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  • Mutation  (782)
  • American Association for the Advancement of Science (AAAS)  (782)
  • American Institute of Physics (AIP)
  • 1995-1999  (595)
  • 1985-1989  (187)
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Keywords
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  • American Association for the Advancement of Science (AAAS)  (782)
  • American Institute of Physics (AIP)
  • Springer  (63)
  • Wiley-Blackwell  (8)
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Year
  • 101
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    Abnormal spindle protein, Asp, and the integrity of mitotic centrosomal microtubule organizing centers (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-03-12
    Description: The product of the abnormal spindle (asp) gene was found to be an asymmetrically localized component of the centrosome during mitosis, required to focus the poles of the mitotic spindle in vivo. Removing Asp protein function from Drosophila melanogaster embryo extracts, either by mutation or immunodepletion, resulted in loss of their ability to restore microtubule-organizing center activity to salt-stripped centrosome preparations. This was corrected by addition of purified Asp protein. Thus, Asp appears to hold together the microtubule-nucleating gamma-tubulin ring complexes that organize the mitotic centrosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉do Carmo Avides, M -- Glover, D M -- New York, N.Y. -- Science. 1999 Mar 12;283(5408):1733-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research Campaign Cell Cycle Genetics Laboratories, Medical Sciences Institute, University of Dundee, Dundee DD1 4HN, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10073938" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies ; Cell Fractionation ; Centrosome/chemistry/*physiology/ultrastructure ; *Drosophila Proteins ; Drosophila melanogaster/embryology/genetics/physiology ; Fluorescent Antibody Technique ; Microtubule-Associated Proteins/analysis/genetics/pharmacology/*physiology ; Microtubules/*physiology ; *Mitosis ; Mutation ; Spindle Apparatus/*physiology/ultrastructure ; Tubulin/analysis/physiology
    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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  • 102
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    Extensive nuclear DNA sequence diversity among chimpanzees (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-11-05
    Description: Although data on nucleotide sequence variation in the human nuclear genome have begun to accumulate, little is known about genomic diversity in chimpanzees (Pan troglodytes) and bonobos (Pan paniscus). A 10,154-base pair sequence on the chimpanzee X chromosome is reported, representing all major subspecies and bonobos. Comparison to humans shows the diversity of the chimpanzee sequences to be almost four times as high and the age of the most recent common ancestor three times as great as the corresponding values of humans. Phylogenetic analyses show the sequences from the different chimpanzee subspecies to be intermixed and the distance between some chimpanzee sequences to be greater than the distance between them and the bonobo sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaessmann, H -- Wiebe, V -- Paabo, S -- New York, N.Y. -- Science. 1999 Nov 5;286(5442):1159-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institute for Evolutionary Anthropology, Inselstrasse 22, D-04103 Leipzig, Germany. kaessmann@eva.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10550054" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA/*genetics ; *Genetic Variation ; *Genome ; Gorilla gorilla/genetics ; Humans ; Molecular Sequence Data ; Mutation ; Pan paniscus/classification/*genetics ; Pan troglodytes/classification/*genetics ; Phylogeny ; Recombination, Genetic ; Species Specificity ; X Chromosome/*genetics
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  • 103
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    Deep Green rewrites evolutionary history of plants (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-09-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, K S -- New York, N.Y. -- Science. 1999 Aug 13;285(5430):990-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10475846" target="_blank"〉PubMed〈/a〉
    Keywords: Angiosperms/*classification/genetics ; Eukaryota/classification/genetics ; Fungi/classification/genetics ; Genes, Plant ; Mutation ; *Phylogeny ; Plants/*classification/genetics ; Terminology as Topic
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  • 104
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    Silencing of genes flanking the P1 plasmid centromere (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-01-23
    Description: Partition modules stabilize bacterial plasmids and chromosomes by actively promoting their segregation into daughter cells. The partition module of plasmid P1 is typical and consists of a centromere site, parS, and genes that encode proteins ParA and ParB. We show that ParB can silence genes flanking parS (to which ParB binds), apparently by polymerizing along the DNA from a nucleation site at parS. Wild-type ParB contacts an extensive region of P1 DNA; silencing-defective ParB proteins, which were found to be partition-defective, are less able to spread. Hence, the silenced structure appears to function in partitioning.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rodionov, O -- Lobocka, M -- Yarmolinsky, M -- New York, N.Y. -- Science. 1999 Jan 22;283(5401):546-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry, National Cancer Institute, 37 Convent Drive, Bethesda, MD 20892-4255, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9915704" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/genetics/*metabolism ; Binding Sites ; Centromere/physiology ; Cross-Linking Reagents ; *DNA Helicases ; DNA, Bacterial/genetics/*metabolism ; *DNA-Binding Proteins ; Escherichia coli/*genetics ; Formaldehyde ; *Gene Expression Regulation, Bacterial ; Genes, Reporter ; Mutation ; Plasmids/*genetics/physiology ; Proteins/genetics/metabolism ; Repressor Proteins/genetics/metabolism ; *Trans-Activators
    Print ISSN: 0036-8075
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  • 105
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    Differences in left-right axis pathways in mouse and chick: functions of FGF8 and SHH (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-07-20
    Description: A molecular pathway leading to left-right asymmetry in the chick embryo has been described, in which FGF8 is a right determinant and Sonic Hedgehog a left determinant. Here evidence is presented that the Fgf8 and Sonic Hedgehog genes are required for left-right axis determination in the mouse embryo, but that they have different functions from those previously reported in the chick. In the mouse FGF8 is a left determinant and Sonic Hedgehog is required to prevent left determinants from being expressed on the right.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meyers, E N -- Martin, G R -- HD01216/HD/NICHD NIH HHS/ -- R01 HD34380/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1999 Jul 16;285(5426):403-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Program in Developmental Biology, School of Medicine, and Department of Pediatrics, School of Medicine, University of California at San Francisco, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10411502" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Body Patterning ; Chick Embryo/*growth & development/metabolism ; Embryo, Mammalian/metabolism ; *Embryonic Induction ; *Embryonic and Fetal Development ; Fibroblast Growth Factor 8 ; Fibroblast Growth Factors/genetics/*physiology ; Gene Expression Regulation, Developmental ; Heart/embryology ; Heart Defects, Congenital/embryology ; Hedgehog Proteins ; Homeodomain Proteins/genetics/physiology ; Left-Right Determination Factors ; Lung/abnormalities/embryology ; Mesoderm/metabolism ; Mice ; Mutation ; Nodal Protein ; *Nuclear Proteins ; Paired Box Transcription Factors ; Proteins/genetics/*physiology ; Recombinant Proteins/metabolism ; *Trans-Activators ; Transcription Factors/genetics/physiology ; Transforming Growth Factor beta/genetics/physiology
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  • 106
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    Interlocked feedback loops within the Drosophila circadian oscillator (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-10-26
    Description: Drosophila Clock (dClk) is rhythmically expressed, with peaks in mRNA and protein (dCLK) abundance early in the morning. dClk mRNA cycling is shown here to be regulated by PERIOD-TIMELESS (PER-TIM)-mediated release of dCLK- and CYCLE (CYC)-dependent repression. Lack of both PER-TIM derepression and dCLK-CYC repression results in high levels of dClk mRNA, which implies that a separate dClk activator is present. These results demonstrate that the Drosophila circadian feedback loop is composed of two interlocked negative feedback loops: a per-tim loop, which is activated by dCLK-CYC and repressed by PER-TIM, and a dClk loop, which is repressed by dCLK-CYC and derepressed by PER-TIM.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Glossop, N R -- Lyons, L C -- Hardin, P E -- NS-31214/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1999 Oct 22;286(5440):766-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Biochemistry and Biological Clocks Program, University of Houston, Houston, TX 77204-5513, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10531060" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Clocks ; CLOCK Proteins ; *Circadian Rhythm ; Dimerization ; Drosophila/*genetics/metabolism ; *Drosophila Proteins ; Feedback ; *Gene Expression Regulation ; Genes, Insect ; Insect Proteins/genetics ; Models, Genetic ; Mutation ; Nuclear Proteins/metabolism ; Period Circadian Proteins ; RNA, Messenger/genetics/metabolism ; Transcription Factors/*genetics/metabolism ; Transcription, Genetic
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  • 107
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    An adenosine deaminase that generates inosine at the wobble position of tRNAs (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-11-05
    Description: Several transfer RNAs (tRNAs) contain inosine (I) at the first position of their anticodon (position 34); this modification is thought to enlarge the codon recognition capacity during protein synthesis. The tRNA-specific adenosine deaminase of Saccharomyces cerevisiae that forms I(34) in tRNAs is described. The heterodimeric enzyme consists of two sequence-related subunits (Tad2p/ADAT2 and Tad3p/ADAT3), both of which contain cytidine deaminase (CDA) motifs. Each subunit is encoded by an essential gene (TAD2 and TAD3), indicating that I(34) is an indispensable base modification in elongating tRNAs. These results provide an evolutionary link between the CDA superfamily and RNA-dependent adenosine deaminases (ADARs/ADATs).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gerber, A P -- Keller, W -- New York, N.Y. -- Science. 1999 Nov 5;286(5442):1146-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Biozentrum, University of Basel, 4056 Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10550050" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Deaminase/*chemistry/genetics/*metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Anticodon/*metabolism ; Cytidine Deaminase/chemistry ; Dimerization ; Evolution, Molecular ; Genes, Essential ; Genes, Fungal ; Inosine/*metabolism ; Molecular Sequence Data ; Mutation ; RNA, Fungal/metabolism ; RNA, Transfer/*metabolism ; Saccharomyces cerevisiae/chemistry/*enzymology/genetics ; Sequence Alignment
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  • 108
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    Control of the DNA damage checkpoint by chk1 and rad53 protein kinases through distinct mechanisms (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-11-05
    Description: In response to DNA damage, cells activate checkpoint pathways that prevent cell cycle progression. In fission yeast and mammals, mitotic arrest in response to DNA damage requires inhibitory Cdk phosphorylation regulated by Chk1. This study indicates that Chk1 is required for function of the DNA damage checkpoint in Saccharomyces cerevisiae but acts through a distinct mechanism maintaining the abundance of Pds1, an anaphase inhibitor. Unlike other checkpoint mutants, chk1 mutants were only mildly sensitive to DNA damage, indicating that checkpoint functions besides cell cycle arrest influence damage sensitivity. Another kinase, Rad53, was required to both maintain active cyclin-dependent kinase 1, Cdk1(Cdc28), and prevent anaphase entry after checkpoint activation. Evidence suggests that Rad53 exerts its role in checkpoint control through regulation of the Polo kinase Cdc5. These results support a model in which Chk1 and Rad53 function in parallel through Pds1 and Cdc5, respectively, to prevent anaphase entry and mitotic exit after DNA damage. This model provides a possible explanation for the role of Cdc5 in DNA damage checkpoint adaptation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sanchez, Y -- Bachant, J -- Wang, H -- Hu, F -- Liu, D -- Tetzlaff, M -- Elledge, S J -- GM44664/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Nov 5;286(5442):1166-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10550056" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase ; Anaphase-Promoting Complex-Cyclosome ; CDC2 Protein Kinase/metabolism ; Cell Cycle Proteins/genetics/metabolism ; Checkpoint Kinase 2 ; Cyclin B/genetics/metabolism ; *DNA Damage ; DNA, Fungal/metabolism ; Fungal Proteins/genetics/metabolism ; Intracellular Signaling Peptides and Proteins ; Ligases/metabolism ; *Mitosis ; Mutation ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein Kinases/genetics/*metabolism ; *Protein-Serine-Threonine Kinases ; RNA-Binding Proteins ; Recombinant Fusion Proteins/metabolism ; S Phase ; Saccharomyces cerevisiae/*cytology/*enzymology/genetics ; *Saccharomyces cerevisiae Proteins ; Securin ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases
    Print ISSN: 0036-8075
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  • 109
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    Regulation of transcription by a protein methyltransferase (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-06-26
    Description: The p160 family of coactivators, SRC-1, GRIP1/TIF2, and p/CIP, mediate transcriptional activation by nuclear hormone receptors. Coactivator-associated arginine methyltransferase 1 (CARM1), a previously unidentified protein that binds to the carboxyl-terminal region of p160 coactivators, enhanced transcriptional activation by nuclear receptors, but only when GRIP1 or SRC-1a was coexpressed. Thus, CARM1 functions as a secondary coactivator through its association with p160 coactivators. CARM1 can methylate histone H3 in vitro, and a mutation in the putative S-adenosylmethionine binding domain of CARM1 substantially reduced both methyltransferase and coactivator activities. Thus, coactivator-mediated methylation of proteins in the transcription machinery may contribute to transcriptional regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, D -- Ma, H -- Hong, H -- Koh, S S -- Huang, S M -- Schurter, B T -- Aswad, D W -- Stallcup, M R -- AG00093/AG/NIA NIH HHS/ -- DK43093/DK/NIDDK NIH HHS/ -- NS17269/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1999 Jun 25;284(5423):2174-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology HMR 301, University of Southern California, 2011 Zonal Avenue, Los Angeles, CA 90033, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10381882" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Histone Acetyltransferases ; Histones/metabolism ; Methylation ; Mice ; Molecular Sequence Data ; Mutation ; Nuclear Receptor Coactivator 1 ; Nuclear Receptor Coactivator 2 ; Nuclear Receptor Coactivator 3 ; Protein-Arginine N-Methyltransferases/chemistry/genetics/*metabolism ; Receptors, Androgen/metabolism ; Receptors, Estrogen/metabolism ; Receptors, Thyroid Hormone/metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Trans-Activators/*metabolism ; Transcription Factors/metabolism ; *Transcriptional Activation ; Transfection
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  • 110
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    Preventing neurodegeneration in the Drosophila mutant bubblegum (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-06-18
    Description: The Drosophila melanogaster recessive mutant bubblegum (bgm) exhibits adult neurodegeneration, with marked dilation of photoreceptor axons. The bubblegum mutant shows elevated levels of very long chain fatty acids (VLCFAs), as seen in the human disease adrenoleukodystrophy (ALD). In ALD, the excess can be lowered by dietary treatment with "Lorenzo's oil," a mixture of unsaturated fatty acids. Feeding the fly mutant one of the components, glyceryl trioleate oil, blocked the accumulation of excess VLCFAs as well as development of the pathology. Mutant flies thus provide a potential model system for studying mechanisms of neurodegenerative disease and screening drugs for treatment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Min, K T -- Benzer, S -- New York, N.Y. -- Science. 1999 Jun 18;284(5422):1985-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology 156-29, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10373116" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenoleukodystrophy/diet therapy/genetics ; Amino Acid Sequence ; Animals ; Coenzyme A Ligases/chemistry/*genetics ; Disease Models, Animal ; *Drosophila Proteins ; Drosophila melanogaster/*genetics/metabolism ; Drug Combinations ; Erucic Acids/administration & dosage/pharmacology ; Fatty Acids/*metabolism ; Female ; Genes, Insect ; Genes, Recessive ; Male ; Molecular Sequence Data ; Mutation ; *Nerve Degeneration ; Photoreceptor Cells, Invertebrate/ultrastructure ; *Repressor Proteins ; *Saccharomyces cerevisiae Proteins ; Sex Characteristics ; Triolein/administration & dosage/*pharmacology
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  • 111
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    Interaction of RAFT1 with gephyrin required for rapamycin-sensitive signaling (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-05-15
    Description: RAFT1 (rapamycin and FKBP12 target 1; also called FRAP or mTOR) is a member of the ATM (ataxia telangiectasia mutated)-related family of proteins and functions as the in vivo mediator of the effects of the immunosuppressant rapamycin and as an important regulator of messenger RNA translation. In mammalian cells RAFT1 interacted with gephyrin, a widely expressed protein necessary for the clustering of glycine receptors at the cell membrane of neurons. RAFT1 mutants that could not associate with gephyrin failed to signal to downstream molecules, including the p70 ribosomal S6 kinase and the eIF-4E binding protein, 4E-BP1. The interaction with gephyrin ascribes a function to the large amino-terminal region of an ATM-related protein and reveals a role in signal transduction for the clustering protein gephyrin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sabatini, D M -- Barrow, R K -- Blackshaw, S -- Burnett, P E -- Lai, M M -- Field, M E -- Bahr, B A -- Kirsch, J -- Betz, H -- Snyder, S H -- DA-00074/DA/NIDA NIH HHS/ -- DA-00266/DA/NIDA NIH HHS/ -- GM-07309/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 May 14;284(5417):1161-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Johns Hopkins University School of Medicine, Department of Neuroscience, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10325225" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Line ; Cell Membrane/metabolism ; Cytoplasm/metabolism ; Gene Expression ; HeLa Cells ; Humans ; Membrane Proteins/*metabolism ; Molecular Sequence Data ; Mutation ; Phosphoproteins/*metabolism ; Phosphorylation ; *Phosphotransferases (Alcohol Group Acceptor) ; Rats ; Receptors, Glycine/metabolism ; Repressor Proteins/metabolism ; Ribosomal Protein S6 Kinases/*metabolism ; *Signal Transduction ; Sirolimus/*pharmacology ; TOR Serine-Threonine Kinases
