N-Glycosylation and Gaucher Disease Mutation Allosterically Alter Active-Site Dynamics of Acid-β-Glucosidase-Reference-Cited by-同舟云学术

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N-Glycosylation and Gaucher Disease Mutation Allosterically Alter Active-Site Dynamics of Acid-β-Glucosidase

Published:2020-01-02 Issue:3 Volume:10 Page:1810-1820
ISSN:2155-5435
Container-title:ACS Catalysis
language:en
Short-container-title:ACS Catal.

Author:

Souffrant Michael Gregory,Yao Xin-Qiu^ORCID,Momin Mohamed^ORCID,Hamelberg Donald^ORCID

Funder

Division of Molecular and Cellular Biosciences

Georgia Research Alliance

U.S. Department of Education

Georgia State University

Publisher

American Chemical Society (ACS)

Subject

Catalysis,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acscatal.9b04404

Reference56 articles.

1. Induced fit, conformational selection and independent dynamic segments: an extended view of binding events

2. Allostery and cooperativity revisited

3. Point mutations and sequence variability in proteins: Redistributions of preexisting populations

4. Is allostery an intrinsic property of all dynamic proteins?

5. Allosteric regulation and catalysis emerge via a common route

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