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
    Electronic Resource
    Electronic Resource
    Distal tubular segments of the rabbit kidney after adaptation to altered Na- and K-intake (1982)
    Springer
    Cell & tissue research 224 (1982), S. 493-504 
    Details
    ISSN: 1432-0878
    Keywords: Na-K-ATPase ; Cell-membrane area ; Renal distal tubule ; Cortical collecting duct ; Mineralocorticoids ; Rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Na-K-ATPase activity was measured in the convoluted part of the distal tubule (DCT), the connecting tubule (CNT) and the cortical collecting duct (CCD). The segments were microdissected from freeze-dried kidney tissue of rabbits adapted to various salt diets and exposed to large differences in endogenous and exogeneous mineralocorticoids. The Na-K-ATPase activity in the DCT is not influenced by mineralocorticoids. They do influence the activity in the CNT and in the CCD. In the CNT the highest activity was found with a low Na-, high K-diet. At the beginning of the CNT the enzyme activity is higher than in the end portion. While canrenoate-K treatment has no effect on Na-K-ATPase activity in the initial portions of the CNT, this drug decreases the Na-K-ATPase activity significantly in the end portion of the CNT. DOCA treatment has a significant effect on the enzyme activity in the CNT only in the end-portion of the segment, but provokes the highest Na-K-ATPase activity in the CCD. The changes in Na-K-ATPase are found to be associated with corresponding changes in the baso-lateral cell-membrane area in the segments affected.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00213747
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    facet.materialart.
    Unknown
    Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-08-26
    Description: In higher eukaryotes, a multiprotein exon junction complex is deposited on spliced messenger RNAs. The complex is organized around a stable core, which serves as a binding platform for numerous factors that influence messenger RNA function. Here, we present the crystal structure of a tetrameric exon junction core complex containing the DEAD-box adenosine triphosphatase (ATPase) eukaryotic initiation factor 4AIII (eIF4AIII) bound to an ATP analog, MAGOH, Y14, a fragment of MLN51, and a polyuracil mRNA mimic. eIF4AIII interacts with the phosphate-ribose backbone of six consecutive nucleotides and prevents part of the bound RNA from being double stranded. The MAGOH and Y14 subunits lock eIF4AIII in a prehydrolysis state, and activation of the ATPase probably requires only modest conformational changes in eIF4AIII motif I.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Andersen, Christian B F -- Ballut, Lionel -- Johansen, Jesper S -- Chamieh, Hala -- Nielsen, Klaus H -- Oliveira, Cristiano L P -- Pedersen, Jan Skov -- Seraphin, Bertrand -- Le Hir, Herve -- Andersen, Gregers Rom -- New York, N.Y. -- Science. 2006 Sep 29;313(5795):1968-72. Epub 2006 Aug 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, University of Aarhus, DK-8000 Aarhus, Denmark.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16931718" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/analogs & derivatives/metabolism ; Adenylyl Imidodiphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Crystallography, X-Ray ; DEAD-box RNA Helicases ; Dimerization ; Drosophila Proteins/chemistry/metabolism ; Eukaryotic Initiation Factor-4A/*chemistry/metabolism ; *Exons ; Humans ; Hydrogen Bonding ; Hydrolysis ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Neoplasm Proteins/*chemistry/metabolism ; Nuclear Proteins/*chemistry/metabolism ; Nucleic Acid Conformation ; Poly U/*chemistry/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA Helicases/chemistry/metabolism ; RNA, Messenger/*chemistry/metabolism ; RNA-Binding Proteins/*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...