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  • 112
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    Protein interaction mapping in C. elegans using proteins involved in vulval development (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-30
    Description: Protein interaction mapping using large-scale two-hybrid analysis has been proposed as a way to functionally annotate large numbers of uncharacterized proteins predicted by complete genome sequences. This approach was examined in Caenorhabditis elegans, starting with 27 proteins involved in vulval development. The resulting map reveals both known and new potential interactions and provides a functional annotation for approximately 100 uncharacterized gene products. A protein interaction mapping project is now feasible for C. elegans on a genome-wide scale and should contribute to the understanding of molecular mechanisms in this organism and in human diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walhout, A J -- Sordella, R -- Lu, X -- Hartley, J L -- Temple, G F -- Brasch, M A -- Thierry-Mieg, N -- Vidal, M -- 1 R21 CA81658 A 01/CA/NCI NIH HHS/ -- 1 RO1 HG01715-01/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2000 Jan 7;287(5450):116-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Massachusetts General Hospital Cancer Center, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10615043" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*genetics/growth & development/*metabolism ; *Caenorhabditis elegans Proteins ; Cloning, Molecular ; Databases, Factual ; Female ; Genes, Helminth ; Genetic Vectors ; *Genome ; Helminth Proteins/*genetics/*metabolism ; Mutation ; Open Reading Frames ; Phenotype ; Repressor Proteins/genetics/metabolism ; Retinoblastoma Protein/genetics/metabolism ; *Two-Hybrid System Techniques ; Vulva/growth & development
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  • 113
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    Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: The T cell receptor (TCR) inherently has dual specificity. T cells must recognize self-antigens in the thymus during maturation and then discriminate between foreign pathogens in the periphery. A molecular basis for this cross-reactivity is elucidated by the crystal structure of the alloreactive 2C TCR bound to self peptide-major histocompatibility complex (pMHC) antigen H-2Kb-dEV8 refined against anisotropic 3.0 angstrom resolution x-ray data. The interface between peptide and TCR exhibits extremely poor shape complementarity, and the TCR beta chain complementarity-determining region 3 (CDR3) has minimal interaction with the dEV8 peptide. Large conformational changes in three of the TCR CDR loops are induced upon binding, providing a mechanism of structural plasticity to accommodate a variety of different peptide antigens. Extensive TCR interaction with the pMHC alpha helices suggests a generalized orientation that is mediated by the Valpha domain of the TCR and rationalizes how TCRs can effectively "scan" different peptides bound within a large, low-affinity MHC structural framework for those that provide the slight additional kinetic stabilization required for signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garcia, K C -- Degano, M -- Pease, L R -- Huang, M -- Peterson, P A -- Teyton, L -- Wilson, I A -- AI42266/AI/NIAID NIH HHS/ -- AI42267/AI/NIAID NIH HHS/ -- R01 CA58896/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1166-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and the Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9469799" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crystallization ; Crystallography, X-Ray ; H-2 Antigens/*chemistry/*immunology/metabolism ; Ligands ; Mice ; Mice, Transgenic ; Models, Molecular ; Mutation ; Oligopeptides/*chemistry/immunology/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Receptors, Antigen, T-Cell, alpha-beta/*chemistry/*immunology/metabolism ; Recombinant Proteins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Identification of alpha-dystroglycan as a receptor for lymphocytic choriomeningitis virus and Lassa fever virus (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-16
    Description: A peripheral membrane protein that is interactive with lymphocytic choriomeningitis virus (LCMV) was purified from cells permissive to infection. Tryptic peptides from this protein were determined to be alpha-dystroglycan (alpha-DG). Several strains of LCMV and other arenaviruses, including Lassa fever virus (LFV), Oliveros, and Mobala, bound to purified alpha-DG protein. Soluble alpha-DG blocked both LCMV and LFV infection. Cells bearing a null mutation of the gene encoding DG were resistant to LCMV infection, and reconstitution of DG expression in null mutant cells restored susceptibility to LCMV infection. Thus, alpha-DG is a cellular receptor for both LCMV and LFV.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cao, W -- Henry, M D -- Borrow, P -- Yamada, H -- Elder, J H -- Ravkov, E V -- Nichol, S T -- Compans, R W -- Campbell, K P -- Oldstone, M B -- AG 00080/AG/NIA NIH HHS/ -- AI 09484/AI/NIAID NIH HHS/ -- DK09712/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 Dec 11;282(5396):2079-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Virology, Department of Neuropharmacology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9851928" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arenavirus/metabolism ; Cell Line ; Cytoskeletal Proteins/chemistry/genetics/*metabolism ; Dystroglycans ; Lassa virus/*metabolism/physiology ; Lymphocytic choriomeningitis virus/*metabolism/physiology ; Membrane Glycoproteins/chemistry/genetics/*metabolism ; Mice ; Molecular Sequence Data ; Mutation ; Receptors, Virus/chemistry/*metabolism ; Recombinant Fusion Proteins/metabolism ; Virus Replication
    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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    Which of our genes makes us human? (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, A -- New York, N.Y. -- Science. 1998 Sep 4;281(5382):1432-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9750111" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; *Chromosomes, Human ; Gene Expression ; *Genome ; *Genome, Human ; Hominidae/*genetics ; *Human Characteristics ; Humans ; Mutation ; Pan troglodytes/genetics ; *Sequence Analysis, DNA ; Sialic Acids/chemistry/physiology ; Species Specificity
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    Role of IQGAP1, a target of the small GTPases Cdc42 and Rac1, in regulation of E-cadherin- mediated cell-cell adhesion (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-07
    Description: The small guanosine triphosphatases (GTPases) Cdc42 and Rac1 regulate E-cadherin-mediated cell-cell adhesion. IQGAP1, a target of Cdc42 and Rac1, was localized with E-cadherin and beta-catenin at sites of cell-cell contact in mouse L fibroblasts expressing E-cadherin (EL cells), and interacted with E-cadherin and beta-catenin both in vivo and in vitro. IQGAP1 induced the dissociation of alpha-catenin from a cadherin-catenin complex in vitro and in vivo. Overexpression of IQGAP1 in EL cells, but not in L cells expressing an E-cadherin-alpha-catenin chimeric protein, resulted in a decrease in E-cadherin-mediated cell-cell adhesive activity. Thus, IQGAP1, acting downstream of Cdc42 and Rac1, appears to regulate cell-cell adhesion through the cadherin-catenin pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuroda, S -- Fukata, M -- Nakagawa, M -- Fujii, K -- Nakamura, T -- Ookubo, T -- Izawa, I -- Nagase, T -- Nomura, N -- Tani, H -- Shoji, I -- Matsuura, Y -- Yonehara, S -- Kaibuchi, K -- New York, N.Y. -- Science. 1998 Aug 7;281(5378):832-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Signal Transduction, Nara Institute of Science and Technology, Ikoma 630-0101, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9694656" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cadherins/*metabolism ; *Cell Adhesion ; Cell Cycle Proteins/*metabolism ; Cell Membrane/metabolism ; Cytoskeletal Proteins/metabolism ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/*metabolism ; GTPase-Activating Proteins ; L Cells (Cell Line) ; Mice ; Mutation ; Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism ; *Trans-Activators ; alpha Catenin ; beta Catenin ; cdc42 GTP-Binding Protein ; rac GTP-Binding Proteins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Essential role of CED-4 oligomerization in CED-3 activation and apoptosis (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-28
    Description: Control of the activation of apoptosis is important both in development and in protection against cancer. In the classic genetic model Caenorhabditis elegans, the pro-apoptotic protein CED-4 activates the CED-3 caspase and is inhibited by the Bcl-2-like protein CED-9. Both processes are mediated by protein-protein interaction. Facilitating the proximity of CED-3 zymogen molecules was found to induce caspase activation and cell death. CED-4 protein oligomerized in cells and in vitro. This oligomerization induced CED-3 proximity and competed with CED-4:CED-9 interaction. Mutations that abolished CED-4 oligomerization inactivated its ability to activate CED-3. Thus, the mechanism of control is that CED-3 in CED-3:CED-4 complexes is activated by CED-4 oligomerization, which is inhibited by binding of CED-9 to CED-4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, X -- Chang, H Y -- Baltimore, D -- CA51462/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 Aug 28;281(5381):1355-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9721101" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; Apoptosis Regulatory Proteins ; Biopolymers ; *Caenorhabditis elegans Proteins ; Calcium-Binding Proteins/*chemistry/genetics/*metabolism ; *Caspases ; Cell Line ; Chemistry, Physical ; Cysteine Endopeptidases/*metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Enzyme Activation ; Enzyme Precursors/metabolism ; HeLa Cells ; Helminth Proteins/*chemistry/genetics/*metabolism ; Humans ; Mutation ; Oligopeptides/pharmacology ; Physicochemical Phenomena ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Recombinant Fusion Proteins/metabolism ; Tacrolimus/pharmacology ; Transfection ; bcl-X Protein
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Differential use of CREB binding protein-coactivator complexes (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-21
    Description: CREB binding protein (CBP) functions as an essential coactivator of transcription factors that are inhibited by the adenovirus early gene product E1A. Transcriptional activation by the signal transducer and activator of transcription-1 (STAT1) protein requires the C/H3 domain in CBP, which is the primary target of E1A inhibition. Here it was found that the C/H3 domain is not required for retinoic acid receptor (RAR) function, nor is it involved in E1A inhibition. Instead, E1A inhibits RAR function by preventing the assembly of CBP-nuclear receptor coactivator complexes, revealing differences in required CBP domains for transcriptional activation by RAR and STAT1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kurokawa, R -- Kalafus, D -- Ogliastro, M H -- Kioussi, C -- Xu, L -- Torchia, J -- Rosenfeld, M G -- Glass, C K -- New York, N.Y. -- Science. 1998 Jan 30;279(5351):700-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cellular and Molecular Medicine, Department of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0651, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9445474" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1A Proteins/*metabolism/pharmacology ; Animals ; Binding Sites ; CREB-Binding Protein ; Cell Differentiation ; Cell Line ; DNA-Binding Proteins/metabolism ; Histone Acetyltransferases ; Humans ; Mutation ; Nuclear Proteins/chemistry/genetics/*metabolism ; Nuclear Receptor Coactivator 1 ; Nuclear Receptor Coactivator 3 ; Protein Binding ; Receptors, Retinoic Acid/metabolism ; Recombinant Fusion Proteins/metabolism ; STAT1 Transcription Factor ; Trans-Activators/metabolism ; Transcription Factors/chemistry/genetics/*metabolism ; *Transcription, Genetic ; Transcriptional Activation ; Tretinoin/pharmacology
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    FADD: essential for embryo development and signaling from some, but not all, inducers of apoptosis (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: FADD (also known as Mort-1) is a signal transducer downstream of cell death receptor CD95 (also called Fas). CD95, tumor necrosis factor receptor type 1 (TNFR-1), and death receptor 3 (DR3) did not induce apoptosis in FADD-deficient embryonic fibroblasts, whereas DR4, oncogenes E1A and c-myc, and chemotherapeutic agent adriamycin did. Mice with a deletion in the FADD gene did not survive beyond day 11.5 of embryogenesis; these mice showed signs of cardiac failure and abdominal hemorrhage. Chimeric embryos showing a high contribution of FADD null mutant cells to the heart reproduce the phenotype of FADD-deficient mutants. Thus, not only death receptors, but also receptors that couple to developmental programs, may use FADD for signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yeh, W C -- de la Pompa, J L -- McCurrach, M E -- Shu, H B -- Elia, A J -- Shahinian, A -- Ng, M -- Wakeham, A -- Khoo, W -- Mitchell, K -- El-Deiry, W S -- Lowe, S W -- Goeddel, D V -- Mak, T W -- CA13106/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 Mar 20;279(5358):1954-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Amgen Institute, University of Toronto, Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9506948" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Animals ; Antigens, CD95/genetics/physiology ; *Apoptosis ; Carrier Proteins/genetics/*physiology ; Cell Transformation, Neoplastic ; Cells, Cultured ; Doxorubicin/pharmacology ; *Embryonic and Fetal Development ; Endothelium, Vascular/embryology ; Fas-Associated Death Domain Protein ; Female ; Gene Expression ; Gene Targeting ; Heart/*embryology ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Mutation ; Oncogenes ; Receptors, Tumor Necrosis Factor/genetics/physiology ; Signal Transduction ; Tumor Necrosis Factor-alpha/pharmacology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    RNA-mediated trans-activation of transcription from a viral RNA (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-07
    Description: The red clover necrotic mosaic virus genome is composed of two single-stranded RNA components, RNA-1 and RNA-2. The viral capsid protein is translated from a subgenomic RNA (sgRNA) that is transcribed from genomic RNA-1. Here, a 34-nucleotide sequence in RNA-2 is shown to be required for transcription of sgRNA. Mutations that prevent base-pairing between the RNA-1 subgenomic promoter and the 34-nucleotide trans-activator prevent expression of a reporter gene. A model is proposed in which direct binding of RNA-2 to RNA-1 trans-activates sgRNA synthesis. This RNA-mediated regulation of transcription is unusual among RNA viruses, which typically rely on protein regulators.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sit, T L -- Vaewhongs, A A -- Lommel, S A -- New York, N.Y. -- Science. 1998 Aug 7;281(5378):829-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Pathology, North Carolina State University, Raleigh, NC 27695-7616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9694655" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; DNA, Complementary ; Gene Expression ; Genes, Reporter ; Green Fluorescent Proteins ; Luminescent Proteins/genetics ; Models, Genetic ; Molecular Sequence Data ; Mosaic Viruses/*genetics ; Mutation ; Nucleic Acid Conformation ; Promoter Regions, Genetic ; RNA, Double-Stranded/genetics/metabolism ; RNA, Messenger/biosynthesis/genetics ; RNA, Viral/biosynthesis/chemistry/*genetics ; Sequence Alignment ; *Transcriptional Activation
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    Ribozyme-mediated repair of sickle beta-globin mRNAs in erythrocyte precursors (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-11
    Description: Sickle cell anemia is the most common heritable hematological disease, yet no curative treatment exists for this disorder. Moreover, the intricacies of globin gene expression have made the development of treatments for hemoglobinopathies based on gene therapy difficult. An alternative genetic approach to sickle cell therapy is based on RNA repair. A trans-splicing group I ribozyme was used to alter mutant beta-globin transcripts in erythrocyte precursors derived from peripheral blood from individuals with sickle cell disease. Sickle beta-globin transcripts were converted into messenger RNAs encoding the anti-sickling protein gamma-globin. These results suggest that RNA repair may become a useful approach in the treatment of genetic disorders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lan, N -- Howrey, R P -- Lee, S W -- Smith, C A -- Sullenger, B A -- HL57606/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 5;280(5369):1593-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Genetic and Cellular Therapies, Department of Surgery, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9616120" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Sickle Cell/*blood/therapy ; Cloning, Molecular ; Erythroid Precursor Cells/*metabolism ; Exons ; Fetal Blood ; Genetic Therapy ; Globins/*genetics ; Humans ; Mutation ; Polymerase Chain Reaction ; *RNA Splicing ; RNA, Catalytic/genetics/*metabolism ; RNA, Messenger/chemistry/*genetics/metabolism ; Transfection ; Uridine/metabolism
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    Dorsal-ventral signaling in the Drosophila eye (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-25
    Description: The development of the Drosophila eye has served as a model system for investigations of tissue patterning and cell-cell communication; however, early eye development has not been well understood. The results presented here indicate that specialized cells are established along the dorsal-ventral midline of the developing eye by Notch-mediated signaling between dorsal and ventral cells, and that Notch activation at the midline plays an essential role both in promoting the growth of the eye primordia and in regulating eye patterning. These observations imply that the developmental homology between Drosophila wings and vertebrate limbs extends to Drosophila eyes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Papayannopoulos, V -- Tomlinson, A -- Panin, V M -- Rauskolb, C -- Irvine, K D -- GM-R01-54594/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 25;281(5385):2031-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Waksman Institute and Department of Molecular Biology and Biochemistry, Rutgers, The State University, Piscataway, NJ 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9748163" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Body Patterning ; Calcium-Binding Proteins ; Drosophila/genetics/*growth & development/metabolism ; *Drosophila Proteins ; Eye Proteins/genetics ; Gene Expression Regulation, Developmental ; Genes, Insect ; Homeodomain Proteins ; Insect Proteins/genetics/physiology ; Intercellular Signaling Peptides and Proteins ; Intracellular Signaling Peptides and Proteins ; Larva/growth & development ; Ligands ; Membrane Proteins/genetics/*physiology ; Morphogenesis ; Mutation ; *N-Acetylglucosaminyltransferases ; Photoreceptor Cells, Invertebrate/cytology/*growth & development ; Receptors, Notch ; Signal Transduction ; *Transcription Factors
