M
Minhui Shen
Researcher at Beth Israel Deaconess Medical Center
Publications - 6
Citations - 2589
Minhui Shen is an academic researcher from Beth Israel Deaconess Medical Center. The author has contributed to research in topics: PIN1 & NIMA-Interacting Peptidylprolyl Isomerase. The author has an hindex of 6, co-authored 6 publications receiving 2500 citations. Previous affiliations of Minhui Shen include Harvard University.
Papers
More filters
Journal ArticleDOI
Sequence-specific and phosphorylation dependent proline isomerization: A potential mitotic regulatory mechanism
Michael B. Yaffe,Mike Schutkowski,Minhui Shen,Xiao Zhen Zhou,P. Todd Stukenberg,Jens Rahfeld,Jian Xu,Jian Kuang,Marc W. Kirschner,Gunter Fischer,Lewis C. Cantley,Kun Ping Lu +11 more
TL;DR: Pin1 is shown to be a phosphorylation-dependent PPIase that specifically recognizes the phosphoserine-proline or phosphothreonine- Proline bonds present in mitotic phosphoproteins, providing the basis for the specific interaction between Pin1 and MPM-2 antigens.
Journal ArticleDOI
Function of WW Domains as Phosphoserine- or Phosphothreonine-Binding Modules
TL;DR: The Pin1 WW domain functioned as a phosphoserine- or phosphothreonine-binding module, with properties similar to those of SRC homology 2 domains, which was required for Pin1 to interact with its substrates in vitro and to perform its essential function in vivo.
Journal ArticleDOI
Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins.
Xiao Zhen Zhou,Oliver Kops,Andreas Werner,Pei Jung Lu,Minhui Shen,Gerlind Stoller,Gerhard Küllertz,Michael J. R. Stark,Gunter Fischer,Kun Ping Lu +9 more
TL;DR: It is shown that the major Pro-directed phosphatase PP2A is conformation-specific and effectively dephosphorylates only the trans pSer/Thr-Pro isomer, and prolyl isomerase activity of Pin1 is essential for cell division in vivo.
Journal ArticleDOI
The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins.
TL;DR: It is reported that in both human cells and Xenopus extracts, Pin1 interacts directly with a subset of mitotic phosphoproteins on phosphorylated Ser/Thr-Pro motifs in a phosphorylation-dependent and mitosis-specific manner.
Journal ArticleDOI
Role of phosphorylation in determining the backbone dynamics of the serine/ threonine-proline motif and pin1 substrate recognition
Mike Schutkowski,Anne Bernhardt,Xiao Zhen Zhou,Minhui Shen,Ulf Reimer,Jens-Ullrich Rahfeld,Kun Ping Lu,Gunter Fischer +7 more
TL;DR: The results demonstrate that protein phosphorylation specifically regulates the backbone dynamics of the Ser/Thr-Pro motifs and that Pin1 specifically isomerizes the certain conformation of the phosphorylated Ser/ threonine-proline motifs.