Phosphorylation and calcium antagonistically tune myosin-binding protein C's structure and function.

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第一作者： Michael J,Previs

第一单位： Department of Molecular Physiology and Biophysics, Cardiovascular Research Institute, University of Vermont, Burlington, VT 05405;

作者： Michael J,Previs ^[1] ; Ji Young,Mun ^[2] ; Arthur J,Michalek ^[1] ; Samantha Beck,Previs ^[1] ; James,Gulick ^[3] ; Jeffrey,Robbins ^[3] ; David M,Warshaw ^[4] ; Roger,Craig ^[5]

作者单位： Department of Molecular Physiology and Biophysics, Cardiovascular Research Institute, University of Vermont, Burlington, VT 05405; ^[1] Department of Cell and Developmental Biology, University of Massachusetts Medical School, Worcester, MA 01655; ^[2] Division of Molecular Cardiovascular Biology, Cincinnati Children's Hospital Medical Center, Cincinnati, OH 45229. ^[3] Department of Molecular Physiology and Biophysics, Cardiovascular Research Institute, University of Vermont, Burlington, VT 05405; david.warshaw@uvm.edu roger.craig@umassmed.edu. ^[4] Department of Cell and Developmental Biology, University of Massachusetts Medical School, Worcester, MA 01655; david.warshaw@uvm.edu roger.craig@umassmed.edu. ^[5]

关键词 cMyBP-C muscle activation muscle regulation structure-function

主题词动物(Animals);钙(Calcium);载体蛋白质类(Carrier Proteins);小鼠(Mice);磷酰化(Phosphorylation);蛋白质构象(Protein Conformation);构效关系(Structure-Activity Relationship)

DOI 10.1073/pnas.1522236113

PMID 26908872

发布时间 2018-11-13

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