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Death-associated protein kinase 1 phosphorylates Pin1 and inhibits its prolyl isomerase activity and cellular function

Academic Article
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  • Identity
  • Additional Document Info
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Overview

authors

  • Lee, T. H.
  • Chen, C. H.
  • Suizu, F.
  • Huang, P.
  • Schiene-Fischer, C.
  • Daum, S.
  • Zhang, Yan Jessie
  • Goate, A.
  • Chen, R. H.
  • Zhou, X. Z.
  • Lu, K. P.

publication date

  • April 2011

journal

  • Molecular Cell  Journal

subject areas

  • Active Transport, Cell Nucleus
  • Animals
  • Apoptosis Regulatory Proteins
  • Breast Neoplasms
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Catalytic Domain
  • Cell Cycle
  • Cell Nucleus
  • Cell Proliferation
  • Cell Transformation, Neoplastic
  • Centrosome
  • Death-Associated Protein Kinases
  • Enzyme Stability
  • Female
  • HeLa Cells
  • Humans
  • Immunohistochemistry
  • Mice
  • Mice, Knockout
  • Microscopy, Fluorescence
  • Mutation
  • NIH 3T3 Cells
  • NIMA-Interacting Peptidylprolyl Isomerase
  • Peptidylprolyl Isomerase
  • Phosphorylation
  • Protein Interaction Domains and Motifs
  • Protein Interaction Mapping
  • Recombinant Fusion Proteins
  • Serine
  • Signal Transduction
  • Time Factors
  • Tissue Array Analysis
  • Transfection
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Identity

PubMed Central ID

  • PMC3088080

International Standard Serial Number (ISSN)

  • 1097-2765

Digital Object Identifier (DOI)

  • 10.1016/j.molcel.2011.03.005

PubMed ID

  • 21497122
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Additional Document Info

start page

  • 147

end page

  • 159

volume

  • 42

issue

  • 2

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