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    BSE and prions: uncertainties about the agent (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chesebro, B -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):42-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Persistent Virus Diseases, Rocky Mountain Laboratories, Hamilton, MT 59840, USA. bchesebro@nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9441410" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid/chemistry ; Amyloidosis/metabolism ; Animals ; Cattle ; Creutzfeldt-Jakob Syndrome/epidemiology/*etiology/transmission ; Disease Susceptibility ; Encephalopathy, Bovine Spongiform/epidemiology/*etiology/transmission ; Gene Expression ; Great Britain/epidemiology ; Humans ; Mice ; Mice, Transgenic ; Mutation ; Prion Diseases/*etiology/transmission ; Prions/chemistry/genetics/metabolism/*pathogenicity ; Virus Physiological Phenomena ; Viruses/pathogenicity
    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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    Direct phosphorylation of IkappaB by IKKalpha and IKKbeta: discrimination between free and NF-kappaB-bound substrate (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-28
    Description: A large protein complex mediates the phosphorylation of the inhibitor of kappaB (IkappaB), which results in the activation of nuclear factor kappaB (NF-kappaB). Two subunits of this complex, IkappaB kinase alpha (IKKalpha) and IkappaB kinase beta (IKKbeta), are required for NF-kappaB activation. Purified recombinant IKKalpha and IKKbeta expressed in insect cells were used to demonstrate that each protein can directly phosphorylate IkappaB proteins. IKKalpha and IKKbeta were found to form both homodimers and heterodimers. Both IKKalpha and IKKbeta phosphorylated IkappaB bound to NF-kappaB more efficiently than they phosphorylated free IkappaB. This result explains how free IkappaB can accumulate in cells in which IKK is still active and thus can contribute to the termination of NF-kappaB activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zandi, E -- Chen, Y -- Karin, M -- AI 43477/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Aug 28;281(5381):1360-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Gene Regulation and Signal Transduction, Department of Pharmacology, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9721103" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Dimerization ; Enzyme Activation ; HeLa Cells ; Helix-Loop-Helix Motifs ; Humans ; I-kappa B Kinase ; Leucine Zippers ; Mutation ; NF-kappa B/antagonists & inhibitors/*metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism ; Spodoptera ; Transcription Factor RelB ; *Transcription Factors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Yeast Ku as a regulator of chromosomal DNA end structure (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-23
    Description: During telomere replication in yeast, chromosome ends acquire an S-phase-specific overhang of the guanosine-rich strand. Here it is shown that in cells lacking Ku, a heterodimeric protein involved in nonhomologous DNA end joining, these overhangs are present throughout the cell cycle. In vivo cross-linking experiments demonstrated that Ku is bound to telomeric DNA. These results show that Ku plays a direct role in establishing a normal DNA end structure on yeast chromosomes, conceivably by functioning as a terminus-binding factor. Because Ku-mediated DNA end joining involving telomeres would result in chromosome instability, our data also suggest that Ku has a distinct function when bound to telomeres.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gravel, S -- Larrivee, M -- Labrecque, P -- Wellinger, R J -- New York, N.Y. -- Science. 1998 May 1;280(5364):741-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement de Microbiologie et Infectiologie, Faculte de Medecine, Universite de Sherbrooke, 3001 12th Avenue Nord, Sherbrooke, Quebec QC J1H 5N4, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9563951" target="_blank"〉PubMed〈/a〉
    Keywords: *Antigens, Nuclear ; Binding Sites ; Chromosomes, Fungal/chemistry/*metabolism ; *DNA Helicases ; DNA, Fungal/chemistry/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Fungal Proteins/*metabolism ; G2 Phase ; Genes, Fungal ; Mitosis ; Mutation ; Nuclear Proteins/genetics/*metabolism ; S Phase ; Saccharomyces cerevisiae/cytology/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Telomerase/genetics/metabolism ; Telomere/*metabolism ; Temperature ; Transformation, Genetic
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    Arabidopsis NPH1: a flavoprotein with the properties of a photoreceptor for phototropism (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-30
    Description: The NPH1 gene of Arabidopsis thaliana encodes a 120-kilodalton serine-threonine protein kinase hypothesized to function as a photoreceptor for phototropism. When expressed in insect cells, the NPH1 protein is phosphorylated in response to blue light irradiation. The biochemical and photochemical properties of the photosensitive protein reflect those of the native protein in microsomal membranes. Recombinant NPH1 noncovalently binds flavin mononucleotide, a likely chromophore for light-dependent autophosphorylation. The fluorescence excitation spectrum of the recombinant protein is similar to the action spectrum for phototropism, consistent with the conclusion that NPH1 is an autophosphorylating flavoprotein photoreceptor mediating phototropic responses in higher plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Christie, J M -- Reymond, P -- Powell, G K -- Bernasconi, P -- Raibekas, A A -- Liscum, E -- Briggs, W R -- New York, N.Y. -- Science. 1998 Nov 27;282(5394):1698-701.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Biology, Carnegie Institution of Washington, 260 Panama Street, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9831559" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arabidopsis/genetics/*physiology ; *Arabidopsis Proteins ; Cell Line ; Cryptochromes ; *Drosophila Proteins ; *Eye Proteins ; Flavin Mononucleotide/metabolism ; Flavoproteins/physiology ; Genes, Plant ; Light ; Mutation ; Phosphoproteins/genetics/*metabolism ; Phosphorylation ; *Photoreceptor Cells, Invertebrate ; *Phototropism ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Receptors, G-Protein-Coupled ; Recombinant Proteins/metabolism ; Spectrometry, Fluorescence ; Spodoptera ; Transfection
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    More deafness genes (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steel, K P -- Brown, S D -- New York, N.Y. -- Science. 1998 May 29;280(5368):1403.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council, Institute of Hearing Research, University Park, Nottingham NG7 2RD, UK. karen@ihr.mrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9634418" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/physiology ; Animals ; Cilia/physiology ; Deafness/*genetics ; Dyneins ; Extracellular Matrix Proteins/*genetics/physiology ; GPI-Linked Proteins ; Hair Cells, Auditory/physiology/ultrastructure ; Hearing ; Humans ; Membrane Glycoproteins/*genetics/physiology ; Mice ; Mice, Mutant Strains ; Mutation ; Myosin Heavy Chains/genetics/physiology ; Myosins/*genetics/physiology ; Tectorial Membrane/physiology
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    How the genome readies itself for evolution (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1998 Aug 21;281(5380):1131,1133-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9735027" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA Repair ; DNA Transposable Elements ; *Evolution, Molecular ; Exons ; Gene Rearrangement ; *Genome ; Humans ; Micronuclei, Chromosome-Defective/genetics ; Multigene Family ; Mutation ; Plants/genetics ; Repetitive Sequences, Nucleic Acid
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    RNAi in C. elegans: soaking in the genome sequence (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tabara, H -- Grishok, A -- Mello, C C -- DK32520-15/DK/NIDDK NIH HHS/ -- R01 HD33769-01/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 16;282(5388):430-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9841401" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*genetics ; *Gene Expression Regulation ; *Genes, Helminth ; Mutation ; Phenotype ; RNA, Antisense/*genetics ; RNA, Double-Stranded/genetics ; RNA, Helminth/*genetics ; RNA, Messenger/genetics ; Transcription, Genetic
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    An essential role for ectodomain shedding in mammalian development (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-13
    Description: The ectodomains of numerous proteins are released from cells by proteolysis to yield soluble intercellular regulators. The responsible protease, tumor necrosis factor-alpha converting enzyme (TACE), has been identified only in the case when tumor necrosis factor-alpha (TNFalpha) is released. Analyses of cells lacking this metalloproteinase-disintegrin revealed an expanded role for TACE in the processing of other cell surface proteins, including a TNF receptor, the L-selectin adhesion molecule, and transforming growth factor-alpha (TGFalpha). The phenotype of mice lacking TACE suggests an essential role for soluble TGFalpha in normal development and emphasizes the importance of protein ectodomain shedding in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peschon, J J -- Slack, J L -- Reddy, P -- Stocking, K L -- Sunnarborg, S W -- Lee, D C -- Russell, W E -- Castner, B J -- Johnson, R S -- Fitzner, J N -- Boyce, R W -- Nelson, N -- Kozlosky, C J -- Wolfson, M F -- Rauch, C T -- Cerretti, D P -- Paxton, R J -- March, C J -- Black, R A -- CA43793/CA/NCI NIH HHS/ -- DK53804/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 13;282(5392):1281-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Corporation, Seattle, WA 98101, USA. peschon@immunex.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9812885" target="_blank"〉PubMed〈/a〉
    Keywords: ADAM Proteins ; Amino Acid Sequence ; Animals ; Catalytic Domain ; Cell Membrane/*metabolism ; Cells, Cultured ; Crosses, Genetic ; *Embryonic and Fetal Development ; L-Selectin/metabolism ; Ligands ; Membrane Proteins/*metabolism ; Metalloendopeptidases/chemistry/genetics/*metabolism ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; Phenotype ; Protein Processing, Post-Translational ; Receptors, Tumor Necrosis Factor/metabolism ; Transforming Growth Factor alpha/metabolism ; Tumor Necrosis Factor-alpha/*metabolism
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    Interaction of short-range repressors with Drosophila CtBP in the embryo (1998)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1998-04-29
    Description: Human CtBP attenuates transcriptional activation and tumorigenesis mediated by the adenovirus E1A protein. The E1A sequence motif that interacts with CtBP, Pro-X-Asp-Leu-Ser-X-Lys (P-DLS-K), is present in the repression domains of two unrelated short-range repressors in Drosophila, Knirps and Snail, and is essential for the interaction of these proteins with Drosophila CtBP (dCtBP). A P-element-induced mutation in dCtBP exhibits gene-dosage interactions with a null mutation in knirps, which is consistent with the occurrence of Knirps-dCtBP interactions in vivo. These observations suggest that CtBP and dCtBP are engaged in an evolutionarily conserved mechanism of transcriptional repression, which is used in both Drosophila and mammals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nibu, Y -- Zhang, H -- Levine, M -- GM46638/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Apr 3;280(5360):101-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Division of Genetics, 401 Barker Hall, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9525852" target="_blank"〉PubMed〈/a〉
    Keywords: Alcohol Oxidoreductases ; Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Cell Nucleus/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Drosophila/*embryology/genetics/metabolism ; *Drosophila Proteins ; Embryo, Nonmammalian/metabolism ; Female ; Gene Dosage ; *Gene Expression Regulation ; Genes, Insect ; Genes, Reporter ; Humans ; Insect Proteins/genetics/metabolism ; Male ; Molecular Sequence Data ; Mutation ; Phosphoproteins/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Repressor Proteins/chemistry/genetics/*metabolism ; *Transcription Factors ; *Transcription, Genetic
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    Membrane phospholipid control of nucleotide sensitivity of KATP channels (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-06
    Description: Adenosine triphosphate (ATP)-sensitive potassium (KATP) channels couple cell metabolism to electrical activity. Phosphatidylinositol phosphates (PIPs) profoundly antagonized ATP inhibition of KATP channels when applied to inside-out membrane patches. It is proposed that membrane-incorporated PIPs can bind to positive charges in the cytoplasmic region of the channel's Kir6.2 subunit, stabilizing the open state of the channel and antagonizing the inhibitory effect of ATP. The tremendous effect of PIPs on ATP sensitivity suggests that in vivo alterations of membrane PIP levels will have substantial effects on KATP channel activity and hence on the gain of metabolism-excitation coupling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shyng, S L -- Nichols, C G -- HL45742/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 6;282(5391):1138-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Physiology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9804554" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Adenosine Triphosphate/metabolism/*pharmacology ; Animals ; Binding Sites ; COS Cells ; Cell Line ; Islets of Langerhans/metabolism ; Mutation ; Myocardium/cytology/metabolism ; Patch-Clamp Techniques ; Phosphatidylinositol 4,5-Diphosphate/*metabolism/pharmacology ; Phosphatidylinositol Phosphates/*metabolism/pharmacology ; Potassium Channels/chemistry/genetics/*metabolism ; *Potassium Channels, Inwardly Rectifying ; Receptors, Drug/metabolism ; Recombinant Fusion Proteins/metabolism ; Sulfonylurea Receptors
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    Activation of the ATM kinase by ionizing radiation and phosphorylation of p53 (1998)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1998-09-11
    Description: The p53 tumor suppressor protein is activated and phosphorylated on serine-15 in response to various DNA damaging agents. The gene product mutated in ataxia telangiectasia, ATM, acts upstream of p53 in a signal transduction pathway initiated by ionizing radiation. Immunoprecipitated ATM had intrinsic protein kinase activity and phosphorylated p53 on serine-15 in a manganese-dependent manner. Ionizing radiation, but not ultraviolet radiation, rapidly enhanced this p53-directed kinase activity of endogenous ATM. These observations, along with the fact that phosphorylation of p53 on serine-15 in response to ionizing radiation is reduced in ataxia telangiectasia cells, suggest that ATM is a protein kinase that phosphorylates p53 in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Canman, C E -- Lim, D S -- Cimprich, K A -- Taya, Y -- Tamai, K -- Sakaguchi, K -- Appella, E -- Kastan, M B -- Siliciano, J D -- CA71387/CA/NCI NIH HHS/ -- ES05777/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 11;281(5383):1677-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Johns Hopkins School of Medicine, Oncology Center, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9733515" target="_blank"〉PubMed〈/a〉
    Keywords: Ataxia Telangiectasia Mutated Proteins ; Cell Cycle Proteins ; Cell Line ; DNA Damage ; DNA-Activated Protein Kinase ; *DNA-Binding Proteins ; Enzyme Activation ; Humans ; Lymphocytes/metabolism/radiation effects ; Mutation ; Nuclear Proteins ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Protein Kinases/*metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Proteins/genetics/*metabolism ; *Radiation, Ionizing ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism ; Signal Transduction ; Transfection ; Tumor Suppressor Protein p53/*metabolism ; Tumor Suppressor Proteins ; Ultraviolet Rays
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    Phytochromes and cryptochromes in the entrainment of the Arabidopsis circadian clock (1998)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1998-11-20
    Description: Circadian clocks are synchronized by environmental cues such as light. Photoreceptor-deficient Arabidopsis thaliana mutants were used to measure the effect of light fluence rate on circadian period in plants. Phytochrome B is the primary high-intensity red light photoreceptor for circadian control, and phytochrome A acts under low-intensity red light. Cryptochrome 1 and phytochrome A both act to transmit low-fluence blue light to the clock. Cryptochrome 1 mediates high-intensity blue light signals for period length control. The presence of cryptochromes in both plants and animals suggests that circadian input pathways have been conserved throughout evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Somers, D E -- Devlin, P F -- Kay, S A -- GM56006/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 20;282(5393):1488-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and National Science Foundation Center for Biological Timing, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92307, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9822379" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*physiology ; Arabidopsis Proteins ; Biological Clocks/*physiology ; Circadian Rhythm/*physiology ; Cryptochromes ; *Drosophila Proteins ; *Eye Proteins ; Flavoproteins/genetics/*physiology ; Light ; Mutation ; *Photoreceptor Cells ; *Photoreceptor Cells, Invertebrate ; Phytochrome/genetics/*physiology ; Phytochrome A ; Phytochrome B ; Plants, Genetically Modified ; Receptors, G-Protein-Coupled ; Signal Transduction ; *Transcription Factors
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    alpha-Synuclein gene and Parkinson's disease. The French Parkinson's Disease Study Group (1998)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1998-03-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1998 Feb 20;279(5354):1116-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9508681" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Chromosomes, Human, Pair 4 ; Female ; France ; Genes, Dominant ; Humans ; Italy ; Male ; Middle Aged ; Mutation ; Nerve Tissue Proteins/*genetics ; Parkinson Disease/*genetics ; Synucleins ; alpha-Synuclein
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    COI1: an Arabidopsis gene required for jasmonate-regulated defense and fertility (1998)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1998-06-06
    Description: The coi1 mutation defines an Arabidopsis gene required for response to jasmonates, which regulate defense against insects and pathogens, wound healing, and pollen fertility. The wild-type allele, COI1, was mapped to a 90-kilobase genomic fragment and located by complementation of coi1-1 mutants. The predicted amino acid sequence of the COI1 protein contains 16 leucine-rich repeats and an F-box motif. It has similarity to the F-box proteins Arabidopsis TIR1, human Skp2, and yeast Grr1, which appear to function by targeting repressor proteins for removal by ubiquitination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xie, D X -- Feys, B F -- James, S -- Nieto-Rostro, M -- Turner, J G -- New York, N.Y. -- Science. 1998 May 15;280(5366):1091-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9582125" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/pharmacology ; Amino Acid Sequence ; Arabidopsis/*genetics/growth & development/physiology ; *Arabidopsis Proteins ; Chromosome Mapping ; Cyclopentanes/*metabolism/pharmacology ; *Genes, Plant ; Genetic Complementation Test ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Oxylipins ; Plant Growth Regulators/*metabolism ; Plant Proteins/chemistry/*genetics/*physiology ; Plants, Genetically Modified ; Polymorphism, Genetic ; Repressor Proteins/metabolism ; Signal Transduction ; Transformation, Genetic ; Ubiquitins/metabolism
