Structure of the Dimeric Exonuclease TREX1 in Complex with DNA Displays a Proline-rich Binding Site for WW Domains-Reference-Cited by-同舟云学术

Structure of the Dimeric Exonuclease TREX1 in Complex with DNA Displays a Proline-rich Binding Site for WW Domains

Published:2007-05 Issue:19 Volume:282 Page:14547-14557
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Brucet Marina,Querol-Audí Jordi,Serra Maria,Ramirez-Espain Ximena,Bertlik Kamila,Ruiz Lidia,Lloberas Jorge,Macias Maria J.,Fita Ignacio,Celada Antonio

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference39 articles.

1. The TREX2 3′→ 5′ Exonuclease Physically Interacts with DNA Polymerase δ and Increases Its Accuracy

2. Properties of Deoxyribonuclease III from Mammalian Tissues

3. Identification of a 3'–>5'-exonuclease that removes cytosine arabinoside monophosphate from 3' termini of DNA.

4. Exonucleases and the incorporation of aranucleotides into DNA

5. Gene-Targeted Mice Lacking the Trex1 (DNase III) 3′→5′ DNA Exonuclease Develop Inflammatory Myocarditis

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