ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Mutation  (15)
  • American Association for the Advancement of Science (AAAS)  (15)
  • American Geophysical Union (AGU)
  • 2000-2004  (15)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (15)
  • American Geophysical Union (AGU)
Years
Year
  • 11
    facet.materialart.
    Unknown
    A basal transcription factor that activates or represses transcription (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-11-04
    Description: We have identified an activity that is required for transcription of downstream promoter element (DPE)-containing core promoters in vitro. The purified factor was found to be the Drosophila homolog of the transcriptional repressor known as NC2 or Dr1-Drap1. Purified recombinant dNC2 activates DPE-driven promoters and represses TATA-driven promoters. A mutant version of dNC2 can activate DPE promoters but is unable to repress TATA promoters. Thus, the activation and repression functions are distinct. These studies reveal that NC2 (Dr1-Drap1) is a bifunctional basal transcription factor that differentially regulates gene transcription through DPE or TATA box motifs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Willy, P J -- Kobayashi, R -- Kadonaga, J T -- CA13106/CA/NCI NIH HHS/ -- GM41249/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Nov 3;290(5493):982-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Molecular Biology and Center for Molecular Genetics, University of California, San Diego, La Jolla, CA 92093-0347, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11062130" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Drosophila/*genetics ; Molecular Weight ; Mutation ; Phosphoproteins/chemistry/genetics/isolation & purification/*metabolism ; *Promoter Regions, Genetic ; Protein Subunits ; Recombinant Proteins/metabolism ; TATA Box ; Transcription Factors/chemistry/genetics/isolation & purification/*metabolism ; *Transcription, Genetic ; *Transcriptional Activation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 12
    facet.materialart.
    Unknown
    Separable roles for rent1/hUpf1 in altered splicing and decay of nonsense transcripts (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-14
    Description: The mechanism by which disruption of reading frame can influence pre-messenger RNA (pre-mRNA) processing is poorly understood. We assessed the role of factors essential for nonsense-mediated mRNA decay (NMD) in nonsense-mediated altered splicing (NAS) with the use of RNA interference (RNAi) in mammalian cells. Inhibition of rent1/hUpf1 expression abrogated both NMD and NAS of nonsense T cell receptor beta transcripts. In contrast, inhibition of rent2/hUpf2 expression did not disrupt NAS despite achieving comparable stabilization of nonsense transcripts. We also demonstrate that NAS and NMD are genetically separable functions of rent1/hUpf1. Additionally, rent1/hUpf1 enters the nucleus where it may directly influence early events in mRNA biogenesis. This provides compelling evidence that NAS relies on a component of the nonsense surveillance machinery but is not an indirect consequence of NMD.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mendell, Joshua T -- ap Rhys, Colette M J -- Dietz, Harry C -- GM55239/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 11;298(5592):419-22. Epub 2002 Sep 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Genetic Medicine and Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, 858 Ross Building, 720 Rutland Avenue, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12228722" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; *Alternative Splicing ; Amino Acid Substitution ; Blotting, Northern ; Cell Nucleus/metabolism ; *Codon, Nonsense ; Cytoplasm/metabolism ; Equilibrative-Nucleoside Transporter 2/genetics/metabolism ; Fatty Acids, Unsaturated/pharmacology ; Gene Silencing ; Genes, T-Cell Receptor beta ; HeLa Cells ; Humans ; Mutation ; RNA Helicases/genetics/*metabolism ; RNA, Messenger/genetics/*metabolism ; RNA, Small Interfering/metabolism ; Recombinant Fusion Proteins/metabolism ; Trans-Activators/genetics/*metabolism ; Transcription Factors/genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 13
    facet.materialart.
    Unknown
    Structural basis of mitochondrial tethering by mitofusin complexes (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-07
    Description: Vesicle fusion involves vesicle tethering, docking, and membrane merger. We show that mitofusin, an integral mitochondrial membrane protein, is required on adjacent mitochondria to mediate fusion, which indicates that mitofusin complexes act in trans (that is, between adjacent mitochondria). A heptad repeat region (HR2) mediates mitofusin oligomerization by assembling a dimeric, antiparallel coiled coil. The transmembrane segments are located at opposite ends of the 95 angstrom coiled coil and provide a mechanism for organelle tethering. Consistent with this proposal, truncated mitofusin, in an HR2-dependent manner, causes mitochondria to become apposed with a uniform gap. Our results suggest that HR2 functions as a mitochondrial tether before fusion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koshiba, Takumi -- Detmer, Scott A -- Kaiser, Jens T -- Chen, Hsiuchen -- McCaffery, J Michael -- Chan, David C -- R01 GM62967/GM/NIGMS NIH HHS/ -- S10 RR019409-01/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2004 Aug 6;305(5685):858-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, 1200 East California Boulevard, MC114-96, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15297672" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Cell Line ; Crystallography, X-Ray ; Dimerization ; GTP Phosphohydrolases/*chemistry/*metabolism ; Humans ; Hybrid Cells ; Hydrophobic and Hydrophilic Interactions ; Intracellular Membranes/physiology/ultrastructure ; Membrane Fusion ; Mice ; Mitochondria/*metabolism/ultrastructure ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Structure, Secondary ; Protein Structure, Tertiary
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 14
    facet.materialart.
    Unknown
    Biomedicine. Parkinson's--divergent causes, convergent mechanisms (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greenamyre, J Timothy -- Hastings, Teresa G -- New York, N.Y. -- Science. 2004 May 21;304(5674):1120-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Emory University School of Medicine, Atlanta, GA 30322, USA. jgreena@emory.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15155938" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; Dopamine/metabolism ; Electron Transport Complex I/metabolism ; Humans ; Intracellular Signaling Peptides and Proteins ; Mitochondria/enzymology/*metabolism ; Mutation ; Nerve Tissue Proteins/genetics/metabolism ; Neurons/metabolism ; Oncogene Proteins/genetics/metabolism ; Oxidative Stress ; Parkinson Disease/*etiology/*genetics/metabolism ; Phosphorylation ; Protein Kinases/*genetics/*metabolism ; Reactive Oxygen Species/metabolism ; Synucleins ; Ubiquitin Thiolesterase/genetics/metabolism ; Ubiquitin-Protein Ligases/genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 15
    facet.materialart.
    Unknown
    Comment on "Uracil DNA glycosylase activity is dispensable for immunoglobulin class switch" (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stivers, James T -- GM56834-09/GM/NIGMS NIH HHS/ -- R01 GM056834/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2042; author reply 2042.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Johns Hopkins Medical School, 725 North Wolfe Street, Baltimore, MD 21205, USA. jstivers@jhmi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604391" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/enzymology/immunology/*physiology ; Catalysis ; DNA/*metabolism ; DNA Damage ; DNA Glycosylases/*metabolism ; DNA Repair ; Humans ; *Immunoglobulin Class Switching ; Mice ; Mutation ; Recombination, Genetic ; Uracil/metabolism ; Uracil-DNA Glycosidase ; Viral Proteins/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...