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  1. Article: PCNA cycling dynamics during DNA replication and repair in mammals.

    Kang, Sukhyun / Yoo, Juyeong / Myung, Kyungjae

    Trends in genetics : TIG

    2024  

    Abstract: Proliferating cell nuclear antigen (PCNA) is a eukaryotic replicative DNA clamp. Furthermore, DNA-loaded PCNA functions as a molecular hub during DNA replication and repair. PCNA forms a closed homotrimeric ring that encircles the DNA, and association ... ...

    Abstract Proliferating cell nuclear antigen (PCNA) is a eukaryotic replicative DNA clamp. Furthermore, DNA-loaded PCNA functions as a molecular hub during DNA replication and repair. PCNA forms a closed homotrimeric ring that encircles the DNA, and association and dissociation of PCNA from DNA are mediated by clamp-loader complexes. PCNA must be actively released from DNA after completion of its function. If it is not released, abnormal accumulation of PCNA on chromatin will interfere with DNA metabolism. ATAD5 containing replication factor C-like complex (RLC) is a PCNA-unloading clamp-loader complex. ATAD5 deficiency causes various DNA replication and repair problems, leading to genome instability. Here, we review recent progress regarding the understanding of the action mechanisms of PCNA unloading complex in DNA replication/repair pathways.
    Language English
    Publishing date 2024-03-13
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 619240-3
    ISSN 1362-4555 ; 0168-9525 ; 0168-9479
    ISSN (online) 1362-4555
    ISSN 0168-9525 ; 0168-9479
    DOI 10.1016/j.tig.2024.02.006
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2272: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    Jg. 1995 - 2021: Lesesall (2.OG)
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  2. Article ; Online: Eukaryotic 4Rs: DNA replication, repair, recombination, and damage response.

    Myung, Kyungjae

    Mutation research

    2018  Volume 809, Page(s) 56–57

    MeSH term(s) Animals ; DNA Damage ; DNA Repair/physiology ; DNA Replication/physiology ; Humans ; Recombination, Genetic/physiology
    Language English
    Publishing date 2018-04-26
    Publishing country Netherlands
    Document type Editorial ; Introductory Journal Article
    ZDB-ID 206607-5
    ISSN 1873-135X ; 1383-5718 ; 0027-5107 ; 0165-1110 ; 0165-1161 ; 0165-7992 ; 0921-8777 ; 0165-1218 ; 1383-5726 ; 0167-8817 ; 0921-8734 ; 1383-5742
    ISSN (online) 1873-135X
    ISSN 1383-5718 ; 0027-5107 ; 0165-1110 ; 0165-1161 ; 0165-7992 ; 0921-8777 ; 0165-1218 ; 1383-5726 ; 0167-8817 ; 0921-8734 ; 1383-5742
    DOI 10.1016/j.mrfmmm.2018.04.002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1316: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
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  3. Article ; Online: Crosstalk between different DNA repair pathways for DNA double strand break repairs.

    Oh, Jung-Min / Myung, Kyungjae

    Mutation research. Genetic toxicology and environmental mutagenesis

    2021  Volume 873, Page(s) 503438

    Abstract: DNA double strand breaks (DSBs) are the most threatening type of DNA lesions and must be repaired properly in order to inhibit severe diseases and cell death. There are four major repair pathways for DSBs: non-homologous end joining (NHEJ), homologous ... ...

    Abstract DNA double strand breaks (DSBs) are the most threatening type of DNA lesions and must be repaired properly in order to inhibit severe diseases and cell death. There are four major repair pathways for DSBs: non-homologous end joining (NHEJ), homologous recombination (HR), single strand annealing (SSA) and alternative end joining (alt-EJ). Cells choose repair pathway depending on the cell cycle phase and the length of 3' end of the DNA when DSBs are generated. Blunt and short regions of the 5' or 3' overhang DNA are repaired by NHEJ, which uses direct ligation or limited resection processing of the broken DNA end. In contrast, HR, SSA and alt-EJ use the resected DNA generated by the MRN (MRE11-RAD50-NBS1) complex and C-terminal binding protein interacting protein (CtIP) activated during the S and G2 phases. Here, we review recent findings on each repair pathway and the choice of repair mechanism and highlight the role of mismatch repair (MMR) protein in HR.
    MeSH term(s) DNA ; DNA Breaks, Double-Stranded ; DNA End-Joining Repair ; DNA Repair ; G2 Phase ; S Phase
    Chemical Substances DNA (9007-49-2)
    Language English
    Publishing date 2021-12-15
    Publishing country Netherlands
    Document type Journal Article ; Review
    ISSN 1879-3592
    ISSN (online) 1879-3592
    DOI 10.1016/j.mrgentox.2021.503438
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Targeting the cancer cell state.

