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  • Male  (1,030)
  • Base Sequence  (883)
  • Cells, Cultured  (380)
  • American Association for the Advancement of Science (AAAS)  (2,156)
  • Annual Reviews
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  • American Association for the Advancement of Science (AAAS)  (2,156)
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  • 1
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    A plant leucine zipper protein that recognizes an abscisic acid response element (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-10-12
    Description: The mechanism by which phytohormones, like abscisic acid (ABA), regulate gene expression is unknown. An activity in nuclear extracts that interacts with the ABA response element (ABRE) from the 5' regulatory region of the wheat Em gene was identified. A complementary DNA clone was isolated whose product is a DNA binding protein (EmBP-1) that interacts specifically with an 8-base pair (bp) sequence (CACGTGGC) in the ABRE. A 2-bp mutation in this sequence prevented binding of EmBP-1. The same mutation reduced the ability of the ABRE to confer ABA responsiveness on a viral promoter in a transient assay. The 8-bp EmBP-1 target sequence was found to be conserved in several other ABA-responsive promoters and in promoters from plants that respond to signals other than ABA. Similar sequences are found in promoters from mammals, yeast, and in the major late promoter of adenovirus. The deduced amino acid sequence of EmBP-1 contains conserved basic and leucine zipper domains found in transcription factors in plants, yeast, and mammals. EmBP-1 may be a member of a highly conserved family of proteins that recognize a core sequence found in the regulatory regions of various genes that are integrated into a number of different response pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guiltinan, M J -- Marcotte, W R Jr -- Quatrano, R S -- New York, N.Y. -- Science. 1990 Oct 12;250(4978):267-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of North Carolina, Chapel Hill 27599-3280.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2145628" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid/*metabolism ; Amino Acid Sequence ; Base Sequence ; Cell Nucleus/metabolism ; DNA/*genetics ; DNA-Binding Proteins/genetics/metabolism ; *Gene Expression Regulation ; *Leucine Zippers/genetics ; Molecular Sequence Data ; Oligonucleotide Probes ; Plants/*genetics ; Sequence Homology, Nucleic Acid ; Triticum/*genetics/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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  • 2
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    Functional evidence for an RNA template in telomerase (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-02-02
    Description: The RNA moiety of the ribonucleoprotein enzyme telomerase from the ciliate Euplotes crassus was identified and its gene was sequenced. Functional analysis, in which oligonucleotides complementary to portions of the telomerase RNA were tested for their ability to prime telomerase in vitro, showed that the sequence 5' CAAAACCCCAAA 3' in this RNA is the template for synthesis of telomeric TTTTGGGG repeats by the Euplotes telomerase. The data provide a direct demonstration of a template function for a telomerase RNA and demarcate the outer boundaries of the telomeric template. Telomerase can now be defined as a specialized reverse transcriptase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shippen-Lentz, D -- Blackburn, E H -- New York, N.Y. -- Science. 1990 Feb 2;247(4942):546-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1689074" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Ciliophora/enzymology/*genetics ; DNA Nucleotidylexotransferase/*genetics ; Genes ; Molecular Sequence Data ; Oligonucleotide Probes ; RNA/*genetics ; Sequence Homology, Nucleic Acid ; *Templates, Genetic
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  • 3
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    Site-specific cleavage of a yeast chromosome by oligonucleotide-directed triple-helix formation (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-07-06
    Description: Oligonucleotides equipped with EDTA-Fe can bind specifically to duplex DNA by triple-helix formation and produce double-strand cleavage at binding sites greater than 12 base pairs in size. To demonstrate that oligonucleotide-directed triple-helix formation is a viable chemical approach for the site-specific cleavage of large genomic DNA, an oligonucleotide with EDTA-Fe at the 5' and 3' ends was targeted to a 20-base pair sequence in the 340-kilobase pair chromosome III of Saccharomyces cerevisiae. Double-strand cleavage products of the correct size and location were observed, indicating that the oligonucleotide bound and cleaved the target site among almost 14 megabase pairs of DNA. Because oligonucleotide-directed triple-helix formation has the potential to be a general solution for DNA recognition, this result has implications for physical mapping of chromosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strobel, S A -- Dervan, P B -- GM 42966/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jul 6;249(4964):73-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Arnold and Mabel Beckman Laboratories of Chemical Synthesis, Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2195655" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Chromosomes, Fungal/*metabolism ; DNA, Fungal/*genetics/metabolism ; Densitometry ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleic Acid Hybridization ; Oligonucleotides/*genetics/metabolism ; Saccharomyces cerevisiae/*genetics
    Print ISSN: 0036-8075
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  • 4
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    Female primatologists confer--without men (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dusheck, J -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1494-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218487" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Congresses as Topic ; Female ; Humans ; Male ; Men ; United States ; *Women
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  • 5
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    Contributions of two types of calcium channels to synaptic transmission and plasticity (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-23
    Description: In Aplysia sensory and motor neurons in culture, the contributions of the major classes of calcium current can be selectively examined while transmitter release and its modulation are examined. A slowly inactivating, dihydropyridine-sensitive calcium current does not contribute either to normal synaptic transmission or to any of three different forms of plasticity: presynaptic inhibition, homosynaptic depression, and presynaptic facilitation. This current does contribute, however, to a fourth form of plasticity--modulation of transmitter release by tonic depolarization of the sensory neuron. By contrast, a second calcium current, which is rapidly inactivating and dihydropyridine-insensitive, contributes to release elicited by the transient depolarization of an action potential and to the other three forms of plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Edmonds, B -- Klein, M -- Dale, N -- Kandel, E R -- New York, N.Y. -- Science. 1990 Nov 23;250(4984):1142-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University College of London, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2174573" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Aplysia/*physiology ; Cadmium/pharmacology ; Calcium Channels/drug effects/*physiology ; Cells, Cultured ; Dihydropyridines/antagonists & inhibitors/pharmacology ; Electric Conductivity ; FMRFamide ; Motor Neurons/physiology ; Neuronal Plasticity/*physiology ; Neurons, Afferent/physiology ; Neuropeptides/pharmacology ; Nifedipine/pharmacology ; Serotonin/pharmacology ; Synapses/*physiology ; Synaptic Transmission/*physiology
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  • 6
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    Transcriptional activation by wild-type but not transforming mutants of the p53 anti-oncogene (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-31
    Description: The protein encoded by the wild-type p53 proto-oncogene has been shown to suppress transformation, whereas certain mutations that alter p53 become transformation competent. Fusion proteins between p53 and the GAL4 DNA binding domain were made to anchor p53 to a DNA target sequence and to allow measurement of transcriptional activation of a reporter plasmid. The wild-type p53 stimulated transcription in this assay, but two transforming mutations in p53 were unable to act as transcriptional activators. Therefore, p53 can activate transcription, and transformation-activating mutations result in a loss of function of the p53 protein. The inability of the p53 mutant proteins to activate transcription may enable them to be transformation competent.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2935288/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2935288/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raycroft, L -- Wu, H Y -- Lozano, G -- CA16672/CA/NCI NIH HHS/ -- CA47296/CA/NCI NIH HHS/ -- R01 CA047296/CA/NCI NIH HHS/ -- R01 CA047296-12/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 31;249(4972):1049-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Texas, M. D. Anderson Cancer Center, Department of Molecular Genetics, Houston 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2144364" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Cell Transformation, Neoplastic ; *Gene Expression Regulation ; HeLa Cells/metabolism ; Humans ; Molecular Sequence Data ; *Mutation ; Nuclear Proteins/genetics ; Oligonucleotide Probes ; Oncogene Proteins/*genetics ; Phosphoproteins/*genetics ; *Proto-Oncogenes ; RNA, Messenger/genetics ; Suppression, Genetic ; Transcription Factors/*genetics ; *Transcription, Genetic ; Tumor Suppressor Protein p53
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  • 7
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    The dominant W42 spotting phenotype results from a missense mutation in the c-kit receptor kinase (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-01-12
    Description: The murine white spotting locus (W) is allelic with the proto-oncogene c-kit, which encodes a transmembrane tyrosine protein kinase receptor for an unknown ligand. Mutations at the W locus affect various aspects of hematopoiesis and the proliferation and migration of primordial germ cells and melanoblasts during development to varying degrees of severity. The W42 mutation has a particularly severe effect in both the homozygous and the heterozygous states. The molecular basis of the W42 mutation was determined. The c-kit protein products in homozygous mutant mast cells were expressed normally but displayed a defective tyrosine kinase activity in vitro. Nucleotide sequence analysis of mutant complementary DNAs revealed a missense mutation that replaces aspartic acid with asparagine at position 790 in the c-kit protein product. Aspartic acid-790 is a conserved residue in all protein kinases. These results provide an explanation for the dominant nature of the W42 mutation and provide insight into the mechanism of c-kit-mediated signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tan, J C -- Nocka, K -- Ray, P -- Traktman, P -- Besmer, P -- P01-CA-16599/CA/NCI NIH HHS/ -- R01-CA-32926/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Jan 12;247(4939):209-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Program, Sloan Kettering Institute, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1688471" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cells, Cultured ; DNA/genetics ; Gene Expression ; Homozygote ; Liver/analysis/cytology/embryology ; Mast Cells/metabolism ; Mice ; Molecular Sequence Data ; *Mutation ; *Phenotype ; Polymerase Chain Reaction ; Protein-Tyrosine Kinases/*genetics ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins c-kit ; RNA/analysis ; Receptors, Cell Surface/genetics ; Signal Transduction
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  • 8
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    Acceleration of diabetes in young NOD mice with a CD4+ islet-specific T cell clone (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-21
    Description: Nonobese diabetic (NOD) mice develop an autoimmune form of diabetes, becoming hyperglycemic after 3 months of age. This process was accelerated by injecting young NOD mice with CD4+ islet-specific T cell clones derived from NOD mice. Overt diabetes developed in 10 of 19 experimental animals by 7 weeks of age, with the remaining mice showing marked signs of the disease in progress. Control mice did not become diabetic and had no significant pancreatic infiltration. This work demonstrates that a CD4 T cell clone is sufficient to initiate the disease process in the diabetes-prone NOD mouse.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haskins, K -- McDuffie, M -- P01 DK40144/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 21;249(4975):1433-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Barbara Davis Center for Childhood Diabetes, University of Colorado Health Sciences Center, Denver 80262.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2205920" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/analysis/*immunology ; Clone Cells ; Diabetes Mellitus, Experimental/*immunology/pathology ; Female ; Islets of Langerhans/*immunology/pathology ; Male ; Mice ; Mice, Inbred Strains ; Mice, Mutant Strains ; T-Lymphocytes/*immunology/transplantation
    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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  • 9
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    GT-1 binding site confers light responsive expression in transgenic tobacco (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-04-27
    Description: Light-dependent expression of rbcS, the gene encoding the small subunit of ribulose-1,5-bisphosphate carboxylase, which is the key enzyme involved in carbon fixation in higher plants, is regulated at the transcriptional level. Sequence analysis of the gene has uncovered a conserved GT motif in the -150 to -100 region of many rbcS promoters. This motif serves as the binding site of a nuclear factor, designated GT-1. Analysis of site-specific mutants of pea rbcS-3A promoter demonstrated that GT-1 binding in vitro is correlated with light-responsive expression of the rbcS promoter in transgenic plants. However, it is not known whether factors other than GT-1 might also be required for activation of transcription by light. A synthetic tetramer of box II (TGTGTGGTTAATATG), the GT-1 binding site located between -152 to -138 of the rbcS-3A promoter, inserted upstream of a truncated cauliflower mosaic virus 35S promoter is sufficient to confer expression in leaves of transgenic tobacco. This expression occurs principally in chloroplast-containing cells, is induced by light, and is correlated with the ability of box II to bind GT-1 in vitro. The data show that the binding site for GT-1 is likely to be a part of the molecular light switch for rbcS activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lam, E -- Chua, N H -- New York, N.Y. -- Science. 1990 Apr 27;248(4954):471-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Plant Molecular Biology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2330508" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Chloramphenicol O-Acetyltransferase/genetics ; Cloning, Molecular ; DNA-Binding Proteins/*metabolism ; Gene Expression Regulation/*physiology ; Genetic Vectors ; *Light ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/*metabolism ; Plant Proteins/*metabolism ; *Plants, Toxic ; Promoter Regions, Genetic/genetics ; Ribulose-Bisphosphate Carboxylase/*genetics ; Tobacco/enzymology/*genetics ; Transcription, Genetic/radiation effects ; Transformation, Genetic
    Print ISSN: 0036-8075
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  • 10
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    De novo design, expression, and characterization of Felix: a four-helix bundle protein of native-like sequence (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-24
    Description: The protein Felix was designed de novo to fold into an antiparallel four-helix bundle of specific topology. Its sequence of 79 amino acid residues is not homologous to any known protein sequence, but is "native-like" in that it is nonrepetitive and contains 19 of the 20 naturally occurring amino acids. Felix has been expressed from a synthetic gene cloned in Escherichia coli, and the protein has been purified to homogeneity. Physical characterization of the purified protein indicates that Felix (i) is monomeric in solution, (ii) is predominantly alpha-helical, (iii) contains a designed intramolecular disulfide bond linking the first and fourth helices, and (iv) buries its single tryptophan in an apolar environment and probably in close proximity with the disulfide bond. These physical properties rule out several alternative structures and indicate that Felix indeed folds into approximately the designed three-dimensional structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hecht, M H -- Richardson, J S -- Richardson, D C -- Ogden, R C -- New York, N.Y. -- Science. 1990 Aug 24;249(4971):884-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Duke University, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2392678" target="_blank"〉PubMed〈/a〉
    Keywords: *Amino Acid Sequence ; Base Sequence ; DNA/genetics ; *Models, Chemical ; Models, Molecular ; Molecular Sequence Data ; *Protein Conformation ; Protein Denaturation ; *Proteins ; *Recombinant Proteins
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  • 11
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    The energetic basis of specificity in the Eco RI endonuclease--DNA interaction (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-09
    Description: High sequence selectivity in DNA-protein interactions was analyzed by measuring discrimination by Eco RI endonuclease between the recognition site GAATTC and systematically altered DNA sites. Base analogue substitutions that preserve the sequence-dependent conformational motif of the GAATTC site permit deletion of single sites of protein-base contact at a cost of +1 to +2 kcal/mol. However, the introduction of any one incorrect natural base pair costs +6 to +13 kcal/mol in transition state interaction energy, the resultant of the following interdependent factors: deletion of one or two hydrogen bonds between the protein and a purine base; unfavourable steric apposition between a group on the protein and an incorrectly placed functional group on a base; disruption of a pyrimidine contact with the protein; loss of some crucial interactions between protein and DNA phosphates; and an increased energetic cost of attaining the required DNA conformation in the transition state complex. Eco RI endonuclease thus achieves stringent discrimination by both "direct readout" (protein-base contracts) and "indirect readout" (protein-phosphate contacts and DNA conformation) of the DNA sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lesser, D R -- Kurpiewski, M R -- Jen-Jacobson, L -- GM-29207/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Nov 9;250(4982):776-86.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Pittsburgh, PA 15260.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2237428" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; DNA/chemistry/genetics/*metabolism ; Deoxyribonuclease EcoRI/chemistry/*metabolism ; Energy Transfer ; Molecular Sequence Data ; Nucleic Acid Conformation ; Phosphates/metabolism ; Substrate Specificity
