Identification of biochemically neutral positions in liver pyruvate kinase
Author:
Affiliation:
1. Department of Biochemistry and Molecular BiologyThe University of Kansas Medical Center Kansas City Kansas USA
2. Department of Family and Community MedicineThe University of Kansas Medical Center Kansas City Kansas USA
Funder
National Institutes of Health
W. M. Keck Foundation
Publisher
Wiley
Subject
Molecular Biology,Biochemistry,Structural Biology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.25953
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4. Mining for allosteric information: Natural mutations and positional sequence conservation in pyruvate kinase
5. Distinguishing the Interactions in the Fructose 1,6-Bisphosphate Binding Site of Human Liver Pyruvate Kinase That Contribute to Allostery
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