    Myung, Kyungjae

    Cell cycle (Georgetown, Tex.)

    2015  Volume 14, Issue 15, Page(s) 2385–2386

    MeSH term(s) Animals ; Brain Neoplasms/genetics ; Cell Cycle Proteins/antagonists & inhibitors ; DNA Damage/drug effects ; ErbB Receptors/biosynthesis ; Glioblastoma/genetics ; Humans ; Protein-Serine-Threonine Kinases/antagonists & inhibitors ; Proto-Oncogene Proteins/antagonists & inhibitors
    Chemical Substances Cell Cycle Proteins ; Proto-Oncogene Proteins ; ErbB Receptors (EC 2.7.10.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2015-06-17
    Publishing country United States
    Document type Editorial ; Comment
    ZDB-ID 2146183-1
    ISSN 1551-4005 ; 1538-4101 ; 1554-8627
    ISSN (online) 1551-4005
    ISSN 1538-4101 ; 1554-8627
    DOI 10.1080/15384101.2015.1063294
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5881: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article ; Online: Alkylation of nucleobases by 2-chloro-

    Wie, Minwoo / Khim, Keon Woo / Groehler Iv, Arnold S / Heo, Soomin / Woo, Junhyeok / Son, Kook / Lee, Eun A / Ra, Jae Sun / Hong, Sung You / Schärer, Orlando D / Choi, Jang Hyun / Myung, Kyungjae

    NAR cancer

    2023  Volume 5, Issue 3, Page(s) zcad042

    Abstract: ... ...

    Abstract Targeting
    Language English
    Publishing date 2023-08-07
    Publishing country England
    Document type Journal Article
    ISSN 2632-8674
    ISSN (online) 2632-8674
    DOI 10.1093/narcan/zcad042
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: RAD51 separation of function mutation disables replication fork maintenance but preserves DSB repair.

    Son, Mi Young / Belan, Ondrej / Spirek, Mario / Cibulka, Jakub / Nikulenkov, Fedor / Kim, You Young / Hwang, Sunyoung / Myung, Kyungjae / Montagna, Cristina / Kim, Tae Moon / Krejci, Lumir / Hasty, Paul

    iScience

    2024  Volume 27, Issue 4, Page(s) 109524

    Abstract: Homologous recombination (HR) protects replication forks (RFs) and repairs DNA double-strand breaks (DSBs). Within HR, BRCA2 regulates RAD51 via two interaction regions: the BRC repeats to form filaments on single-stranded DNA and exon 27 (Ex27) to ... ...

    Abstract Homologous recombination (HR) protects replication forks (RFs) and repairs DNA double-strand breaks (DSBs). Within HR, BRCA2 regulates RAD51 via two interaction regions: the BRC repeats to form filaments on single-stranded DNA and exon 27 (Ex27) to stabilize the filament. Here, we identified a RAD51 S181P mutant that selectively disrupted the RAD51-Ex27 association while maintaining interaction with BRC repeat and proficiently forming filaments capable of DNA binding and strand invasion. Interestingly, RAD51 S181P was defective for RF protection/restart but proficient for DSB repair. Our data suggest that Ex27-mediated stabilization of RAD51 filaments is required for the protection of RFs, while it seems dispensable for the repair of DSBs.
    Language English
    Publishing date 2024-03-16
    Publishing country United States
    Document type Journal Article
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2024.109524
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Distinct Motifs in ATAD5 C-Terminal Domain Modulate PCNA Unloading Process.

    Ryu, Eunjin / Ha, Na Young / Jung, Woojae / Yoo, Juyeong / Myung, Kyungjae / Kang, Sukhyun

    Cells

    2022  Volume 11, Issue 11

    Abstract: Proliferating cell nuclear antigen (PCNA) is a DNA clamp that functions in key roles for DNA replication and repair. After the completion of DNA synthesis, PCNA should be unloaded from DNA in a timely way. The ATAD5-RFC-Like Complex (ATAD5-RLC) unloads ... ...

    Abstract Proliferating cell nuclear antigen (PCNA) is a DNA clamp that functions in key roles for DNA replication and repair. After the completion of DNA synthesis, PCNA should be unloaded from DNA in a timely way. The ATAD5-RFC-Like Complex (ATAD5-RLC) unloads PCNA from DNA. However, the mechanism of the PCNA-unloading process remains unclear. In this study, we determined the minimal PCNA-unloading domain (ULD) of ATAD5. We identified several motifs in the ATAD5 ULD that are essential in the PCNA-unloading process. The C-terminus of ULD is required for the stable association of RFC2-5 for active RLC formation. The N-terminus of ULD participates in the opening of the PCNA ring. ATAD5-RLC was more robustly bound to open-liable PCNA compared to the wild type. These results suggest that distinct motifs of the ATAD5 ULD participate in each step of the PCNA-unloading process.
    MeSH term(s) DNA/metabolism ; DNA Damage ; DNA Replication ; DNA-Binding Proteins/metabolism ; Proliferating Cell Nuclear Antigen/metabolism
    Chemical Substances DNA-Binding Proteins ; Proliferating Cell Nuclear Antigen ; DNA (9007-49-2)
    Language English
    Publishing date 2022-06-03
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells11111832
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Cobll1: A new player in CML.