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  • 12
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    Cloning of a 67-kD neutrophil oxidase factor with similarity to a noncatalytic region of p60c-src (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-05-11
    Description: Chronic granulomatous diseases (CGDs) are characterized by recurrent infections resulting from impaired superoxide production by a phagocytic cell, nicotinamide adenine dinucleotide phosphate (reduced) (NADPH) oxidase. Complementary DNAs were cloned that encode the 67-kilodalton (kD) cytosolic oxidase factor (p67), which is deficient in 5% of CGD patients. Recombinant p67 (r-p67) partially restored NADPH oxidase activity to p67-deficient neutrophil cytosol from these patients. The p67 cDNA encodes a 526-amino acid protein with acidic middle and carboxyl-terminal domains that are similar to a sequence motif found in the noncatalytic domain of src-related tyrosine kinases. This motif was recently noted in phospholipase C-gamma, nonerythroid alpha-spectrin (fodrin), p21ras-guanosine triphophatase-activating protein (GAP), myosin-1 isoforms, yeast proteins cdc-25 and fus-1, and the 47-kD phagocyte oxidase factor (p47), which suggests the possibility of common regulatory features.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leto, T L -- Lomax, K J -- Volpp, B D -- Nunoi, H -- Sechler, J M -- Nauseef, W M -- Clark, R A -- Gallin, J I -- Malech, H L -- I01 BX000513/BX/BLRD VA/ -- New York, N.Y. -- Science. 1990 May 11;248(4956):727-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Clinical Investigation, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1692159" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; Granulomatous Disease, Chronic/blood/enzymology/genetics ; Humans ; Molecular Sequence Data ; NADH, NADPH Oxidoreductases/blood/*genetics ; NADPH Oxidase ; Neutrophils/*enzymology ; Protein-Tyrosine Kinases/genetics ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins pp60(c-src) ; Sequence Homology, Nucleic Acid
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  • 13
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    Identification of a sequence in the PEPCK gene that mediates a negative effect of insulin on transcription (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-03
    Description: Phosphoenolpyruvate carboxykinase (PEPCK) governs the rate-limiting step in gluconeogenesis. Glucocorticoids and adenosine 3',5'-monophosphate (cAMP) increase PEPCK gene transcription and gluconeogenesis, whereas insulin has the opposite effect. Insulin is dominant, since it prevents cAMP and glucocorticoid-stimulated transcription. Glucocorticoid and cAMP response elements have been located in the PEPCK gene and now a 15-base pair insulin-responsive sequence (IRS) is described. Evidence for a binding activity that recognizes this sequence is presented.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Brien, R M -- Lucas, P C -- Forest, C D -- Magnuson, M A -- Granner, D K -- DK 20593/DK/NIDDK NIH HHS/ -- DK 35107/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):533-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Physiology and Biophysics, Vanderbilt University Medical School, Nashville, TN 37232-0615.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2166335" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Line ; Chloramphenicol O-Acetyltransferase/genetics/metabolism ; Cyclic AMP/analogs & derivatives/physiology ; Dexamethasone/pharmacology ; *Genes, Regulator ; Insulin/*pharmacology ; Molecular Sequence Data ; Phosphoenolpyruvate Carboxykinase (GTP)/*genetics/metabolism ; RNA, Messenger/drug effects/genetics ; Recombinant Fusion Proteins/metabolism ; Thionucleotides ; Transcription, Genetic/*drug effects ; Transfection
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  • 14
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    RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J recombination (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-06-22
    Description: The vast repertoire of immunoglobulins and T cell receptors is generated, in part, by V(D)J recombination, a series of genomic rearrangements that occur specifically in developing lymphocytes. The recombination activating gene, RAG-1, which is a gene expressed exclusively in maturing lymphoid cells, was previously isolated. RAG-1 inefficiently induced V(D)J recombinase activity when transfected into fibroblasts, but cotransfection with an adjacent gene, RAG-2, has resulted in at least a 1000-fold increase in the frequency of recombination. The 2.1-kilobase RAG-2 complementary DNA encodes a putative protein of 527 amino acids whose sequence is unrelated to that of RAG-1. Like RAG-1, RAG-2 is conserved between species that carry out V(D)J recombination, and its expression pattern correlates precisely with that of V(D)J recombinase activity. In addition to being located just 8 kilobases apart, these convergently transcribed genes are unusual in that most, if not all, of their coding and 3' untranslated sequences are contained in single exons. RAG-1 and RAG-2 might activate the expression of the V(D)J recombinase but, more likely, they directly participate in the recombination reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oettinger, M A -- Schatz, D G -- Gorka, C -- Baltimore, D -- GM39458/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 22;248(4962):1517-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2360047" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biological Evolution ; Cattle ; Cell Line ; Chickens ; Cricetinae ; DNA/*genetics ; DNA Nucleotidyltransferases/*genetics ; *DNA-Binding Proteins ; Dogs ; Female ; *Gene Rearrangement, B-Lymphocyte ; *Gene Rearrangement, T-Lymphocyte ; *Homeodomain Proteins ; Humans ; Male ; Mice ; Molecular Sequence Data ; *Multigene Family ; Nuclear Proteins ; Nucleic Acid Hybridization ; Opossums ; Proteins/*genetics ; Rabbits ; Recombination, Genetic/*genetics ; Restriction Mapping ; Transfection ; Turtles ; VDJ Recombinases
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  • 15
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    Design of DNA-binding peptides based on the leucine zipper motif (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-17
    Description: A class of transcriptional regulator proteins bind to DNA at dyad-symmetric sites through a motif consisting of (i) a "leucine zipper" sequence that associates into noncovalent, parallel, alpha-helical dimers and (ii) a covalently connected basic region necessary for binding DNA. The basic regions are predicted to be disordered in the absence of DNA and to form alpha helices when bound to DNA. These helices bind in the major groove forming multiple hydrogen-bonded and van der Waals contacts with the nucleotide bases. To test this model, two peptides were designed that were identical to natural leucine zipper proteins only at positions hypothesized to be critical for dimerization and DNA recognition. The peptides form dimers that bind specifically to DNA with their basic regions in alpha-helical conformations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Neil, K T -- Hoess, R H -- DeGrado, W F -- New York, N.Y. -- Science. 1990 Aug 17;249(4970):774-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Central Research and Development Department, E.I. du Pont de Nemours & Co., Wilmington, DE 19880-0328.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2389143" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Chemistry, Physical ; Circular Dichroism ; Computer Simulation ; DNA/*metabolism ; DNA-Binding Proteins/*metabolism ; Hydrogen Bonding ; *Leucine ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Physicochemical Phenomena ; Protein Conformation
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  • 16
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    An insertion in the human thyrotropin receptor critical for high affinity hormone binding (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-21
    Description: Thyrotropin (TSH), luteinizing hormone (LH), and chorionic gonadotropin (CG) are structurally related glycoprotein hormones, which bind to receptors that share a high degree of sequence similarity. However, comparison of the primary amino acid sequences of the TSH and LH-CG receptors reveals two unique insertions of 8 and 50 amino acids in the extracellular domain of the TSH receptor. The functional significance of these insertions were determined by site-directed mutagenesis. Deletion of the 50-amino acid tract (residues 317 to 366) had no effect on TSH binding or on TSH and thyroid-stimulating immunoglobulin (TSI) biological activities. In contrast, either deletion or substitution of the eight-amino acid region (residues 38 to 45) abolished these activities. This eight-amino acid tract near the amino terminus of the TSH receptor appears to be an important site of interaction for both TSH and TSI.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wadsworth, H L -- Chazenbalk, G D -- Nagayama, Y -- Russo, D -- Rapoport, B -- DK-19289/DK/NIDDK NIH HHS/ -- DK-36182/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 21;249(4975):1423-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Veterans Administration Medical Center, San Francisco, CA 94121.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2169649" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cell Line ; Chromosome Deletion ; Clone Cells ; Cyclic AMP/metabolism ; Humans ; Molecular Sequence Data ; Mutation ; Oligonucleotide Probes ; Receptors, Thyrotropin/*genetics/metabolism ; Thyrotropin/*metabolism/pharmacology ; Transfection
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  • 17
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    Template supercoiling by a chimera of yeast GAL4 protein and phage T7 RNA polymerase (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-09-14
    Description: Fusion of the DNA-binding domain of yeast GAL4 protein to the amino terminus of bacteriophage T7 RNA polymerase yields a chimera that retains the characteristics of its components. The presence of the GAL4 peptide allows the chimeric enzyme to anchor itself on the DNA template, and this anchoring in turn drives the formation of a supercoiled DNA loop, in linear or circular templates, when RNA synthesis at the polymerase site forces a translocation of the DNA relative to the site. Nonspecific interaction between the chimeric enzyme and DNA appears to be sufficient to effect supercoiling during transcription. Transcription by the chimeric polymerase is strictly dependent on the presence of a T7 promoter; thus it provides a tool in vitro and in vivo for specifically supercoiling DNA segments containing T7 promoter sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ostrander, E A -- Benedetti, P -- Wang, J C -- GM24544/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 14;249(4974):1261-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2399463" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA, Superhelical/*metabolism ; DNA-Binding Proteins/*physiology ; DNA-Directed RNA Polymerases/*physiology ; Fungal Proteins/*metabolism ; Macromolecular Substances ; Molecular Sequence Data ; Promoter Regions, Genetic/physiology ; Recombinant Fusion Proteins/metabolism ; *Saccharomyces cerevisiae Proteins ; T-Phages/*enzymology ; Transcription Factors/physiology ; Transcription, Genetic/*physiology ; Viral Proteins
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  • 18
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    "Pure" human hematopoietic progenitors: permissive action of basic fibroblast growth factor (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-28
    Description: Methodology has been developed that enables virtually complete purification and abundant recovery of early hematopoietic progenitors from normal human adult peripheral blood. A fraction of the pure progenitors is multipotent (generates mixed colonies) and exhibits self-renewal capacity (gives rise to blast cell colonies). This methodology provides a fundamental tool for basic and clinical studies on hematopoiesis. Optimal in vitro cloning of virtually pure progenitors requires not only the stimulatory effect of interleukin-3, granulocyte-macrophage colony-stimulating factor, and erythropoietin, but also the permissive action of basic fibroblast growth factor. These findings suggest a regulatory role for this growth factor in early hematopoiesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabbianelli, M -- Sargiacomo, M -- Pelosi, E -- Testa, U -- Isacchi, G -- Peschle, C -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1561-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Hematology and Oncology, Istituto Superiore di Sanita, Rome, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218497" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Antibodies, Monoclonal/immunology ; Cell Separation ; Cells, Cultured ; Clone Cells ; Erythropoietin/pharmacology ; Fibroblast Growth Factor 2/*pharmacology ; Granulocyte-Macrophage Colony-Stimulating Factor/pharmacology ; Hematopoietic Stem Cells/*cytology/drug effects ; Humans ; Interleukin-3/pharmacology ; Monocytes/*cytology/drug effects ; Recombinant Proteins/pharmacology
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  • 19
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    Tissue, developmental, and tumor-specific expression of divergent transcripts in Wilms tumor (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-11-16
    Description: The Wilms tumor locus on chromosome 11p13 has been mapped to a region defined by overlapping, tumor-specific deletions. Complementary DNA clones representing transcripts of 2.5 (WIT-1) and 3.5 kb (WIT-2) mapping to this region were isolated from a kidney complementary DNA library. Expression of WIT-1 and WIT-2 was restricted to kidney and spleen. RNase protection revealed divergent transcription of WIT-1 and WIT-2, originating from a DNA region of less than 600 bp. Both transcripts were present at high concentrations in fetal kidney and at much reduced amounts in 5-year-old and adult kidneys. Eleven of 12 Wilms tumors classified as histopathologically heterogeneous exhibited absent or reduced expression of WIT-2, whereas only 4 of 14 histopathologically homogeneous tumors showed reduced expression. These data demonstrate a molecular basis for the pathogenetic heterogeneity in Wilms tumorigenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, A -- Campbell, C E -- Bonetta, L -- McAndrews-Hill, M S -- Chilton-MacNeill, S -- Coppes, M J -- Law, D J -- Feinberg, A P -- Yeger, H -- Williams, B R -- New York, N.Y. -- Science. 1990 Nov 16;250(4983):991-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Hospital for Sick Children, Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2173145" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blotting, Northern ; DNA/genetics ; Genes, Wilms Tumor/*genetics ; Humans ; Kidney Neoplasms/*genetics ; Molecular Sequence Data ; Transcription, Genetic ; Wilms Tumor/*genetics
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  • 20
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    Involvement of the silencer and UAS binding protein RAP1 in regulation of telomere length (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-10-26
    Description: The yeast protein RAP1, initially described as a transcriptional regulator, binds in vitro to sequences found in a number of seemingly unrelated genomic loci. These include the silencers at the transcriptionally repressed mating-type genes, the promoters of many genes important for cell growth, and the poly[(cytosine)1-3 adenine] [poly(C1-3A)] repeats of telomeres. Because RAP1 binds in vitro to the poly(C1-3A) repeats of telomeres, it has been suggested that RAP1 may be involved in telomere function in vivo. In order to test this hypothesis, the telomere tract lengths of yeast strains that contained conditionally lethal (ts) rap1 mutations were analyzed. Several rap1ts alleles reduced telomere length in a temperature-dependent manner. In addition, plasmids that contain small, synthetic telomeres with intact or mutant RAP1 binding sites were tested for their ability to function as substrates for poly(C1-3A) addition in vivo. Mutations in the RAP1 binding sites reduced the efficiency of the addition reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lustig, A J -- Kurtz, S -- Shore, D -- GM 40094/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Oct 26;250(4980):549-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Memorial Sloan-Kettering Cancer Center, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2237406" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Chromosomes, Fungal/metabolism/*ultrastructure ; DNA-Binding Proteins/metabolism ; Fungal Proteins/genetics/*metabolism ; *Genes, Fungal ; *Genes, Mating Type, Fungal ; Molecular Sequence Data ; Mutation ; Plasmids ; Poly A/metabolism ; Poly C/metabolism ; Repetitive Sequences, Nucleic Acid ; Saccharomyces cerevisiae/*genetics ; Temperature ; *Transcription Factors ; Transformation, Genetic
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  • 21
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    Two G protein oncogenes in human endocrine tumors (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-08-10
    Description: Somatic mutations in a subset of growth hormone (GH)-secreting pituitary tumors convert the gene for the alpha polypeptide chain (alpha s) of Gs into a putative oncogene, termed gsp. These mutations, which activate alpha s by inhibiting its guanosine triphosphatase (GTPase) activity, are found in codons for either of two amino acids, each of which is completely conserved in all known G protein alpha chains. The likelihood that similar mutations would activate other G proteins prompted a survey of human tumors for mutations that replace either of these two amino acids in other G protein alpha chain genes. The first gene so far tested, which encodes the alpha chain of Gi2, showed mutations that replaced arginine-179 with either cysteine or histidine in 3 of 11 tumors of the adrenal cortex and 3 of 10 endocrine tumors of the ovary. The mutant alpha i2 gene is a putative oncogene, referred to as gip2. In addition, gsp mutations were found in 18 of 42 GH-secreting pituitary tumors and in an autonomously functioning thyroid adenoma. These findings suggest that human tumors may harbor oncogenic mutations in various G protein alpha chain genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lyons, J -- Landis, C A -- Harsh, G -- Vallar, L -- Grunewald, K -- Feichtinger, H -- Duh, Q Y -- Clark, O H -- Kawasaki, E -- Bourne, H R -- New York, N.Y. -- Science. 1990 Aug 10;249(4969):655-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics, Cetus Corporation, Emeryville CA 94608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2116665" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA, Neoplasm/genetics ; Endocrine System Diseases/*genetics ; Female ; GTP Phosphohydrolases/genetics/metabolism ; GTP-Binding Proteins/*genetics/metabolism ; Humans ; Male ; Molecular Sequence Data ; *Mutation ; Neoplasms/*genetics ; Oligonucleotide Probes ; *Oncogenes ; Pituitary Neoplasms/*genetics ; Polymerase Chain Reaction
