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Alexey Bochkarev

Researcher at Structural Genomics Consortium

Publications -  64
Citations -  5513

Alexey Bochkarev is an academic researcher from Structural Genomics Consortium. The author has contributed to research in topics: Replication protein A & Crystal structure. The author has an hindex of 34, co-authored 64 publications receiving 5183 citations. Previous affiliations of Alexey Bochkarev include University of Oklahoma Health Sciences Center & University of Toronto.

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Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA

TL;DR: The crystal structure at 2.4 Å resolution of the single-stranded- DNA-binding domain of human replication protein A (RPA) bound to DNA is reported, indicating that the mechanism of ssDNA-binding is conserved.
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Structure of the RPA trimerization core and its role in the multistep DNA‐binding mechanism of RPA

TL;DR: The data indicate that switching from 8–10 to 30 nt mode is mediated by DNA binding with the trimerization core, and this work demonstrates that the OB‐fold of DBD‐C possesses unique structural features; embedded zinc ribbon and helix–turn–helix motifs.
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Single-stranded DNA mimicry in the p53 transactivation domain interaction with replication protein A

TL;DR: The crystal structure of RPA residues 1–120 (RPA70N) bound to the N-terminal transactivation domain of p53 and NMR spectroscopy characterize two mechanisms by which the RPA/p53 interaction can be modulated suggest a mechanism for DNA damage signaling that can explain a threshold response to DNA damage.
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Structural Basis for the Recognition of DNA Repair Proteins UNG2, XPA, and RAD52 by Replication Factor RPA

TL;DR: NMR structures of the RPA32 domain were determined, defining a common structural basis for linking RPA to the nucleotide excision, base excison, and recombinational pathways of repairing damaged DNA, and support a hand-off model for the assembly and coordination of different components of the DNA repair machinery.