A dynamic allosteric pathway underlies Rad50 ABC ATPase function in DNA repair
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Title
A dynamic allosteric pathway underlies Rad50 ABC ATPase function in DNA repair
Authors
Keywords
-
Journal
Scientific Reports
Volume 8, Issue 1, Pages -
Publisher
Springer Nature
Online
2018-01-22
DOI
10.1038/s41598-018-19908-8
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Related references
Note: Only part of the references are listed.- Advances in NMR Methods To Map Allosteric Sites: From Models to Translation
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- ATP-driven Rad50 conformations regulate DNA tethering, end resection, and ATM checkpoint signaling
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- ATP Hydrolysis by RAD50 Protein Switches MRE11 Enzyme from Endonuclease to Exonuclease
- (2011) Jerzy Majka et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methyl–methyl nuclear overhauser enhancement spectroscopy
- (2011) Vincenzo Venditti et al. JOURNAL OF BIOMOLECULAR NMR
- An Optimized Relaxation-Based Coherence Transfer NMR Experiment for the Measurement of Side-Chain Order in Methyl-Protonated, Highly Deuterated Proteins
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- Regulated functional alternative splicing in Drosophila
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- Nbs1 Flexibly Tethers Ctp1 and Mre11-Rad50 to Coordinate DNA Double-Strand Break Processing and Repair
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- (2008) R. Scott Williams et al. CELL
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