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    Role of the CLOCK protein in the mammalian circadian mechanism (1998)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1998-06-11
    Description: The mouse Clock gene encodes a bHLH-PAS protein that regulates circadian rhythms and is related to transcription factors that act as heterodimers. Potential partners of CLOCK were isolated in a two-hybrid screen, and one, BMAL1, was coexpressed with CLOCK and PER1 at known circadian clock sites in brain and retina. CLOCK-BMAL1 heterodimers activated transcription from E-box elements, a type of transcription factor-binding site, found adjacent to the mouse per1 gene and from an identical E-box known to be important for per gene expression in Drosophila. Mutant CLOCK from the dominant-negative Clock allele and BMAL1 formed heterodimers that bound DNA but failed to activate transcription. Thus, CLOCK-BMAL1 heterodimers appear to drive the positive component of per transcriptional oscillations, which are thought to underlie circadian rhythmicity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gekakis, N -- Staknis, D -- Nguyen, H B -- Davis, F C -- Wilsbacher, L D -- King, D P -- Takahashi, J S -- Weitz, C J -- New York, N.Y. -- Science. 1998 Jun 5;280(5369):1564-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, Boston MA 02115, USA. 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9616112" target="_blank"〉PubMed〈/a〉
    Keywords: ARNTL Transcription Factors ; Animals ; Basic Helix-Loop-Helix Transcription Factors ; Biological Clocks ; CLOCK Proteins ; Cell Cycle Proteins ; Circadian Rhythm/genetics/*physiology ; Cloning, Molecular ; Cricetinae ; DNA/metabolism ; Dimerization ; Feedback ; Gene Expression ; Helix-Loop-Helix Motifs ; Male ; Mesocricetus ; Mice ; Mutation ; Nuclear Proteins/*genetics/metabolism ; Period Circadian Proteins ; Promoter Regions, Genetic ; Retina/metabolism ; Suprachiasmatic Nucleus/metabolism ; Trans-Activators/genetics/*metabolism ; Transcription Factors/genetics/*metabolism ; *Transcriptional Activation
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    Single gene controls fruit fly life-span (1998)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1998-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1998 Oct 30;282(5390):856.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9841425" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/genetics ; Animals ; Caenorhabditis elegans Proteins ; Drosophila/*genetics/physiology ; *Drosophila Proteins ; GTP-Binding Proteins/chemistry/*genetics/metabolism/physiology ; *Genes, Insect ; Longevity/genetics ; Mutation ; Receptor, Insulin/genetics/physiology ; Receptors, Cell Surface/chemistry/*genetics/physiology ; *Receptors, G-Protein-Coupled ; Signal Transduction
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    Identification of a cullin homology region in a subunit of the anaphase-promoting complex (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: The anaphase-promoting complex is composed of eight protein subunits, including BimE (APC1), CDC27 (APC3), CDC16 (APC6), and CDC23 (APC8). The remaining four human APC subunits, APC2, APC4, APC5, and APC7, as well as human CDC23, were cloned. APC7 contains multiple copies of the tetratrico peptide repeat, similar to CDC16, CDC23, and CDC27. Whereas APC4 and APC5 share no similarity to proteins of known function, APC2 contains a region that is similar to a sequence in cullins, a family of proteins implicated in the ubiquitination of G1 phase cyclins and cyclin-dependent kinase inhibitors. The APC2 gene is essential in Saccharomyces cerevisiae, and apc2 mutants arrest at metaphase and are defective in the degradation of Pds1p. APC2 and cullins may be distantly related members of a ubiquitin ligase family that targets cell cycle regulators for degradation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, H -- Peters, J M -- King, R W -- Page, A M -- Hieter, P -- Kirschner, M W -- CA16519/CA/NCI NIH HHS/ -- GM26875-17/GM/NIGMS NIH HHS/ -- GM39023-08/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1219-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9469815" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Anaphase ; Anaphase-Promoting Complex-Cyclosome ; Animals ; Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome ; Apc2 Subunit, Anaphase-Promoting Complex-Cyclosome ; Apc4 Subunit, Anaphase-Promoting Complex-Cyclosome ; Apc5 Subunit, Anaphase-Promoting Complex-Cyclosome ; Apc7 Subunit, Anaphase-Promoting Complex-Cyclosome ; Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome ; Cell Cycle/*physiology ; Cell Cycle Proteins/chemistry ; Cloning, Molecular ; *Cullin Proteins ; Helminth Proteins/chemistry ; Humans ; Ligases/*chemistry/genetics/metabolism ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Phylogeny ; Proteins/chemistry ; Saccharomyces cerevisiae/chemistry/cytology/genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Alignment ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases
    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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    Training viruses to attack cancers (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1998 Nov 13;282(5392):1244-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9867627" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division ; Clinical Trials as Topic ; Combined Modality Therapy ; *Genes, p53 ; *Genes, ras ; Humans ; Mice ; Mutation ; Neoplasms/genetics/pathology/*therapy/virology ; *Virus Physiological Phenomena ; Virus Replication
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 141
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    The bare bones of catalysis (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stokstad, E -- New York, N.Y. -- Science. 1998 Mar 20;279(5358):1852.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9537901" target="_blank"〉PubMed〈/a〉
    Keywords: Catalysis ; Chorismate Mutase/*chemistry/genetics/*metabolism ; Dimerization ; *Directed Molecular Evolution ; Escherichia coli/genetics ; Mutation ; Protein Conformation ; *Protein Engineering ; Protein Structure, Secondary ; Selection, Genetic ; Staphylococcal Protein A/chemistry/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Jumbo gene offers clue to Parkinson's (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, M -- New York, N.Y. -- Science. 1998 Apr 10;280(5361):203.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9565530" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Mapping ; Chromosomes, Human, Pair 6/genetics ; Cloning, Molecular ; Humans ; *Ligases ; Mutation ; Parkinson Disease/*genetics/metabolism ; Proteins/chemistry/*genetics/physiology ; Substantia Nigra/metabolism ; *Ubiquitin-Protein Ligases
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 143
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    Docking phospholipase A2 on membranes using electrostatic potential-modulated spin relaxation magnetic resonance (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: A method involving electron paramagnetic resonance spectroscopy of a site-selectively spin-labeled peripheral membrane protein in the presence and absence of membranes and of a water-soluble spin relaxant (chromium oxalate) has been developed to determine how bee venom phospholipase A2 sits on the membrane. Theory based on the Poisson-Boltzmann equation shows that the rate of spin relaxation of a protein-bound nitroxide by a membrane-impermeant spin relaxant depends on the distance (up to tens of angstroms) from the spin probe to the membrane. The measurements define the interfacial binding surface of this secreted phospholipase A2.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3443684/" 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/PMC3443684/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, Y -- Nielsen, R -- Murray, D -- Hubbell, W L -- Mailer, C -- Robinson, B H -- Gelb, M H -- GM32681/GM/NIGMS NIH HHS/ -- HL36235/HL/NHLBI NIH HHS/ -- P30 ES07033/ES/NIEHS NIH HHS/ -- R01 CA052874/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 Mar 20;279(5358):1925-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Biochemistry, University of Washington, Box 351700, Seattle, WA 98195-1700, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9506941" target="_blank"〉PubMed〈/a〉
    Keywords: Bee Venoms/chemistry ; Binding Sites ; Chromates ; Electron Spin Resonance Spectroscopy ; *Glycerophospholipids ; Liposomes ; Membrane Proteins/analysis/*chemistry/genetics/metabolism ; *Membranes, Artificial ; Models, Molecular ; Mutation ; Oxalates ; Phosphatidic Acids ; Phospholipases A/analysis/*chemistry/genetics/metabolism ; Phospholipases A2 ; Spin Labels ; Surface Properties
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    A calcium sensor homolog required for plant salt tolerance (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-25
    Description: Excessive sodium (Na+) in salinized soils inhibits plant growth and development. A mutation in the SOS3 gene renders Arabidopsis thaliana plants hypersensitive to Na+-induced growth inhibition. SOS3 encodes a protein that shares significant sequence similarity with the calcineurin B subunit from yeast and neuronal calcium sensors from animals. The results suggest that intracellular calcium signaling through a calcineurin-like pathway mediates the beneficial effect of calcium on plant salt tolerance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, J -- Zhu, J K -- New York, N.Y. -- Science. 1998 Jun 19;280(5371):1943-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Sciences, University of Arizona, Tucson, AZ 85721, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9632394" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arabidopsis/*genetics/*growth & development/metabolism ; *Arabidopsis Proteins ; Binding Sites ; Calcineurin/chemistry ; Calcium/*metabolism/pharmacology ; Calcium-Binding Proteins/chemistry ; Chromosome Mapping ; Cloning, Molecular ; Genes, Plant ; Ion Transport ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Plant Proteins/*chemistry/*genetics ; Saccharomyces cerevisiae/chemistry ; Signal Transduction ; Sodium/metabolism/*pharmacology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 145
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    Regulation of flowering time by Arabidopsis photoreceptors (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: The shift in plants from vegetative growth to floral development is regulated by red-far-red light receptors (phytochromes) and blue-ultraviolet A light receptors (cryptochromes). A mutation in the Arabidopsis thaliana CRY2 gene encoding a blue-light receptor apoprotein (CRY2) is allelic to the late-flowering mutant, fha. Flowering in cry2/fha mutant plants is only incompletely responsive to photoperiod. Cryptochrome 2 (cry2) is a positive regulator of the flowering-time gene CO, the expression of which is regulated by photoperiod. Analysis of flowering in cry2 and phyB mutants in response to different wavelengths of light indicated that flowering is regulated by the antagonistic actions of phyB and cry2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guo, H -- Yang, H -- Mockler, T C -- Lin, C -- GM08375/GM/NIGMS NIH HHS/ -- GM56265/GM/NIGMS NIH HHS/ -- R01 GM056265/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Feb 27;279(5355):1360-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cell and Developmental Biology, and Molecular Biology Institute, University of California, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9478898" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*physiology ; *Arabidopsis Proteins ; Chromosome Mapping ; Cryptochromes ; DNA-Binding Proteins/genetics ; *Drosophila Proteins ; *Eye Proteins ; Flavoproteins/genetics/*physiology ; Gene Expression Regulation, Plant ; Genes, Plant ; *Light ; Molecular Sequence Data ; Mutation ; Photoperiod ; *Photoreceptor Cells ; *Photoreceptor Cells, Invertebrate ; Phytochrome/genetics/physiology ; Phytochrome A ; Phytochrome B ; Plant Proteins/genetics/*physiology ; Plants, Genetically Modified ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism ; Receptors, G-Protein-Coupled ; Transcription Factors/genetics
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  • 146
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    Molecular analysis of cellulose biosynthesis in Arabidopsis (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-21
    Description: Cellulose, an abundant, crystalline polysaccharide, is central to plant morphogenesis and to many industries. Chemical and ultrastructural analyses together with map-based cloning indicate that the RSW1 locus of Arabidopsis encodes the catalytic subunit of cellulose synthase. The cloned gene complements the rsw1 mutant whose temperature-sensitive allele is changed in one amino acid. The mutant allele causes a specific reduction in cellulose synthesis, accumulation of noncrystalline beta-1,4-glucan, disassembly of cellulose synthase, and widespread morphological abnormalities. Microfibril crystallization may require proper assembly of the RSW1 gene product into synthase complexes whereas glucan biosynthesis per se does not.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arioli, T -- Peng, L -- Betzner, A S -- Burn, J -- Wittke, W -- Herth, W -- Camilleri, C -- Hofte, H -- Plazinski, J -- Birch, R -- Cork, A -- Glover, J -- Redmond, J -- Williamson, R E -- New York, N.Y. -- Science. 1998 Jan 30;279(5351):717-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cooperative Research Centre for Plant Science, Australian National University, Post Office Box 475, Canberra, ACT 2601, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9445479" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/enzymology/*genetics/*metabolism ; *Arabidopsis Proteins ; Cell Membrane/chemistry/ultrastructure ; Cellulose/*biosynthesis/chemistry/genetics ; Chromosome Mapping ; Cloning, Molecular ; Crystallization ; Freeze Fracturing ; *Genes, Plant ; Genetic Complementation Test ; Glucans/metabolism ; Glucosyltransferases/chemistry/*genetics ; Molecular Sequence Data ; Mutation ; Plant Roots/chemistry/ultrastructure ; Plant Shoots/chemistry
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    High-resolution protein design with backbone freedom (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-20
    Description: Recent advances in computational techniques have allowed the design of precise side-chain packing in proteins with predetermined, naturally occurring backbone structures. Because these methods do not model protein main-chain flexibility, they lack the breadth to explore novel backbone conformations. Here the de novo design of a family of alpha-helical bundle proteins with a right-handed superhelical twist is described. In the design, the overall protein fold was specified by hydrophobic-polar residue patterning, whereas the bundle oligomerization state, detailed main-chain conformation, and interior side-chain rotamers were engineered by computational enumerations of packing in alternate backbone structures. Main-chain flexibility was incorporated through an algebraic parameterization of the backbone. The designed peptides form alpha-helical dimers, trimers, and tetramers in accord with the design goals. The crystal structure of the tetramer matches the designed structure in atomic detail.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harbury, P B -- Plecs, J J -- Tidor, B -- Alber, T -- Kim, P S -- GM44162/GM/NIGMS NIH HHS/ -- GM48598/GM/NIGMS NIH HHS/ -- GM55758/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 20;282(5393):1462-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Howard Hughes Medical Institute and Department of Biology, Massachusetts Institute of Technology, Nine Cambridge Center, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9822371" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Circular Dichroism ; Computer Simulation ; Crystallography, X-Ray ; Dimerization ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Peptides/chemical synthesis/*chemistry ; *Protein Conformation ; Protein Denaturation ; *Protein Engineering ; *Protein Folding ; Protein Structure, Secondary ; Proteins/chemical synthesis/*chemistry ; Thermodynamics
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  • 148
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    Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-11
    Description: The tumor suppressor PTEN is a phosphatase with sequence similarity to the cytoskeletal protein tensin. Here the cellular roles of PTEN were investigated. Overexpression of PTEN inhibited cell migration, whereas antisense PTEN enhanced migration. Integrin-mediated cell spreading and the formation of focal adhesions were down-regulated by wild-type PTEN but not by PTEN with an inactive phosphatase domain. PTEN interacted with the focal adhesion kinase FAK and reduced its tyrosine phosphorylation. Overexpression of FAK partially antagonized the effects of PTEN. Thus, PTEN phosphatase may function as a tumor suppressor by negatively regulating cell interactions with the extracellular matrix.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tamura, M -- Gu, J -- Matsumoto, K -- Aota, S -- Parsons, R -- Yamada, K M -- New York, N.Y. -- Science. 1998 Jun 5;280(5369):1614-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Craniofacial Developmental Biology and Regeneration Branch, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892-4370, USA. mtamura@yoda.nidr.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9616126" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; *Cell Adhesion ; Cell Adhesion Molecules/metabolism ; Cell Line ; *Cell Movement ; Cell Size ; Concanavalin A ; Down-Regulation ; Ecdysone/pharmacology ; Fibronectins ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; Genes, Tumor Suppressor ; Humans ; Integrins/physiology ; Mice ; Mutation ; PTEN Phosphohydrolase ; *Phosphoric Monoester Hydrolases ; Phosphorylation ; Polylysine ; Protein Tyrosine Phosphatases/genetics/metabolism/pharmacology/*physiology ; Protein-Tyrosine Kinases/metabolism ; Recombinant Proteins/pharmacology ; Signal Transduction ; Transfection ; Tumor Cells, Cultured ; *Tumor Suppressor Proteins
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    Rad53 FHA domain associated with phosphorylated Rad9 in the DNA damage checkpoint (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-10
    Description: The Rad53 protein kinase of Saccharomyces cerevisiae is required for checkpoints that prevent cell division in cells with damaged or incompletely replicated DNA. The Rad9 protein was phosphorylated in response to DNA damage, and phosphorylated Rad9 interacted with the COOH-terminal forkhead homology-associated (FHA) domain of Rad53. Inactivation of this domain abolished DNA damage-dependent Rad53 phosphorylation, G2/M cell cycle phase arrest, and increase of RNR3 transcription but did not affect replication inhibition-dependent Rad53 phosphorylation. Thus, Rad53 integrates DNA damage signals by coupling with phosphorylated Rad9. The hitherto uncharacterized FHA domain appears to be a modular protein-binding domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sun, Z -- Hsiao, J -- Fay, D S -- Stern, D F -- New York, N.Y. -- Science. 1998 Jul 10;281(5374):272-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Yale University, New Haven, CT 06511, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9657725" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Cell Cycle Proteins ; Checkpoint Kinase 2 ; *DNA Damage ; DNA Replication/drug effects ; Fungal Proteins/*metabolism ; G2 Phase ; Hydroxyurea/pharmacology ; Methyl Methanesulfonate/pharmacology ; Mitosis ; Mutation ; Oligopeptides ; Peptides ; Phosphorylation ; Protein Kinases/chemistry/genetics/*metabolism ; *Protein-Serine-Threonine Kinases ; Saccharomyces cerevisiae/cytology/*metabolism ; *Saccharomyces cerevisiae Proteins ; Transcription, Genetic
