of G alpha i2 in the control of stem cell differentiation and provide insight into the involvement of G proteins in growth regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watkins, D C -- Johnson, G L -- Malbon, C C -- New York, N.Y. -- Science. 1992 Nov 20;258(5086):1373-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Diabetes and Metabolic Diseases Research Program, State University of New York, Stony Brook 11794.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1455234" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Animals ; Base Sequence ; *Cell Differentiation/drug effects ; GTP-Binding Proteins/genetics/*physiology ; Gene Expression ; Mice ; Molecular Sequence Data ; RNA, Antisense ; Teratoma/*pathology ; Thrombin/pharmacology ; Tretinoin/pharmacology ; Tumor Cells, Cultured
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  • 71
    Publication Date: 1992-12-21
    Description: Interferon-gamma (IFN-gamma) induces the transcription of the gene encoding a guanylate binding protein by activating a latent cytoplasmic factor, GAF (gamma-activated factor). GAF is translocated to the nucleus and binds a DNA element, the gamma-activated site. Through cross-linking and the use of specific antibodies GAF was found to be a 91-kilodalton DNA binding protein that was previously identified as one of four proteins in interferon-stimulated gene factor-3 (ISGF-3), a transcription complex activated by IFN-alpha. The IFN-gamma-dependent activation of the 91-kilodalton DNA binding protein required cytoplasmic phosphorylation of the protein on tyrosine. The 113-kilodalton ISGF-3 protein that is phosphorylated in response to IFN-alpha was not phosphorylated nor translocated to the nucleus in response to IFN-gamma. Thus the two different ligands result in tyrosine phosphorylation of different combinations of latent cytoplasmic transcription factors that then act at different DNA binding sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shuai, K -- Schindler, C -- Prezioso, V R -- Darnell, J E Jr -- New York, N.Y. -- Science. 1992 Dec 11;258(5089):1808-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1281555" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cell Line ; Cell Nucleus/metabolism ; DNA-Binding Proteins/isolation & purification/*metabolism ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; GTP-Binding Proteins/*genetics ; Gene Expression Regulation/drug effects ; Interferon-alpha/pharmacology ; Interferon-gamma/*pharmacology ; Models, Biological ; Molecular Sequence Data ; Molecular Weight ; Oligodeoxyribonucleotides ; Phosphorylation ; Phosphotyrosine ; Promoter Regions, Genetic ; STAT1 Transcription Factor ; Signal Transduction/drug effects ; *Trans-Activators ; *Transcription, Genetic/drug effects ; Tyrosine/analogs & derivatives/analysis
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  • 72
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-12-18
    Description: The sunY ribozyme is derived from a self-splicing RNA group I intron. This ribozyme was chosen as a starting point for the design of a self-replicating RNA because of its small size. As a means of facilitating the self-replication process, the size of this ribozyme was decreased by the deletion of nonconserved structural domains; however, when such deletions were made, there were severe losses of enzymatic activity. In vitro genetic selection was used to identify mutations that reactivate a virtually inactive sunY deletion mutant. A selected mutant with five substitution mutations scattered throughout the primary sequence showed greater catalytic activity than the original ribozyme under the selection conditions. The sunY ribozyme and its small selected variant can both catalyze template-directed oligonucleotide assembly. The small size and reduced secondary structure of the selected variant results in an enhancement, relative to that of the original ribozyme, of its rate of self-copying. This engineered ribozyme is able to function effectively both as a catalyst and as a template in self-copying reactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Green, R -- Szostak, J W -- New York, N.Y. -- Science. 1992 Dec 18;258(5090):1910-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1470913" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage T4/*genetics ; Base Sequence ; Escherichia coli/*genetics ; Exons ; Introns ; Models, Structural ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Oligodeoxyribonucleotides ; Oligoribonucleotides ; Polymerase Chain Reaction ; RNA, Catalytic/*biosynthesis/chemistry/genetics ; Sequence Deletion ; Templates, Genetic
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  • 73
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-07-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1992 Jul 17;257(5068):323.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1631550" target="_blank"〉PubMed〈/a〉
    Keywords: History, 20th Century ; National Institutes of Health (U.S.) ; Scientific Misconduct/*legislation & jurisprudence ; United States
