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- W1590499319 abstract "Many fundamental biological processes, such as signal transduction and cell cycle regulation, are carried out by dynamic, multi-protein complexes. Understanding the high-resolution structures of these complexes is one of the major challenges facing molecular and cellular biologists. Our laboratory is studying protein complexes containing proliferating cell nuclear antigen (PCNA). PCNA is a key replication accessory factor, which is best known for its ability to confer high processivity to DNA polymerases. PCNA interacts with a wide range of proteins that function in replication, repair, and recombination thereby regulating their access to replication forks. In addition, PCNA is post-translationally modified by ubiquitylation and SUMOylation, which promote the replication of damaged DNA and inhibit homologous recombination, respectively. We are using a combination of approaches including X-ray crystallography, small-angle X-ray scattering, single-molecule fluorescence, and Brownian dynamics simulations to study the structure and dynamics of ubiquitin-modified and SUMO-modified PCNA and the multi-protein complexes in which they function." @default.
- W1590499319 created "2016-06-24" @default.
- W1590499319 creator A5079313612 @default.
- W1590499319 date "2014-04-01" @default.
- W1590499319 modified "2023-10-16" @default.
- W1590499319 title "Architecture and dynamics of protein complexes containing proliferating cell nuclear antigen (352.3)" @default.
- W1590499319 doi "https://doi.org/10.1096/fasebj.28.1_supplement.352.3" @default.
- W1590499319 hasPublicationYear "2014" @default.
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