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Biochimie|January 1, 1995
Cryoenzymology: how to practice kinetic and structural studiesF Travers, T BarmanBiochemistry|February 20, 1990
Cryoenzymic studies on actomyosin ATPase. Evidence that the degree of saturation of actin with myosin subfragment 1 affects the kinetics of the binding of ATPC Tesi, F Travers, T BarmanBiochemistry|February 11, 1992
Ca(2+)-activated myofibrillar ATPase: transient kinetics and the titration of its active sitesM Houadjeto, F Travers, T BarmanBiophysical Journal|February 1, 1996
Mechanochemical coupling in muscle: attempts to measure simultaneously shortening and ATPase rates in myofibrilsC Lionne, F Travers, T BarmanFEBS Letters|April 9, 1991
What is the true ATPase activity of contracting myofibrils?M Houadjeto, T Barman, F TraversFEBS Letters|January 29, 1990
Is a four-state model sufficient to describe actomyosin ATPase?C Tesi, T Barman, F TraversBiochemistry|June 28, 1988
Transient kinetics of the interaction of 1,N6-ethenoadenosine 5'-triphosphate with myosin subfragment 1 under normal and cryoenzymic conditions: a comparison with adenosine 5'-triphosphateC Tesi, F Travers, T BarmanFEBS Letters|August 15, 1988
Sulphate is a competitive inhibitor of the binding of nucleotide to myosin. A comparison with phosphateC Tesi, T Barman, F TraversBiochemistry|January 24, 1995
Transient and equilibrium kinetic studies on yeast 3-phosphoglycerate kinase. Evidence that an intermediate containing 1,3-bisphosphoglycerate accumulates in the steady stateP P Schmidt, F Travers, T BarmanBiochemistry|April 12, 1994
Correlation of ActoS1, myofibrillar, and muscle fiber ATPasesC Herrmann, C Lionne, F Travers, et al.Pageof 7