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  • 74
    Publication Date: 1992-02-28
    Description: The primary defect arising from Zellweger syndrome appears to be linked to impaired assembly of peroxisomes. A human complementary DNA has been cloned that complements the disease's symptoms (including defective peroxisome assembly) in fibroblasts from a patient with Zellweger syndrome. The cause of the syndrome in this patient was a point mutation that resulted in the premature termination of peroxisome assembly factor-1. The homozygous patient apparently inherited the mutation from her parents, each of whom was heterozygous for that mutation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shimozawa, N -- Tsukamoto, T -- Suzuki, Y -- Orii, T -- Shirayoshi, Y -- Mori, T -- Fujiki, Y -- New York, N.Y. -- Science. 1992 Feb 28;255(5048):1132-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Gifu University School of Medicine, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546315" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cricetinae ; DNA Mutational Analysis ; Genes ; Genetic Complementation Test ; Humans ; Membrane Proteins/*genetics ; Microbodies/*ultrastructure ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry ; Pedigree ; Polymerase Chain Reaction ; Transfection ; Zellweger Syndrome/*genetics
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  • 75
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-10-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1992 Oct 30;258(5083):732, 734.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439774" target="_blank"〉PubMed〈/a〉
    Keywords: *Biomedical Research ; *Breast Neoplasms ; *Federal Government ; Female ; Financing, Government/*economics ; Humans ; Lobbying ; National Institutes of Health (U.S.) ; Research Support as Topic/*economics ; Resource Allocation ; United States
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  • 76
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-02-14
    Description: The opening of duplex DNA in the elongation phase of transcription by Escherichia coli RNA polymerase in vivo was detected at a regulatory site where a prolonged pause in transcription occurs. Single-stranded DNA in the transcription bubble was identified by its reactivity with potassium permanganate (KMnO4). The elongation structure in vivo was similar to that of transcription complexes made in vitro with some differences. The observed reactivity to KMnO4 of the DNA template strand was consistent with the existence of an RNA-DNA hybrid of about 12 nucleotides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kainz, M -- Roberts, J -- GM 21941/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Feb 14;255(5046):838-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Biochemistry, Molecular, and Cell Biology, Cornell University, Ithaca, NY 14853.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1536008" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA-Directed RNA Polymerases/physiology ; Escherichia coli/*genetics ; Molecular Sequence Data ; Peptide Chain Elongation, Translational ; Plasmids ; Potassium Permanganate ; Promoter Regions, Genetic/genetics ; Templates, Genetic ; Transcription, Genetic/*physiology
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  • 77
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-04-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1992 Apr 10;256(5054):172-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1566065" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*transmission ; Female ; *Fetal Tissue Transplantation ; Government Agencies ; Humans ; Male ; National Institutes of Health (U.S.) ; Research Support as Topic/*legislation & jurisprudence ; Sexual Behavior ; United States
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  • 78
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-12-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bereano, P L -- Wilker, N L -- New York, N.Y. -- Science. 1992 Dec 4;258(5088):1561-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1455238" target="_blank"〉PubMed〈/a〉
    Keywords: *Food ; Genetic Engineering/*legislation & jurisprudence ; United States ; *United States Food and Drug Administration
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  • 79
    Publication Date: 1992-08-21
