Structure Basis for Shaping the Nse4 protein by the Nse1 and Nse3 dimer within the Smc5/6 complex
Published 2021 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Structure Basis for Shaping the Nse4 protein by the Nse1 and Nse3 dimer within the Smc5/6 complex
Authors
Keywords
the Smc5/6 complex, Nse1-Nse3-Nse4, kleisin-KITE complex, DNA replication and repair, chromosome structure
Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume -, Issue -, Pages 166910
Publisher
Elsevier BV
Online
2021-03-05
DOI
10.1016/j.jmb.2021.166910
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Molecular Insights into the Architecture of the Human SMC5/6 Complex
- (2020) M. Adamus et al. JOURNAL OF MOLECULAR BIOLOGY
- Cryo-EM structure of the human cohesin-NIPBL-DNA complex
- (2020) Zhubing Shi et al. SCIENCE
- A Structure-Based Mechanism for DNA Entry into the Cohesin Ring
- (2020) Torahiko L. Higashi et al. MOLECULAR CELL
- Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism
- (2020) Byung-Gil Lee et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6
- (2020) Lucie Vondrova et al. Scientific Reports
- Purified Smc5/6 Complex Exhibits DNA Substrate Recognition and Compaction
- (2020) Pilar Gutierrez-Escribano et al. MOLECULAR CELL
- The Smc5/6 Core Complex Is a Structure-Specific DNA Binding and Compacting Machine
- (2020) Diego Serrano et al. MOLECULAR CELL
- Molecular Basis for Control of Diverse Genome Stability Factors by the Multi-BRCT Scaffold Rtt107
- (2019) Bingbing Wan et al. MOLECULAR CELL
- Real-time imaging of DNA loop extrusion by condensin
- (2018) Mahipal Ganji et al. SCIENCE
- Structural basis for Scc3-dependent cohesin recruitment to chromatin
- (2018) Yan Li et al. eLife
- SMC5/6: Multifunctional Player in Replication
- (2018) Jan Palecek Genes
- Bacillus subtilis SMC complexes juxtapose chromosome arms as they travel from origin to terminus
- (2017) Xindan Wang et al. SCIENCE
- Overall Shapes of the SMC-ScpAB Complex Are Determined by Balance between Constraint and Relaxation of Its Structural Parts
- (2017) Katsuhiko Kamada et al. STRUCTURE
- Destabilized SMC5/6 complex leads to chromosome breakage syndrome with severe lung disease
- (2016) Saskia N. van der Crabben et al. JOURNAL OF CLINICAL INVESTIGATION
- SMC complexes: from DNA to chromosomes
- (2016) Frank Uhlmann NATURE REVIEWS MOLECULAR CELL BIOLOGY
- Structures of Two Melanoma-Associated Antigens Suggest Allosteric Regulation of Effector Binding
- (2016) Joseph A. Newman et al. PLoS One
- DNA Entry into and Exit out of the Cohesin Ring by an Interlocking Gate Mechanism
- (2015) Yasuto Murayama et al. CELL
- The Phyre2 web portal for protein modeling, prediction and analysis
- (2015) Lawrence A Kelley et al. Nature Protocols
- Chromatin association of the SMC5/6 complex is dependent on binding of its NSE3 subunit to DNA
- (2015) Katerina Zabrady et al. NUCLEIC ACIDS RESEARCH
- Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links
- (2015) M. Raschle et al. SCIENCE
- Kite Proteins: a Superfamily of SMC/Kleisin Partners Conserved Across Bacteria, Archaea, and Eukaryotes
- (2015) Jan J. Palecek et al. STRUCTURE
- The Smc5/6 Complex Is an ATP-Dependent Intermolecular DNA Linker
- (2015) Takaharu Kanno et al. Cell Reports
- SMC condensin entraps chromosomal DNA by an ATP hydrolysis dependent loading mechanism in Bacillus subtilis
- (2015) Larissa Wilhelm et al. eLife
- Closing the cohesin ring: Structure and function of its Smc3-kleisin interface
- (2014) T. G. Gligoris et al. SCIENCE
- An asymmetric SMC–kleisin bridge in prokaryotic condensin
- (2013) Frank Bürmann et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Molecular Basis of SMC ATPase Activation: Role of Internal Structural Changes of the Regulatory Subcomplex ScpAB
- (2013) Katsuhiko Kamada et al. STRUCTURE
- NIH Image to ImageJ: 25 years of image analysis
- (2012) Caroline A Schneider et al. NATURE METHODS
- Analysis of the Nse3/MAGE-Binding Domain of the Nse4/EID Family Proteins
- (2012) Marc Guerineau et al. PLoS One
- iMOSFLM: a new graphical interface for diffraction-image processing withMOSFLM
- (2011) T. Geoff G. Battye et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Condensin structures chromosomal DNA through topological links
- (2011) Sara Cuylen et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Interactions between the Nse3 and Nse4 Components of the SMC5-6 Complex Identify Evolutionarily Conserved Interactions between MAGE and EID Families
- (2011) Jessica J. R. Hudson et al. PLoS One
- PHENIX: a comprehensive Python-based system for macromolecular structure solution
- (2010) Paul D. Adams et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- MAGE-RING Protein Complexes Comprise a Family of E3 Ubiquitin Ligases
- (2010) Jennifer M. Doyle et al. MOLECULAR CELL
- The HADDOCK web server for data-driven biomolecular docking
- (2010) Sjoerd J de Vries et al. Nature Protocols
- Structural Studies of a Bacterial Condensin Complex Reveal ATP-Dependent Disruption of Intersubunit Interactions
- (2009) Jae-Sung Woo et al. CELL
- Structural and Functional Insights into the Roles of the Mms21 Subunit of the Smc5/6 Complex
- (2009) Xinyuan Duan et al. MOLECULAR CELL
- Web 3DNA--a web server for the analysis, reconstruction, and visualization of three-dimensional nucleic-acid structures
- (2009) G. Zheng et al. NUCLEIC ACIDS RESEARCH
- Nse1 RING-like Domain Supports Functions of the Smc5-Smc6 Holocomplex in Genome Stability
- (2008) Stephanie Pebernard et al. MOLECULAR BIOLOGY OF THE CELL
- PROMALS3D: a tool for multiple protein sequence and structure alignments
- (2008) Jimin Pei et al. NUCLEIC ACIDS RESEARCH
Create your own webinar
Interested in hosting your own webinar? Check the schedule and propose your idea to the Peeref Content Team.
Create NowAsk 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