Pin1-Dependent Prolyl Isomerization Regulates Dephosphorylation of Cdc25C and Tau Proteins-Reference-Cited by-同舟云学术

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Pin1-Dependent Prolyl Isomerization Regulates Dephosphorylation of Cdc25C and Tau Proteins

Published:2000-10 Issue:4 Volume:6 Page:873-883
ISSN:1097-2765
Container-title:Molecular Cell
language:en
Short-container-title:Molecular Cell

Author:

Zhou Xiao Zhen,Kops Oliver,Werner Andreas,Lu Pei-Jung,Shen Minhui,Stoller Gerlind,Küllertz Gerhard,Stark Michael,Fischer Gunter,Lu Kun Ping

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference45 articles.

1. A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase Pin1;Albert;J. Cell Sci.,1999

2. A phosphatase activity in Xenopus oocyte extracts preferentially dephosphorylates the MPM-2 epitope;Che;FEBS Lett.,1998

3. Dephosphorylation of cdc25-C by a type-2A protein phosphatase;Clarke;Mol. Biol. Cell,1993

4. The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1;Crenshaw;EMBO J.,1998

5. All cyclophilins and FKBPs are dispensible for viability in Saccharomyces cerevisiae;Dolinski;Proc. Natl. Acad. Sci. USA,1997

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