    Description: Cells with distinct developmental histories can respond differentially to identical signals, suggesting that signals are interpreted in a fashion that reflects a cell's identity. How this might occur is suggested by the observation that proteins of the homeodomain family, including a newly identified human protein, enhance the DNA-binding activity of serum response factor, a protein required for the induction of genes by growth and differentiation factors. Interaction with proteins of the serum response factor family may allow homeodomain proteins to specify the transcriptional response to inductive signals. Moreover, because the ability to enhance the binding of serum response factor to DNA residues within the homeodomain but is independent of homeodomain DNA-binding activity, this additional activity of the homeodomain may account for some of specificity of action of homeodomain proteins in development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grueneberg, D A -- Natesan, S -- Alexandre, C -- Gilman, M Z -- CA08968/CA/NCI NIH HHS/ -- CA45642/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 21;257(5073):1089-95.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1509260" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; DNA/genetics/*metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism/*pharmacology ; Drosophila/genetics ; *Drosophila Proteins ; Fungal Proteins/chemistry/pharmacology ; *Homeodomain Proteins ; Humans ; Minichromosome Maintenance 1 Protein ; Molecular Sequence Data ; Nuclear Proteins/*metabolism ; Saccharomyces cerevisiae/genetics ; Serum Response Factor ; Transcription Factors/chemistry/*metabolism/pharmacology ; Transfection
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  • 80
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-06-05
    Description: Regulation of interleukin-2 (IL-2) gene expression by the p50 and p65 subunits of the DNA binding protein NF-kappa B was studied in nontransformed CD4+ T lymphocyte clones. A homodimeric complex of the NF-kappa B p50 subunit was found in resting T cells. The amount of p50-p50 complex decreased after full antigenic stimulation, whereas the amount of the NF-kappa B p50-p65 heterodimer was increased. Increased expression of the IL-2 gene and activity of the IL-2 kappa B DNA binding site correlated with a decrease in the p50-p50 complex. Overexpression of p50 repressed IL-2 promoter expression. The switch from p50-p50 to p50-p65 complexes depended on a protein that caused sequestration of the p50-p50 complex in the nucleus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kang, S M -- Tran, A C -- Grilli, M -- Lenardo, M J -- New York, N.Y. -- Science. 1992 Jun 5;256(5062):1452-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunology, National Institute for Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1604322" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/*immunology ; Base Sequence ; Binding Sites ; Cell Line ; Cell Nucleus/physiology ; Chloramphenicol O-Acetyltransferase/genetics/metabolism ; Clone Cells ; Columbidae ; DNA/genetics ; *Gene Expression Regulation ; Interleukin-2/*genetics ; Macromolecular Substances ; Mice ; Molecular Sequence Data ; NF-kappa B/*metabolism ; Oligonucleotide Probes ; Promoter Regions, Genetic ; RNA, Messenger/metabolism ; Recombinant Fusion Proteins/metabolism ; T-Lymphocyte Subsets/*immunology ; Transfection ; Tumor Necrosis Factor-alpha/pharmacology
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  • 81
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-04-03
    Description: Population genetic analyses that depend on the assumption of neutrality for allozyme markers are used widely. Restriction fragment length polymorphisms in nuclear DNA of the American oyster evidence a pronounced population subdivision concordant with mitochondrial DNA. This finding contrasts with a geographic uniformity in allozyme frequencies previously thought to reflect high gene flow mediated by the pelagic gametes and larvae. The discordance likely is due to selection on protein electrophoretic characters that balances allozyme frequencies in the face of severe constraints to gene flow. These results raise a cautionary note for studies that rely on assumptions of neutrality for allozyme markers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karl, S A -- Avise, J C -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):100-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1348870" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Base Sequence ; Cell Nucleus/*physiology ; DNA/genetics ; Gene Frequency ; Geography ; Isoenzymes/*genetics ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Ostreidae/enzymology/*genetics ; *Polymorphism, Restriction Fragment Length ; United States
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  • 82
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-10-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, D D -- New York, N.Y. -- Science. 1992 Oct 23;258(5082):529.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411549" target="_blank"〉PubMed〈/a〉
    Keywords: Financing, Government/*methods ; National Institutes of Health (U.S.)/*economics ; Research Design ; *Research Support as Topic ; United States
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  • 83
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-10-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, K J -- New York, N.Y. -- Science. 1992 Oct 23;258(5082):532.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411562" target="_blank"〉PubMed〈/a〉
