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The Journal of Biological Chemistry|March 25, 1981
Evidence for a calcium-sensitive factor which alters the alkaline pH sensitivity of sarcoplasmic reticulum calcium transportC A Tate, A Chu, J McMillin-Wood, et al.
The Journal of Biological Chemistry|February 10, 1983
Anion effects on in vitro sarcoplasmic reticulum function. The relationship between anions and calcium fluxA Chu, C A Tate, R J Bick, et al.
The Journal of Biological Chemistry|September 10, 1983
Anion effects on in vitro sarcoplasmic reticulum function. Co-transport of anions with calciumA Chu, R J Bick, C A Tate, et al.
Archives of Biochemistry and Biophysics|May 1, 1991
Unsaturated aminophospholipids are preferentially retained by the fast skeletal muscle CaATPase during detergent solubilization. Evidence for a specific association between aminophospholipids and the calcium pump proteinR J Bick, K A Youker, H J Pownall, et al.
The Journal of Biological Chemistry|October 10, 1982
Evidence for membrane microheterogeneity in the sarcoplasmic reticulum of fast twitch skeletal muscleW B Van Winkle, R J Bick, D E Tucker, et al.
Biochimica Et Biophysica Acta|February 19, 1976
The rate of calcium uptake into sarcoplasmic reticulum of cardiac muscle and skeletal muscle. Effects of cyclic AMP-dependent protein kinase and phosphorylase b kinaseA Schwartz, M L Entman, K Kaniike, et al.
Biochimica Et Biophysica Acta|July 14, 1977
Cyclic AMP modulation of calcium accumulation by sarcoplasmic reticulum from fast skeletal muscleE P Bornet, M L Entman, W B Van Winkle, et al.
The Biochemical Journal|February 15, 1983
Alteration of sarcoplasmic reticulum after denervation of chicken pectoralis muscleC A Tate, R J Bick, T D Myers, et al.
Biochemistry|July 28, 1987
Phospholipid fatty acyl chain asymmetry in the membrane bilayer of isolated skeletal muscle sarcoplasmic reticulumR J Bick, W B Van Winkle, C A Tate, et al.
The American Journal of Anatomy|June 1, 1977
The fenestrated collar of mammalian cardiac sarcoplasmic reticulum: a freeze-fracture studyW B Van Winkle
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