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  • 22
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    Characterization of naturally occurring minor histocompatibility peptides including H-4 and H-Y (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-07-20
    Description: Minor histocompatibility (H) antigens can be peptides derived from cellular proteins that are presented on the cell surface by major histocompatibility complex (MHC) class I molecules. This is similar to viral antigens, because in both cases cytotoxic T lymphocytes (CTLs) recognize artificially produced peptides loaded on target cells. Naturally processed minor H peptides were found to be similar to those artificial CTL-epitopes, as far as size and hydrophobicity is concerned. The peptides studied were isolated from a transfectant that expressed a model CTL-defined antigen, beta-galactosidase, from male cells that express H-Y, which has been known operationally since 1955, and from cells that express H-4, known since 1961.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rotzschke, O -- Falk, K -- Wallny, H J -- Faath, S -- Rammensee, H G -- New York, N.Y. -- Science. 1990 Jul 20;249(4966):283-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biologie, Abteilung Immungenetik, Tubingen, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1695760" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Epitopes/isolation & purification ; Female ; H-Y Antigen/*analysis/immunology ; Male ; Mice ; Mice, Inbred Strains ; Minor Histocompatibility Antigens/*analysis/immunology ; Molecular Sequence Data ; Peptides/chemical synthesis ; Species Specificity ; Spleen/immunology ; T-Lymphocytes, Cytotoxic/*immunology
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  • 23
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    Recovery of mitogenic activity of a growth factor mutant with a nuclear translocation sequence (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-09-28
    Description: Heparin-binding growth factor-1 (HBGF-1) is an angiogenic polypeptide mitogen for mesoderm- and neuroectoderm-derived cells in vitro and remains biologically active after truncation of the amino-terminal domain (HBGF-1 alpha) of the HBGF-1 beta precursor. Polymerase chain reaction mutagenesis and prokaryotic expression systems were used to prepare a mutant of HBGF-1 alpha lacking a putative nuclear translocation sequence (amino acid residues 21 to 27; HBGF-1U). Although HBGF-1U retains its ability to bind to heparin, HBGF-1U fails to induce DNA synthesis and cell proliferation at concentrations sufficient to induce intracellular receptor-mediated tyrosine phosphorylation and c-fos expression. Attachment of the nuclear translocation sequence from yeast histone 2B at the amino terminus of HBGF-1U yields a chimeric polypeptide (HBGF-1U2) with mitogenic activity in vitro and indicates that nuclear translocation is important for this biological response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Imamura, T -- Engleka, K -- Zhan, X -- Tokita, Y -- Forough, R -- Roeder, D -- Jackson, A -- Maier, J A -- Hla, T -- Maciag, T -- HL 32348/HL/NHLBI NIH HHS/ -- HL 35627/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1567-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, Jerome H. Holland Laboratory for the Biomedical Sciences, American Red Cross, Rockville, MD 20855.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1699274" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding, Competitive ; Cattle ; Cell Division/drug effects ; Cell Line ; Cell Nucleus/metabolism ; Cells, Cultured ; DNA Replication/drug effects ; Endothelium, Vascular/drug effects/metabolism ; Fibroblast Growth Factor 1/*genetics/metabolism/pharmacology ; Kinetics ; Mice ; Mitogens/pharmacology ; Molecular Sequence Data ; *Mutation ; Oligonucleotide Probes ; Receptors, Mitogen/metabolism ; Receptors, Vascular Endothelial Growth Factor ; Recombinant Proteins/metabolism/pharmacology ; Transcription, Genetic/drug effects
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  • 24
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    Conserved residues make similar contacts in two repressor-operator complexes (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-03-09
    Description: Comparison of a lambda repressor-operator complex and a 434 repressor-operator complex reveals that three conserved residues in the helix-turn-helix (HTH) region make similar contacts in each of the crystallographically determined structures. These conserved residues and their interactions with phosphodiester oxygens help establish a frame of reference within which other HTH residues make contacts that are critical for site-specific recognition. Such "positioning contacts" may be important conserved features within families of HTH proteins. In contrast, the structural comparisons appear to rule out any simple "recognition code" at the level of detailed side chain-base pair interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pabo, C O -- Aggarwal, A K -- Jordan, S R -- Beamer, L J -- Obeysekare, U R -- Harrison, S C -- GM 29109/GM/NIGMS NIH HHS/ -- GM 31471/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Mar 9;247(4947):1210-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2315694" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Asparagine ; Base Composition ; Base Sequence ; Binding Sites ; *DNA-Binding Proteins ; Glutamine ; Hydrogen Bonding ; Molecular Sequence Data ; Molecular Structure ; *Operator Regions, Genetic ; Protein Conformation ; Repressor Proteins/*metabolism ; Transcription Factors/*metabolism ; Viral Proteins ; Viral Regulatory and Accessory Proteins
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  • 25
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    Mapping of herpes simplex virus-1 neurovirulence to gamma 134.5, a gene nonessential for growth in culture (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-30
    Description: The gene designated gamma 134.5 maps in the inverted repeats flanking the long unique sequence of herpes simplex virus-1 (HSV-1) DNA, and therefore it is present in two copies per genome. This gene is not essential for viral growth in cell culture. Four recombinant viruses were genetically engineered to test the function of this gene. These were (i) a virus from which both copies of the gene were deleted, (ii) a virus containing a stop codon in both copies of the gene, (iii) a virus containing after the first codon an insert encoding a 16-amino acid epitope known to react with a specific monoclonal antibody, and (iv) a virus in which the deleted sequences were restored. The viruses from which the gene was deleted or which carried stop codons were avirulent on intracerebral inoculation of mice. The virus with the gene tagged by the sequence encoding the epitope was moderately virulent, whereas the restored virus reacquired the phenotype of the parent virus. Significant amounts of virus were recovered only from brains of animals inoculated with virulent viruses. Inasmuch as the product of the gamma 134.5 gene extended the host range of the virus by enabling it to replicate and destroy brain cells, it is a viral neurovirulence factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chou, J -- Kern, E R -- Whitley, R J -- Roizman, B -- AI 1588-11/AI/NIAID NIH HHS/ -- AI 24009/AI/NIAID NIH HHS/ -- CA 47451/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Nov 30;250(4985):1262-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Marjorie B. Kovler Viral Oncology Laboratories, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2173860" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Antigens, Viral/genetics/immunology ; Base Sequence ; Chromosome Deletion ; *Chromosome Mapping ; Codon ; DNA, Viral/genetics ; Encephalitis/*microbiology ; *Genes, Viral ; Herpes Simplex/*microbiology ; Humans ; *Immediate-Early Proteins ; Molecular Sequence Data ; Rabbits ; Repetitive Sequences, Nucleic Acid ; Simplexvirus/*genetics/growth & development/pathogenicity ; Thymidine Kinase/genetics ; Transfection ; Viral Proteins/*genetics ; Viral Regulatory and Accessory Proteins/genetics/immunology
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    Translation initiation and ribosomal biogenesis: involvement of a putative rRNA helicase and RPL46 (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-03-02
    Description: Cold-sensitive mutations in the SPB genes (spb1-spb7) of Saccharomyces cerevisiae suppress the inhibition of translation initiation resulting from deletion of the poly(A)-binding protein gene (PAB1). The SPB4 protein belongs to a family of adenosine triphosphate (ATP)-dependent RNA helicases. The aberrant production of 25S ribosomal RNA (rRNA) occurring in spb4-1 mutants or the deletion of SPB2 (RPL46) permits the deletion of PAB1. These data suggest that mutations affecting different steps of 60S subunit formation can allow PAB-independent translation, and they indicate that further characterization of the spb mutations could lend insight into the biogenesis of the ribosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sachs, A B -- Davis, R W -- R37 GM 21891/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Mar 2;247(4946):1077-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Stanford Medical Center, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2408148" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Carrier Proteins/genetics/metabolism ; DEAD-box RNA Helicases ; Molecular Sequence Data ; Mutation ; Poly(A)-Binding Proteins ; *Protein Biosynthesis ; RNA Nucleotidyltransferases/genetics/*metabolism ; RNA Processing, Post-Transcriptional ; RNA, Fungal/genetics/metabolism ; RNA, Ribosomal/genetics/*metabolism ; Ribosomal Proteins/genetics/*metabolism ; Ribosomes/*metabolism ; Saccharomyces cerevisiae/enzymology/*genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Homology, Nucleic Acid
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    Gerontology research comes of age (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, A -- New York, N.Y. -- Science. 1990 Nov 2;250(4981):622-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2237413" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*physiology ; Animals ; Cells, Cultured ; DNA Damage ; Free Radicals ; Humans ; Life Expectancy
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    Effect of phospholipase C-gamma overexpression on PDGF-induced second messengers and mitogenesis (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-05-04
    Description: Platelet-derived growth factor (PDGF) stimulates phospholipase C (PLC) activity and the phosphorylation of the gamma isozyme of PLC (PLC-gamma) in vitro and in living cells. The role of PLC-gamma in the phosphoinositide signaling pathway was addressed by examining the effect of overexpression of PLC-gamma on cellular responses to PDGF. Overexpression of PLC-gamma correlated with PDGF-induced tyrosine phosphorylation of PLC-gamma and with PDGF-induced breakdown of phosphatidylinositol 4,5-bisphosphate (PIP2). However, neither bradykinin- nor lysophosphatidic acid-induced phosphoinositide metabolism was enhanced in the transfected cells, suggesting that the G protein-coupled phosphoinositide responses to these ligands are mediated by other PLC isozymes. The enhanced PDGF-induced generation of inositol trisphosphate (IP3) did not enhance intracellular calcium signaling or influence PDGF-induced DNA synthesis. Thus, enzymes other than PLC-gamma may limit PDGF-induced calcium signaling and DNA synthesis. Alternatively, PDGF-induced calcium signaling and DNA synthesis may use biochemical pathways other than phosphoinositide metabolism for signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Margolis, B -- Zilberstein, A -- Franks, C -- Felder, S -- Kremer, S -- Ullrich, A -- Rhee, S G -- Skorecki, K -- Schlessinger, J -- New York, N.Y. -- Science. 1990 May 4;248(4955):607-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rorer Biotechnology, King of Prussia, PA 19406.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2333512" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/physiology ; Cattle ; Cell Division/*drug effects ; Cells, Cultured ; DNA Replication/drug effects ; Genetic Vectors ; Inositol Phosphates/metabolism ; Isoenzymes/biosynthesis/*genetics/metabolism ; Kinetics ; Mice ; Platelet-Derived Growth Factor/*pharmacology ; Second Messenger Systems/*drug effects ; Transfection ; Type C Phospholipases/biosynthesis/*genetics/metabolism
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    T cells responsive to myelin basic protein in patients with multiple sclerosis (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-02-09
    Description: Gene mutation in vivo in human T lymphocytes appears to occur preferentially in dividing cells. Individuals with multiple sclerosis (MS) are assumed to have one or more populations of diving T cells that are being stimulated by autoantigens. Mutant T cell clones from MS patients were isolated and tested for reactivity to myelin basic protein, an antigen that is thought to participate in the induction of the disease. The hypoxanthine guanine phosphoribosyltransferase (hprt) clonal assay was used to determine mutant frequency values in MS patients with chronic progressive disease. Eleven of 258 thioguanine-resistant (hprt-) T cell clones from five of the six MS patients who were tested proliferated in response to human myelin basic protein without prior in vitro exposure to this antigen. No wild-type clones from these patients, nor any hprt- or wild-type clones from three healthy individuals responded to myelin basic protein. Thus, T cell clones that react with myelin basic protein can be isolated from the peripheral blood of MS patients.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allegretta, M -- Nicklas, J A -- Sriram, S -- Albertini, R J -- CA30688-07/CA/NCI NIH HHS/ -- NS00849/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Feb 9;247(4943):718-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genetics Laboratory, University of Vermont, Burlington 05401.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1689076" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Autoantigens/immunology ; Cell Division ; Clone Cells/immunology ; Female ; Humans ; Hypoxanthine Phosphoribosyltransferase/genetics ; Male ; Middle Aged ; Multiple Sclerosis/genetics/*immunology ; Mutation ; Myelin Basic Protein/*immunology ; T-Lymphocytes/drug effects/*immunology ; Thioguanine/pharmacology ; X Chromosome
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    Phencyclidine, dizocilpine, and cerebrocortical neurons (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-01-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allen, H L -- Iversen, L L -- New York, N.Y. -- Science. 1990 Jan 12;247(4939):221.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Merck Sharp & Dohme Research Laboratories, West Point, PA 19486.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2403696" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cerebral Cortex/drug effects/*ultrastructure ; Dibenzocycloheptenes/administration & dosage/*pharmacology ; Dizocilpine Maleate ; Male ; Neurons/drug effects/*ultrastructure ; Phencyclidine/*pharmacology ; Rats ; Vacuoles/drug effects
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    Experts clash over cancer data (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1990 Nov 16;250(4983):900-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2237436" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Female ; Humans ; Male ; Middle Aged ; Neoplasms/*mortality ; United States
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    Smokers: black and white (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-07-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schneiderman, M -- Davis, D L -- Wagener, D K -- New York, N.Y. -- Science. 1990 Jul 20;249(4966):228-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2374921" target="_blank"〉PubMed〈/a〉
    Keywords: African Americans ; European Continental Ancestry Group ; Female ; Humans ; Lung Neoplasms/mortality ; Male ; Prevalence ; Smoking/*epidemiology ; United States
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    The human genome project: past, present, and future (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-04-06
    Description: This article presents a short discussion of the development of the human genome program in the United States, a summary of the current status of the organization and administration of the National Institutes of Health component of the program, and some prospects for the future directions of the program and the applications of genome information.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watson, J D -- New York, N.Y. -- Science. 1990 Apr 6;248(4951):44-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Center for Human Genome Research, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2181665" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Budgets ; Dna ; Federal Government ; *Human Genome Project/economics/organization & administration ; Humans ; International Cooperation ; Internationality ; National Institutes of Health (U.S.)/organization & administration ; Research Support as Topic ; Risk Assessment ; United States
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    A mouse model of the aniridia-Wilms tumor deletion syndrome (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-09