    Keywords: Financing, Government/*methods ; National Institutes of Health (U.S.)/*economics ; *Research Support as Topic/*economics ; United States
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  • 84
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-04-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1992 Apr 24;256(5056):439.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1570505" target="_blank"〉PubMed〈/a〉
    Keywords: Budgets/*legislation & jurisprudence ; *Research Support as Topic ; United States
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  • 85
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-02-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Elkan, C -- New York, N.Y. -- Science. 1992 Feb 7;255(5045):663.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1590848" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Databases, Factual ; *Genome, Human ; Humans ; *Information Storage and Retrieval
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  • 86
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-09-04
    Description: A histone, macroH2A, nearly three times the size of conventional H2A histone, was found in rat liver nucleosomes. Its N-terminal third is 64 percent identical to a full-length mouse H2A. However, it also contains a large nonhistone region. This region has a segment that resembles a leucine zipper, a structure known to be involved in dimerization of some transcription factors. Nucleosomes containing macroH2A may have novel functions, possibly involving interactions with other nuclear proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pehrson, J R -- Fried, V A -- CA 06927/CA/NCI NIH HHS/ -- GM 24019/GM/NIGMS NIH HHS/ -- RR 05539/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1992 Sep 4;257(5075):1398-400.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fox Chase Cancer Center, Institute for Cancer Research, Philadelphia, PA 19111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1529340" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA/chemistry ; Histones/*chemistry/genetics ; Leucine Zippers ; Liver/*ultrastructure ; Macromolecular Substances ; Mice ; Molecular Sequence Data ; Nucleosomes/*chemistry ; Polymerase Chain Reaction ; Rats ; Sequence Homology, Nucleic Acid
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  • 87
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-02-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1992 Feb 14;255(5046):788, 790-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1536002" target="_blank"〉PubMed〈/a〉
    Keywords: Foundations/*organization & administration ; *Government ; United States
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  • 88
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-08-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Emiliani, C -- New York, N.Y. -- Science. 1992 Aug 28;257(5074):1188-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1519049" target="_blank"〉PubMed〈/a〉
    Keywords: Humans ; *National Academy of Sciences (U.S.) ; United States
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  • 89
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-10-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pelli, D -- New York, N.Y. -- Science. 1992 Oct 23;258(5082):531.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411558" target="_blank"〉PubMed〈/a〉
    Keywords: *National Institutes of Health (U.S.) ; Peer Review/*methods ; *Research ; United States
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  • 90
    Publication Date: 1992-05-08
    Description: Mutant forms of the gene encoding the tumor suppressor p53 are found in numerous human malignancies, but the physiologic function of p53 and the effects of mutations on this function are unknown. The p53 protein binds DNA in a sequence-specific manner and thus may regulate gene transcription. Cotransfection experiments showed that wild-type p53 activated the expression of genes adjacent to a p53 DNA binding site. The level of activation correlated with DNA binding in vitro. Oncogenic forms of p53 lost this activity. Moreover, all mutants inhibited the activity of coexpressed wild-type p53, providing a basis for the selection of such mutants during tumorigenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kern, S E -- Pietenpol, J A -- Thiagalingam, S -- Seymour, A -- Kinzler, K W -- Vogelstein, B -- CA06973/CA/NCI NIH HHS/ -- CA09243/CA/NCI NIH HHS/ -- CA35494/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 May 8;256(5058):827-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21231.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1589764" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Line ; Chloramphenicol O-Acetyltransferase/genetics/metabolism ; DNA-Binding Proteins/*genetics/*metabolism ; Exons ; *Gene Expression Regulation, Neoplastic ; *Genes, p53 ; Genetic Vectors ; Humans ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction/methods ; Recombinant Fusion Proteins/metabolism ; Repetitive Sequences, Nucleic Acid ; Saccharomyces cerevisiae/genetics/growth & development ; *Transcription, Genetic ; Transfection ; Tumor Suppressor Protein p53/*genetics/*metabolism ; beta-Galactosidase/genetics/metabolism
