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  1. Problems and paradigms: Multifunctional proteins suggest connections between transcriptional and post‐transcriptional processes.Michael Ladomery - 1997 - Bioessays 19 (10):903-909.
    Recent findings indicate that substantial cross‐talk may exist between transcriptional and post‐transcriptional processes. Firstly, there are suggestions that specific promoters influence the post‐transcriptional fate of transcripts, pointing to communication between protein complexes assembled on DNA and nascent pre‐mRNA. Secondly, an increasing number of proteins appear to be multifunctional, participating in transcriptional and post‐transcriptional events. The classic example is TFIIIA, required for both the transcription of 5S rRNA genes and the packaging of 5S rRNA. TFIIIA is now joined by the Y‐box (...)
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  • Cold shock and adaptation.Heather A. Thieringer, Pamela G. Jones & Masayori Inouye - 1998 - Bioessays 20 (1):49-57.
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  • The pleiotropic functions of the Y‐box‐binding protein, YB‐1.Kimitoshi Kohno, Hiroto Izumi, Takeshi Uchiumi, Megumi Ashizuka & Michihiko Kuwano - 2003 - Bioessays 25 (7):691-698.
    The Y‐box‐binding protein (YB‐1) represents the most evolutionary conserved nucleic‐acid‐binding protein currently known. YB‐1 is a member of the cold‐shock domain (CSD) protein superfamily. It performs a wide variety of cellular functions, including transcriptional regulation, translational regulation, DNA repair, drug resistance and stress responses to extracellular signals. As a result, YB‐1 expression is closely associated with cell proliferation. In this review, we will begin by briefly describing the characteristics of YB‐1 and will then summarize the pleiotropic functions brought about via (...)
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  • Cold shock and adaptation.Robert L. Margolis & Leslie Wilson - 1998 - Bioessays 20 (1):49-57.
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  • A case of convergent evolution of nucleic acid binding modules.Peter Graumann & Moharned A. Marahiel - 1996 - Bioessays 18 (4):309-315.
    Divergent evolution can explain how many proteins containing structurally similar domains, which perform a variety of related functions, have evolved from a relatively small number of modules or protein domains. However, it cannot explain how protein domains with similar, but distinguishable, functions and similar, but distinguishable, structures have evolved. Examples of this are the RNA‐binding proteins containing the RNA‐binding domain (RBD), and a newly established protein group, the cold‐shock domain (CSD) protein family. Both protein domains contain conserved RNP motifs on (...)
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