Literature DB >> 7517674

BiP is a substrate for src kinase in vitro.

A Carlino1, H Toledo, V Vidal, B Redfield, J Strassman, M Abdel-Ghany, E Racker, H Weissbach, N Brot.   

Abstract

In a study to investigate the ability of chaperones to modulate src kinase activity, it was observed that BiP, a member of the HSP70 family found in the endoplasmic reticulum, is an excellent substrate for src kinase in vitro. The reaction requires polylysine and the results suggest that two tyrosine residues are phosphorylated. Although there is no evidence for this reaction in vivo, it does provide a very efficient method to label BiP.

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Year:  1994        PMID: 7517674     DOI: 10.1006/bbrc.1994.1880

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

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Journal:  Protein J       Date:  2006-06       Impact factor: 2.371

2.  A proteomic screen identified stress-induced chaperone proteins as targets of Akt phosphorylation in mesangial cells.

Authors:  Michelle T Barati; Madhavi J Rane; Jon B Klein; Kenneth R McLeish
Journal:  J Proteome Res       Date:  2006-07       Impact factor: 4.466

3.  Identification of phosphoproteins as possible differentiation markers in all-trans-retinoic acid-treated neuroblastoma cells.

Authors:  Giorgia Mandili; Cristina Marini; Franco Carta; Cristina Zanini; Mauro Prato; Amina Khadjavi; Franco Turrini; Giuliana Giribaldi
Journal:  PLoS One       Date:  2011-05-05       Impact factor: 3.240

  3 in total

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