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  • 91
    Publication Date: 1992-07-31
    Description: Calcium-dependent glutamate secretion was reconstituted in Xenopus oocytes by injecting the oocyte with total rat cerebellar messenger RNA (mRNA). Co-injection of total mRNA with antisense oligonucleotides to synaptophysin message decreased the expression of synaptophysin in the oocyte and reduced the calcium-dependent secretion. A similar effect on secretion was observed for oocytes injected with total mRNA together with an antibody to rat synaptophysin. These results indicate that synaptophysin is necessary for transmitter secretion and that the oocyte expression system may be useful for dissecting the molecular events associated with the secretory process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alder, J -- Lu, B -- Valtorta, F -- Greengard, P -- Poo, M M -- MH 39327/MH/NIMH NIH HHS/ -- NS 22764/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 31;257(5070):657-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Columbia University, New York, NY 10027.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1353905" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blotting, Western ; Calcimycin/pharmacology ; Calcium/*pharmacology ; Cerebellum/chemistry ; Fluorescent Antibody Technique ; Gene Expression ; Glutamates/*secretion ; Glutamic Acid ; Kinetics ; Liver/chemistry ; Microscopy, Immunoelectron ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacology ; Oocytes/*physiology ; RNA, Messenger/genetics ; Rats ; Synaptophysin/genetics/*physiology ; Transfection ; Xenopus
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  • 92
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aldhous, P -- New York, N.Y. -- Science. 1992 Dec 18;258(5090):1876-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1470909" target="_blank"〉PubMed〈/a〉
    Keywords: *Biology ; Government Agencies ; Molecular Biology ; *Research Support as Topic ; Spain ; United States
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  • 93
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-09-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamilton, D P -- New York, N.Y. -- Science. 1992 Sep 4;257(5075):1341.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1529331" target="_blank"〉PubMed〈/a〉
    Keywords: Confidentiality/*legislation & jurisprudence ; *Scientific Misconduct ; United States ; United States Public Health Service
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  • 94
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-10-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, G E Jr -- New York, N.Y. -- Science. 1992 Oct 9;258(5080):200-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411514" target="_blank"〉PubMed〈/a〉
    Keywords: *Financing, Government ; Policy Making ; *Research Support as Topic/trends ; United States
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 95
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-04-17
    Description: The Escherichia coli Rep helicase unwinds duplex DNA during replication. The functional helicase appears to be a dimer that forms only on binding DNA. Both protomers of the dimer can bind either single-stranded or duplex DNA. Because binding and hydrolysis of adenosine triphosphate (ATP) are essential for helicase function, the energetics of DNA binding and DNA-induced Rep dimerization were studied quantitatively in the presence of the nucleotide cofactors adenosine diphosphate (ADP) and the nonhydrolyzable ATP analog AMPP(NH)P. Large allosteric effects of nucleotide cofactors on DNA binding to Rep were observed. Binding of ADP favored Rep dimers in which both protomers bound single-stranded DNA, whereas binding of AMPP(NH)P favored simultaneous binding of both single-stranded and duplex DNA to the Rep dimer. A rolling model for the active unwinding of duplex DNA by the dimeric Rep helicase is proposed that explains vectorial unwinding and predicts that helicase translocation along DNA is coupled to ATP binding, whereas ATP hydrolysis drives unwinding of multiple DNA base pairs for each catalytic event.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wong, I -- Lohman, T M -- GM30498/GM/NIGMS NIH HHS/ -- GM45948/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 17;256(5055):350-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1533057" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine Nucleotides/*pharmacology ; Adenosine Diphosphate/metabolism/pharmacology ; Adenosine Triphosphatases/*metabolism ; Adenosine Triphosphate/metabolism ; Adenylyl Imidodiphosphate/pharmacology ; Base Sequence ; Binding Sites ; Binding, Competitive ; DNA/chemistry/*metabolism ; *DNA Helicases ; DNA, Single-Stranded/metabolism ; DNA, Viral/metabolism ; Escherichia coli/*enzymology ; Escherichia coli Proteins ; Macromolecular Substances ; Magnesium/pharmacology ; Molecular Sequence Data ; Nucleic Acid Conformation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 96
