A novel DNA damage recognition protein in Schizosaccharomyces pombe

S. J. Pearson

doi:10.1093/nar/gkl270

Characterization of a DNA-damage-recognition protein from F9 teratocarcinoma cells, which is inducible by retinoic acid and cyclic AMP

Biochemical Journal ◽

10.1042/bj2930879 ◽

1993 ◽

Vol 293 (3) ◽

pp. 879-879

Keyword(s):

Dna Damage ◽

Retinoic Acid ◽

Cyclic Amp ◽

Damage Recognition ◽

Teratocarcinoma Cells ◽

Recognition Protein ◽

F9 Teratocarcinoma ◽

Dna Damage Recognition

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Characterization of a DNA damage-recognition protein from mammalian cells that binds specifically to intrastrand d(GpG) and d(ApG) DNA adducts of the anticancer drug cisplatin

Biochemistry ◽

10.1021/bi00476a032 ◽

1990 ◽

Vol 29 (24) ◽

pp. 5872-5880 ◽

Cited By ~ 83

Author(s):

Brian A. Donahue ◽

Marianne Augot ◽

Steven F. Bellon ◽

Daniel K. Treiber ◽

Jeffrey H. Toney ◽

...

Keyword(s):

Dna Damage ◽

Anticancer Drug ◽

Dna Adducts ◽

Mammalian Cells ◽

Damage Recognition ◽

Recognition Protein ◽

Dna Damage Recognition

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Distribution of mutations in the human xeroderma pigmentosum group A gene and their relationships to the functional regions of the DNA damage recognition protein

Human Mutation ◽

10.1002/(sici)1098-1004(1998)12:2<103::aid-humu5>3.3.co;2-y ◽

1998 ◽

Vol 12 (2) ◽

pp. 103-113

Author(s):

J.C. States ◽

E.R. McDuffie ◽

S.P. Myrand ◽

M. McDowell ◽

J.E. Cleaver

Keyword(s):

Dna Damage ◽

Xeroderma Pigmentosum ◽

Functional Regions ◽

Damage Recognition ◽

Recognition Protein ◽

Group A ◽

Xeroderma Pigmentosum Group A ◽

Dna Damage Recognition

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Damage-recognition proteins as a potential indicator of DNA-damage-mediated sensitivity or resistance of human cells to ultraviolet radiation

Biochemical Journal ◽

10.1042/bj2820203 ◽

1992 ◽

Vol 282 (1) ◽

pp. 203-207 ◽

Cited By ~ 13

Author(s):

C C K Chao

Keyword(s):

Dna Damage ◽

Dna Repair ◽

Hela Cells ◽

Xeroderma Pigmentosum ◽

Cross Linking ◽

Damage Recognition ◽

Modified Dna ◽

Potential Indicator ◽

Recognition Protein ◽

Dna Damage Recognition

We have previously identified damage-recognition proteins that bind to cisplatin[cis-diamminedichloroplatinum(II), a DNA cross-linking agent]- or u.v.-modified DNA in HeLa cells [Chao, Huang, Huang & Lin-Chao (1991) Mol. Cell. Biol. 11, 2075-2080; Chao, Huang, Lee & Lin-Chao (1991) Biochem. J. 277, 875-878]. In the present study we compared damage-recognition proteins in cells expressing different sensitivities to DNA damage. An increase in damage-recognition proteins and an enhancement of plasmid re-activation were detected in HeLa cells resistant to cisplatin and u.v. However, repair-defective cells derived from xeroderma-pigmentosum (a rare skin disease) patients did not express less cisplatin damage-recognition proteins than repair-competent cells, suggesting that damage-recognition-protein expression may not be related to DNA repair. By contrast, cells resistant to DNA damage consistently expressed high levels of u.v.-modified-DNA damage-recognition proteins. The results support the notion that u.v. damage-recognition proteins are different from those that bind to cisplatin. These findings also suggest that the damage-recognition proteins identified could be used as potential indicators of the sensitivity or resistance of cells to u.v.

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Distribution of mutations in the human xeroderma pigmentosum group A gene and their relationships to the functional regions of the DNA damage recognition protein

Human Mutation ◽

10.1002/(sici)1098-1004(1998)12:2<103::aid-humu5>3.0.co;2-6 ◽

1998 ◽

Vol 12 (2) ◽

pp. 103-113 ◽

Cited By ~ 38

Author(s):

JC States ◽

ER McDuffie ◽

SP Myrand ◽

M McDowell ◽

JE Cleaver

Keyword(s):

Dna Damage ◽

Xeroderma Pigmentosum ◽

Functional Regions ◽

Damage Recognition ◽

Recognition Protein ◽

Group A ◽

Xeroderma Pigmentosum Group A ◽

Dna Damage Recognition

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Faculty Opinions recommendation of A molecular mechanism for DNA damage recognition by the xeroderma pigmentosum group C protein complex.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1011200.178317 ◽

2003 ◽

Author(s):

Errol C Friedberg

Keyword(s):

Dna Damage ◽

Molecular Mechanism ◽

Protein Complex ◽

Xeroderma Pigmentosum ◽

C Protein ◽

Damage Recognition ◽

Dna Damage Recognition

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Targeting Protein-Protein Interactions in the DNA Damage Response Pathways for Cancer Chemotherapy

RSC Chemical Biology ◽

10.1039/d1cb00101a ◽

2021 ◽

Author(s):

Kerry Silva McPherson ◽

Dmitry Korzhnev

Keyword(s):

Dna Damage ◽

Dna Damage Response ◽

Protein Interactions ◽

Cell Cycle Progression ◽

Protein Protein Interactions ◽

Cycle Progression ◽

Damage Recognition ◽

Damage Response ◽

Cellular Dna ◽

Dna Damage Recognition

Cellular DNA damage response (DDR) is an extensive signaling network that orchestrates DNA damage recognition, repair and avoidance, cell cycle progression and cell death. DDR alternation is a hallmark of...

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SETD2 alterations impair DNA damage recognition and lead to resistance to chemotherapy in leukemia

Blood ◽

10.1182/blood-2017-03-775569 ◽

2017 ◽

Vol 130 (24) ◽

pp. 2631-2641 ◽

Cited By ~ 46

Author(s):

Brenton G. Mar ◽

S. Haihua Chu ◽

Josephine D. Kahn ◽

Andrei V. Krivtsov ◽

Richard Koche ◽

...

Keyword(s):

Dna Damage ◽

Dna Damage Response ◽

Mutation Rate ◽

Histone 3 ◽

Damage Recognition ◽

Key Points ◽

Damage Response ◽

Dna Damage Recognition ◽

Resistance To Chemotherapy

Key Points Alterations of SETD2, a histone 3 lysine 36 trimethyl (H3K36me3) transferase leads to resistance to DNA damaging-chemotherapy in leukemia. Low H3K36me3 levels impair DNA damage response and increase mutation rate, which may be targeted by H3K36me3 demethylase inhibition.

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