    Description: Deletion of chromosome 11p13 in humans produces the WAGR syndrome, consisting of aniridia (an absence or malformation of the iris), Wilms tumor (nephroblastoma), genitourinary malformations, and mental retardation. An interspecies backcross between Mus musculus/domesticus and Mus spretus was made in order to map the homologous chromosomal region in the mouse genome and to define an animal model of this syndrome. Nine evolutionarily conserved DNA clones from proximal human 11p were localized on mouse chromosome 2 near Small-eyes (Sey), a semidominant mutation that is phenotypically similar to aniridia. Analysis of Dickie's Small-eye (SeyDey), a poorly viable allele that has pleiotropic effects, revealed the deletion of three clones, f3, f8, and k13, which encompass the aniridia (AN2) and Wilms tumor susceptibility genes in man. Unlike their human counterparts, SeyDey/+ mice do not develop nephroblastomas. These findings suggest that the Small-eye defect is genetically equivalent to human aniridia, but that loss of the murine homolog of the Wilms tumor gene is not sufficient for tumor initiation. A comparison among Sey alleles suggests that the AN2 gene product is required for induction of the lens and nasal placodes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Glaser, T -- Lane, J -- Housman, D -- 2 T32 GMO7753-11/GM/NIGMS NIH HHS/ -- GM27882/GM/NIGMS NIH HHS/ -- T32 GM007753/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Nov 9;250(4982):823-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Cancer Research, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2173141" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aniridia/*genetics ; Blotting, Southern ; Chromosome Deletion ; Chromosome Mapping ; DNA/analysis ; *Disease Models, Animal ; Eye/embryology/pathology ; Female ; Genes, Wilms Tumor/*genetics ; Genetic Markers ; Kidney Neoplasms/*genetics ; Male ; Mice ; Mice, Inbred C3H ; Mice, Inbred C57BL ; Muridae ; Mutation ; Phenotype ; Polymorphism, Genetic ; Syndrome ; Wilms Tumor/*genetics
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    HTLV-I trans-activator protein, tax, is a trans-repressor of the human beta-polymerase gene (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-03-02
    Description: Human T cell leukemia virus type I (HTLV-I) is the etiological agent for adult T cell leukemia (ATL). The HTLV-I trans-activator protein Tax can activate the expression of its own long terminal repeat (LTR) and many cellular and viral genes. Tax down-regulated the expression of human beta-polymerase (hu beta-pol), a cellular enzyme involved in host cell DNA repair. This finding suggests a possible correlation between HTLV-I infection and host chromosomal damage, which is often seen in ATL cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jeang, K T -- Widen, S G -- Semmes, O J 4th -- Wilson, S H -- New York, N.Y. -- Science. 1990 Mar 2;247(4946):1082-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Microbiology, National Institute of 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/2309119" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Line ; Cell Line, Transformed ; DNA Polymerase I/*genetics ; DNA, Viral/genetics ; Gene Expression Regulation, Enzymologic ; Gene Expression Regulation, Viral ; Human T-lymphotropic virus 1/*genetics ; Humans ; Molecular Sequence Data ; Plasmids ; Promoter Regions, Genetic ; RNA, Messenger/biosynthesis ; Repetitive Sequences, Nucleic Acid ; Repressor Proteins/biosynthesis/*genetics ; Trans-Activators/biosynthesis/*genetics ; Transcription Factors/*genetics ; Transfection
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    Requirement for activin A and transforming growth factor--beta 1 pro-regions in homodimer assembly (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-03-16
    Description: Many proteins are initially synthesized as part of a large precursor. The role of the pro-region in the biosynthesis of transforming growth factor--beta 1 (TGF-beta 1) and activin A, two structurally related disulfide-linked homodimers synthesized as large precursors, was studied. Vectors that expressed either the pro-region or the mature regions of these molecules were used in complementation experiments, only when the pro-region was coexpressed with the mature region did intracellular dimerization and secretion of biologically active homodimers occur. The pro-regions of activin A and TGF-beta 1, therefore, aid the folding, disulfide bond formation, and export of their respective homodimers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gray, A M -- Mason, A J -- New York, N.Y. -- Science. 1990 Mar 16;247(4948):1328-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology, Genentech, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2315700" target="_blank"〉PubMed〈/a〉
    Keywords: Activins ; Amino Acid Sequence ; Cells, Cultured ; Genetic Complementation Test ; Humans ; Inhibins/*biosynthesis/ultrastructure ; Macromolecular Substances ; Molecular Sequence Data ; Protein Processing, Post-Translational ; Protein Sorting Signals/physiology ; Transfection ; Transforming Growth Factors/*biosynthesis
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    Hair analysis (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-11-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martinez, F -- Poet, T S -- Watson, R R -- New York, N.Y. -- Science. 1990 Nov 23;250(4984):1070.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2251495" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cocaine/metabolism/pharmacokinetics ; Hair/*chemistry/metabolism ; Humans ; Male ; Mice ; Morphine/metabolism/pharmacokinetics ; *Substance Abuse Detection
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    Subtle cerebellar phenotype in mice homozygous for a targeted deletion of the En-2 homeobox (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-08
    Description: The two mouse genes, En-1 and En-2, that are homologs of the Drosophila segmentation gene engrailed, show overlapping spatially restricted patterns of expression in the neural tube during embryogenesis, suggestive of a role in regional specification. Mice homozygous for a targeted mutation that deletes the homeobox were viable and showed no obvious defects in embryonic development. This may be due to functional redundancy of En-2 and the related En-1 gene product during embryogenesis. Consistent with this hypothesis, the mutant mice showed abnormal foliation in the adult cerebellum, where En-2, and not En-1, is normally expressed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joyner, A L -- Herrup, K -- Auerbach, B A -- Davis, C A -- Rossant, J -- HD25334/HD/NICHD NIH HHS/ -- NS18381/NS/NINDS NIH HHS/ -- NS20591/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1239-43.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1672471" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastocyst ; Cell Line ; Cerebellum/*anatomy & histology/embryology/pathology ; Chimera ; *Chromosome Deletion ; Female ; *Genes, Homeobox ; Male ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Nervous System/embryology ; Phenotype
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    The combination of symbolic and numerical computation for three-dimensional modeling of RNA (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-09-13
    Description: Three-dimensional (3-D) structural models of RNA are essential for understanding of the cellular roles played by RNA. Such models have been obtained by a technique based on a constraint satisfaction algorithm that allows for the facile incorporation of secondary and other structural information. The program generates 3-D structures of RNA with atomic-level resolution that can be refined by numerical techniques such as energy minimization. The precision of this technique was evaluated by comparing predicted transfer RNA loop and RNA pseudoknot structures with known or consensus structures. The root-mean-square deviation (2.0 to 3.0 angstroms before minimization) between predicted and control structures reveal this system to be an effective method in modeling RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Major, F -- Turcotte, M -- Gautheret, D -- Lapalme, G -- Fillion, E -- Cedergren, R -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1255-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement d'Informatique et de Recherche Operationnelle, Universite de Montreal, Quebec, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716375" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Anticodon/chemistry ; Base Sequence ; *Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA/*chemistry ; RNA, Transfer/*chemistry
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    A multisubunit ribozyme that is a catalyst of and template for complementary strand RNA synthesis (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-29
    Description: Derivatives of the sunY self-splicing intron efficiently catalyzed the synthesis of complementary strand RNA by template-directed assembly of oligonucleotides. These ribozymes were separated into three short RNA fragments that formed active catalytic complexes. One of the multisubunit sunY derivatives catalyzed the synthesis of a strand of RNA complementary to one of its own subunits. These results suggest that prebiotically synthesized oligonucleotides might have been able to assemble into a complex capable of self-replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doudna, J A -- Couture, S -- Szostak, J W -- New York, N.Y. -- Science. 1991 Mar 29;251(5001):1605-8.〈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/1707185" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Base Sequence ; *Introns ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligoribonucleotides/metabolism ; RNA/*biosynthesis/genetics ; RNA Splicing ; RNA, Catalytic/*metabolism ; Templates, Genetic ; Tetrahymena/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 41
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    Group I intron self-splicing with adenosine: evidence for a single nucleoside-binding site (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-04-19
    Description: For self-splicing of Tetrahymena ribosomal RNA precursor, guanosine binding is required for 5' splice-site cleavage and exon ligation. Whether these two reactions use the same or different guanosine-binding sites has been debated. A double mutation in a previously identified guanosine-binding site within the intron resulted in preference for adenosine (or adenosine triphosphate) as the substrate for cleavage at the 5' splice site. However, splicing was blocked in the exon ligation step. Blockage was reversed by a change from guanine to adenine at the 3' splice site. These results indicate that a single determinant specifies nucleoside binding for both steps of splicing. Furthermore, it suggests that RNA could form an active site specific for adenosine triphosphate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Been, M D -- Perrotta, A T -- GM-40689/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Apr 19;252(5004):434-7.〈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/2017681" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/*metabolism ; Adenosine Triphosphate/pharmacology ; Animals ; Base Sequence ; Binding Sites ; Exons ; Guanosine/metabolism ; *Introns ; Magnesium/pharmacology ; Molecular Sequence Data ; Molecular Structure ; Mutagenesis ; RNA Precursors/chemistry/genetics ; *RNA Splicing ; RNA, Catalytic/metabolism ; Tetrahymena/genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Identification of the DNA binding site for NGFI-B by genetic selection in yeast (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-31
    Description: An in vivo selection system for isolating targets of DNA binding proteins in yeast was developed and used to identify the DNA binding site for the NGFI-B protein, a member of the steroid-thyroid hormone receptor superfamily. The feasibility of the technique was verified by selecting DNA fragments that contained binding sites for GCN4, a well-characterized yeast transcriptional activator. The DNA binding domain of NGFI-B, expressed as part of a LexA-NGFI-B-GAL4 chimeric activator, was then used to isolate a rat genomic DNA fragment that contained an NGFI-B binding site. The NGFI-B response element (NBRE) is similar to but functionally distinct from elements recognized by the estrogen and thyroid hormone receptors and the hormone receptor-like proteins COUP-TF, CF1, and H-2RIIBP. Cotransfection experiments in mammalian cells demonstrated that NGFI-B can activate transcription from the NBRE with or without its putative ligand binding domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, T E -- Fahrner, T J -- Johnston, M -- Milbrandt, J -- NS01018/NS/NINDS NIH HHS/ -- P01 CA49712/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 31;252(5010):1296-300.〈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/1925541" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/metabolism ; Base Sequence ; Binding Sites ; Cloning, Molecular ; DNA, Fungal/*metabolism ; DNA-Binding Proteins/genetics/*metabolism/pharmacology ; Fungal Proteins/metabolism ; Molecular Sequence Data ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Plasmids ; *Protein Kinases ; Rats ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid ; Repressor Proteins ; Saccharomyces cerevisiae/*genetics ; *Saccharomyces cerevisiae Proteins ; *Serine Endopeptidases ; Transcription Factors/genetics/*metabolism/pharmacology ; Transcription, Genetic ; Transfection
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    Isolation of an active human transposable element (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-30
    Description: Two de novo insertions of truncated L1 elements into the factor VIII gene on the X chromosome have been identified that produced hemophilia A. A full-length L1 element that is the likely progenitor of one of these insertions was isolated by its sequence identity to the factor VIII insertion. This L1 element contains two open-reading frames and is one of at least four alleles of a locus on chromosome 22 that has been occupied by an L1 element for at least 6 million years.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dombroski, B A -- Mathias, S L -- Nanthakumar, E -- Scott, A F -- Kazazian, H H Jr -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1805-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1662412" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Chromosomes, Human, Pair 22 ; *DNA Transposable Elements ; Factor VIII/*genetics ; Genome, Human ; Hemophilia A/*genetics ; Humans ; Molecular Sequence Data ; Open Reading Frames ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; X Chromosome
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    Repression of HIV-1 transcription by a cellular protein (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-22
    Description: A cellular DNA binding protein, LBP-1, sequentially interacts in a concentration-dependent manner with two sites that surround the transcriptional initiation site of the human immunodeficiency virus type 1 (HIV-1) promoter. Although sequences in the downstream site (site I) were found to enhance transcription, purified LBP-1 specifically repressed transcription in vitro by binding to the upstream site (site II), which overlaps the TATA element. The binding of human TATA binding factor (TFIID) to the promoter before LBP-1 blocked repression, suggesting that repression resulted from an inhibition of TFIID binding to the TATA element. Furthermore, mutations that eliminated binding to site II both prevented repression in vitro and increased HIV-1 transcription in stably transformed cells. These findings suggest that a cellular factor regulates HIV-1 transcription in a manner that is characteristic of bacterial repressors and that this factor could be important in HIV-1 latency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kato, H -- Horikoshi, M -- Roeder, R G -- AI27397/AI/NIAID NIH HHS/ -- CA42567/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 22;251(5000):1476-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006421" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA-Binding Proteins/genetics ; *Gene Expression Regulation, Viral ; HIV-1/*genetics ; Molecular Sequence Data ; Promoter Regions, Genetic ; Repressor Proteins/*genetics ; Transcription Factor TFIID ; Transcription Factors/metabolism ; Transcription, Genetic
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  • 45
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    A phosphorylation site in the Na+ channel required for modulation by protein kinase C (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-08
    Description: Voltage-gated sodium channels are responsible for generation of action potentials in excitable cells. Activation of protein kinase C slows inactivation of sodium channels and reduces peak sodium currents. Phosphorylation of a single residue, serine 1506, that is located in the conserved intracellular loop between domains III and IV and is involved in inactivation of the sodium channel, is required for both modulatory effects. Mutant sodium channels lacking this phosphorylation site have normal functional properties in unstimulated cells but do not respond to activation of protein kinase C. Phosphorylation of this conserved site in sodium channel alpha subunits may regulate electrical activity in a wide range of excitable cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉West, J W -- Numann, R -- Murphy, B J -- Scheuer, T -- Catterall, W A -- GM07270/GM/NIGMS NIH HHS/ -- NS15751/NS/NINDS NIH HHS/ -- NS25704/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):866-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658937" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Membrane/physiology ; Cells, Cultured ; Membrane Potentials ; Models, Structural ; Molecular Sequence Data ; Phosphorylation ; Protein Conformation ; Protein Kinase C/*metabolism ; Sodium Channels/metabolism/*physiology
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    Identification of p53 gene mutations in bladder cancers and urine samples (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-05-03
    Description: Although bladder cancers are very common, little is known about their molecular pathogenesis. In this study, invasive bladder cancers were evaluated for the presence of gene mutations in the p53 suppressor gene. Of 18 tumors evaluated, 11 (61 percent) were found to have genetic alterations of p53. The alterations included ten point mutations resulting in single amino acid substitutions, and one 24-base pair deletion. In all but one case, the mutations were associated with chromosome 17p allelic deletions, leaving the cells with only mutant forms of the p53 gene products. Through the use of the polymerase chain reaction and oligomer-specific hybridization, p53 mutations were identified in 1 to 7 percent of the cells within the urine sediment of each of three patients tested. The p53 mutations are the first genetic alterations demonstrated to occur in a high proportion of primary invasive bladder cancers. Detection of such mutations ex vivo has clinical implications for monitoring individuals whose tumor cells are shed extracorporeally.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sidransky, D -- Von Eschenbach, A -- Tsai, Y C -- Jones, P -- Summerhayes, I -- Marshall, F -- Paul, M -- Green, P -- Hamilton, S R -- Frost, P -- CA09071/CA/NCI NIH HHS/ -- CA43460/CA/NCI NIH HHS/ -- CA49758/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):706-9.〈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/2024123" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Chromosome Deletion ; Chromosomes, Human, Pair 17 ; *Genes, p53 ; Humans ; Molecular Sequence Data ; *Mutation ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Polymerase Chain Reaction ; Urinary Bladder Neoplasms/*genetics/urine ; Urine/cytology
