Structural basis for conformational switching and GTP loading of the large G protein atlastin-Reference-Cited by-同舟云学术

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Structural basis for conformational switching and GTP loading of the large G protein atlastin

Published:2013-01-18 Issue:3 Volume:32 Page:369-384
ISSN:0261-4189
Container-title:The EMBO Journal
language:
Short-container-title:EMBO J

Author:

Byrnes Laura J,Singh Avtar,Szeto Kylan,Benvin Nicole M,O’Donnell John P,Zipfel Warren R,Sondermann Holger

Publisher

Wiley

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Reference45 articles.

1. PHENIX: building new software for automated crystallographic structure determination

2. GTPase Cycle of Dynamin Is Coupled to Membrane Squeeze and Release, Leading to Spontaneous Fission

3. Structures of the atlastin GTPase provide insight into homotypic fusion of endoplasmic reticulum membranes

4. Structural basis for the nucleotide-dependent dimerization of the large G protein atlastin-1/SPG3A

5. G domain dimerization controls dynamin's assembly-stimulated GTPase activity

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