Literature DB >> 6260185

The phosphorylation of the proteins of rat liver heterogeneous ribonucleoprotein particles by an endogenous kinase activity.

A F Wilks, J T Knowler.   

Abstract

An endogenous protein kinase activity of liver heterogeneous nuclear ribonucleoprotein particles has been characterized and the particle proteins which it phosphorylates in vitro have been fractionated on two-dimensional polyacrylamide gels. The activity is dependent on Mg2+ and is further stimulated by cyclic AMP, polyamines and Mn2+.

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Year:  1981        PMID： 6260185     DOI： 10.1016/0005-2787(81)90226-4

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  3 in total

1.  Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles.

Authors:  B M Merrill; S F Barnett; W M LeStourgeon; K R Williams
Journal:  Nucleic Acids Res       Date:  1989-11-11       Impact factor: 16.971

2.  Two endogenous protein kinase activities in heterogeneous nuclear ribonucleoprotein particles (hnRNP).

Authors:  C W McGregor; J T Knowler
Journal:  Mol Biol Rep       Date:  1987       Impact factor: 2.316

3.  Phosphorylation of human hnRNP protein A1 abrogates in vitro strand annealing activity.

Authors:  F Cobianchi; C Calvio; M Stoppini; M Buvoli; S Riva
Journal:  Nucleic Acids Res       Date:  1993-02-25       Impact factor: 16.971
  3 in total

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