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    Impairment of mycobacterial immunity in human interleukin-12 receptor deficiency (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: In humans, interferon gamma (IFN-gamma) receptor deficiency leads to a predisposition to mycobacterial infections and impairs the formation of mature granulomas. Interleukin-12 (IL-12) receptor deficiency was found in otherwise healthy individuals with mycobacterial infections. Mature granulomas were seen, surrounded by T cells and centered with epithelioid and multinucleated giant cells, yet reduced IFN-gamma concentrations were found to be secreted by activated natural killer and T cells. Thus, IL-12-dependent IFN-gamma secretion in humans seems essential in the control of mycobacterial infections, despite the formation of mature granulomas due to IL-12-independent IFN-gamma secretion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altare, F -- Durandy, A -- Lammas, D -- Emile, J F -- Lamhamedi, S -- Le Deist, F -- Drysdale, P -- Jouanguy, E -- Doffinger, R -- Bernaudin, F -- Jeppsson, O -- Gollob, J A -- Meinl, E -- Segal, A W -- Fischer, A -- Kumararatne, D -- Casanova, J L -- New York, N.Y. -- Science. 1998 May 29;280(5368):1432-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INSERM U429, Hopital Necker-Enfants Malades, Paris 75015, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9603732" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cytotoxicity, Immunologic ; Female ; Granuloma/immunology ; Humans ; Hypersensitivity, Delayed ; Interferon-gamma/biosynthesis/immunology/secretion ; Interleukin-12/*immunology ; Killer Cells, Natural/immunology ; Lymphocyte Activation ; Male ; Mice ; Mice, Knockout ; Mutation ; Mycobacterium avium-intracellulare Infection/*immunology ; *Mycobacterium bovis ; Pedigree ; Receptors, Interferon/genetics/immunology ; Receptors, Interleukin/deficiency/*genetics ; Receptors, Interleukin-12 ; T-Lymphocytes/immunology ; Tuberculosis/*immunology
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  • 151
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    Dimerization-induced inhibition of receptor protein tyrosine phosphatase function through an inhibitory wedge (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-24
    Description: The function and regulation of the receptorlike transmembrane protein tyrosine phosphatases (RPTPs) are not well understood. Ligand-induced dimerization inhibited the function of the epidermal growth factor receptor (EGFR)-RPTP CD45 chimera (EGFR-CD45) in T cell signal transduction. Properties of mutated EGFR-CD45 chimeras supported a general model for the regulation of RPTPs, derived from the crystal structure of the RPTPalpha membrane-proximal phosphatase domain. The phosphatase domain apparently forms a symmetrical dimer in which the catalytic site of one molecule is blocked by specific contacts with a wedge from the other.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Majeti, R -- Bilwes, A M -- Noel, J P -- Hunter, T -- Weiss, A -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):88-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of California, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417031" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD45/chemistry/*metabolism ; Binding Sites ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Dimerization ; Epidermal Growth Factor/metabolism/pharmacology ; Humans ; Ligands ; Lymphocyte Activation ; Mutation ; Phosphorylation ; Protein Tyrosine Phosphatases/*antagonists & inhibitors/chemistry/metabolism ; Protein-Tyrosine Kinases/metabolism ; Receptor, Epidermal Growth Factor/chemistry/metabolism ; Receptors, Antigen, T-Cell/metabolism ; Recombinant Fusion Proteins/antagonists & inhibitors/chemistry/metabolism ; Signal Transduction ; T-Lymphocytes/immunology/*metabolism ; Tumor Cells, Cultured ; ZAP-70 Protein-Tyrosine Kinase
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    Boundary formation in Drosophila wing: Notch activity attenuated by the POU protein Nubbin (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-17
    Description: Cell interactions mediated by Notch-family receptors have been implicated in the specification of tissue boundaries in vertebrate and insect development. Although Notch ligands are often widely expressed, tightly localized activation of Notch is critical for the formation of sharp boundaries. Evidence is presented here that the POU domain protein Nubbin contributes to the formation of a sharp dorsoventral boundary in the Drosophila wing. Nubbin represses Notch-dependent target genes and sets a threshold for Notch activity that defines the spatial domain of boundary-specific gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neumann, C J -- Cohen, S M -- New York, N.Y. -- Science. 1998 Jul 17;281(5375):409-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9665883" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium-Binding Proteins ; Drosophila/genetics/*growth & development/metabolism ; *Drosophila Proteins ; Enhancer Elements, Genetic ; *Gene Expression Regulation ; Genes, Insect ; Homeodomain Proteins/genetics/metabolism/*physiology ; Insect Proteins/genetics/physiology ; Intercellular Signaling Peptides and Proteins ; Intracellular Signaling Peptides and Proteins ; Ligands ; Membrane Proteins/genetics/*physiology ; Mutation ; *N-Acetylglucosaminyltransferases ; Nuclear Proteins/genetics/physiology ; POU Domain Factors ; Proto-Oncogene Proteins/genetics/physiology ; Receptors, Notch ; Signal Transduction ; Transcription Factors/genetics/metabolism/*physiology ; Wings, Animal/*growth & development/metabolism ; Wnt1 Protein
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Limitations of a molecular clock applied to considerations of the origin of HIV-1 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Korber, B -- Theiler, J -- Wolinsky, S -- 3-Y01-AI-70001-13/AI/NIAID NIH HHS/ -- R01-HD-31756/HD/NICHD NIH HHS/ -- Y1-A1-4058-03/PHS HHS/ -- etc. -- New York, N.Y. -- Science. 1998 Jun 19;280(5371):1868-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Theoretical Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9669945" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines ; Disease Progression ; *Evolution, Molecular ; Gene Products, env/chemistry/genetics ; Genetic Variation ; Genome, Viral ; HIV Envelope Protein gp120/chemistry/genetics ; HIV Infections/*virology ; HIV-1/chemistry/classification/*genetics ; Humans ; Mutation ; Peptide Fragments/chemistry/genetics ; *Phylogeny ; Recombination, Genetic ; Selection, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 154
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    Regulation of cell death protease caspase-9 by phosphorylation (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-13
    Description: Caspases are intracellular proteases that function as initiators and effectors of apoptosis. The kinase Akt and p21-Ras, an Akt activator, induced phosphorylation of pro-caspase-9 (pro-Casp9) in cells. Cytochrome c-induced proteolytic processing of pro-Casp9 was defective in cytosolic extracts from cells expressing either active Ras or Akt. Akt phosphorylated recombinant Casp9 in vitro on serine-196 and inhibited its protease activity. Mutant pro-Casp9(Ser196Ala) was resistant to Akt-mediated phosphorylation and inhibition in vitro and in cells, resulting in Akt-resistant induction of apoptosis. Thus, caspases can be directly regulated by protein phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cardone, M H -- Roy, N -- Stennicke, H R -- Salvesen, G S -- Franke, T F -- Stanbridge, E -- Frisch, S -- Reed, J C -- CA-69381/CA/NCI NIH HHS/ -- CA-69515/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 13;282(5392):1318-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program on Apoptosis and Cell Death Research, The Burnham Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9812896" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; Caspase 9 ; Caspase Inhibitors ; Caspases/*metabolism ; Cell Line ; Cytochrome c Group/pharmacology ; Enzyme Precursors/metabolism ; Humans ; Mass Spectrometry ; Mutation ; Peptide Fragments/metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; Proto-Oncogene Proteins p21(ras)/metabolism ; Recombinant Fusion Proteins/metabolism ; Transfection
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    Transcription factor-specific requirements for coactivators and their acetyltransferase functions (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-21
    Description: Different classes of mammalian transcription factors-nuclear receptors, cyclic adenosine 3',5'-monophosphate-regulated enhancer binding protein (CREB), and signal transducer and activator of transcription-1 (STAT-1)-functionally require distinct components of the coactivator complex, including CREB-binding protein (CBP/p300), nuclear receptor coactivators (NCoAs), and p300/CBP-associated factor (p/CAF), based on their platform or assembly properties. Retinoic acid receptor, CREB, and STAT-1 also require different histone acetyltransferase (HAT) activities to activate transcription. Thus, transcription factor-specific differences in configuration and content of the coactivator complex dictate requirements for specific acetyltransferase activities, providing an explanation, at least in part, for the presence of multiple HAT components of the complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Korzus, E -- Torchia, J -- Rose, D W -- Xu, L -- Kurokawa, R -- McInerney, E M -- Mullen, T M -- Glass, C K -- Rosenfeld, M G -- New York, N.Y. -- Science. 1998 Jan 30;279(5351):703-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California San Diego (UCSD), 9500 Gilman Drive, La Jolla, CA 92093-0648, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9445475" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/genetics/*metabolism ; CREB-Binding Protein ; Cell Cycle Proteins/genetics/*metabolism ; Cyclic AMP/metabolism ; Cyclic AMP Response Element-Binding Protein/metabolism ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation ; HeLa Cells ; Histone Acetyltransferases ; Humans ; Ligands ; Mutation ; Nuclear Proteins/*metabolism ; Nuclear Receptor Co-Repressor 1 ; Nuclear Receptor Coactivator 1 ; Nuclear Receptor Coactivator 3 ; Promoter Regions, Genetic ; Receptors, Retinoic Acid/metabolism ; Repressor Proteins/metabolism ; STAT1 Transcription Factor ; *Saccharomyces cerevisiae Proteins ; Trans-Activators/metabolism ; Transcription Factors/genetics/*metabolism ; *Transcription, Genetic ; Transcriptional Activation ; p300-CBP Transcription Factors
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    C1 transfer enzymes and coenzymes linking methylotrophic bacteria and methanogenic Archaea (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-04
    Description: Methanogenic and sulfate-reducing Archaea are considered to have an energy metabolism involving C1 transfer coenzymes and enzymes unique for this group of strictly anaerobic microorganisms. An aerobic methylotrophic bacterium, Methylobacterium extorquens AM1, was found to contain a cluster of genes that are predicted to encode some of these enzymes and was shown to contain two of the enzyme activities and one of the methanogenic coenzymes. Insertion mutants were all unable to grow on C1 compounds, suggesting that the archaeal enzymes function in aerobic C1 metabolism. Thus, methylotrophy and methanogenesis involve common genes that cross the bacterial/archaeal boundaries.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chistoserdova, L -- Vorholt, J A -- Thauer, R K -- Lidstrom, M E -- GM36296/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jul 3;281(5373):99-102.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9651254" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aminohydrolases/chemistry/genetics/isolation & purification/*metabolism ; Biological Evolution ; Escherichia coli/enzymology/genetics ; Euryarchaeota/*enzymology/genetics ; Genes, Archaeal ; Genes, Bacterial ; Gram-Negative Aerobic Rods and Cocci/*enzymology/genetics ; Hydroxymethyl and Formyl Transferases/chemistry/genetics/isolation & ; purification/*metabolism ; Methanol/metabolism ; Molecular Sequence Data ; Mutation ; NAD/metabolism ; NADP/metabolism ; Oxidation-Reduction ; Pterins/chemistry/isolation & purification/*metabolism ; Sequence Alignment ; Succinic Acid/metabolism ; Transformation, Bacterial
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    Role of farnesyltransferase in ABA regulation of guard cell anion channels and plant water loss (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-09
    Description: Desiccation of plants during drought can be detrimental to agricultural production. The phytohormone abscisic acid (ABA) reduces water loss by triggering stomatal pore closure in leaves, a process requiring ion-channel modulation by cytoplasmic proteins. Deletion of the Arabidopsis farnesyltransferase gene ERA1 or application of farnesyltransferase inhibitors resulted in ABA hypersensitivity of guard cell anion-channel activation and of stomatal closing. ERA1 was expressed in guard cells. Double-mutant analyses of era1 with the ABA-insensitive mutants abi1 and abi2 showed that era1 suppresses the ABA-insensitive phenotypes. Moreover, era1 plants exhibited a reduction in transpirational water loss during drought treatment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pei, Z M -- Ghassemian, M -- Kwak, C M -- McCourt, P -- Schroeder, J I -- New York, N.Y. -- Science. 1998 Oct 9;282(5387):287-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Center for Molecular Genetics, University of California, San Diego, La Jolla, CA 92093-0116, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9765153" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid/*metabolism/pharmacology ; Alkyl and Aryl Transferases/antagonists & inhibitors/genetics/*metabolism ; Anions ; Arabidopsis/cytology/genetics/*metabolism ; *Arabidopsis Proteins ; Enzyme Inhibitors/pharmacology ; Farnesol/analogs & derivatives/pharmacology ; Gene Deletion ; Gene Expression ; Genes, Plant ; Ion Channels/*metabolism ; Mutation ; Organophosphonates/pharmacology ; Patch-Clamp Techniques ; Phosphoprotein Phosphatases/genetics/metabolism ; Plant Leaves/cytology/genetics/metabolism ; Plants, Genetically Modified ; Polyenes/pharmacology ; Polyunsaturated Alkamides ; Protein Prenylation ; Signal Transduction ; Water/*metabolism
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    Alopecia universalis associated with a mutation in the human hairless gene (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-21
    Description: There are several forms of hereditary human hair loss, known collectively as alopecias, the molecular bases of which are entirely unknown. A kindred with a rare, recessively inherited type of alopecia universalis was used to search for a locus by homozygosity mapping, and linkage was established in a 6-centimorgan interval on chromosome 8p12 (the logarithm of the odds favoring linkage score was 6.19). The human homolog of a murine gene, hairless, was localized in this interval by radiation hybrid mapping, and a missense mutation was found in affected individuals. Human hairless encodes a putative single zinc finger transcription factor protein with restricted expression in the brain and skin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ahmad, W -- Faiyaz ul Haque, M -- Brancolini, V -- Tsou, H C -- ul Haque, S -- Lam, H -- Aita, V M -- Owen, J -- deBlaquiere, M -- Frank, J -- Cserhalmi-Friedman, P B -- Leask, A -- McGrath, J A -- Peacocke, M -- Ahmad, M -- Ott, J -- Christiano, A M -- HG-00008/HG/NHGRI NIH HHS/ -- P30AR44535/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 30;279(5351):720-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Dermatology, Columbia University, 630 West 168 Street, VC-15-526, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9445480" target="_blank"〉PubMed〈/a〉
    Keywords: Alopecia/*genetics ; Amino Acid Sequence ; Animals ; Brain/metabolism ; Chromosome Mapping ; Chromosomes, Human, Pair 8 ; DNA-Binding Proteins/genetics ; Female ; Forkhead Transcription Factors ; Gene Expression ; Genes, Recessive ; Homozygote ; Humans ; Male ; Mice ; Mice, Hairless/genetics ; Microsatellite Repeats ; Molecular Sequence Data ; Mutation ; Pedigree ; Proteins/chemistry/*genetics ; Rats ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; Skin/metabolism ; Transcription Factors/genetics ; *Zinc Fingers
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    Extended life-span and stress resistance in the Drosophila mutant methuselah (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-30
    Description: Toward a genetic dissection of the processes involved in aging, a screen for gene mutations that extend life-span in Drosophila melanogaster was performed. The mutant line methuselah (mth) displayed approximately 35 percent increase in average life-span and enhanced resistance to various forms of stress, including starvation, high temperature, and dietary paraquat, a free-radical generator. The mth gene predicted a protein with homology to several guanosine triphosphate-binding protein-coupled seven-transmembrane domain receptors. Thus, the organism may use signal transduction pathways to modulate stress response and life-span.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, Y J -- Seroude, L -- Benzer, S -- AG12289/AG/NIA NIH HHS/ -- EY09278/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 30;282(5390):943-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9794765" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Base Sequence ; Cloning, Molecular ; DNA Transposable Elements ; *Drosophila Proteins ; Drosophila melanogaster/*genetics/*physiology ; Female ; Food Deprivation ; GTP-Binding Proteins/chemistry/*genetics/metabolism/physiology ; *Genes, Insect ; Hot Temperature ; Insecticide Resistance ; Longevity/genetics ; Male ; Molecular Sequence Data ; Mutation ; Oxidative Stress ; Paraquat/pharmacology ; Receptors, Cell Surface/chemistry/*genetics/metabolism/physiology ; *Receptors, G-Protein-Coupled ; Signal Transduction
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    New gene found for inherited macular degeneration (1998)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1998-07-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1998 Jul 3;281(5373):31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9679014" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Chloride Channels ; Chromosome Mapping ; *Chromosomes, Human, Pair 11 ; Eye Proteins/*genetics ; Gene Expression ; Humans ; Macular Degeneration/*genetics/metabolism ; Mutation ; Pigment Epithelium of Eye/metabolism ; Sweden
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  • 161
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    Maternal control of embryogenesis by MEDEA, a polycomb group gene in Arabidopsis (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-09
    Description: The gametophytic maternal effect mutant medea (mea) shows aberrant growth regulation during embryogenesis in Arabidopsis thaliana. Embryos derived from mea eggs grow excessively and die during seed desiccation. Embryo lethality is independent of the paternal contribution and gene dosage. The mea phenotype is consistent with the parental conflict theory for the evolution of parent-of-origin-specific effects. MEA encodes a SET domain protein similar to Enhancer of zeste, a member of the Polycomb group. In animals, Polycomb group proteins ensure the stable inheritance of expression patterns through cell division and regulate the control of cell proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grossniklaus, U -- Vielle-Calzada, J P -- Hoeppner, M A -- Gagliano, W B -- New York, N.Y. -- Science. 1998 Apr 17;280(5362):446-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, 1 Bungtown Road, Post Office Box 100, Cold Spring Harbor, NY 11724, USA. grossnik@cshl.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9545225" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Arabidopsis/*embryology/*genetics ; *Arabidopsis Proteins ; Cell Division ; Cloning, Molecular ; Crosses, Genetic ; *Drosophila Proteins ; Gene Dosage ; *Gene Expression Regulation, Plant ; Genes, Plant ; Insect Proteins/genetics ; Molecular Sequence Data ; Morphogenesis ; Mutation ; Nuclear Proteins/chemistry/genetics ; Plant Proteins/chemistry/*genetics/physiology ; Polycomb Repressive Complex 1 ; Polycomb Repressive Complex 2 ; *Repressor Proteins ; Seeds/genetics/growth & development ; Sequence Alignment
