NMR Analysis of the Architecture and Functional Remodeling of a Modular Multidomain Protein, RPA
Author:
Affiliation:
1. Departments of Biochemistry and Chemistry, and Center for Structural Biology, Vanderbilt University, Nashville, Tennessee 37232-8725
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja9013634
Reference14 articles.
1. Structural Mechanisms of DNA Replication, Repair, and Recombination
2. Replication Protein A (RPA): The Eukaryotic SSB
3. A dynamic model for replication protein A (RPA) function in DNA processing pathways
4. Solution NMR Techniques for Large Molecular and Supramolecular Structures
5. Quantitative NMR Studies of High Molecular Weight Proteins: Application to Domain Orientation and Ligand Binding in the 723 Residue Enzyme Malate Synthase G
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3. A disease-associated XPA allele interferes with TFIIH binding and primarily affects transcription-coupled nucleotide excision repair;Proceedings of the National Academy of Sciences;2023-03-09
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5. Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair;Proceedings of the National Academy of Sciences;2022-08-15
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