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    Gallo concedes contamination (again) (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1991 Jun 7;252(5011):1369.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047847" target="_blank"〉PubMed〈/a〉
    Keywords: *Hiv ; History, 20th Century ; Humans ; Male ; National Institutes of Health (U.S.) ; United States ; Virus Cultivation
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  • 48
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    Molecular nature of the Drosophila sex determination signal and its link to neurogenesis (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-01
    Description: In 1921 it was discovered that the sexual fate of Drosophila is determined by the ratio of X chromosomes to sets of autosomes. Only recently has it been found that the X chromosome to autosome (X:A) ratio is communicated in part by the dose of sisterless-b (sis-b), an X-linked genetic element located within the achaete-scute complex of genes involved in neurogenesis. In this report, the molecular nature of the primary sex determination signal and its relation to these proneural genes was determined by analysis of sis-b+ germline transformants. The sis-b+ function is confered by protein T4, a member of the helix-loop-helix family of transcription factors. Although T4 is shared by sis-b and scute-alpha, the regulatory regions of sis-b, which control T4 expression in sex determination, are both separable from and simpler than those of scute-alpha, which control T4 expression in neurogenesis. Dose-sensitive cooperative interactions in the assembly or binding of sis-dependent transcription factors may directly determine the activity of the female-specific promoter of Sex-lethal, the master regulator of sexual development. In this model there is no need to invoke the existence of analogous autosomal negative regulators of Sex-lethal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erickson, J W -- Cline, T W -- GM 23468/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 1;251(4997):1071-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1900130" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; DNA Mutational Analysis ; Dosage Compensation, Genetic ; Drosophila melanogaster/*genetics ; Female ; Genes ; Genes, Lethal ; Male ; *Nervous System Physiological Phenomena ; Restriction Mapping ; *Sex Determination Analysis ; Transcription, Genetic ; X Chromosome/physiology
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    Leadership shuffle at Sloan Kettering (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-06-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1991 Jun 7;252(5011):1372.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047849" target="_blank"〉PubMed〈/a〉
    Keywords: Cancer Care Facilities/*organization & administration ; History, 20th Century ; Humans ; Male
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    Function of the homeodomain protein GHF1 in pituitary cell proliferation (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-07-12
    Description: Mutations that cause pituitary dwarfism in the mouse reside in the gene encoding the transcription factor growth hormone factor 1 (GHF1 or pit1). These dwarf mice (dw and dwJ) are deficient in growth hormone (GH) and prolactin (PRL) synthesis and exhibit pituitary hypoplasia, suggesting a stem cell defect. With antisense oligonucleotide technology, a cell culture model of this genetic defect was developed. Specific inhibition of GHF1 synthesis by complementary oligonucleotides led to a marked decrease in GH and PRL expression and to a marked decrease in proliferation of somatotrophic cell lines. These results provide direct evidence that the homeodomain protein GHF1 is required not only for the establishment and maintenance of the differentiated phenotype but for cell proliferation as well.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castrillo, J L -- Theill, L E -- Karin, M -- DK38527/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):197-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1677216" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antisense Elements (Genetics) ; Base Sequence ; *Cell Division ; Cells, Cultured ; DNA/biosynthesis ; DNA-Binding Proteins/*physiology ; Dwarfism/genetics ; Gene Expression Regulation ; *Genes, Homeobox ; Growth Hormone/genetics ; In Vitro Techniques ; Mice ; Molecular Sequence Data ; Pituitary Gland/*cytology/physiology ; Prolactin/genetics ; Transcription Factor Pit-1 ; Transcription Factors/*physiology
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    Cloning and expression of a cocaine-sensitive rat dopamine transporter (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-10-25
    Description: The action of dopamine and other monoamine neurotransmitters at synapses is terminated predominantly by high-affinity reuptake into presynaptic terminals by specific sodium-dependent neurotransmitter transport proteins. A complementary DNA encoding a rat dopamine transporter has been isolated that exhibits high sequence similarity with the previously cloned norepinephrine and gamma-aminobutyric acid transporters. Transient expression of the complementary DNA in HeLa cells confirms the cocaine sensitivity of this transporter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kilty, J E -- Lorang, D -- Amara, S G -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):578-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Yale University, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948035" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/drug effects/*genetics/metabolism ; Cloning, Molecular ; Cocaine/*pharmacology ; Dopamine/*metabolism ; Dopamine Plasma Membrane Transport Proteins ; Gene Expression ; HeLa Cells ; Humans ; Kinetics ; *Membrane Glycoproteins ; *Membrane Transport Proteins ; Molecular Sequence Data ; *Nerve Tissue Proteins ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction/methods ; Rats ; Sequence Homology, Nucleic Acid ; Transfection
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    A genetic model for interaction of the homeodomain recognition helix with DNA (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-01-25
    Description: The Bicoid homeodomain protein controls anterior development in the Drosophila embryo by binding to DNA and regulating gene expression. With the use of genetic assays in yeast, the interaction between the Bicoid homeodomain and a series of mutated DNA sites was studied. These experiments defined important features of homeodomain binding sites, identified specific amino acid-base pair contacts, and suggested a model for interaction of the recognition alpha-helices of Bicoid and Antennapedia-class homeodomain proteins with DNA. The model is in general agreement with results of crystallographic and magnetic resonance studies, but differs in important details. It is likely that genetic studies of protein-DNA interaction will continue to complement conventional structural approaches.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hanes, S D -- Brent, R -- New York, N.Y. -- Science. 1991 Jan 25;251(4992):426-30.〈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/1671176" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA/*metabolism ; DNA-Binding Proteins/*genetics/metabolism ; Drosophila ; Gene Expression Regulation ; Genes, Homeobox/*genetics ; *Homeodomain Proteins ; Insect Hormones/*genetics/metabolism ; *Models, Genetic ; Molecular Sequence Data ; *Trans-Activators ; Transcription, Genetic
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    Visualizing the higher order folding of a catalytic RNA molecule (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-01-25
    Description: The higher order folding process of the catalytic RNA derived from the self-splicing intron of Tetrahymena thermophila was monitored with the use of Fe(II)-EDTA-induced free radical chemistry. The overall tertiary structure of the RNA molecule forms cooperatively with the uptake of at least three magnesium ions. Local folding transitions display different metal ion dependencies, suggesting that the RNA tertiary structure assembles through a specific folding intermediate before the catalytic core is formed. Enzymatic activity, assayed with an RNA substrate that is complementary to the catalytic RNA active site, coincides with the cooperative structural transition. The higher order RNA foldings produced by Mg(II), Ca(II), and Sr(II) are similar; however, only the Mg(II)-stabilized RNA is catalytically active. Thus, these results directly demonstrate that divalent metal ions participate in general folding of the ribozyme tertiary structure, and further indicate a more specific involvement of Mg(II) in catalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Celander, D W -- Cech, T R -- New York, N.Y. -- Science. 1991 Jan 25;251(4992):401-7.〈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/1989074" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Calcium/metabolism ; Densitometry ; Kinetics ; Magnesium/metabolism ; Magnesium Chloride/pharmacology ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA, Catalytic/*chemistry/drug effects/metabolism ; Strontium/metabolism ; Tetrahymena
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    Resistance to ddI and sensitivity to AZT induced by a mutation in HIV-1 reverse transcriptase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-27
    Description: Serial human immunodeficiency virus type-1 (HIV-1) isolates were obtained from five individuals with acquired immunodeficiency syndrome (AIDS) who changed therapy to 2',3'-dideoxyinosine (ddI) after at least 12 months of treatment with 3'-azido-3'-deoxythymidine (zidovudine, AZT). The in vitro sensitivity to ddI decreased during the 12 months following ddI initiation, whereas AZT sensitivity increased. Analysis of the reverse transcriptase coding region revealed a mutation associated with reduced sensitivity to ddI. When this mutation was present in the same genome as a mutation known to confer AZT resistance, the isolates showed increased sensitivity to AZT. Analysis of HIV-1 variants confirmed that the ddI resistance mutation alone conferred ddI and 2',3'-dideoxycytidine resistance, and suppressed the effect of the AZT resistance mutation. The use of combination therapy for HIV-1 disease may prevent drug-resistant isolates from emerging.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉St Clair, M H -- Martin, J L -- Tudor-Williams, G -- Bach, M C -- Vavro, C L -- King, D M -- Kellam, P -- Kemp, S D -- Larder, B A -- New York, N.Y. -- Science. 1991 Sep 27;253(5027):1557-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Virology, Burroughs Wellcome Co., Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716788" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*drug therapy/microbiology ; Base Sequence ; DNA, Viral/*genetics ; Didanosine/*pharmacology/*therapeutic use ; Drug Resistance, Microbial ; Genotype ; HIV-1/*drug effects/enzymology/isolation & purification ; Humans ; Molecular Sequence Data ; *Mutation ; Oligodeoxyribonucleotides ; RNA-Directed DNA Polymerase/*genetics/metabolism ; Zidovudine/pharmacology/*therapeutic use
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    Exchange of conduction pathways between two related K+ channels (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-02-22
    Description: The structure of the ion conduction pathway or pore of voltage-gated ion channels is unknown, although the linker between the membrane spanning segments S5 and S6 has been suggested to form part of the pore in potassium channels. To test whether this region controls potassium channel conduction, a 21-amino acid segment of the S5-S6 linker was transplanted from the voltage-activated potassium channel NGK2 to another potassium channel DRK1, which has very different pore properties. In the resulting chimeric channel, the single channel conductance and blockade by external and internal tetraethylammonium (TEA) ion were characteristic of the donor NGK2 channel. Thus, this 21-amino acid segment controls the essential biophysical properties of the pore and may form the conduction pathway of these potassium channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hartmann, H A -- Kirsch, G E -- Drewe, J A -- Taglialatela, M -- Joho, R H -- Brown, A M -- NS08805/NS/NINDS NIH HHS/ -- NS23877/NS/NINDS NIH HHS/ -- NS28407/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 22;251(4996):942-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2000495" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/physiology ; Chimera ; Cloning, Molecular ; Female ; Ion Channel Gating ; Membrane Potentials ; Molecular Sequence Data ; Oligonucleotide Probes ; Oocytes/physiology ; Polymerase Chain Reaction ; Potassium Channels/drug effects/genetics/*physiology ; Rats ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; Tetraethylammonium ; Tetraethylammonium Compounds/pharmacology ; Xenopus
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    Interaction of the IL-2 receptor with the src-family kinase p56lck: identification of novel intermolecular association (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-14
    Description: In the interleukin-2 (IL-2) system, intracellular signal transduction is triggered by the beta chain of the IL-2 receptor (IL-2R beta); however, the responsible signaling mechanism remains unidentified. Evidence for the formation of a stable complex of IL-2R beta and the lymphocyte-specific protein tyrosine kinase p56lck is presented. Specific association sites were identified in the tyrosine kinase catalytic domain of p56lck and in the cytoplasmic domain of IL-2R beta. As a result of interaction, IL-2R beta became phosphorylated in vitro by p56lck. Treatment of T lymphocytes with IL-2 promotes p56lck kinase activity. These data suggest the participation of p56lck as a critical signaling molecule downstream of IL-2R via a novel interaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hatakeyama, M -- Kono, T -- Kobayashi, N -- Kawahara, A -- Levin, S D -- Perlmutter, R M -- Taniguchi, T -- New York, N.Y. -- Science. 1991 Jun 14;252(5012):1523-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular and Cellular Biology, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047859" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animals ; Antigens, CD/immunology ; Base Sequence ; Binding Sites ; Cell Division/drug effects ; Cell Line ; Humans ; Interleukin-2/pharmacology ; Killer Cells, Natural/cytology/drug effects/immunology ; Lymphocyte Activation ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) ; Lymphocytes/drug effects/*immunology ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Weight ; Oligonucleotide Probes ; Protein-Tyrosine Kinases/genetics/isolation & purification/*metabolism ; Receptors, Interleukin-2/genetics/isolation & purification/*physiology ; *Signal Transduction ; Transfection
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    Deregulation of a homeobox gene, HOX11, by the t(10;14) in T cell leukemia (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-05
    Description: Molecular cloning of the t(10;14)(q24;q11) recurrent breakpoint of T cell acute lymphoblastic leukemia has demonstrated a transcript for the candidate gene TCL3. Characterization of this gene from chromosome segment 10q24 revealed it to be a new homeobox, HOX11. The HOX11 homeodomain is most similar to that of the murine gene Hlx and possesses a markedly glycine-rich variable region and an acidic carboxyl terminus. HOX11, while expressed in liver, was not detected in normal thymus or T cells. This lineage-restricted homeobox gene is deregulated upon translocation into the T cell receptor locus where it may act as an oncogene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hatano, M -- Roberts, C W -- Minden, M -- Crist, W M -- Korsmeyer, S J -- 1 PO1 CA49712/CA/NCI NIH HHS/ -- CA 21765/CA/NCI NIH HHS/ -- CA 30969/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 5;253(5015):79-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, 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/1676542" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Chromosomes, Human, Pair 10 ; Chromosomes, Human, Pair 14 ; Cloning, Molecular ; *Gene Expression Regulation, Neoplastic ; *Genes, Homeobox ; Humans ; Leukemia-Lymphoma, Adult T-Cell/*genetics ; Mice ; Molecular Sequence Data ; Receptors, Antigen, T-Cell/genetics ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; *Translocation, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Selective activation of the B natriuretic peptide receptor by C-type natriuretic peptide (CNP) (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-04-05
    Description: The natriuretic peptides are hormones that can stimulate natriuretic, diuretic, and vasorelaxant activity in vivo, presumably through the activation of two known cell surface receptor guanylyl cyclases (ANPR-A and ANPR-B). Although atrial natriuretic peptide (ANP) and, to a lesser extent, brain natriuretic peptide (BNP) are efficient activators of the ANPR-A guanylyl cyclase, neither hormone can significantly stimulate ANPR-B. A member of this hormone family, C-type natriuretic peptide (CNP), potently and selectively activated the human ANPR-B guanylyl cyclase. CNP does not increase guanosine 3',5'-monophosphate accumulation in cells expressing human ANPR-A. The affinity of CNP for ANPR-B is 50- or 500-fold higher than ANP or BNP, respectively. This ligand-receptor pair may be involved in the regulation of fluid homeostasis by the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koller, K J -- Lowe, D G -- Bennett, G L -- Minamino, N -- Kangawa, K -- Matsuo, H -- Goeddel, D V -- New York, N.Y. -- Science. 1991 Apr 5;252(5002):120-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Genentech, Inc., South San Francisco 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1672777" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Atrial Natriuretic Factor/*physiology ; Cells, Cultured ; Cercopithecus aethiops ; Cloning, Molecular ; Dose-Response Relationship, Drug ; Guanylate Cyclase/metabolism ; Humans ; Natriuretic Peptide, Brain ; Natriuretic Peptide, C-Type ; Nerve Tissue Proteins/*pharmacology ; Receptors, Atrial Natriuretic Factor ; Receptors, Cell Surface/*physiology ; Recombinant Proteins ; Signal Transduction
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    Longitudinal studies of effects of divorce on children in Great Britain and the United States (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-07