    Kim, Hongtae / Kim, Dong-Wook / Myung, Kyungjae

    Oncotarget

    2017  Volume 8, Issue 53, Page(s) 90626–90627

    Language English
    Publishing date 2017-10-31
    Publishing country United States
    Document type Editorial
    ZDB-ID 2560162-3
    ISSN 1949-2553 ; 1949-2553
    ISSN (online) 1949-2553
    ISSN 1949-2553
    DOI 10.18632/oncotarget.21705
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: PCNA Ser46-Leu47 residues are crucial in preserving genomic integrity.

    Sangin Kim / Yeongjae Kim / Youyoung Kim / Suhyeon Yoon / Kyoo-Young Lee / Yoonsung Lee / Sukhyun Kang / Kyungjae Myung / Chang-Kyu Oh

    PLoS ONE, Vol 18, Iss 5, p e

    2023  Volume 0285337

    Abstract: Proliferating cell nuclear antigen (PCNA) is a maestro of DNA replication. PCNA forms a homotrimer and interacts with various proteins, such as DNA polymerases, DNA ligase I (LIG1), and flap endonuclease 1 (FEN1) for faithful DNA replication. Here, we ... ...

    Abstract Proliferating cell nuclear antigen (PCNA) is a maestro of DNA replication. PCNA forms a homotrimer and interacts with various proteins, such as DNA polymerases, DNA ligase I (LIG1), and flap endonuclease 1 (FEN1) for faithful DNA replication. Here, we identify the crucial role of Ser46-Leu47 residues of PCNA in maintaining genomic integrity using in vitro, and cell-based assays and structural prediction. The predicted PCNAΔSL47 structure shows the potential distortion of the central loop and reduced hydrophobicity. PCNAΔSL47 shows a defective interaction with PCNAWT leading to defects in homo-trimerization in vitro. PCNAΔSL47 is defective in the FEN1 and LIG1 interaction. PCNA ubiquitination and DNA-RNA hybrid processing are defective in PCNAΔSL47-expressing cells. Accordingly, PCNAΔSL47-expressing cells exhibit an increased number of single-stranded DNA gaps and higher levels of γH2AX, and sensitivity to DNA-damaging agents, highlighting the importance of PCNA Ser46-Leu47 residues in maintaining genomic integrity.
    Keywords Medicine ; R ; Science ; Q
    Subject code 612
    Language English
    Publishing date 2023-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article ; Online: Distinct Motifs in ATAD5 C-Terminal Domain Modulate PCNA Unloading Process

    Eunjin Ryu / Na Young Ha / Woojae Jung / Juyeong Yoo / Kyungjae Myung / Sukhyun Kang

    Cells, Vol 11, Iss 1832, p

    2022  Volume 1832

    Abstract: Proliferating cell nuclear antigen (PCNA) is a DNA clamp that functions in key roles for DNA replication and repair. After the completion of DNA synthesis, PCNA should be unloaded from DNA in a timely way. The ATAD5-RFC-Like Complex (ATAD5-RLC) unloads ... ...

    Abstract Proliferating cell nuclear antigen (PCNA) is a DNA clamp that functions in key roles for DNA replication and repair. After the completion of DNA synthesis, PCNA should be unloaded from DNA in a timely way. The ATAD5-RFC-Like Complex (ATAD5-RLC) unloads PCNA from DNA. However, the mechanism of the PCNA-unloading process remains unclear. In this study, we determined the minimal PCNA-unloading domain (ULD) of ATAD5. We identified several motifs in the ATAD5 ULD that are essential in the PCNA-unloading process. The C-terminus of ULD is required for the stable association of RFC2-5 for active RLC formation. The N-terminus of ULD participates in the opening of the PCNA ring. ATAD5-RLC was more robustly bound to open-liable PCNA compared to the wild type. These results suggest that distinct motifs of the ATAD5 ULD participate in each step of the PCNA-unloading process.
    Keywords ATAD5 ; PCNA ; PCNA unloading ; RFC-like complex ; RLC ; SUMOylation ; Biology (General) ; QH301-705.5
    Subject code 612
    Language English
    Publishing date 2022-06-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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