Single-particle analysis of full-length human poly(ADP-ribose) polymerase 1-Reference-Cited by-同舟云学术

Single-particle analysis of full-length human poly(ADP-ribose) polymerase 1

Published:2019 Issue:0 Volume:16 Page:59-67
ISSN:2189-4779
Container-title:Biophysics and Physicobiology
language:en
Short-container-title:BIOPHYSICS

Author:

Kouyama Kenichi¹,Mayanagi Kouta²,Nakae Setsu¹,Nishi Yoshisuke¹,Miwa Masanao¹,Shirai Tsuyoshi¹

Affiliation:

1. Nagahama Institute of BioScience and Technology

2. Medical Institute of Bioregulation, Kyushu University

Publisher

Biophysical Society of Japan

Subject

General Medicine

Link

https://www.jstage.jst.go.jp/article/biophysico/16/0/16_59/_pdf

Reference9 articles.

1. [2] Sugimura, T. Poly(adenosine diphosphate ribose). Prog. Nucleic Acid Res. Mol. Biol. 13, 127–151 (1973).

2. [3] Miwa, M., Ishihara, M., Takishima, S., Takasuka, N., Maeda, M., Yamaizumi, Z., et al. The branching and linear portions of poly(adenosine diphosphate ribose) have the same alpha (1 leads to 2) ribose-ribose linkage. J. Biol. Chem. 256, 2916–2921 (1981).

3. [6] Miwa, M. & Masutani, M. PolyADP-ribosylation and cancer. Cancer Sci. 98, 1528–1535 (2007).

4. [9] Menissier-de Murcia, J., Molinete, M., Gradwohl, G., Simonin, F. & de Murcia, G. Zinc-binding domain of poly(ADP-ribose)polymerase participates in the recognition of single strand breaks on DNA. J. Mol. Biol. 210, 229–233 (1989).

5. [12] Masson, M., Niedergang, C., Schreiber, V., Muller, S., Menissier-de Murcia, J. & de Murcia, G. XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage. Mol. Cell. Biol. 18, 3563–3571 (1998).

Cited by 5 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Cooperative nucleic acid binding by Poly ADP-ribose polymerase 1;Scientific Reports;2024-03-29

2. Parthanatos: Mechanisms, modulation, and therapeutic prospects in neurodegenerative disease and stroke;Biochemical Pharmacology;2024-03

3. PARP1-DNA co-condensation drives DNA repair site assembly to prevent disjunction of broken DNA ends;Cell;2024-02

4. Exploring the interplay between PARP1 and circRNA biogenesis and function;WIREs RNA;2023-11-13

5. Functional Roles of PARP2 in Assembling Protein–Protein Complexes Involved in Base Excision DNA Repair;International Journal of Molecular Sciences;2021-04-28