    Description: National, longitudinal surveys from Great Britain and the United States were used to investigate the effects of divorce on children. In both studies, a subsample of children who were in two-parent families during the initial interview (at age 7 in the British data and at ages 7 to 11 in the U.S. data) were followed through the next interview (at age 11 and ages 11 to 16, respectively). At both time points in the British data, parents and teachers independently rated the children's behavior problems, and the children were given reading and mathematics achievement tests. At both time points in the U.S. data, parents rated the children's behavior problems. Children whose parents divorced or separated between the two time points were compared to children whose families remained intact. For boys, the apparent effect of separation or divorce on behavior problems and achievement at the later time point was sharply reduced by considering behavior problems, achievement levels, and family difficulties that were present at the earlier time point, before any of the families had broken up. For girls, the reduction in the apparent effect of divorce occurred to a lesser but still noticeable extent once preexisting conditions were considered.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cherlin, A J -- Furstenberg, F F Jr -- Chase-Lansdale, L -- Kiernan, K E -- Robins, P K -- Morrison, D R -- Teitler, J O -- HD25936/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 7;252(5011):1386-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Sociology, Johns Hopkins University, Baltimore, MD 21218.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047851" target="_blank"〉PubMed〈/a〉
    Keywords: Achievement ; Adolescent ; Child ; Child Behavior ; Divorce/*psychology ; England ; Female ; Humans ; Longitudinal Studies ; Male ; United States
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    Structural features that give rise to the unusual stability of RNA hairpins containing GNRA loops (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-12
    Description: The most frequently occurring RNA hairpins in 16S and 23S ribosomal RNA contain a tetranucleotide loop that has a GNRA consensus sequence. The solution structures of the GCAA and GAAA hairpins have been determined by nuclear magnetic resonance spectroscopy. Both loops contain an unusual G-A base pair between the first and last residue in the loop, a hydrogen bond between a G base and a phosphate, extensive base stacking, and a hydrogen bond between a sugar 2'-end OH and a base. These interactions explain the high stability of these hairpins and the sequence requirements for the variant and invariant nucleotides in the GNRA tetranucleotide loop family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heus, H A -- Pardi, A -- AI 27026/AI/NIAID NIH HHS/ -- AI 30726/AI/NIAID NIH HHS/ -- RR03283/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):191-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1712983" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Computer Graphics ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligoribonucleotides/chemistry ; RNA/chemistry/*ultrastructure ; Structure-Activity Relationship ; Thermodynamics
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    Name of the game? (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fox, C H -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1075.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1887232" target="_blank"〉PubMed〈/a〉
    Keywords: *Ethics, Professional ; Female ; Humans ; Laboratories/organization & administration ; Male ; Research Support as Topic ; Scientific Misconduct ; United States
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    Targets for dioxin: genes for plasminogen activator inhibitor-2 and interleukin-1 beta (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-18
    Description: Dioxin (2,3,7,8-tetrachlorodibenzo-p-dioxin, TCDD), a widespread environmental contaminant, may elicit its effects by altering gene expression in susceptible cells. Five TCDD-responsive complementary DNA clones were isolated from a human keratinocyte cell line. One of these clones encodes plasminogen activator inhibitor-2, a factor that influences growth and differentiation by regulating proteolysis of the extracellular matrix. Another encodes the cytokine interleukin-1 beta. Thus, TCDD alters the expression of growth regulatory genes and has effects similar to those of other tumor-promoting agents that affect both inflammation and differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sutter, T R -- Guzman, K -- Dold, K M -- Greenlee, W F -- New York, N.Y. -- Science. 1991 Oct 18;254(5030):415-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chemical Industry Institute of Toxicology, Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925598" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blood Physiological Phenomena ; Blotting, Northern ; Calcium/pharmacology ; Cell Line ; Cloning, Molecular ; Cycloheximide/pharmacology ; Gene Expression Regulation/drug effects ; Humans ; Interleukin-1/*genetics ; *Plasminogen Inactivators ; RNA, Messenger/drug effects ; Tetrachlorodibenzodioxin/*pharmacology ; Transcription, Genetic/drug effects
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    Fatal sibling aggression, precocial development, and androgens in neonatal spotted hyenas (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-03
    Description: Fatal neonatal sibling aggression is common in predatory birds but has not been previously reported in wild mammals. Spotted hyena females are strongly masculinized, both anatomically and behaviorally, apparently by high levels of androgens during ontogeny. Neonates display elevated androgen levels, precocial motor development, and fully erupted front teeth. Litters are usually twins, and siblings fight violently at birth, apparently leading to the death of one sibling in same-sex litters, whereas in mixed-sex litters both siblings usually survive.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frank, L G -- Glickman, S E -- Licht, P -- MH39917/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):702-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2024122" target="_blank"〉PubMed〈/a〉
    Keywords: Aggression/*physiology ; Androgens/*blood ; Animals ; Animals, Newborn/*physiology ; Behavior, Animal/*physiology ; Carnivora/*physiology ; Dentition ; Female ; Male ; Motor Activity/physiology ; *Sex Characteristics ; Sex Ratio ; Sibling Relations ; Tooth Eruption/physiology
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    Multiple representations of pain in human cerebral cortex (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-15
    Description: The representation of pain in the cerebral cortex is less well understood than that of any other sensory system. However, with the use of magnetic resonance imaging and positron emission tomography in humans, it has now been demonstrated that painful heat causes significant activation of the contralateral anterior cingulate, secondary somatosensory, and primary somatosensory cortices. This contrasts with the predominant activation of primary somatosensory cortex caused by vibrotactile stimuli in similar experiments. Furthermore, the unilateral cingulate activation indicates that this forebrain area, thought to regulate emotions, contains an unexpectedly specific representation of pain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Talbot, J D -- Marrett, S -- Evans, A C -- Meyer, E -- Bushnell, M C -- Duncan, G H -- New York, N.Y. -- Science. 1991 Mar 15;251(4999):1355-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de neurophysiologie comportementale, Faculte de medecine dentaire, Universite de Montreal, Quebec, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2003220" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animals ; Anxiety/physiopathology ; Brain Mapping ; Cerebral Cortex/*physiology ; Functional Laterality ; Hot Temperature ; Humans ; Magnetic Resonance Imaging ; Male ; Pain/*physiopathology ; Tomography, Emission-Computed
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    Mapping of DNA instability at the fragile X to a trinucleotide repeat sequence p(CCG)n (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-21
    Description: The sequence of a Pst I restriction fragment was determined that demonstrate instability in fragile X syndrome pedigrees. The region of instability was localized to a trinucleotide repeat p(CCG)n. The sequence flanking this repeat were identical in normal and affected individuals. The breakpoints in two somatic cell hybrids constructed to break at the fragile site also mapped to this repeat sequence. The repeat exhibits instability both when cloned in a nonhomologous host and after amplification by the polymerase chain reaction. These results suggest variation in the trinucleotide repeat copy number as the molecular basis for the instability and possibly the fragile site. This would account for the observed properties of this region in vivo and in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kremer, E J -- Pritchard, M -- Lynch, M -- Yu, S -- Holman, K -- Baker, E -- Warren, S T -- Schlessinger, D -- Sutherland, G R -- Richards, R I -- New York, N.Y. -- Science. 1991 Jun 21;252(5013):1711-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cytogenetics and Molecular Genetics, Adelaide Children's Hospital, South Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1675488" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blotting, Southern ; Chromosome Mapping ; Fragile X Syndrome/*genetics ; Humans ; Molecular Sequence Data ; Pedigree ; Polymerase Chain Reaction ; Polymorphism, Restriction Fragment Length ; Repetitive Sequences, Nucleic Acid ; Restriction Mapping ; X Chromosome/ultrastructure
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    HRR25, a putative protein kinase from budding yeast: association with repair of damaged DNA (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-30
    Description: In simple eukaryotes, protein kinases regulate mitotic and meiotic cell cycles, the response to polypeptide pheromones, and the initiation of nuclear DNA synthesis. The protein HRR25 from the budding yeast Saccharomyces cerevisiae was defined by the mutation hrr25-1. This mutation resulted in sensitivity to continuous expression of the HO double-strand endonuclease, to methyl methanesulfonate, and to x-irradiation. Homozygotes of hrr25-1 were unable to sporulate and disruption and deletion of HRR25 interfered with mitotic and meiotic cell division. Sequence analysis revealed two distinctive regions in the protein. The NH2-terminus of HRR25 contains the hallmark features of protein kinases, whereas the COOH-terminus is rich in proline and glutamine. Mutations in HRR25 at conserved residues found in all protein kinases inactivated the gene, and these mutants exhibited the hrr25 null phenotypes. Taken together, the hrr25 mutant phenotypes and the features of the gene product indicate that HRR25 is a distinctive member of the protein kinase superfamily.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoekstra, M F -- Liskay, R M -- Ou, A C -- DeMaggio, A J -- Burbee, D G -- Heffron, F -- New York, N.Y. -- Science. 1991 Aug 30;253(5023):1031-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology and Virology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92186.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1887218" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Casein Kinase I ; *DNA Damage ; *DNA Repair ; Fungal Proteins/*genetics/metabolism ; Gene Library ; Genes, Fungal ; Meiosis ; Methyl Methanesulfonate/pharmacology ; Molecular Sequence Data ; Mutagenesis, Insertional ; Mutagenesis, Site-Directed ; Oligonucleotide Probes ; Phenotype ; *Protein Kinases ; Restriction Mapping ; Saccharomyces cerevisiae/enzymology/*genetics/physiology ; *Saccharomyces cerevisiae Proteins ; Sequence Homology, Nucleic Acid
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Biology and homosexuality (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1991 Nov 1;254(5032):630.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948038" target="_blank"〉PubMed〈/a〉
    Keywords: Brain/*physiology ; Female ; *Homosexuality ; Humans ; Male ; Sexual Behavior/*physiology
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    Control of alternative splicing by the differential binding of U1 small nuclear ribonucleoprotein particle (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-01
    Description: Cellular factors controlling alternative splicing of precursor messenger RNA are largely unknown, even though this process plays a central role in specifying the diversity of proteins in the eukaryotic cell. For the identification of such factors, a segment of the rat preprotachykinin gene was used in which differential expression of neuropeptides gamma and K is dependent on alternative splicing of the fourth exon (E4). Sequence variants of the three-exon segment, (E3-E4-E5) were created, resulting in a sensitive assay for factors mediating the splicing switch between E4-skipping and E4-inclusion. A dinucleotide mutation in the 5' splice site of E4 that increase base-pairing of this site to U1 small nuclear RNA resulted in uniform selection of E4, whereas a control mutation that destroyed base-pairing resulted in uniform E4-skipping. Affinity selection of spliceosomes formed on these functionally distinct substrates revealed that the extreme difference in splicing was mediated by differential binding of the U1 small nuclear ribonucleoprotein particle (snRNP) to the 5' splice site of E4. These data show that, apart from its established role in selecting 5' splice sites, U1 snRNP plays a fundamental role in 3' exon selection and provides insight into possible mechanisms of alternative splicing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuo, H C -- Nasim, F H -- Grabowski, P J -- GM-39695/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 1;251(4997):1045-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Biochemistry, Brown University, Providence, RI 02912.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1825520" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA Mutational Analysis ; Exons ; Hydrogen Bonding ; Macromolecular Substances ; Molecular Sequence Data ; Protein Precursors/*genetics ; *RNA Splicing ; RNA, Messenger/*metabolism ; RNA, Small Nuclear/*physiology ; Rats ; Ribonucleoproteins/chemistry/*physiology ; Ribonucleoproteins, Small Nuclear ; Structure-Activity Relationship ; Tachykinins/*genetics
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    Translational potentiation of messenger RNA with secondary structure in Xenopus (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-02-15
    Description: Differential translation of messenger RNA (mRNA) with stable secondary structure in the 5' untranslated leader may contribute to the dramatic changes in protein synthetic patterns that occur during oogenesis and early development. Plasmids that contained the bacterial gene chloramphenicol acetyltransferase and which encoded mRNA with (hpCAT) or without (CAT) a stable hairpin secondary structure in the 5' noncoding region were transcribed in vitro, and the resulting mRNAs were injected into Xenopus oocytes, eggs, and early embryos. During early oogenesis, hpCAT mRNA was translated at less than 3 percent of the efficiency of CAT mRNA. The relative translational potential of hpCAT reached 100 percent in the newly fertilized egg and returned to approximately 3 percent after the midblastula transition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fu, L N -- Ye, R Q -- Browder, L W -- Johnston, R N -- New York, N.Y. -- Science. 1991 Feb 15;251(4995):807-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Calgary, Alberta, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1990443" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chloramphenicol O-Acetyltransferase/genetics ; Egg Proteins/biosynthesis/genetics ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oogenesis/genetics ; Plasmids ; *Protein Biosynthesis ; RNA, Messenger/*genetics ; Xenopus laevis/embryology/*genetics
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    Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-26
    Description: Malignant hyperthermia (MH) causes neurological, liver, and kidney damage and death in humans and major economic losses in the swine industry. A single point mutation in the porcine gene for the skeletal muscle ryanodine receptor (ryr1) was found to be correlated with MH in five major breeds of lean, heavily muscled swine. Haplotyping suggests that the mutation in all five breeds has a common origin. Assuming that this is the causal mutation for MH, the development of a noninvasive diagnostic test will provide the basis for elimination of the MH gene or its controlled inclusion in swine breeding programs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fujii, J -- Otsu, K -- Zorzato, F -- de Leon, S -- Khanna, V K -- Weiler, J E -- O'Brien, P J -- MacLennan, D H -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):448-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1862346" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Codon/genetics ; Haplotypes ; Malignant Hyperthermia/genetics/*veterinary ; Molecular Sequence Data ; *Mutation ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Receptors, Cholinergic/*genetics ; Restriction Mapping ; Ryanodine/metabolism ; Ryanodine Receptor Calcium Release Channel ; Species Specificity ; Swine ; Swine Diseases/*genetics
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    Cloning of a factor required for activity of the Ah (dioxin) receptor (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-05-17
    Description: The aryl hydrocarbon (Ah) receptor binds various environmental pollutants, such as polycyclic aromatic hydrocarbons, heterocyclic amines, and polychlorinated aromatic compounds (dioxins, dibenzofurans, and biphenyls), and mediates the carcinogenic effects of these agents. The complementary DNA and part of the gene for an 87-kilodalton human protein that is necessary for Ah receptor function have been cloned. The protein is not the ligand-binding subunit of the receptor but is a factor that is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after binding ligand. The requirement for this factor distinguishes the Ah receptor from the glucocorticoid receptor, to which the Ah receptor has been presumed to be similar. Two portions of the 87-kilodalton protein share sequence similarities with two Drosophila proteins, Per and Sim. Another segment of the protein shows conformity to the consensus sequence for the basic helix-loop-helix motif found in proteins that bind DNA as homodimers or heterodimers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, E C -- Reyes, H -- Chu, F F -- Sander, F -- Conley, L H -- Brooks, B A -- Hankinson, O -- CA 16048/CA/NCI NIH HHS/ -- CA 28868/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 17;252(5008):954-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1852076" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aryl Hydrocarbon Receptor Nuclear Translocator ; Base Sequence ; Cell Line ; Cell Nucleus/metabolism ; Cloning, Molecular ; Cytosol/metabolism ; *DNA-Binding Proteins ; Humans ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Weight ; Oligonucleotide Probes ; Proteins/*genetics/metabolism ; RNA, Messenger/genetics ; Receptors, Aryl Hydrocarbon ; Receptors, Drug/genetics/*metabolism ; Sequence Homology, Nucleic Acid ; Tetrachlorodibenzodioxin/*metabolism ; *Transcription Factors ; Transfection
