M
Min Soo Park
Researcher at Los Alamos National Laboratory
Publications - 44
Citations - 2673
Min Soo Park is an academic researcher from Los Alamos National Laboratory. The author has contributed to research in topics: DNA repair & Medicine. The author has an hindex of 20, co-authored 34 publications receiving 2600 citations.
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Journal ArticleDOI
Radiation-induced Assembly of Rad51 and Rad52 Recombination Complex Requires ATM and c-Abl
Gang Chen,Shyng Shiou F Yuan,Wei Liu,Yang Xu,Kelly M. Trujillo,Binwei Song,Feng Cong,Stephen P. Goff,Yun Wu,Ralph B. Arlinghaus,David Baltimore,Paul J. Gasser,Min Soo Park,Patrick Sung,Eva Y.-H. P. Lee +14 more
TL;DR: This work demonstrates that there is an I-R-induced Rad51 tyrosine phosphorylation, and this induction is dependent on both ATM and c-Abl, and suggests signaling mediated through ATM is required for the correct post-translational modification of Rad51, which is critical for the assembly of Rad 51 repair protein complex following I- R.
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The DNA Repair Endonuclease XPG Binds to Proliferating Cell Nuclear Antigen (PCNA) and Shares Sequence Elements with the PCNA-binding Regions of FEN-1 and Cyclin-dependent Kinase Inhibitor p21
TL;DR: The direct physical interaction of PCNA with xeroderma pigmentosum (XP) G, a structure-specific repair endonuclease that is homologous to FEN-1, raises the possibility of a mechanistic linkage between excision and repair synthesis that is mediated by PCNA.
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Physical interaction between human rad52 and rpa is required for homologous recombination in mammalian cells
TL;DR: It is suggested that direct physical interactions between RAD52 and RPA are essential for homologous recombination in mammalian cells.
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Specific Interactions between the Human RAD51 and RAD52 Proteins
TL;DR: The results suggest that RAD52 may modulate the catalytic activities of RAD51 protein such as homologous pairing and strand exchange through a direct physical interaction.
Journal ArticleDOI
DNA ligase I is recruited to sites of DNA replication by an interaction with proliferating cell nuclear antigen: identification of a common targeting mechanism for the assembly of replication factories
Alessandra Montecucco,Rossella Rossi,David S. Levin,Ronald K. Gary,Min Soo Park,Teresa A. Motycka,Giovanni Ciarrocchi,Antonello Villa,Giuseppe Biamonti,Alan E. Tomkinson +9 more
TL;DR: It is proposed that, in addition to functioning as a DNA polymerase processivity factor, PCNA plays a central role in the recruitment and stable association of DNA replication proteins at replication factories.