SAP domain forms a flexible part of DNA aperture in Ku70/80-Reference-Cited by-同舟云学术

SAP domain forms a flexible part of DNA aperture in Ku70/80

Published:2021-02-16 Issue:14 Volume:288 Page:4382-4393
ISSN:1742-464X
Container-title:The FEBS Journal
language:en
Short-container-title:FEBS J

Author:

Hnízda Aleš¹^ORCID,Tesina Petr²,Nguyen Thanh‐Binh³⁴,Kukačka Zdeněk⁵,Kater Lukas²,Chaplin Amanda K.¹,Beckmann Roland²,Ascher David B.¹³⁴⁶,Novák Petr⁵,Blundell Tom L.¹

Affiliation:

1. Department of Biochemistry University of Cambridge Cambridge UK

2. Gene Center and Department of Biochemistry University of Munich Germany

3. Computational and Systems Biology Bio21 Institute University of Melbourne Parkville VIC Australia

4. Computational Biology and Clinical Informatics Baker Heart and Diabetes Institute Melbourne VIC Australia

5. Institute of Microbiology Academy of Sciences of the Czech Republic Prague Czech Republic

6. Department of Biochemistry and Molecular Biology University of Melbourne Parkville VIC Australia

Funder

Ministerstvo Školství, Mládeže a Tělovýchovy

Jack Brockhoff Foundation

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.15732

Reference43 articles.

1. Plugged into the Ku-DNA hub: The NHEJ network

2. The Principal Role of Ku in Telomere Length Maintenance Is Promotion of Est1 Association with Telomeres

3. NHEJ pathway is involved in post-integrational DNA repair due to Ku70 binding to HIV-1 integrase

4. Role of Ku70 in deubiquitination of Mcl-1 and suppression of apoptosis

5. Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair

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