标题
Structural Basis for DNA Damage-Dependent Poly(ADP-ribosyl)ation by Human PARP-1
作者
关键词
-
出版物
SCIENCE
Volume 336, Issue 6082, Pages 728-732
出版商
American Association for the Advancement of Science (AAAS)
发表日期
2012-05-11
DOI
10.1126/science.1216338
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Visualization of a DNA-PK/PARP1 complex
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- Crystal Structures of Poly(ADP-ribose) Polymerase-1 (PARP-1) Zinc Fingers Bound to DNA
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- The DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc Finger
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- XDS
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- The PARP Side of the Nucleus: Molecular Actions, Physiological Outcomes, and Clinical Targets
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- Structural and Biophysical Studies of Human PARP-1 in Complex with Damaged DNA
- (2009) Wayne Lilyestrom et al. JOURNAL OF MOLECULAR BIOLOGY
- Identification of the ADP-Ribosylation Sites in the PARP-1 Automodification Domain: Analysis and Implications
- (2009) Zhihua Tao et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Inhibition of Poly(ADP-Ribose) Polymerase in Tumors fromBRCAMutation Carriers
- (2009) Peter C. Fong et al. NEW ENGLAND JOURNAL OF MEDICINE
- Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites
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- Domain C of Human Poly(ADP-ribose) Polymerase-1 Is Important for Enzyme Activity and Contains a Novel Zinc-Ribbon Motif†,‡
- (2008) Zhihua Tao et al. BIOCHEMISTRY
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