Molecular Basis of the Interaction of the Human Protein Tyrosine Phosphatase Non-receptor Type 4 (PTPN4) with the Mitogen-activated Protein Kinase p38γ
Published 2016 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Molecular Basis of the Interaction of the Human Protein Tyrosine Phosphatase Non-receptor Type 4 (PTPN4) with the Mitogen-activated Protein Kinase p38γ
Authors
Keywords
-
Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 291, Issue 32, Pages 16699-16708
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2016-06-01
DOI
10.1074/jbc.m115.707208
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Phosphatase PTPN4 Preferentially Inhibits TRIF-Dependent TLR4 Pathway by Dephosphorylating TRAM
- (2015) Wanwan Huai et al. JOURNAL OF IMMUNOLOGY
- Strategies to interfere with PDZ-mediated interactions in neurons: What we can learn from the rabies virus
- (2015) Célia Caillet-Saguy et al. PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY
- Regulation of the catalytic activity of the human phosphatase PTPN4 by its PDZ domain
- (2014) Pierre Maisonneuve et al. FEBS Journal
- Reciprocal allosteric regulation of p38 and PTPN3 involves a PDZ domain-modulated complex formation
- (2014) K.-E. Chen et al. Science Signaling
- How good are my data and what is the resolution?
- (2013) Philip R. Evans et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- The 2 glutamate receptor gates long-term depression by coordinating interactions between two AMPA receptor phosphorylation sites
- (2013) K. Kohda et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Overview of theCCP4 suite and current developments
- (2011) Martyn D. Winn et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Structural basis of p38α regulation by hematopoietic tyrosine phosphatase
- (2011) Dana M Francis et al. Nature Chemical Biology
- Peptides Targeting the PDZ Domain of PTPN4 Are Efficient Inducers of Glioblastoma Cell Death
- (2011) Nicolas Babault et al. STRUCTURE
- XDS
- (2010) Wolfgang Kabsch ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- PTPH1 Dephosphorylates and Cooperates with p38γ MAPK to Increase Ras Oncogenesis through PDZ-Mediated Interaction
- (2010) Song-Wang Hou et al. CANCER RESEARCH
- PDZ domains and their binding partners: structure, specificity, and modification
- (2010) Ho-Jin Lee et al. Cell Communication and Signaling
- Loss of p38 MAPK induces pleiotropic mitotic defects and massive cell death
- (2010) A. Kukkonen-Macchi et al. JOURNAL OF CELL SCIENCE
- Attenuation of Rabies Virulence: Takeover by the Cytoplasmic Domain of Its Envelope Protein
- (2010) C. Prehaud et al. Science Signaling
- MolProbity: all-atom structure validation for macromolecular crystallography
- (2009) Vincent B. Chen et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- The protein tyrosine phosphatase PTPN4/PTP-MEG1, an enzyme capable of dephosphorylating the TCR ITAMs and regulating NF-κB, is dispensable for T cell development and/or T cell effector functions
- (2008) Jennifer A. Young et al. MOLECULAR IMMUNOLOGY
Publish scientific posters with Peeref
Peeref publishes scientific posters from all research disciplines. Our Diamond Open Access policy means free access to content and no publication fees for authors.
Learn MoreAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started