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  • Articles  (41,733)
  • 1990-1994  (32,002)
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1994 Dec 23;266(5193):1923.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17836504" target="_blank"〉PubMed〈/a〉
    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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  • 12
    Publication Date: 1994-12-23
    Description: Initiation of ribosomal RNA synthesis by RNA polymerase I requires the promoter selectivity factor SL1, which consists of the TATA-binding protein, TBP, and three associated factors, TAFIS 110, 63, and 48. Here the in vivo and in vitro assembly of functional SL1 complexes from recombinant TAFIS and TBP are reported. Complexes containing TBP and all three TAFIS were as active in supporting transcription from the human ribosomal RNA gene promoter as endogenous SL1, whereas partial complexes without TBP did not efficiently direct transcription in vitro. These results suggest that TAFIS 110, 63, and 48, together with TBP, are necessary and sufficient to reconstitute a transcriptionally active SL1 complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zomerdijk, J C -- Beckmann, H -- Comai, L -- Tjian, R -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):2015-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California, Berkeley 94720-3204.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7801130" target="_blank"〉PubMed〈/a〉
    Keywords: DNA-Binding Proteins/chemistry/*metabolism ; HeLa Cells ; Humans ; *Pol1 Transcription Initiation Complex Proteins ; Promoter Regions, Genetic ; RNA, Ribosomal/*genetics ; Recombinant Fusion Proteins/metabolism ; TATA Box ; *TATA-Binding Protein Associated Factors ; TATA-Box Binding Protein ; *Transcription Factor TFIID ; Transcription Factors/chemistry/*metabolism ; *Transcription, Genetic
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Culotta, E -- Koshland, D E Jr -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):1926-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7801115" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; DNA Damage ; DNA Ligases/*metabolism ; DNA Polymerase I/metabolism ; *DNA Repair ; DNA Replication ; Humans ; Neoplasms/genetics ; Science ; Transcription, Genetic
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sancar, A -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):1954-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7801120" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Antineoplastic Agents/therapeutic use ; Cell Division ; DNA/metabolism ; DNA Adducts/metabolism ; DNA Damage ; *DNA Repair ; DNA Replication ; Endodeoxyribonucleases/metabolism ; Escherichia coli/metabolism ; *Escherichia coli Proteins ; Humans ; Models, Biological ; Neoplasms/drug therapy
    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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  • 15
    Publication Date: 1994-12-23
    Description: The reduction in vigor of aneuploids was classically thought to be due to the imbalance of gene products expressed from the varied chromosome relative to those from the remainder of the genome. In this study, the dosage of chromosomal segments was varied, but the transcript level of most genes encoded therein showed compensation for the number of copies of the gene. Genes whose dosage was not altered were affected by aneuploidy of unlinked chromosomal segments. The phenotypic effects of aneuploidy and of a substantial fraction of quantitative variation are hypothesized to be the consequence of an altered dosage-sensitive regulatory system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guo, M -- Birchler, J A -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):1999-2002.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17836517" target="_blank"〉PubMed〈/a〉
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 16
    Publication Date: 1994-12-23
    Description: HIV integrase is the enzyme responsible for inserting the viral DNA into the host chromosome; it is essential for HIV replication. The crystal structure of the catalytically active core domain (residues 50 to 212) of HIV-1 integrase was determined at 2.5 A resolution. The central feature of the structure is a five-stranded beta sheet flanked by helical regions. The overall topology reveals that this domain of integrase belongs to a superfamily of polynucleotidyl transferases that includes ribonuclease H and the Holliday junction resolvase RuvC. The active site region is identified by the position of two of the conserved carboxylate residues essential for catalysis, which are located at similar positions in ribonuclease H. In the crystal, two molecules form a dimer with a extensive solvent-inaccessible interface of 1300 A2 per monomer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dyda, F -- Hickman, A B -- Jenkins, T M -- Engelman, A -- Craigie, R -- Davies, D R -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):1981-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892-0560.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7801124" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA Nucleotidyltransferases/*chemistry ; HIV-1/*enzymology ; Hydrogen Bonding ; Integrases ; Models, Molecular ; Molecular Sequence Data ; Protein Folding ; Protein Structure, Secondary ; Ribonuclease H/chemistry ; Solubility ; Virus Integration
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Travis, J -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):1947-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17836513" target="_blank"〉PubMed〈/a〉
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krige, J -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):2028-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17836520" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 19
    Publication Date: 1994-12-23
    Description: Hemolysin of Escherichia coli is activated by fatty acylation of the protoxin, directed by the putative acyl transferase HlyC and by acyl carrier protein (ACP). Mass spectrometry and Edman degradation of proteolytic products from mature toxin activated in vitro with tritium-labeled acylACP revealed two fatty-acylated internal lysine residues, lysine 564 and lysine 690. Resistance of the acylation to chemical treatments suggested that fatty acid was amide linked. Substitution of the two lysines confirmed that they were the only sites of acylation and showed that although each was acylated in the absence of the other, both sites were required for in vivo toxin activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stanley, P -- Packman, L C -- Koronakis, V -- Hughes, C -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):1992-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Cambridge University, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7801126" target="_blank"〉PubMed〈/a〉
    Keywords: Acyl Carrier Protein/metabolism ; Acylation ; Acyltransferases/metabolism ; Amino Acid Sequence ; Animals ; Bacterial Proteins/chemistry/metabolism/*toxicity ; Bacterial Toxins/chemistry/metabolism/*toxicity ; *Escherichia coli ; *Escherichia coli Proteins ; Hemolysin Proteins/chemistry/metabolism/*toxicity ; Hemolysis ; Horses ; Lysine/metabolism ; Mass Spectrometry ; Molecular Sequence Data ; Protein Precursors/metabolism ; Sequence Alignment
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Modrich, P -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):1959-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7801122" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Colorectal Neoplasms, Hereditary Nonpolyposis/*genetics ; DNA Damage ; *DNA Repair ; DNA Replication ; Escherichia coli/genetics ; Genome, Bacterial ; Humans ; Mutation ; Neoplasms/*genetics ; Recombination, Genetic
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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