    Publication Date: 1992-12-11
    Description: In order to function, transcription factors must compete for DNA binding with structural components of chromatin, including nucleosomes. Mechanisms that could be used in this competition have been characterized with the use of the DNA binding domain of the yeast GAL4 protein. The binding of GAL4 to a nucleosome core resulted in a ternary complex containing GAL4, the core histone proteins, and DNA. This ternary complex was unstable; upon the addition of nonspecific competitor DNA, it dissociated into either the original nucleosome core particle or GAL4 bound to naked DNA. Nucleosome core destabilization by GAL4 did not require a transcriptional activation domain. These data demonstrate the displacement of nucleosome cores as a direct result of binding by a regulatory factor. Similar mechanisms might affect the establishment of factor occupancy of promoters and enhancers in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Workman, J L -- Kingston, R E -- New York, N.Y. -- Science. 1992 Dec 11;258(5089):1780-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1465613" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/genetics/isolation & purification/metabolism ; DNA-Binding Proteins ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; Fungal Proteins/isolation & purification/*metabolism ; HeLa Cells ; Histones/isolation & purification/metabolism ; Humans ; Molecular Sequence Data ; Nucleosomes/*metabolism ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction/methods ; Protein Binding ; Saccharomyces cerevisiae/genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/isolation & purification/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 97
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-08-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamilton, D P -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):737.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1496387" target="_blank"〉PubMed〈/a〉
    Keywords: *Government Agencies ; Physical Phenomena ; Physics ; Politics ; *Research Support as Topic ; United States
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-05-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1992 May 29;256(5061):1277.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1598569" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome ; Dietary Fats ; Hazardous Substances ; Humans ; Periodicals as Topic/*standards ; *Science ; Television ; Tobacco Smoke Pollution/adverse effects ; United States ; *Writing
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-07-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1992 Jul 3;257(5066):22-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1621088" target="_blank"〉PubMed〈/a〉
    Keywords: Amitriptyline/*toxicity ; Animals ; Breast Neoplasms/drug therapy/prevention & control ; Carcinogens/*toxicity ; Female ; Fluoxetine/*toxicity ; Humans ; Mice ; Neoplasms, Experimental/chemically induced ; Rats ; Tamoxifen/therapeutic use ; United States ; United States Food and Drug Administration
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
    Publication Date: 1992-04-03
    Description: Steroid-thyroid hormone receptors typically bind as dimers to DNA sequences that contain repeated elements termed half-sites. NGFI-B, an early response protein and orphan member of this receptor superfamily, binds to a DNA sequence that contains only one half-site (5'-AAAGGTCA-3'). A domain separate from the NGFI-B zinc fingers, termed the A box, was identified and is required for recognition of the two adenine-thymidine (A-T) base pairs at the 5' end of the NGFI-B DNA binding element. In addition, a domain downstream of the zinc fingers of the orphan receptor H-2 region II binding protein, termed the T box, determined binding to tandem repeats of the estrogen receptor half-site (5'-AGGTCA-3').〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, T E -- Paulsen, R E -- Padgett, K A -- Milbrandt, J -- NS01018/NS/NINDS NIH HHS/ -- P01 CA49712/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):107-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1314418" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; CHO Cells ; Cell Nucleus/*physiology ; Cricetinae ; DNA/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Kinetics ; Mice ; Molecular Sequence Data ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Oligodeoxyribonucleotides/metabolism ; Polymerase Chain Reaction ; Receptors, Cell Surface/*metabolism ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Nucleic Acid ; Substrate Specificity ; Transcription Factors/genetics/*metabolism ; Transfection ; Zinc Fingers/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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