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
  • 1
    facet.materialart.
    Unknown
    Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-03-27
    Description: Expanded polyglutamine repeats have been proposed to cause neuronal degeneration in Huntington's disease (HD) and related disorders, through abnormal interactions with other proteins containing short polyglutamine tracts such as the transcriptional coactivator CREB binding protein, CBP. We found that CBP was depleted from its normal nuclear location and was present in polyglutamine aggregates in HD cell culture models, HD transgenic mice, and human HD postmortem brain. Expanded polyglutamine repeats specifically interfere with CBP-activated gene transcription, and overexpression of CBP rescued polyglutamine-induced neuronal toxicity. Thus, polyglutamine-mediated interference with CBP-regulated gene transcription may constitute a genetic gain of function, underlying the pathogenesis of polyglutamine disorders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nucifora , F C Jr -- Sasaki, M -- Peters, M F -- Huang, H -- Cooper, J K -- Yamada, M -- Takahashi, H -- Tsuji, S -- Troncoso, J -- Dawson, V L -- Dawson, T M -- Ross, C A -- NS16375/NS/NINDS NIH HHS/ -- NS34172/NS/NINDS NIH HHS/ -- NS37090/NS/NINDS NIH HHS/ -- NS38144/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2001 Mar 23;291(5512):2423-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neurobiology, Department of Psychiatry, The Johns Hopkins University School of Medicine, Baltimore, MD 21205-2196, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11264541" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; CREB-Binding Protein ; Cell Nucleus/metabolism ; Cell Survival ; Cells, Cultured ; Humans ; Huntington Disease/genetics/*metabolism ; Mice ; Mice, Transgenic ; Mutation ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Neurons/cytology/*metabolism ; Nuclear Proteins/chemistry/genetics/*metabolism ; Peptides/chemistry/*metabolism ; Repetitive Sequences, Amino Acid ; Trans-Activators/chemistry/*metabolism ; *Transcription, Genetic ; Transfection ; Tumor Cells, Cultured
    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
  • 2
    facet.materialart.
    Unknown
    Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-17
    Description: Transient interactions of platelet-receptor glycoprotein Ibalpha (GpIbalpha) and the plasma protein von Willebrand factor (VWF) reduce platelet velocity at sites of vascular damage and play a role in haemostasis and thrombosis. Here we present structures of the GpIbalpha amino-terminal domain and its complex with the VWF domain A1. In the complex, GpIbalpha wraps around one side of A1, providing two contact areas bridged by an area of solvated charge interaction. The structures explain the effects of gain-of-function mutations related to bleeding disorders and provide a model for shear-induced activation. These detailed insights into the initial interactions in platelet adhesion are relevant to the development of antithrombotic drugs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huizinga, Eric G -- Tsuji, Shizuko -- Romijn, Roland A P -- Schiphorst, Marion E -- de Groot, Philip G -- Sixma, Jan J -- Gros, Piet -- New York, N.Y. -- Science. 2002 Aug 16;297(5584):1176-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, Netherlands. e.g.huizinga@chem.uu.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12183630" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Bernard-Soulier Syndrome/genetics/metabolism ; Binding Sites ; Blood Platelets/metabolism/physiology ; Crystallization ; Crystallography, X-Ray ; Humans ; Hydrogen Bonding ; Ligands ; Models, Molecular ; Mutation ; Platelet Adhesiveness ; Platelet Glycoprotein GPIb-IX Complex/*chemistry/genetics/*metabolism ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; Repetitive Sequences, Amino Acid ; Static Electricity ; von Willebrand Diseases/genetics/metabolism ; von Willebrand Factor/*chemistry/*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...