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    Specific DNA binding by c-Myb: evidence for a double helix-turn-helix-related motif (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-09-06
    Description: The c-Myb protein is a sequence-specific DNA binding protein that activates transcription in hematopoietic cells. Three imperfect repeats (R1, R2, and R3) that contain regularly spaced tryptophan residues form the DNA binding domain of c-Myb. A fragment of c-Myb that contained the R2 and R3 regions bound specifically to a DNA sequence recognized by c-Myb plus ten additional base pairs at the 3' end of the element. The R2R3 fragment was predicted to contain two consecutive helix-turn-helix (HTH) motifs with unconventional turns. Mutagenesis of amino acids in R2R3 at positions that correspond to DNA-contacting amino acids in other HTH-containing proteins abolished specific DNA binding without affecting nonspecific DNA interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabrielsen, O S -- Sentenac, A -- Fromageot, P -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1140-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire d'Ingenierie des Proteines, Centre d'Etudes de Saclay, Gif-sur-Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1887237" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Chickens ; DNA/*metabolism ; DNA-Binding Proteins/*metabolism ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligonucleotide Probes ; Oncogenes ; Polymerase Chain Reaction ; Protein Conformation ; Proto-Oncogene Proteins/genetics/*metabolism ; Proto-Oncogene Proteins c-myb ; Recombinant Proteins/metabolism ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; Transcription Factors/*metabolism
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    Another sex survey bites the dust (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moffat, A S -- New York, N.Y. -- Science. 1991 Sep 27;253(5027):1483.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1896855" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/prevention & control ; Adolescent ; Adult ; Female ; *Health Surveys ; Humans ; Male ; National Institutes of Health (U.S.) ; *Sexual Behavior ; Sexually Transmitted Diseases/prevention & control ; United States
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    GRAIL seeks out genes buried in DNA sequence (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):805.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948063" target="_blank"〉PubMed〈/a〉
    Keywords: *Artificial Intelligence ; Base Sequence ; DNA/*genetics ; *Genes ; *Genome, Human ; Humans ; Molecular Sequence Data ; Software
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    Triplex DNA finally comes of age (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-06-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moffat, A S -- New York, N.Y. -- Science. 1991 Jun 7;252(5011):1374-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047850" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/*chemistry ; DNA Replication ; Genes, myc ; Models, Molecular ; Molecular Sequence Data ; Transcription, Genetic/drug effects
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    Maintenance of normoglycemia in diabetic mice by subcutaneous xenografts of encapsulated islets (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-20
    Description: The goal of islet transplantation in human diabetes is to maintain the islet grafts in the recipients without the use of immunosuppression. One approach is to encapsulate the donor islets in permselective membranes. Hollow fibers fabricated from an acrylic copolymer were used to encapsulate small numbers of rat islets that were immobilized in an alginate hydrogel for transplantation in diabetic mice. The fibers were biocompatible, prevented rejection, and maintained normoglycemia when transplanted intraperitoneally; hyperglycemia returned when the fibers were removed at 60 days. Normoglycemia was also maintained by subcutaneous implants that had an appropriately constructed outer surface on the fibers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lacy, P E -- Hegre, O D -- Gerasimidi-Vazeou, A -- Gentile, F T -- Dionne, K E -- DK01226/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1782-4.〈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/1763328" target="_blank"〉PubMed〈/a〉
    Keywords: *Acrylic Resins ; Animals ; Animals, Newborn ; Blood Glucose/*metabolism ; Diabetes Mellitus, Experimental/blood/*surgery ; In Vitro Techniques ; Insulin/secretion ; Islets of Langerhans/*secretion ; Islets of Langerhans Transplantation/*physiology ; Male ; Membranes, Artificial ; Mice ; Mice, Inbred C57BL ; *Polyvinyl Chloride ; Rats ; Rats, Inbred WF ; Time Factors ; Transplantation, Heterologous
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    Phosphorylation of c-Src on tyrosine 527 by another protein tyrosine kinase (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-10-25
    Description: The protein tyrosine kinase activity of the cellular Src protein is negatively regulated by phosphorylation at tyrosine residue 527 (Tyr527). It has not been established whether this regulatory modification of Src is mediated by autophosphorylation or by another cellular protein kinase. The phosphorylation of a modified form of c-Src that lacks kinase activity was examined in mouse cells that do not express endogenous Src (because of the targeted disruption of both src alleles). Phosphorylation of the inactive form of Src on Tyr527 occurred to a similar extent in cells lacking endogenous Src as it did in cells expressing Src. Therefore, Tyr527 phosphorylation, and thus negative control of Src kinase activity, is mediated by another cellular protein tyrosine kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thomas, J E -- Soriano, P -- Brugge, J S -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):568-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1719633" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cells, Cultured ; Cyanogen Bromide ; Embryo, Mammalian ; Mice ; Peptide Mapping ; Phosphopeptides/isolation & purification ; Phosphorylation ; Protein-Tyrosine Kinases ; Proto-Oncogene Proteins pp60(c-src)/*metabolism ; *Tyrosine
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    Regulation of the apolipoprotein AI gene by ARP-1, a novel member of the steroid receptor superfamily (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-02-01
    Description: Apolipoprotein AI (apoAI) is a lipid-binding protein that participates in the transport of cholesterol and other lipids in the plasma. A complementary DNA clone for a protein that bound to regulatory elements of the apoAI gene was isolated. This protein, designated apoAI regulatory protein-1 (ARP-1), is a novel member of the steroid hormone receptor superfamily. ARP-1 bound to DNA as a dimer, and its dimerization domain was localized to the COOH-terminal region. ARP-1 also bound to a thyroid hormone-responsive element and to regulatory regions of the apoB, apoCIII, insulin, and ovalbumin genes. In cotransfection experiments, ARP-1 downregulated the apoAI gene. The involvement of ARP-1 in the regulation of apoAI gene expression suggests that it may participate in lipid metabolism and cholesterol homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ladias, J A -- Karathanasis, S K -- New York, N.Y. -- Science. 1991 Feb 1;251(4993):561-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cardiology, Children's Hospital, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1899293" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Apolipoprotein A-I ; Apolipoproteins A/*genetics ; Base Sequence ; COUP Transcription Factor II ; COUP Transcription Factors ; Cloning, Molecular ; DNA/metabolism ; DNA-Binding Proteins/*metabolism ; Gene Expression Regulation ; Humans ; Lipoproteins, HDL/*genetics ; Molecular Sequence Data ; Oligonucleotide Probes ; Receptors, Steroid/*metabolism ; Regulatory Sequences, Nucleic Acid ; *Transcription Factors
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    Characterization of a human TAR RNA-binding protein that activates the HIV-1 LTR (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-29
    Description: Human immunodeficiency virus type 1 (HIV-1) gene expression is activated by Tat, a virally encoded protein. Tat trans-activation requires viral (trans-activation--responsive; TAR) RNA sequences located in the R region of the long terminal repeat (LTR). Existing evidence suggests that Tat probably cooperates with cellular factors that bind to TAR RNA in the overall trans-activation process. A HeLa complementary DNA was isolated and characterized that encodes a TAR RNA-binding protein (TRBP). TRBP activated the HIV-1 LTR and was synergistic with Tat function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gatignol, A -- Buckler-White, A -- Berkhout, B -- Jeang, K T -- New York, N.Y. -- Science. 1991 Mar 29;251(5001):1597-600.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Microbiology, National Institute of 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/2011739" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Carrier Proteins/*genetics ; Endoribonucleases/genetics ; Escherichia coli/enzymology ; *Escherichia coli Proteins ; Gene Products, tat/metabolism ; *HIV Long Terminal Repeat ; HIV-1/*genetics ; Humans ; Molecular Sequence Data ; Nucleic Acid Conformation ; Plasmids ; RNA, Viral/genetics ; *RNA-Binding Proteins ; Ribonuclease III ; Sequence Homology, Nucleic Acid ; tat Gene Products, Human Immunodeficiency Virus
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    Convergence of Ets- and notch-related structural motifs in a heteromeric DNA binding complex (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-16
    Description: Analysis of the heteromeric DNA binding protein GABP has revealed the interaction of two distinct peptide sequence motifs normally associated with proteins located in different cellular compartments. The alpha subunit of GABP contains an 85-amino acid segment related to the Ets family of DNA binding proteins. The ETS domain of GABP alpha facilitates weak binding to DNA and, together with an adjacent segment of 37 amino acids, mediates stable interaction with GABP beta. The beta subunit of GABP contains four imperfect repeats of a sequence present in several transmembrane proteins including the product of the Notch gene of Drosophila melanogaster. These amino-terminal repeats of GABP beta mediate stable interaction with GABP alpha and, when complexed with GABP alpha, directly contact DNA. These observations provide evidence for a distinct biochemical role for the 33-amino acid repeats, and suggest that they may serve as a module for the generation of specific dimerization interfaces.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thompson, C C -- Brown, T A -- McKnight, S L -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):762-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Research Laboratories, Carnegie Institution of Washington, Department of Embryology, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1876833" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cross-Linking Reagents ; DNA/metabolism ; DNA-Binding Proteins/*chemistry/metabolism ; GA-Binding Protein Transcription Factor ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Weight ; Multigene Family ; Nuclear Proteins/*chemistry/metabolism ; Oligonucleotides/chemistry ; Proto-Oncogene Proteins/chemistry ; Proto-Oncogene Proteins c-ets ; Rats ; Recombinant Proteins ; Structure-Activity Relationship ; Transcription Factors/*chemistry/metabolism
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    Cell-free, de novo synthesis of poliovirus (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-13
    Description: Cell-free translation of poliovirus RNA in an extract of uninfected human (HeLa) cells yielded viral proteins through proteolysis of the polyprotein. In the extract, newly synthesized proteins catalyzed poliovirus-specific RNA synthesis, and formed infectious poliovirus de novo. Newly formed virions were neutralized by type-specific antiserum, and infection of human cells with them was prevented by poliovirus receptor-specific antibodies. Poliovirus synthesis was increased nearly 70-fold when nucleoside triphosphates were added, but it was abolished in the presence of inhibitors of translation or viral genome replication. The ability to conduct cell-free synthesis of poliovirus will aid in the study of picornavirus proliferation and in the search for the control of picornaviral disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Molla, A -- Paul, A V -- Wimmer, E -- AI-15122/AI/NIAID NIH HHS/ -- CA-28146/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1647-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, School of Medicine, 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/1661029" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell-Free System ; HeLa Cells ; Humans ; In Vitro Techniques ; Molecular Sequence Data ; Molecular Weight ; Oligodeoxyribonucleotides/chemistry ; Poliovirus/*growth & development ; Polymerase Chain Reaction ; RNA, Viral/analysis/biosynthesis ; Time Factors ; Viral Proteins/biosynthesis/chemistry ; *Virus Replication
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    New role found for a common protein "motif" (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, M -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):742.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1831563" target="_blank"〉PubMed〈/a〉
    Keywords: Ankyrins ; Base Sequence ; Binding Sites ; Blood Proteins/*chemistry ; Membrane Proteins/*chemistry ; Molecular Sequence Data ; *Protein Binding ; Structure-Activity Relationship ; Transcription Factors/chemistry
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 83
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    Stimulation of protein tyrosine phosphorylation by NMDA receptor activation (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-23
    Description: The N-methyl-D-aspartate (NMDA) receptor, a subtype of glutamate receptors, plays a key role in synaptic plasticity in the nervous system. After NMDA receptor activation, calcium entry into the postsynaptic neuron is a critical initial event. However, the subsequent mechanisms by which the NMDA receptor signal is processed are incompletely understood. Stimulation of cultured rat hippocampal cells with glutamate resulted in the rapid and transient tyrosine phosphorylation of a 39-kilodalton protein (p39). Tyrosine phosphorylation of p39 was triggered by the NMDA receptor and required an influx of Ca2+ from the extracellular medium. Because p39 was found to be highly related or identical to the microtubule-associated protein 2 kinase, the NMDA receptor signal may be processed by a sequential activation of protein kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bading, H -- Greenberg, M E -- CA 43855/CA/NCI NIH HHS/ -- NS 28829/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):912-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1715095" target="_blank"〉PubMed〈/a〉
    Keywords: 2-Amino-5-phosphonovalerate/pharmacology ; Animals ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases ; Cells, Cultured ; Glutamates/pharmacology ; Glutamic Acid ; Hippocampus/drug effects/metabolism ; Immunoblotting ; Kinetics ; Phosphoproteins/*metabolism ; Phosphorylation ; Phosphotyrosine ; Protein Kinases/metabolism ; Rats ; Receptors, N-Methyl-D-Aspartate/*metabolism ; Tyrosine/*analogs & derivatives/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 84
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    Unraveling the genetics of fragile X syndrome (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, M -- New York, N.Y. -- Science. 1991 May 24;252(5009):1070.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2031180" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Chromosome Mapping ; Female ; Fragile X Syndrome/*genetics ; Humans ; Male ; *Mutation ; X Chromosome
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 85
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    Finding DNA sequencing errors (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1991 May 31;252(5010):1255-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925537" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Dna ; Databases, Factual/*standards ; Humans ; National Library of Medicine (U.S.) ; Software ; United States
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 86
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    Oligoclonal expansion and CD1 recognition by human intestinal intraepithelial lymphocytes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-20
    Description: A human intestinal intraepithelial lymphocyte (IEL) T cell line was established from jejunum to characterize the structure and function of the alpha beta T cell antigen receptors (TCRs) expressed by this population. Single-sided polymerase chain reaction (PCR) amplification cloning and quantitative PCR amplification of the TCR chains from the cell line and from fresh IELs demonstrated that IELs were oligoclonal. The IEL T cell line exhibited CD1-specific cytotoxicity and a dominant IEL T cell clone was CD1c-specific. Thus, human jejunal intraepithelial lymphocytes are oligoclonal and recognize members of the CD1 gene family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balk, S P -- Ebert, E C -- Blumenthal, R L -- McDermott, F V -- Wucherpfennig, K W -- Landau, S B -- Blumberg, R S -- 5 KO8 DK01886/DK/NIDDK NIH HHS/ -- CA-01310/CA/NCI NIH HHS/ -- DK42166/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 20;253(5026):1411-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hematology-Oncology Division, Beth Israel Hospital, Harvard Medical School, Boston, MA 02215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716785" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, CD/*genetics/immunology ; Antigens, CD1 ; Base Sequence ; Cell Line ; Clone Cells ; Epithelium/physiology ; Humans ; Jejunum/immunology ; Molecular Sequence Data ; Oligonucleotide Probes ; Polymerase Chain Reaction/methods ; Receptors, Antigen, T-Cell/*genetics ; T-Lymphocytes/*immunology
    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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  • 87
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    Three-dimensional readout of flash x-ray images of living sperm in water by atomic-force microscopy (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-03
