Actin filament‐ and Wiskott‐Aldrich syndrome protein‐binding sites on fructose‐1,6‐bisphosphate aldolase are functionally distinct from the active site
Author:
Affiliation:
1. Department of Biology Boston University Boston Massachusetts USA
2. Program in Cell, Molecular, and Developmental Biology, and Biophysics Johns Hopkins University Baltimore Maryland USA
Funder
New England Biolabs Foundation
Publisher
Wiley
Subject
Cell Biology,Structural Biology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/cm.21646
Reference58 articles.
1. Quantitative Comparison of the Binding of Various Glycolytic Enzymes to F-Actin and the Interaction of Aldolase with G-Actin
2. Binding of Aldolase and Triosephosphate Dehydrogenase to F-Actin and Modification of Catalytic Properties of Aldolase
3. Identification of Neuronal Isozyme Specific Residues by Comparison of Goldfish Aldolase C to Other Aldolases
4. Aldolase provides an unusual binding site for thrombospondin-related anonymous protein in the invasion machinery of the malaria parasite
5. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
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