Aldolases Utilize Different Oligomeric States To Preserve Their Functional Dynamics-Reference-Cited by-同舟云学术

Aldolases Utilize Different Oligomeric States To Preserve Their Functional Dynamics

Published:2015-05-27 Issue:22 Volume:54 Page:3543-3554
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Katebi Ataur R.¹,Jernigan Robert L.¹

Affiliation:

1. L. H. Baker Center for Bioinformatics and Biological Statistics, Department of Biochemistry, Biophysics and Molecular Biology, and Interdepartmental Program for Bioinformatics and Computational Biology, Iowa State University, Ames, Iowa 50011-3020, United States

Funder

Division of Molecular and Cellular Biosciences

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b00042

Reference35 articles.

1. Mechanism of the Schiff Base Forming Fructose-1,6-bisphosphate Aldolase: Structural Analysis of Reaction Intermediates

2. Structural Insights into the Substrate Binding and Stereoselectivity of Giardia Fructose-1,6-bisphosphate Aldolase,

3. Structural investigation of the Na–Fe–Mo–O system

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