Crossref journal-article
Wiley
Journal of Neurochemistry (311)
Abstract

Abstract: The neuronal phosphoprotein B‐50/GAP‐43 is associated with growth and regeneration within the nervous system and its posttranslational status can be correlated with its cellular localization during growth and regeneration. Recently, B‐50 has been shown to interact with certain G protein subunits. Regulation of G protein‐mediated signal transduction may involve ADP‐ribosylation in vivo. In the present study we have demonstrated that B‐50 is a substrate for endogenous ADP‐ribosyltransferases. The results are discussed with respect to the possible interaction of B‐50 with G proteins, but also with regard to the posttranslational modification of B‐50 by all major regulatory mechanisms that act at, or through, the neuronal membrane.

Authors 4
  1. Philip J. Coggins (first)
  2. Kim McLean (additional)
  3. Andy Nagy (additional)
  4. Henk Zwiers (additional)
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Dates
Type When
Created 18 years, 10 months ago (Oct. 5, 2006, 11:40 p.m.)
Deposited 1 year, 10 months ago (Oct. 25, 2023, 7:08 p.m.)
Indexed 1 year, 10 months ago (Oct. 26, 2023, 8:35 p.m.)
Issued 32 years, 8 months ago (Jan. 1, 1993)
Published 32 years, 8 months ago (Jan. 1, 1993)
Published Online 18 years, 10 months ago (Oct. 5, 2006)
Published Print 32 years, 8 months ago (Jan. 1, 1993)
Funders 0

None

@article{Coggins_1993, title={ADP‐Ribosylation of the Neuronal Phosphoprotein B‐50/GAP‐43}, volume={60}, ISSN={1471-4159}, url={http://dx.doi.org/10.1111/j.1471-4159.1993.tb05862.x}, DOI={10.1111/j.1471-4159.1993.tb05862.x}, number={1}, journal={Journal of Neurochemistry}, publisher={Wiley}, author={Coggins, Philip J. and McLean, Kim and Nagy, Andy and Zwiers, Henk}, year={1993}, month=jan, pages={368–371} }