    Description: The imaging of living specimens in water by x-ray microscopy can be greatly enhanced with the use of an intense flash x-ray source and sophisticated technologies for reading x-ray images. A subnanosecond [corrected] x-ray pulse from a laser-produced plasma was used to record the x-ray image of living sea urchin sperm in an x-ray resist. The resist relief was visualized at high resolution by atomic-force microscopy. Internal structure of the sperm head was evident, and the carbon density in a flagellum was estimated from the relief height.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomie, T -- Shimizu, H -- Majima, T -- Yamada, M -- Kanayama, T -- Kondo, H -- Yano, M -- Ono, M -- New York, N.Y. -- Science. 1991 May 3;252(5006):691-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Electrotechnical Laboratory, Ibaraki, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2024121" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/ultrastructure ; Male ; Methylmethacrylates ; Microscopy/*methods ; Mitochondria/ultrastructure ; *Sea Urchins ; Seawater ; Sperm Tail/*ultrastructure ; X-Rays
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  • 88
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    Inhibition of morphine tolerance and dependence by the NMDA receptor antagonist MK-801 (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-01-04
    Description: The N-methyl-D-aspartate (NMDA) subtype of the glutamate receptor is an important mediator of several forms of neural and behavioral plasticity. The present studies examined whether NMDA receptors might be involved in the development of opiate tolerance and dependence, two examples of behavioral plasticity. The noncompetitive NMDA receptor antagonist MK-801 attenuated the development of tolerance to the analgesic effect of morphine without affecting acute morphine analgesia. In addition, MK-801 attenuated the development of morphine dependence as assessed by naloxone-precipitated withdrawal. These results suggest that NMDA receptors may be important in the development of opiate tolerance and dependence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trujillo, K A -- Akil, H -- DA02265/DA/NIDA NIH HHS/ -- DA05336/DA/NIDA NIH HHS/ -- MH422251/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1991 Jan 4;251(4989):85-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mental Health Research Institute, University of Michigan, Ann Arbor 48109-0720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1824728" target="_blank"〉PubMed〈/a〉
    Keywords: *Analgesia ; Animals ; Behavior, Animal/drug effects ; Dizocilpine Maleate/*pharmacology ; Drug Tolerance ; Male ; *Morphine ; Naloxone/pharmacology ; Pain Measurement ; Rats ; Rats, Inbred Strains ; Receptors, N-Methyl-D-Aspartate/antagonists & inhibitors/*physiology ; *Substance-Related Disorders
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 89
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    Conserved sequence and structural elements in the HIV-1 principal neutralizing determinant: corrections and clarifications (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-02-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉LaRosa, G J -- Davide, J P -- Weinhold, K -- Waterbury, J A -- Profy, A T -- Lewis, J A -- Langlois, A J -- Dreesman, G R -- Boswell, R N -- Shadduck, P -- New York, N.Y. -- Science. 1991 Feb 15;251(4995):811.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1990444" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; HIV-1/*genetics ; Molecular Sequence Data
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 90
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    FTZ-F1, a steroid hormone receptor-like protein implicated in the activation of fushi tarazu (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-10
    Description: The Drosophila homeobox segmentation gene fushi tarazu (ftz) is expressed in a seven-stripe pattern during early embryogenesis. This characteristic pattern is largely specified by the zebra element located immediately upstream of the ftz transcriptional start site. The FTZ-F1 protein, one of multiple DNA binding factors that interacts with the zebra element, is implicated in the activation of ftz transcription, especially in stripes 1, 2, 3, and 6. An FTZ-F1 complementary DNA has been cloned by recognition site screening of a Drosophila expression library. The identity of the FTZ-F1 complementary DNA clone was confirmed by immunological cross-reaction with antibodies to FTZ-F1 and by sequence analysis of peptides from purified FTZ-F1 protein. The predicted amino acid sequence of FTZ-F1 revealed that the protein is a member of the nuclear hormone receptor superfamily. This finding raises the possibility that a hormonal ligand affects the expression of a homeobox segmentation gene early in embryonic development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lavorgna, G -- Ueda, H -- Clos, J -- Wu, C -- New York, N.Y. -- Science. 1991 May 10;252(5007):848-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry, National Cancer 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/1709303" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Blotting, Southern ; Blotting, Western ; Chromosome Mapping ; Cloning, Molecular ; Drosophila Proteins ; Drosophila melanogaster ; Fushi Tarazu Transcription Factors ; Gene Expression Regulation ; Genes, Homeobox ; *Homeodomain Proteins ; Insect Hormones/*chemistry ; Molecular Sequence Data ; Open Reading Frames ; RNA/analysis ; Receptors, Steroid/genetics ; Sequence Homology, Nucleic Acid ; Transcription, Genetic ; Zinc Fingers
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  • 91
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    The brain as "sexual organ" (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, A -- New York, N.Y. -- Science. 1991 Aug 30;253(5023):957-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1887226" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*anatomy & histology/physiology ; Corpus Callosum/anatomy & histology/physiology ; Female ; Humans ; Hypothalamus/*anatomy & histology/physiology ; Male ; Rats ; *Sex Characteristics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 92
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    A difference in hypothalamic structure between heterosexual and homosexual men (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-30
    Description: The anterior hypothalamus of the brain participates in the regulation of male-typical sexual behavior. The volumes of four cell groups in this region [interstitial nuclei of the anterior hypothalamus (INAH) 1, 2, 3, and 4] were measured in postmortem tissue from three subject groups: women, men who were presumed to be heterosexual, and homosexual men. No differences were found between the groups in the volumes of INAH 1, 2, or 4. As has been reported previously, INAH 3 was more than twice as large in the heterosexual men as in the women. It was also, however, more than twice as large in the heterosexual men as in the homosexual men. This finding indicates that INAH is dimorphic with sexual orientation, at least in men, and suggests that sexual orientation has a biological substrate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉LeVay, S -- New York, N.Y. -- Science. 1991 Aug 30;253(5023):1034-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Salk Institute for Biological Studies, San Diego, CA 92186.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1887219" target="_blank"〉PubMed〈/a〉
    Keywords: Anterior Hypothalamic Nucleus/*anatomy & histology/cytology ; Female ; *Homosexuality ; Humans ; Male ; Optic Chiasm/anatomy & histology ; Sexual Behavior/*physiology
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  • 93
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    Dynamic tracking of cardiac vulnerability by complex demodulation of the T wave (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-04-19
    Description: A link is found between T wave alternans and vulnerability to ventricular fibrillation, and a new approach is provided for quantification of susceptibility to malignant arrhythmias. Complex demodulation reveals that alternation of the electrocardiogram is concentrated during the first half of the T wave, coinciding with the vulnerable period of the cardiac cycle. During myocardial ischemia and reperfusion, there are marked increases in the degree of T wave alternans that parallel the established time course of changes in vulnerability. The influence of the sympathetic nervous system in arrhythmogenesis is also accurately detected. Ultimately, complex demodulation of the electrocardiogram could provide a technique for identification and management of individuals at risk for sudden cardiac death.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nearing, B D -- Huang, A H -- Verrier, R L -- HL-33567/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Apr 19;252(5004):437-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Georgetown University School of Medicine, Washington, DC 20007.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2017682" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Constriction ; Coronary Vessels ; Dogs ; Electric Stimulation ; *Electrocardiography ; Electrophysiology ; Female ; Heart Conduction System/*physiopathology ; Kinetics ; Male ; Mathematics ; Reperfusion ; Ventricular Fibrillation/*physiopathology
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  • 94
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    Tissue-specific splicing in vivo of the beta-tropomyosin gene: dependence on an RNA secondary structure (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-28
    Description: The beta-tropomyosin gene in chicken contains two mutually exclusive exons (exons 6A and 6B) which are used by the splicing apparatus in myogenic cells, respectively, before (myoblast stage) and after (myotube stage) differentiation. The myoblast splicing pattern is shown to depend on multiple sequence elements that are located in the upstream intron and in the exon 6B and that exert a negative control over exon 6B splicing. This regulation of splicing is due, at least in part, to a secondary structure of the primary transcript, which limits in vivo the accessibility of exon 6B in myoblasts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Libri, D -- Piseri, A -- Fiszman, M Y -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1842-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut Pasteur, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2063196" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chickens ; Exons ; Introns ; Models, Molecular ; Molecular Sequence Data ; Muscles/physiology ; Mutagenesis, Site-Directed ; Nucleic Acid Conformation ; RNA Precursors/*genetics ; *RNA Splicing ; RNA, Messenger/*genetics ; Transcription, Genetic ; Tropomyosin/*genetics
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  • 95
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    Is homosexuality biological? (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1991 Aug 30;253(5023):956-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1887225" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; *Homosexuality ; Humans ; Hypothalamus/cytology/*physiology ; Male ; Sex Characteristics ; Sexual Behavior/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 96
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    Functional contribution of neuronal AChR subunits revealed by antisense oligonucleotides (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-06
    Description: Although multiple related genes encoding nicotinic acetylcholine receptor (AChR) subunits have been identified, how each of these subunits contributes to AChRs in neurons is not known. Sympathetic neurons express four classes of AChR channels and six AChR subunit genes (alpha 3, alpha 4, alpha 5, alpha 7, beta 2, and beta 4). The contribution of individual subunits to AChR channel subtypes in these neurons was examined by selective deletion with antisense oligonucleotides. An alpha 3 antisense oligonucleotide decreased the number and altered the properties of the normally expressed ACh-activated channels. The remaining AChR channels have distinct biophysical and pharmacological properties that indicate an important functional contribution of the alpha 7 subunit.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2366811/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2366811/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Listerud, M -- Brussaard, A B -- Devay, P -- Colman, D R -- Role, L W -- NS 29071/NS/NINDS NIH HHS/ -- NS27680/NS/NINDS NIH HHS/ -- R01 NS029071/NS/NINDS NIH HHS/ -- R01 NS029071-09/NS/NINDS NIH HHS/ -- R01 NS029071-10/NS/NINDS NIH HHS/ -- R01 NS029071-11/NS/NINDS NIH HHS/ -- R01 NS029071-12/NS/NINDS NIH HHS/ -- R01 NS029071-13/NS/NINDS NIH HHS/ -- R01 NS029071-13S1/NS/NINDS NIH HHS/ -- R01 NS029071-14/NS/NINDS NIH HHS/ -- R01 NS029071-15/NS/NINDS NIH HHS/ -- R01 NS029071-16/NS/NINDS NIH HHS/ -- R01 NS029071-17/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1518-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Cell Biology, Columbia College of Physicians and Surgeons, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1720573" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Bungarotoxins/pharmacology ; Chick Embryo ; Gene Expression ; Ion Channel Gating ; Ion Channels/*physiology ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacology ; Polymerase Chain Reaction ; RNA, Messenger/genetics ; Receptors, Nicotinic/*physiology/ultrastructure ; Structure-Activity Relationship ; Sympathetic Nervous System/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 97
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    Using immunity to block conception (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1991 Mar 1;251(4997):1020-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1998115" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Contraception/*methods ; Egg Proteins/immunology ; Female ; Male ; Spermatozoa/immunology ; Vaccines
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
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    Regulation of transendothelial neutrophil migration by endogenous interleukin-8 (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-04
    Description: Movement of neutrophils from the bloodstream to inflamed tissue depends on the activation of both the neutrophil and the endothelial cell. Endothelial cells lining the postcapillary venule respond to proinflammatory mediators by expressing adhesion molecules and synthesizing a variety of neutrophil-activating factors. Endothelial cell production of a 77-amino acid variant of interleukin-8 (IL-8) was found to be a requirement for the invasion of neutrophils through a vessel wall model. IL-8 secreted by cytokine- or lipopolysaccharide-stimulated endothelial cells induced the rapid shedding of neutrophil lectin adhesion molecule-1, the up-regulation of leukocyte beta 2 integrins, and the attachment and transmigration of the neutrophils. Thus, endogenous endothelial IL-8 regulates transvenular traffic during acute inflammatory responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huber, A R -- Kunkel, S L -- Todd, R F 3rd -- Weiss, S J -- CA 39064/CA/NCI NIH HHS/ -- HL 28024/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):99-102.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, University of Michigan, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1718038" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD/metabolism ; Antigens, CD18 ; Blotting, Northern ; Cell Adhesion Molecules/metabolism ; Cell Movement ; Cells, Cultured ; Chemotaxis, Leukocyte ; E-Selectin ; Endothelium, Vascular/*physiology ; Gene Expression ; Humans ; In Vitro Techniques ; Integrins/metabolism ; Intercellular Adhesion Molecule-1 ; Interleukin-1/pharmacology ; Interleukin-8/genetics/*physiology ; Lipopolysaccharides ; Neutrophils/*physiology ; Tumor Necrosis Factor-alpha/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 99
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    Increased osteoclast development after estrogen loss: mediation by interleukin-6 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-03
    Description: Osteoclasts, the cells that resorb bone, develop from hematopoietic precursors of the bone marrow under the control of factors produced in their microenvironment. The cytokine interleukin-6 can promote hematopoiesis and osteoclastogenesis. Interleukin-6 production by bone and marrow stromal cells is suppressed by 17 beta-estradiol in vitro. In mice, estrogen loss (ovariectomy) increased the number of colony-forming units for granulocytes and macrophages, enhanced osteoclast development in ex vivo cultures of marrow, and increased the number of osteoclasts in trabecular bone. These changes were prevented by 17 beta-estradiol or an antibody to interleukin-6. Thus, estrogen loss results in an interleukin-6-mediated stimulation of osteoclastogenesis, which suggests a mechanism for the increased bone resorption in postmenopausal osteoporosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jilka, R L -- Hangoc, G -- Girasole, G -- Passeri, G -- Williams, D C -- Abrams, J S -- Boyce, B -- Broxmeyer, H -- Manolagas, S C -- AI21761/AI/NIAID NIH HHS/ -- AR41313/AR/NIAMS NIH HHS/ -- CA36464/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Jul 3;257(5066):88-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Veterans Affairs Medical Center, Indiana University School of Medicine, Indianapolis 46202.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1621100" target="_blank"〉PubMed〈/a〉
    Keywords: Analysis of Variance ; Animals ; Antibodies, Monoclonal ; Bone Marrow Cells ; Cells, Cultured ; Estradiol/*pharmacology ; Female ; Granulocyte-Macrophage Colony-Stimulating Factor/pharmacology ; Immunoglobulin G ; Interleukin-6/immunology/*physiology ; Mice ; Osteoclasts/*cytology/drug effects ; *Ovariectomy ; Recombinant Proteins/pharmacology ; Spleen/cytology ; Stem Cells/cytology/drug effects
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 100
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    High probability opening of NMDA receptor channels by L-glutamate (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-24
    Description: Synaptic plasticity can be triggered by calcium flux into neurons through synaptically activated N-methyl-D-aspartate (NMDA) receptor channels. The amplitude and time course of the resulting intracellular calcium transient depend on the number of open NMDA receptor channels and the kinetics of their activation. Short applications of L-glutamate to outside-out patches from hippocampal neurons in the presence and absence of MK-801 revealed that about 30 percent of L-glutamate-bound channels are open at the peak of the current. This high probability of opening suggests that very few channels are required to guarantee a large, localized postsynaptic calcium transient.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jahr, C E -- NS21419/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 24;255(5043):470-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute L474, Oregon Health Sciences University, Portland 97201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1346477" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Cells, Cultured ; Dizocilpine Maleate/pharmacology ; Glutamates/*physiology ; Glutamic Acid ; Hippocampus/physiology ; In Vitro Techniques ; *Ion Channel Gating ; Rats ; Receptors, N-Methyl-D-Aspartate/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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