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    The search for human obesity genes (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: Understanding of the genetic influences on obesity has increased at a tremendous rate in recent years. By some estimates, 40 to 70 percent of the variation in obesity-related phenotypes in humans is heritable. Although several single-gene mutations have been shown to cause obesity in animal models, the situation in humans is considerably more complex. The most common forms of human obesity arise from the interactions of multiple genes, environmental factors, and behavior, and this complex etiology makes the search for obesity genes especially challenging. This article discusses the strategies currently being used to search for human obesity genes and recent promising results from these efforts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Comuzzie, A G -- Allison, D B -- DK47256/DK/NIDDK NIH HHS/ -- HL28972/HL/NHLBI NIH HHS/ -- HL45522/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 May 29;280(5368):1374-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Southwest Foundation for Biomedical Research, P.O. Box 760549, San Antonio, TX 78245-0549, USA. agcom@darwin.sfbr.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9603720" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; Ethnic Groups ; *Genes ; Genetic Predisposition to Disease ; *Genetic Techniques ; Genetic Testing ; Humans ; Mutation ; Obesity/*genetics ; Phenotype ; Sampling Studies
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    Genetic classification of primary neurodegenerative disease (1998)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1998-11-06
    Description: Review During the past 10 years (the "decade of the brain"), some of the genetic causes of many of the primary neurodegenerative diseases, which include Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis, prion disease, and many ataxic syndromes, have been found. These breakthroughs mean that for many of these diseases we now know the initiating trigger as well as the final outcome. These diseases have many pathological mechanisms in common, and there may be relatively few pathways to neuronal death seen in these disorders. Thus, treatment strategies developed for a particular disease may be found to have efficacy in more than one disorder.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hardy, J -- Gwinn-Hardy, K -- New York, N.Y. -- Science. 1998 Nov 6;282(5391):1075-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Mayo Clinic Jacksonville, Jacksonville, FL 32224, USA. hardy@mayo.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9804538" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/classification/genetics/pathology ; Brain/pathology ; Genes, Dominant ; Humans ; Mutation ; Nerve Tissue Proteins/genetics ; Neurodegenerative Diseases/*classification/*genetics/pathology ; Parkinson Disease/classification/genetics/pathology ; Peptides/genetics/metabolism ; Synucleins ; Trinucleotide Repeats ; tau Proteins/genetics
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    The battle over BRCA1 goes to court; BRCA2 may be next (1998)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1998-01-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1997 Dec 12;278(5345):1874.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417630" target="_blank"〉PubMed〈/a〉
    Keywords: BRCA2 Protein ; Breast Neoplasms/*genetics ; Consensus Sequence ; Female ; *Genes, BRCA1 ; Genetic Predisposition to Disease ; Genetic Testing/legislation & jurisprudence ; Humans ; Mutation ; Neoplasm Proteins/*genetics ; Ovarian Neoplasms/genetics ; *Patents as Topic ; Transcription Factors/*genetics ; United States
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  • 165
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    Inhibitory function of p21Cip1/WAF1 in differentiation of primary mouse keratinocytes independent of cell cycle control (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-06
    Description: The cyclin-dependent kinase inhibitor p21(Cip1/WAF1) has been implicated as an inducer of differentiation. However, although expression of p21 is increased in postmitotic cells immediately adjacent to the proliferative compartment, its expression is decreased in cells further along the differentiation program. Expression of the p21 protein was decreased in terminally differentiated primary keratinocytes of mice, and this occurred by a proteasome-dependent pathway. Forced expression of p21 in these cells inhibited the expression of markers of terminal differentiation at both the protein and messenger RNA levels. These inhibitory effects on differentiation were not observed with a carboxyl-terminal truncation mutant or with the unrelated cyclin-dependent kinase inhibitor p16(INK4a), although all these molecules exerted similar inhibition of cell growth. These findings reveal an inhibitory role of p21 in the late stages of differentiation that does not result from the effects of p21 on the cell cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Di Cunto, F -- Topley, G -- Calautti, E -- Hsiao, J -- Ong, L -- Seth, P K -- Dotto, G P -- AR39190/AR/NIAMS NIH HHS/ -- CA16038/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 May 15;280(5366):1069-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cutaneous Biology Research Center, Massachusetts General Hospital and Harvard Medical School, 13th Street, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9582119" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcysteine/analogs & derivatives/pharmacology ; Adenoviridae/genetics/physiology ; Animals ; Animals, Newborn ; *Cell Cycle ; *Cell Differentiation ; Cells, Cultured ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclin-Dependent Kinases/antagonists & inhibitors/metabolism ; Cyclins/genetics/*metabolism ; Enzyme Inhibitors/metabolism ; Gene Expression Regulation ; Keratinocytes/*cytology/metabolism/virology ; Leupeptins/pharmacology ; Membrane Proteins/biosynthesis/genetics ; Mice ; Mutation ; Promoter Regions, Genetic ; Protein Precursors/biosynthesis/genetics ; RNA, Messenger/genetics/metabolism ; Succinates/pharmacology ; Transfection
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  • 166
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    Monoallelic expression of the interleukin-2 locus (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: The lymphokine interleukin-2 (IL-2) is responsible for autocrine cell cycle progression and regulation of immune responses. Uncontrolled secretion of IL-2 results in adverse reactions ranging from anergy, to aberrant T cell activation, to autoimmunity. With the use of fluorescent in situ hybridization and single-cell polymerase chain reaction in cells with different IL-2 alleles, IL-2 expression in mature thymocytes and T cells was found to be tightly controlled by monoallelic expression. Because IL-2 is encoded at a nonimprinted autosomal locus, this result represents an unusual regulatory mode for controlling the precise expression of a single gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hollander, G A -- Zuklys, S -- Morel, C -- Mizoguchi, E -- Mobisson, K -- Simpson, S -- Terhorst, C -- Wishart, W -- Golan, D E -- Bhan, A K -- Burakoff, S J -- P01 CA39542-09/CA/NCI NIH HHS/ -- R01 AI17258-18/AI/NIAID NIH HHS/ -- R01 DK47677/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 Mar 27;279(5359):2118-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pediatric Immunology, Department of Research and Children's Hospital, Basel University Medical School, 4031 Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9516115" target="_blank"〉PubMed〈/a〉
    Keywords: *Alleles ; Animals ; CD4-Positive T-Lymphocytes/cytology/*immunology ; Concanavalin A/pharmacology ; DNA Replication ; Female ; Flow Cytometry ; *Gene Expression Regulation ; Heterozygote ; In Situ Hybridization, Fluorescence ; Interleukin-2/biosynthesis/*genetics ; Lymphocyte Activation ; Male ; Mice ; Mice, Inbred C57BL ; Muridae ; Mutation ; Polymerase Chain Reaction ; S Phase ; Transcription, Genetic
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  • 167
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    Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-30
    Description: A combinatorial disulfide cross-linking strategy was used to prepare a stalled complex of human immunodeficiency virus-type 1 (HIV-1) reverse transcriptase with a DNA template:primer and a deoxynucleoside triphosphate (dNTP), and the crystal structure of the complex was determined at a resolution of 3.2 angstroms. The presence of a dideoxynucleotide at the 3'-primer terminus allows capture of a state in which the substrates are poised for attack on the dNTP. Conformational changes that accompany formation of the catalytic complex produce distinct clusters of the residues that are altered in viruses resistant to nucleoside analog drugs. The positioning of these residues in the neighborhood of the dNTP helps to resolve some long-standing puzzles about the molecular basis of resistance. The resistance mutations are likely to influence binding or reactivity of the inhibitors, relative to normal dNTPs, and the clustering of the mutations correlates with the chemical structure of the drug.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, H -- Chopra, R -- Verdine, G L -- Harrison, S C -- GM-18621/GM/NIGMS NIH HHS/ -- GM-39589/GM/NIGMS NIH HHS/ -- GM-44853/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 27;282(5394):1669-75.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9831551" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-HIV Agents/metabolism/*pharmacology ; Binding Sites ; Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; DNA Primers/chemistry/metabolism ; DNA, Viral/chemistry/metabolism ; Deoxyribonucleotides/chemistry/metabolism ; Dimerization ; Drug Resistance, Microbial ; HIV Reverse Transcriptase/*chemistry/genetics/metabolism ; HIV-1/*drug effects/enzymology ; Humans ; Hydrogen Bonding ; Models, Molecular ; Mutation ; Nucleic Acid Conformation ; Protein Conformation ; Reverse Transcriptase Inhibitors/metabolism/*pharmacology ; Templates, Genetic
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  • 168
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    Systems for identifying new drugs are often faulty (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gura, T -- New York, N.Y. -- Science. 1997 Nov 7;278(5340):1041-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381203" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antineoplastic Agents/*therapeutic use ; Disease Models, Animal ; *Drug Screening Assays, Antitumor ; Genes, Tumor Suppressor/genetics ; Humans ; Mice ; Mice, Knockout ; Mice, Mutant Strains ; Mutation ; Neoplasm Transplantation ; Neoplasms/*drug therapy/genetics ; Oncogenes/genetics ; Transplantation, Heterologous ; Tumor Cells, Cultured ; *Tumor Stem Cell Assay
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 169
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    Is apoptosis key in Alzheimer's disease? (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1998 Aug 28;281(5381):1303-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9735049" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/metabolism/*pathology ; Amyloid beta-Peptides/biosynthesis/physiology ; *Apoptosis ; Brain/metabolism/*pathology ; Cells, Cultured ; Cysteine Endopeptidases/metabolism ; DNA Fragmentation ; Humans ; Membrane Proteins/genetics/physiology ; Mutation ; Neurons/metabolism/*pathology ; Presenilin-1 ; Presenilin-2
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 170
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    Positive selection through a motif in the alphabeta T cell receptor (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-07
    Description: The two lineages of T cells, alphabeta and gammadelta, differ in their developmental requirements: only alphabeta T cells require major histocompatibility complex recognition, a process known as positive selection. The alphabeta T cell receptor (TCR), but not its gammadelta counterpart, contains a motif within the alpha-chain connecting peptide domain (alpha-CPM) that has been conserved over the last 500 million years. In transgenic mice expressing an alphabeta TCR lacking the alpha-CPM, thymocytes were blocked in positive selection but could undergo negative selection. Thus, the alpha-CPM seems to participate in the generation of signals required for positive selection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Backstrom, B T -- Muller, U -- Hausmann, B -- Palmer, E -- New York, N.Y. -- Science. 1998 Aug 7;281(5378):835-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Basel Institute for Immunology, CH-4005 Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9694657" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigen-Presenting Cells/immunology ; Antigens, CD3/analysis ; CD4-Positive T-Lymphocytes/immunology ; Cell Lineage ; Cells, Cultured ; Histocompatibility Antigens Class II/immunology ; Ligands ; Lymphocyte Count ; Membrane Proteins/analysis ; Mice ; Mice, Inbred C57BL ; Mice, Nude ; Mice, Transgenic ; Molecular Sequence Data ; Mutation ; Receptor-CD3 Complex, Antigen, T-Cell/immunology/metabolism ; Receptors, Antigen, T-Cell/analysis ; Receptors, Antigen, T-Cell, alpha-beta/*chemistry/genetics/*immunology ; Signal Transduction ; T-Lymphocyte Subsets/*immunology ; Thymus Gland/immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 171
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    Cell surface trafficking of Fas: a rapid mechanism of p53-mediated apoptosis (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-09
    Description: p53 acts as a tumor suppressor by inducing both growth arrest and apoptosis. p53-induced apoptosis can occur without new RNA synthesis through an unknown mechanism. In human vascular smooth muscle cells, p53 activation transiently increased surface Fas (CD95) expression by transport from the Golgi complex. Golgi disruption blocked both p53-induced surface Fas expression and apoptosis. p53 also induced Fas-FADD binding and transiently sensitized cells to Fas-induced apoptosis. In contrast, lpr and gld fibroblasts were resistant to p53-induced apoptosis. Thus, p53 can mediate apoptosis through Fas transport from cytoplasmic stores.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bennett, M -- Macdonald, K -- Chan, S W -- Luzio, J P -- Simari, R -- Weissberg, P -- HL34073/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 9;282(5387):290-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Cambridge, Addenbrooke's Hospital, Cambridge CB2 2QQ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9765154" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Animals ; Antigens, CD95/genetics/*metabolism ; *Apoptosis/drug effects ; Brefeldin A/pharmacology ; Carrier Proteins/metabolism ; Cell Membrane/*metabolism ; Cells, Cultured ; Enzyme Inhibitors/pharmacology ; Etoposide/pharmacology ; Fas Ligand Protein ; Fas-Associated Death Domain Protein ; Golgi Apparatus/metabolism ; Humans ; Membrane Glycoproteins/genetics/metabolism ; Mice ; Muscle, Smooth, Vascular/cytology ; Mutation ; Protein Synthesis Inhibitors/pharmacology ; Rats ; Topoisomerase II Inhibitors ; Tumor Suppressor Protein p53/*physiology
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  • 172
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    Determinants of kinesin motor polarity (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-26
    Description: The kinesin motor protein family members move along microtubules with characteristic polarity. Chimeric motors containing the stalk and neck of the minus-end-directed motor, Ncd, fused to the motor domain of plus-end-directed kinesin were analyzed. The Ncd stalk and neck reversed kinesin motor polarity, but mutation of the Ncd neck reverted the chimeric motor to plus-end movement. Thus, residues or regions contributing to motor polarity must be present in both the Ncd neck and the kinesin motor core. The neck-motor junction was critical for Ncd minus-end movement; attachment of the neck to the stalk may also play a role.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Endow, S A -- Waligora, K W -- R01 GM046225/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Aug 21;281(5380):1200-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Duke University Medical Center, Durham, NC 27710, USA. endow@galactose.mc.duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9712586" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Drosophila Proteins ; Drosophila melanogaster ; Kinesin/*chemistry/genetics/metabolism ; Microtubules/metabolism ; Molecular Sequence Data ; Mutation ; Protein Structure, Secondary ; Recombinant Fusion Proteins/chemistry/metabolism
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  • 173
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    Meiotic synapsis in the absence of recombination (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-28
    Description: Although in Saccharomyces cerevisiae the initiation of meiotic recombination, as indicated by double-strand break formation, appears to be functionally linked to the initiation of synapsis, meiotic chromosome synapsis in Drosophila females occurs in the absence of meiotic exchange. Electron microscopy of oocytes from females homozygous for either of two meiotic mutants (mei-W68 and mei-P22), which eliminate both meiotic crossing over and gene conversion, revealed normal synaptonemal complex formation. Thus, synapsis in Drosophila is independent of meiotic recombination, consistent with a model in which synapsis is required for the initiation of meiotic recombination. Furthermore, the basic processes of early meiosis may have different functional or temporal relations, or both, in yeast and Drosophila.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McKim, K S -- Green-Marroquin, B L -- Sekelsky, J J -- Chin, G -- Steinberg, C -- Khodosh, R -- Hawley, R S -- New York, N.Y. -- Science. 1998 Feb 6;279(5352):876-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Molecular and Cellular Biology, University of California, Davis, CA 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9452390" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosomes/genetics/*physiology/ultrastructure ; Crossing Over, Genetic ; Drosophila melanogaster/genetics/*physiology ; Female ; Gene Conversion ; *Meiosis ; Mutation ; Oocytes/physiology ; *Recombination, Genetic ; Saccharomyces cerevisiae/genetics/physiology ; Sister Chromatid Exchange ; Synaptonemal Complex/*physiology
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  • 174
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    Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-24
    Description: The preferred antitubercular drug isoniazid specifically targets a long-chain enoyl-acyl carrier protein reductase (InhA), an enzyme essential for mycolic acid biosynthesis in Mycobacterium tuberculosis. Despite the widespread use of this drug for more than 40 years, its precise mode of action has remained obscure. Data from x-ray crystallography and mass spectrometry reveal that the mechanism of isoniazid action against InhA is covalent attachment of the activated form of the drug to the nicotinamide ring of nicotinamide adenine dinucleotide bound within the active site of InhA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rozwarski, D A -- Grant, G A -- Barton, D H -- Jacobs, W R Jr -- Sacchettini, J C -- AI-36849/AI/NIAID NIH HHS/ -- GM-45859/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):98-102.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417034" target="_blank"〉PubMed〈/a〉
