cell protein
; phosphoprotein phosphatase 1
; SDS22 protein
; unclassified drug
; Article
; binding affinity
; binding site
; biogenesis
; biophysics
; catalysis
; controlled study
; crystallography
; enzyme regulation
; enzyme specificity
; immunoblotting
; in vivo study
; nonhuman
; polyacrylamide gel electrophoresis
; priority journal
; protein aggregation
; protein conformation
; protein expression
; protein interaction
Choy, M.S., Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, United States; Moon, T.M., Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, United States; Ravindran, R., Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA 71130, United States; Bray, J.A., Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, United States; Robinson, L.C., Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA 71130, United States; Archuleta, T.L., Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, United States; Shi, W., Department of Energy and Photon Sciences, Brookhaven National Laboratory, Upton, NY 11973, United States; Peti, W., Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, United States; Tatchell, K., Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA 71130, United States; Page, R., Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, United States
Recommended Citation:
Choy M.S.,Moon T.M.,Ravindran R.,et al. SDS22 selectively recognizes and traps metal-deficient inactive PP1[J]. Proceedings of the National Academy of Sciences of the United States of America,2019-01-01,116(41)