标题
3.9 Å structure of the yeast Mec1-Ddc2 complex, a homolog of human ATR-ATRIP
作者
关键词
-
出版物
SCIENCE
Volume 358, Issue 6367, Pages 1206-1209
出版商
American Association for the Advancement of Science (AAAS)
发表日期
2017-12-01
DOI
10.1126/science.aan8414
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- DNA-PKcs structure suggests an allosteric mechanism modulating DNA double-strand break repair
- (2017) Bancinyane L. Sibanda et al. SCIENCE
- The Dimeric Architecture of Checkpoint Kinases Mec1ATRand Tel1ATMReveal a Common Structural Organization
- (2016) Marta Sawicka et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- ETAA1 acts at stalled replication forks to maintain genome integrity
- (2016) Thomas E. Bass et al. NATURE CELL BIOLOGY
- Structure of the intact ATM/Tel1 kinase
- (2016) Xuejuan Wang et al. Nature Communications
- Tor forms a dimer through an N-terminal helical solenoid with a complex topology
- (2016) Domagoj Baretić et al. Nature Communications
- 4.4 Å Resolution Cryo-EM structure of human mTOR Complex 1
- (2016) Huirong Yang et al. Protein & Cell
- Regulation of Mec1 kinase activity by the SWI/SNF chromatin remodeling complex
- (2015) Prabodh Kapoor et al. GENES & DEVELOPMENT
- Probing the Mec1ATRCheckpoint Activation Mechanism with Small Peptides
- (2015) Paulina H. Wanrooij et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- ATM and ATR as therapeutic targets in cancer
- (2015) Anika Maria Weber et al. PHARMACOLOGY & THERAPEUTICS
- Architecture of human mTOR complex 1
- (2015) C. H. S. Aylett et al. SCIENCE
- Mutation of Serine 1333 in the ATR HEAT Repeats Creates a Hyperactive Kinase
- (2014) Jessica W. Luzwick et al. PLoS One
- The structural basis for mTOR function
- (2014) Domagoj Baretić et al. SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
- Ddc2 Mediates Mec1 Activation through a Ddc1- or Dpb11-Independent Mechanism
- (2014) Amitava Bandhu et al. PLoS Genetics
- mTOR kinase structure, mechanism and regulation
- (2013) Haijuan Yang et al. NATURE
- Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
- (2013) Xueming Li et al. NATURE METHODS
- RELION: Implementation of a Bayesian approach to cryo-EM structure determination
- (2012) Sjors H.W. Scheres JOURNAL OF STRUCTURAL BIOLOGY
- Analysis of Mutations That Dissociate G2and Essential S Phase Functions of Human Ataxia Telangiectasia-mutated and Rad3-related (ATR) Protein Kinase
- (2011) Edward A. Nam et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- The Unstructured C-terminal Tail of Yeast Dpb11 (Human TopBP1) Protein Is Dispensable for DNA Replication and the S Phase Checkpoint but Required for the G2/M Checkpoint
- (2011) Vasundhara M. Navadgi-Patil et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Thr-1989 Phosphorylation Is a Marker of Active Ataxia Telangiectasia-mutated and Rad3-related (ATR) Kinase
- (2011) Edward A. Nam et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- ATR Autophosphorylation as a Molecular Switch for Checkpoint Activation
- (2011) Shizhou Liu et al. MOLECULAR CELL
- Features and development ofCoot
- (2010) P. Emsley et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- PHENIX: a comprehensive Python-based system for macromolecular structure solution
- (2010) Paul D. Adams et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- The Mek1 phosphorylation cascade plays a role in meiotic recombination ofSchizosaccharomyces pombe
- (2010) Takahiro Tougan et al. CELL CYCLE
- DoG Picker and TiltPicker: Software tools to facilitate particle selection in single particle electron microscopy
- (2009) N.R. Voss et al. JOURNAL OF STRUCTURAL BIOLOGY
- Crystal structure of DNA-PKcs reveals a large open-ring cradle comprised of HEAT repeats
- (2009) Bancinyane L. Sibanda et al. NATURE
- TopBP1 activates ATR through ATRIP and a PIKK regulatory domain
- (2008) D. A. Mordes et al. GENES & DEVELOPMENT
Find the ideal target journal for your manuscript
Explore over 38,000 international journals covering a vast array of academic fields.
SearchAsk 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