    Keywords: Antitubercular Agents/metabolism/*pharmacology ; Bacterial Proteins ; Binding Sites ; Biotransformation ; Crystallography, X-Ray ; Drug Resistance, Microbial ; Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) ; Fatty Acid Synthases/antagonists & inhibitors/chemistry/genetics/metabolism ; Isoniazid/metabolism/*pharmacology ; Mass Spectrometry ; Models, Molecular ; Mutation ; Mycobacterium tuberculosis/*drug effects/enzymology ; Mycolic Acids/metabolism ; NAD/chemistry/*metabolism ; Oxidoreductases/*antagonists & inhibitors/chemistry/genetics/metabolism
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  • 175
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    Inhibition of a Mycobacterium tuberculosis beta-ketoacyl ACP synthase by isoniazid (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-11
    Description: Although isoniazid (isonicotinic acid hydrazide, INH) is widely used for the treatment of tuberculosis, its molecular target has remained elusive. In response to INH treatment, saturated hexacosanoic acid (C26:0) accumulated on a 12-kilodalton acyl carrier protein (AcpM) that normally carried mycolic acid precursors as long as C50. A protein species purified from INH-treated Mycobacterium tuberculosis was shown to consist of a covalent complex of INH, AcpM, and a beta-ketoacyl acyl carrier protein synthase, KasA. Amino acid-altering mutations in the KasA protein were identified in INH-resistant patient isolates that lacked other mutations associated with resistance to this drug.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mdluli, K -- Slayden, R A -- Zhu, Y -- Ramaswamy, S -- Pan, X -- Mead, D -- Crane, D D -- Musser, J M -- Barry, C E 3rd -- AI37004/AI/NIAID NIH HHS/ -- Z01 AI000783-11/Intramural NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 5;280(5369):1607-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tuberculosis Research Unit, Laboratory of Intracellular Parasites, Rocky Mountain Laboratories, National Institute for Allergy and Infectious Diseases (NIAID), National Institutes of Health, Hamilton, MT 59840, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9616124" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/*antagonists & ; inhibitors/chemistry/genetics ; Acyl Carrier Protein/chemistry/genetics/metabolism ; Amino Acid Sequence ; Antitubercular Agents/*pharmacology ; Drug Resistance, Microbial ; Enzyme Inhibitors/pharmacology ; Fatty Acids/metabolism ; Genes, Bacterial ; Humans ; Isoniazid/*pharmacology ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Mycobacterium tuberculosis/drug effects/*enzymology/genetics ; Mycolic Acids/metabolism ; Tuberculosis/microbiology ; Up-Regulation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 176
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    Another p53 Doppelganger? (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaelin, W G Jr -- New York, N.Y. -- Science. 1998 Jul 3;281(5373):57-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Dana-Farber Cancer Institute and Harvard Medical School, Boston, MA 02115, USA. William_Kaelin@dfci.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9679018" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; DNA-Binding Proteins/chemistry/genetics/*physiology ; Genes, Tumor Suppressor ; Genes, p53 ; Humans ; Mutation ; Neoplasms/*etiology/genetics/therapy ; Nuclear Proteins/chemistry/genetics/*physiology ; *Phosphoproteins ; *Trans-Activators ; Transcription Factors ; Tumor Suppressor Protein p53/chemistry/genetics/*physiology ; Tumor Suppressor Proteins
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  • 177
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    Type IV pili, transient bacterial aggregates, and virulence of enteropathogenic Escherichia coli (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-26
    Description: Type IV bundle-forming pili of enteropathogenic Escherichia coli are required for the localized adherence and autoaggregation phenotypes. Whether these pili are also required for virulence was tested in volunteers by inactivating bfpA or bfpT (perA) encoding, respectively, the pilus subunit and the bfp operon transcriptional activator. Both mutants caused significantly less diarrhea. Mutation of the bfpF nucleotide-binding domain caused increased piliation, enhanced localized adherence, and abolished the twitching motility-dispersal phase of the autoaggregation phenotype. The bfpF mutant colonized the human intestine but was about 200-fold less virulent. Thus, BfpF is required for dispersal from the bacterial aggregate and for full virulence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bieber, D -- Ramer, S W -- Wu, C Y -- Murray, W J -- Tobe, T -- Fernandez, R -- Schoolnik, G K -- 1RO1-AI39521/AI/NIAID NIH HHS/ -- 1RO3-DK52038/DK/NIDDK NIH HHS/ -- MO1-RR00070/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 26;280(5372):2114-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Division of Infectious Diseases and Geographical Medicine, Stanford Program for Vaccine Research, Stanford University Medical Center, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9641917" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Agglutination ; Bacterial Adhesion ; Cell Membrane/ultrastructure ; Diarrhea/*microbiology ; Epithelial Cells/microbiology ; Escherichia coli/genetics/*pathogenicity/physiology/ultrastructure ; Escherichia coli Infections/*microbiology ; Fimbriae, Bacterial/genetics/*physiology/ultrastructure ; Humans ; Intestinal Mucosa/microbiology ; Middle Aged ; Mutation ; Operon ; Phenotype ; Tumor Cells, Cultured ; Virulence
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  • 178
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    Unconventional myosins in cell movement, membrane traffic, and signal transduction (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-07
    Description: In the past few years genetic, biochemical, and cytolocalization data have implicated members of the myosin superfamily of actin-based molecular motors in a variety of cellular functions including membrane trafficking, cell movements, and signal transduction. The importance of myosins is illustrated by the identification of myosin genes as targets for disease-causing mutations. The task at hand is to decipher how the multitude of myosins function at both the molecular and cellular level-a task facilitated by our understanding of myosin structure and function in muscle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mermall, V -- Post, P L -- Mooseker, M S -- DK25387/DK/NIDDK NIH HHS/ -- DK38979/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 23;279(5350):527-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Yale University 342 KBT, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9438839" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/*metabolism ; *Cell Movement ; Hearing ; Humans ; Models, Biological ; Mutation ; Myosins/chemistry/genetics/*physiology ; Organelles/*physiology ; *Signal Transduction ; Vision, Ocular
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    Attenuation of virulence by disruption of the Mycobacterium tuberculosis erp gene (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-23
    Description: The virulence of the mycobacteria that cause tuberculosis depends on their ability to multiply in mammalian hosts. Disruption of the bacterial erp gene, which encodes the exported repetitive protein, impaired multiplication of M. tuberculosis and M. bovis Bacille Calmette-Guerin in cultured macrophages and mice. Reintroduction of erp into the mutants restored their ability to multiply. These results indicate that erp contributes to the virulence of M. tuberculosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berthet, F X -- Lagranderie, M -- Gounon, P -- Laurent-Winter, C -- Ensergueix, D -- Chavarot, P -- Thouron, F -- Maranghi, E -- Pelicic, V -- Portnoi, D -- Marchal, G -- Gicquel, B -- AI 35207/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 23;282(5389):759-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite de Genetique Mycobacterienne, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9784137" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; BCG Vaccine ; Bacterial Proteins/analysis/genetics/*physiology ; Cell Line ; Genes, Bacterial ; Genetic Complementation Test ; Immunohistochemistry ; Lung/microbiology ; Macrophages/microbiology ; Membrane Proteins/analysis/genetics/*physiology ; Mice ; Mice, Inbred BALB C ; Mutation ; Mycobacterium bovis/genetics/growth & development ; Mycobacterium tuberculosis/genetics/growth & ; development/metabolism/*pathogenicity ; Phagosomes/microbiology ; Recombinant Fusion Proteins ; Tuberculosis/microbiology ; Vaccines, Attenuated ; Virulence/genetics
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    A matter of life and cell death (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-28
    Description: In multicellular organisms, mutations in somatic cells affecting critical genes that regulate cell proliferation and survival cause fatal cancers. Repair of the damage is one obvious option, although the relative inconsequence of individual cells in metazoans means that it is often a "safer" strategy to ablate the offending cell. Not surprisingly, corruption of the machinery that senses or implements DNA damage greatly predisposes to cancer. Nonetheless, even when oncogenic mutations do occur, there exist potent mechanisms that limit the expansion of affected cells by suppressing their proliferation or triggering their suicide. Growing understanding of these innate mechanisms is suggesting novel therapeutic strategies for cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evan, G -- Littlewood, T -- New York, N.Y. -- Science. 1998 Aug 28;281(5381):1317-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Imperial Cancer Research Fund Laboratories, 44, Lincoln's Inn Fields, London WC2A 3PX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9721090" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Cell Division ; Cell Survival ; DNA Damage ; Genes, Tumor Suppressor ; Humans ; Mutation ; Neoplasms/metabolism/pathology/therapy ; Oncogene Proteins/metabolism ; Oncogenes ; Tumor Suppressor Protein p53/metabolism
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    A tangled tale of E. coli virulence (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weidenbach, K -- New York, N.Y. -- Science. 1998 Jun 26;280(5372):2048.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9669959" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Adhesion ; Diarrhea/*microbiology ; Epithelial Cells/microbiology ; Escherichia coli/genetics/*pathogenicity/ultrastructure ; Escherichia coli Infections/*microbiology ; Fimbriae, Bacterial/genetics/*physiology/ultrastructure ; Humans ; Intestinal Mucosa/microbiology ; Mutation ; Virulence
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    Telomeres--unsticky ends (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shore, D -- New York, N.Y. -- Science. 1998 Sep 18;281(5384):1818-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement de Biologie Moleculaire, Universite de Geneve, Switzerland. david.shore@molbiol.unige.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9776685" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, Nuclear ; *DNA Helicases ; DNA Repair ; DNA-Binding Proteins/genetics/metabolism/*physiology ; Fungal Proteins/metabolism ; Gene Expression Regulation ; Mutation ; Nuclear Proteins/genetics/metabolism/*physiology ; Recombination, Genetic ; Saccharomyces cerevisiae/metabolism ; *Saccharomyces cerevisiae Proteins ; *Silent Information Regulator Proteins, Saccharomyces cerevisiae ; Telomerase/metabolism ; Telomere/metabolism/*physiology/ultrastructure ; Telomeric Repeat Binding Protein 2
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    A signaling complex of Ca2+-calmodulin-dependent protein kinase IV and protein phosphatase 2A (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: Stimulation of T lymphocytes results in a rapid increase in intracellular calcium concentration ([Ca2+]i) that parallels the activation of Ca2+-calmodulin-dependent protein kinase IV (CaMKIV), a nuclear enzyme that can phosphorylate and activate the cyclic adenosine monophosphate (cAMP) response element-binding protein (CREB). However, inactivation of CaMKIV occurs despite the sustained increase in [Ca2+]i that is required for T cell activation. A stable and stoichiometric complex of CaMKIV with protein serine-threonine phosphatase 2A (PP2A) was identified in which PP2A dephosphorylates CaMKIV and functions as a negative regulator of CaMKIV signaling. In Jurkat T cells, inhibition of PP2A activity by small t antigen enhanced activation of CREB-mediated transcription by CaMKIV. These findings reveal an intracellular signaling mechanism whereby a protein serine-threonine kinase (CaMKIV) is regulated by a tightly associated protein serine-threonine phosphatase (PP2A).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Westphal, R S -- Anderson, K A -- Means, A R -- Wadzinski, B E -- GM33976/GM/NIGMS NIH HHS/ -- GM51366/GM/NIGMS NIH HHS/ -- HD07503/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 May 22;280(5367):1258-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9596578" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Polyomavirus Transforming/metabolism ; Brain/enzymology ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinase Type 4 ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/isolation & ; purification/*metabolism ; Calmodulin/metabolism ; Coenzymes/metabolism ; Cyclic AMP Response Element-Binding Protein/metabolism ; Enzyme Activation ; Humans ; Jurkat Cells ; Lymphocyte Activation ; Mutation ; Phosphoprotein Phosphatases/isolation & purification/*metabolism ; Phosphorylation ; Protein Phosphatase 2 ; Rats ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; T-Lymphocytes/*enzymology ; Transcription, Genetic
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  • 184
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    Role of mouse cryptochrome blue-light photoreceptor in circadian photoresponses (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-20
    Description: Cryptochromes are photoactive pigments in the eye that have been proposed to function as circadian photopigments. Mice lacking the cryptochrome 2 blue-light photoreceptor gene (mCry2) were tested for circadian clock-related functions. The mutant mice had a lower sensitivity to acute light induction of mPer1 in the suprachiasmatic nucleus (SCN) but exhibited normal circadian oscillations of mPer1 and mCry1 messenger RNA in the SCN. Behaviorally, the mutants had an intrinsic circadian period about 1 hour longer than normal and exhibited high-amplitude phase shifts in response to light pulses administered at circadian time 17. These data are consistent with the hypothesis that CRY2 protein modulates circadian responses in mice and suggest that cryptochromes have a role in circadian photoreception in mammals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thresher, R J -- Vitaterna, M H -- Miyamoto, Y -- Kazantsev, A -- Hsu, D S -- Petit, C -- Selby, C P -- Dawut, L -- Smithies, O -- Takahashi, J S -- Sancar, A -- GM20069/GM/NIGMS NIH HHS/ -- GM31082/GM/NIGMS NIH HHS/ -- P0 AG11412/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 20;282(5393):1490-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9822380" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Cycle Proteins ; Circadian Rhythm/*physiology ; Cryptochromes ; *Drosophila Proteins ; *Eye Proteins ; Female ; Flavoproteins/genetics/*physiology ; Gene Expression Regulation ; Gene Targeting ; In Situ Hybridization ; *Light ; Male ; Mice ; Mice, Inbred C57BL ; Motor Activity ; Mutation ; Nuclear Proteins/genetics ; Period Circadian Proteins ; *Photoreceptor Cells, Invertebrate ; Photoreceptor Cells, Vertebrate/*physiology ; Receptors, G-Protein-Coupled ; Suprachiasmatic Nucleus/metabolism
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    Disruption of splicing regulated by a CUG-binding protein in myotonic dystrophy (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-23
    Description: Myotonic dystrophy (DM) is caused by a CTG expansion in the 3' untranslated region of the DM gene. One model of DM pathogenesis suggests that RNAs from the expanded allele create a gain-of-function mutation by the inappropriate binding of proteins to the CUG repeats. Data presented here indicate that the conserved heterogeneous nuclear ribonucleoprotein, CUG-binding protein (CUG-BP), may mediate the trans-dominant effect of the RNA. CUG-BP was found to bind to the human cardiac troponin T (cTNT) pre-messenger RNA and regulate its alternative splicing. Splicing of cTNT was disrupted in DM striated muscle and in normal cells expressing transcripts that contain CUG repeats. Altered expression of genes regulated posttranscriptionally by CUG-BP therefore may contribute to DM pathogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Philips, A V -- Timchenko, L T -- Cooper, T A -- AR 44387/AR/NIAMS NIH HHS/ -- HL45565/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1998 May 1;280(5364):737-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9563950" target="_blank"〉PubMed〈/a〉
    Keywords: *Alternative Splicing ; CELF1 Protein ; Cell Line ; Cell Nucleus/metabolism ; Exons ; Humans ; Introns ; Muscle, Skeletal/cytology/embryology/metabolism ; Mutation ; Myotonic Dystrophy/*genetics/metabolism ; Myotonin-Protein Kinase ; Phosphorylation ; Protein-Serine-Threonine Kinases/*genetics ; RNA Precursors/metabolism ; RNA, Messenger/*genetics/metabolism ; RNA-Binding Proteins/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Ribonucleoproteins/genetics/*metabolism ; Transcription, Genetic ; Transfection ; *Trinucleotide Repeats ; Troponin/genetics ; Troponin T
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    Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-28
    Description: Eps15 homology (EH) domains are eukaryotic signaling modules that recognize proteins containing Asn-Pro-Phe (NPF) sequences. The structure of the central EH domain of Eps15 has been solved by heteronuclear magnetic resonance spectroscopy. The fold consists of a pair of EF hand motifs, the second of which binds tightly to calcium. The NPF peptide is bound in a hydrophobic pocket between two alpha helices, and binding is mediated by a critical aromatic interaction as revealed by structure-based mutagenesis. The fold is predicted to be highly conserved among 30 identified EH domains and provides a structural basis for defining EH-mediated events in protein trafficking and growth factor signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Beer, T -- Carter, R E -- Lobel-Rice, K E -- Sorkin, A -- Overduin, M -- New York, N.Y. -- Science. 1998 Aug 28;281(5381):1357-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Colorado Health Sciences Center, 4200 East Ninth Avenue, Denver, CO 80262, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9721102" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Calcium/metabolism ; Calcium-Binding Proteins/*chemistry/metabolism ; Helix-Loop-Helix Motifs ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; Oligopeptides/chemistry/*metabolism ; Phosphoproteins/*chemistry/metabolism ; Protein Binding ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Signal Transduction
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    Coupling termination of transcription to messenger RNA maturation in yeast (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-02
