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  • 1995-1999  (2)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    [s.l.] : Macmillan Magazines Ltd.
    Nature 391 (1998), S. 99-102 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Ribonuclease (RNase) E is an extensively studied enzyme from Escherichia coli whose site-specific endoribonuclease activity on single-stranded RNA has a central role in the processing of ribosomal RNA, the degradation of messenger RNA and the control of replication of ColE1-type plasmids (for ...
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cancer and metastasis reviews 15 (1996), S. 429-444 
    ISSN: 1573-7233
    Keywords: intermediate filaments ; keratins ; phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Intermediate filament (IF) proteins, a large family of tissue specific proteins, undergo several posttranslational modifications, with phosphorylation being the most studied modification. IF protein phosphorylation is highly dynamic and involves the head and/or tail domains of these proteins, which are the domains that impart most of the structural heterogeneity and hence presumed tissue specific functions. Although the function of IF proteins remains poorly understood, several regulatory roles for IF protein phosphorylation have been identified or are emerging. Those roles include filament disassembly and reorganization, solubility, localization within specific cellular domains, association with other cytoplasmic or membrane associated proteins, protection against physiologic stress and mediation of tissue-specific functions. Understanding the mechanistic and functional aspects of IF protein phosphorylation is providing insights not only regarding the function of this modification, but also regarding the function of IF proteins.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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