Conformational Change of Human Checkpoint Kinase 1 (Chk1) Induced by DNA Damage
Published 2016 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Conformational Change of Human Checkpoint Kinase 1 (Chk1) Induced by DNA Damage
Authors
Keywords
-
Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 291, Issue 25, Pages 12951-12959
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2016-04-19
DOI
10.1074/jbc.m115.713248
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Phosphorylation of Minichromosome Maintenance 3 (MCM3) by Checkpoint Kinase 1 (Chk1) Negatively Regulates DNA Replication and Checkpoint Activation
- (2015) Xiangzi Han et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Interaction of Chk1 with Treslin Negatively Regulates the Initiation of Chromosomal DNA Replication
- (2015) Cai Guo et al. MOLECULAR CELL
- KA1-targeted regulatory domain mutations activate Chk1 in the absence of DNA damage
- (2015) Eun-Yeung Gong et al. Scientific Reports
- The Interaction between Checkpoint Kinase 1 (Chk1) and the Minichromosome Maintenance (MCM) Complex Is Required for DNA Damage-induced Chk1 Phosphorylation
- (2014) Xiangzi Han et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- UbcH7 regulates 53BP1 stability and DSB repair
- (2014) Xiangzi Han et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Roles of Chk1 in cell biology and cancer therapy
- (2013) Youwei Zhang et al. INTERNATIONAL JOURNAL OF CANCER
- Autoregulatory Mechanisms of Phosphorylation of Checkpoint Kinase 1
- (2012) J. Wang et al. CANCER RESEARCH
- Coupling Cellular Localization and Function of Checkpoint Kinase 1 (Chk1) in Checkpoints and Cell Viability
- (2012) Jingna Wang et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- CHK1 targets spleen tyrosine kinase (L) for proteolysis in hepatocellular carcinoma
- (2012) Jian Hong et al. JOURNAL OF CLINICAL INVESTIGATION
- Suppressed miR-424 expression via upregulation of target gene Chk1 contributes to the progression of cervical cancer
- (2012) J Xu et al. ONCOGENE
- Conserved ATRMec1phosphorylation-independent activation of Chk1 by single amino acid substitution in the GD domain
- (2011) Elizabeth Pereira et al. CELL CYCLE
- Quantitative Co-Expression of Proteins at the Single Cell Level – Application to a Multimeric FRET Sensor
- (2011) Joachim Goedhart et al. PLoS One
- Checkpoint kinase 1 (Chk1)-short is a splice variant and endogenous inhibitor of Chk1 that regulates cell cycle and DNA damage checkpoints
- (2011) N. Pabla et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Förster resonance energy transfer as a tool to study photoreceptor biology
- (2010) Stephanie C. Hovan et al. JOURNAL OF BIOMEDICAL OPTICS
- The F Box Protein Fbx6 Regulates Chk1 Stability and Cellular Sensitivity to Replication Stress
- (2009) You-Wei Zhang et al. MOLECULAR CELL
- The DNA-damage response in human biology and disease
- (2009) Stephen P. Jackson et al. NATURE
- Chk1 C-terminal regulatory phosphorylation mediates checkpoint activation by de-repression of Chk1 catalytic activity
- (2009) M Walker et al. ONCOGENE
- Bimolecular Fluorescence Complementation (BiFC) Analysis as a Probe of Protein Interactions in Living Cells
- (2008) Tom K. Kerppola Annual Review of Biophysics
- ATRMec1Phosphorylation-independent Activation of Chk1in Vivo
- (2008) Yinhuai Chen et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Regulation of Chk1 by Its C-terminal Domain
- (2008) Ana Kosoy et al. MOLECULAR BIOLOGY OF THE CELL
- Essential function of Chk1 can be uncoupled from DNA damage checkpoint and replication control
- (2008) D. Wilsker et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Find the ideal target journal for your manuscript
Explore over 38,000 international journals covering a vast array of academic fields.
SearchCreate your own webinar
Interested in hosting your own webinar? Check the schedule and propose your idea to the Peeref Content Team.
Create Now