    Description: The direct association between messenger RNA (mRNA) 3'-end processing and the termination of transcription was established for the CYC1 gene of Saccharomyces cerevisiae. The mutation of factors involved in the initial cleavage of the primary transcript at the poly(A) site (RNA14, RNA15, and PCF11) disrupted transcription termination at the 3' end of the CYC1 gene. In contrast, the mutation of factors involved in the subsequent polyadenylation step (PAP1, FIP1, and YTH1) had little effect. Thus, cleavage factors link transcription termination of RNA polymerase II with pre-mRNA 3'-end processing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Birse, C E -- Minvielle-Sebastia, L -- Lee, B A -- Keller, W -- Proudfoot, N J -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1998 Apr 10;280(5361):298-301.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sir William Dunn School of Pathology, South Parks Road, University of Oxford, Oxford OX1 3RE, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9535662" target="_blank"〉PubMed〈/a〉
    Keywords: Cytochrome c Group/*genetics ; *Cytochromes c ; Fungal Proteins/genetics/metabolism ; Genes, Fungal ; Mutation ; Nuclear Proteins/genetics/metabolism ; Poly A/metabolism ; RNA Polymerase II/metabolism ; RNA Precursors/*metabolism ; RNA, Fungal/*metabolism ; RNA, Messenger/*metabolism ; RNA-Binding Proteins/genetics/metabolism ; Saccharomyces cerevisiae/*genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Temperature ; *Transcription, Genetic ; mRNA Cleavage and Polyadenylation Factors
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    SIV vaccine for AIDS (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Farthing, C F -- Sullivan, J L -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):14-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9441400" target="_blank"〉PubMed〈/a〉
    Keywords: *AIDS Vaccines/adverse effects ; Animals ; Clinical Trials as Topic ; *Genes, nef ; HIV/*genetics ; HIV Infections/immunology/*virology ; Haplorhini ; Humans ; Mutation ; SAIDS Vaccines/*adverse effects ; Simian Acquired Immunodeficiency Syndrome/virology ; Simian Immunodeficiency Virus/genetics ; Vaccines, Attenuated/adverse effects
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  • 189
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    Congenital heart disease caused by mutations in the transcription factor NKX2-5 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-04
    Description: Mutations in the gene encoding the homeobox transcription factor NKX2-5 were found to cause nonsyndromic, human congenital heart disease. A dominant disease locus associated with cardiac malformations and atrioventricular conduction abnormalities was mapped to chromosome 5q35, where NKX2-5, a Drosophila tinman homolog, is located. Three different NKX2-5 mutations were identified. Two are predicted to impair binding of NKX2-5 to target DNA, resulting in haploinsufficiency, and a third potentially augments target-DNA binding. These data indicate that NKX2-5 is important for regulation of septation during cardiac morphogenesis and for maturation and maintenance of atrioventricular node function throughout life.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schott, J J -- Benson, D W -- Basson, C T -- Pease, W -- Silberbach, G M -- Moak, J P -- Maron, B J -- Seidman, C E -- Seidman, J G -- New York, N.Y. -- Science. 1998 Jul 3;281(5373):108-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics and Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9651244" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Atrioventricular Node/physiopathology ; Chromosome Mapping ; Chromosomes, Human, Pair 5 ; Codon ; Female ; Genes, Dominant ; Genetic Linkage ; Heart Block/*genetics/physiopathology ; Heart Septal Defects, Atrial/*genetics/physiopathology ; Homeodomain Proteins/*genetics/metabolism ; Humans ; Male ; Mice ; Molecular Sequence Data ; Mutation ; Pedigree ; Protein Biosynthesis ; Transcription Factors/*genetics/metabolism ; *Xenopus Proteins
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    Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: MAP kinase phosphatase-3 (MKP-3) dephosphorylates phosphotyrosine and phosphothreonine and inactivates selectively ERK family mitogen-activated protein (MAP) kinases. MKP-3 was activated by direct binding to purified ERK2. Activation was independent of protein kinase activity and required binding of ERK2 to the noncatalytic amino-terminus of MKP-3. Neither the gain-of-function Sevenmaker ERK2 mutant D319N nor c-Jun amino-terminal kinase-stress-activated protein kinase (JNK/SAPK) or p38 MAP kinases bound MKP-3 or caused its catalytic activation. These kinases were also resistant to enzymatic inactivation by MKP-3. Another homologous but nonselective phosphatase, MKP-4, bound and was activated by ERK2, JNK/SAPK, and p38 MAP kinases. Catalytic activation of MAP kinase phosphatases through substrate binding may regulate MAP kinase activation by a large number of receptor systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Camps, M -- Nichols, A -- Gillieron, C -- Antonsson, B -- Muda, M -- Chabert, C -- Boschert, U -- Arkinstall, S -- New York, N.Y. -- Science. 1998 May 22;280(5367):1262-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geneva Biomedical Research Institute, Glaxo Wellcome Research and Development S.A., CH-1228 Plan-les-Ouates, Geneva, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9596579" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; COS Cells ; Calcium-Calmodulin-Dependent Protein Kinases/antagonists & ; inhibitors/genetics/*metabolism ; Catalysis ; Dual Specificity Phosphatase 6 ; Enzyme Activation ; Epidermal Growth Factor/pharmacology ; Mitogen-Activated Protein Kinase 1 ; Mitogen-Activated Protein Kinase 12 ; Mitogen-Activated Protein Kinase 9 ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein Kinases/metabolism ; Protein Tyrosine Phosphatases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transfection ; p38 Mitogen-Activated Protein Kinases
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    Requirement of Ras-GTP-Raf complexes for activation of Raf-1 by protein kinase C (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-29
    Description: Receptor tyrosine kinase-mediated activation of the Raf-1 protein kinase is coupled to the small guanosine triphosphate (GTP)-binding protein Ras. By contrast, protein kinase C (PKC)-mediated activation of Raf-1 is thought to be Ras independent. Nevertheless, stimulation of PKC in COS cells led to activation of Ras and formation of Ras-Raf-1 complexes containing active Raf-1. Raf-1 mutations that prevent its association with Ras blocked activation of Raf-1 by PKC. However, the activation of Raf-1 by PKC was not blocked by dominant negative Ras, indicating that PKC activates Ras by a mechanism distinct from that initiated by activation of receptor tyrosine kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marais, R -- Light, Y -- Mason, C -- Paterson, H -- Olson, M F -- Marshall, C J -- New York, N.Y. -- Science. 1998 Apr 3;280(5360):109-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CRC Centre for Cell and Molecular Biology, Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9525855" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; COS Cells ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Cercopithecus aethiops ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Epidermal Growth Factor/pharmacology ; Guanosine Triphosphate/*metabolism ; Indoles/pharmacology ; Mutation ; Protein Kinase C/antagonists & inhibitors/*metabolism ; Proto-Oncogene Proteins c-raf/genetics/*metabolism ; Receptors, Muscarinic/metabolism ; Signal Transduction ; Tetradecanoylphorbol Acetate/pharmacology ; ras Proteins/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    A transmembrane form of the prion protein in neurodegenerative disease (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-28
    Description: At the endoplasmic reticulum membrane, the prion protein (PrP) can be synthesized in several topological forms. The role of these different forms was explored with transgenic mice expressing PrP mutations that alter the relative ratios of the topological forms. Expression of a particular transmembrane form (termed CtmPrP) produced neurodegenerative changes in mice similar to those of some genetic prion diseases. Brains from these mice contained CtmPrP but not PrPSc, the PrP isoform responsible for transmission of prion diseases. Furthermore, in one heritable prion disease of humans, brain tissue contained CtmPrP but not PrPSc. Thus, aberrant regulation of protein biogenesis and topology at the endoplasmic reticulum can result in neurodegeneration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hegde, R S -- Mastrianni, J A -- Scott, M R -- DeFea, K A -- Tremblay, P -- Torchia, M -- DeArmond, S J -- Prusiner, S B -- Lingappa, V R -- AG02132/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1998 Feb 6;279(5352):827-34.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California, San Francisco, CA 94143-0444, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9452375" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/metabolism/pathology ; Cricetinae ; Endopeptidases/metabolism ; Endoplasmic Reticulum/chemistry/*metabolism ; Gerstmann-Straussler-Scheinker Disease/metabolism ; Humans ; Intracellular Membranes/chemistry ; Mesocricetus ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Mutation ; Neurodegenerative Diseases/*etiology/metabolism/pathology ; PrPC Proteins/biosynthesis/*chemistry/genetics/*metabolism ; PrPSc Proteins/chemistry/metabolism ; Prion Diseases/etiology/metabolism/pathology ; Prions/biosynthesis/*chemistry/genetics/*metabolism ; Protein Conformation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 193
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    Bacteria diversify through warfare (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1997 Oct 24;278(5338):575.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381164" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*genetics ; Biological Evolution ; Colicins/*genetics/pharmacology ; Escherichia coli/*genetics/physiology ; Genes, Bacterial ; *Genetic Variation ; Mutation ; *Selection, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 194
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    Regulation of meiotic S phase by Ime2 and a Clb5,6-associated kinase in Saccharomyces cerevisiae (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-22
    Description: Cyclin-dependent kinase (Cdk) mutations that prevent entry into the mitotic cell cycle of budding yeast fail to block meiotic DNA replication, suggesting there may be fundamental differences between these pathways. However, S phase in meiosis was found to depend on the same B-type cyclins (Clb5 and Clb6) as it does in mitosis. Meiosis differs instead in the mechanism that controls removal of the Cdk inhibitor Sic1. Destruction of Sic1 and activation of a Clb5-dependent kinase in meiotic cells required the action of the meiosis-specific protein kinase Ime2, thereby coupling early meiotic gene expression to control of DNA replication for meiosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dirick, L -- Goetsch, L -- Ammerer, G -- Byers, B -- GM 18541/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 18;281(5384):1854-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Box 357360, University of Washington, Seattle, WA 98195-7360, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9743499" target="_blank"〉PubMed〈/a〉
    Keywords: CDC28 Protein Kinase, S cerevisiae/metabolism ; *Cell Cycle Proteins ; *Cyclin B ; Cyclin-Dependent Kinase Inhibitor Proteins ; Cyclin-Dependent Kinases/*metabolism ; Cyclins/genetics/*metabolism ; DNA Replication ; Enzyme Inhibitors/metabolism ; Fungal Proteins/genetics/*metabolism ; Genes, Fungal ; Intracellular Signaling Peptides and Proteins ; *Meiosis ; Mutation ; Protein Kinases/genetics/*metabolism ; Protein-Serine-Threonine Kinases ; *S Phase ; Saccharomyces cerevisiae/*cytology/genetics/metabolism ; *Saccharomyces cerevisiae Proteins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 195
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    Progression to AIDS (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Donfield, S M -- Lynn, H S -- Hilgartner, M W -- New York, N.Y. -- Science. 1998 Jun 19;280(5371):1819-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9669928" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/genetics/*immunology ; CD4 Lymphocyte Count ; Cell Line ; Cohort Studies ; Disease Progression ; Genotype ; HIV Infections/genetics/*immunology ; HIV Seropositivity ; Humans ; Mutation ; Receptors, CCR2 ; Receptors, Chemokine/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 196
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    Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: Topoisomerases I promote the relaxation of DNA superhelical tension by introducing a transient single-stranded break in duplex DNA and are vital for the processes of replication, transcription, and recombination. The crystal structures at 2.1 and 2.5 angstrom resolution of reconstituted human topoisomerase I comprising the core and carboxyl-terminal domains in covalent and noncovalent complexes with 22-base pair DNA duplexes reveal an enzyme that "clamps" around essentially B-form DNA. The core domain and the first eight residues of the carboxyl-terminal domain of the enzyme, including the active-site nucleophile tyrosine-723, share significant structural similarity with the bacteriophage family of DNA integrases. A binding mode for the anticancer drug camptothecin is proposed on the basis of chemical and biochemical information combined with these three-dimensional structures of topoisomerase I-DNA complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Redinbo, M R -- Stewart, L -- Kuhn, P -- Champoux, J J -- Hol, W G -- CA65656/CA/NCI NIH HHS/ -- GM49156/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Mar 6;279(5356):1504-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biomolecular Structure Center and Department of Biological Structure, Box 357742, School of Medicine, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9488644" target="_blank"〉PubMed〈/a〉
    Keywords: Antineoplastic Agents, Phytogenic/metabolism/pharmacology ; Binding Sites ; Camptothecin/analogs & derivatives/metabolism/pharmacology ; Crystallography, X-Ray ; DNA/chemistry/*metabolism ; DNA Topoisomerases, Type I/*chemistry/genetics/metabolism ; *DNA-Binding Proteins ; Homeodomain Proteins/chemistry ; Host Cell Factor C1 ; Humans ; Hydrogen Bonding ; Integrases/chemistry ; Models, Molecular ; Mutation ; Nucleic Acid Conformation ; Octamer Transcription Factor-1 ; Oligodeoxyribonucleotides/chemistry/metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Recombinant Proteins/chemistry ; Transcription Factors/chemistry ; Tyrosine/chemistry/metabolism
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  • 197
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    An Arabidopsis mutant defective in the plastid general protein import apparatus (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-02
    Description: Elaborate mechanisms have evolved for the translocation of nucleus-encoded proteins across the plastid envelope membrane. Although putative components of the import apparatus have been identified biochemically, their role in import remains to be proven in vivo. An Arabidopsis mutant lacking a new component of the import machinery [translocon at the outer envelope membrane of chloroplasts (Toc33), a 33-kilodalton protein] has been isolated. The functional similarity of Toc33 to another translocon component (Toc34) implies that multiple different translocon complexes are present in plastids. Processes that are mediated by Toc33 operate during the early stages of plastid and leaf development. The data demonstrate the in vivo role of a translocon component in plastid protein import.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jarvis, P -- Chen, L J -- Li, H -- Peto, C A -- Fankhauser, C -- Chory, J -- New York, N.Y. -- Science. 1998 Oct 2;282(5386):100-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Biology Laboratory, Salk Institute, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9756470" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/chemistry/*genetics/growth & development/metabolism ; *Arabidopsis Proteins ; Biological Transport ; Chlorophyll/metabolism ; Chloroplasts/*metabolism/ultrastructure ; Gene Expression Regulation, Plant ; Intracellular Membranes/metabolism ; Membrane Proteins/chemistry/*genetics/*metabolism/*secretion ; Molecular Sequence Data ; Mutation ; Phenotype ; Plant Leaves/metabolism ; Plant Proteins/*metabolism ; Plants, Genetically Modified ; Sequence Alignment
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 198
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    Complexity matters (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wagner, G -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1158-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolutionary Biology, Yale University, New Haven, CT 06520-8106, USA. gpwag@peaplant.biology.yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9508689" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Gene Frequency ; Genetic Variation ; *Genetics, Population ; Genotype ; *Models, Genetic ; Mutation ; Selection, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 199
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    New gene tied to common form of Alzheimer's (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1998 Jul 24;281(5376):507, 509.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9705719" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics/metabolism ; Amyloid beta-Peptides/metabolism ; Animals ; Apolipoprotein E4 ; Apolipoproteins E/genetics/metabolism ; Brain/metabolism ; Genetic Linkage ; Genetic Predisposition to Disease ; Humans ; Low Density Lipoprotein Receptor-Related Protein-1 ; Mice ; Mutation ; Receptors, Immunologic/metabolism ; Risk Factors ; Sequence Deletion ; alpha-Macroglobulins/*genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 200
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    Expression of a gene cluster kaiABC as a circadian feedback process in cyanobacteria (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-04
    Description: Cyanobacteria are the simplest organisms known to have a circadian clock. A circadian clock gene cluster kaiABC was cloned from the cyanobacterium Synechococcus. Nineteen clock mutations were mapped to the three kai genes. Promoter activities upstream of the kaiA and kaiB genes showed circadian rhythms of expression, and both kaiA and kaiBC messenger RNAs displayed circadian cycling. Inactivation of any single kai gene abolished these rhythms and reduced kaiBC-promoter activity. Continuous kaiC overexpression repressed the kaiBC promoter, whereas kaiA overexpression enhanced it. Temporal kaiC overexpression reset the phase of the rhythms. Thus, a negative feedback control of kaiC expression by KaiC generates a circadian oscillation in cyanobacteria, and KaiA sustains the oscillation by enhancing kaiC expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ishiura, M -- Kutsuna, S -- Aoki, S -- Iwasaki, H -- Andersson, C R -- Tanabe, A -- Golden, S S -- Johnson, C H -- Kondo, T -- MH01179/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 4;281(5382):1519-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biological Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8602, Japan. ishiura@bio.nagoya-u.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9727980" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*genetics ; Biological Clocks/*genetics ; Circadian Rhythm/*genetics ; Circadian Rhythm Signaling Peptides and Proteins ; Cloning, Molecular ; Cyanobacteria/*genetics/physiology ; Feedback ; *Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Genes, Reporter ; Luminescence ; Models, Biological ; Molecular Sequence Data ; Multigene Family ; Mutation ; Promoter Regions, Genetic ; Recombinant Fusion Proteins ; Transcription, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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