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S M Pemrick

Showing results (1-10 of 15) with videos related to

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Biochemical and Biophysical Research Communications|April 8, 1974
The effect of treatment with 5,5'-dithiobis-(2-nitrobenzoic acid) on the initial rapid proton liberation during hydrolysis of adenosine triphosphate by myosinS M Pemrick
Biochemical and Biophysical Research Communications|October 15, 1981
Evidence that the actin site is impaired by Ca2+-activated degradation of the heavy chain of dystrophic myosinS M Pemrick
The Journal of Biological Chemistry|September 25, 1980
The phosphorylated L2 light chain of skeletal myosin is a modifier of the actomyosin ATPaseS M Pemrick
Biochemistry|September 6, 1977
Comparison of the calcium sensitivity of actomyosin from native and L-2-deficient myosinS M Pemrick
Journal of Insect Physiology|June 1, 1970
RNA synthesis of the fat body of adult Tenebrio molitorS M Pemrick, A Butz
Journal of Insect Physiology|July 1, 1970
Common electrophoretic properties of the fat body, haemolymph, and oöcytes of adult Tenebrio molitorS M Pemrick, A Butz
The Journal of General Physiology|November 1, 1974
Differences in the charge distribution of glycerol-extracted muscle fibers in rigor, relaxation, and contractionS M Pemrick, C Edwards
The Journal of Cell Biology|December 1, 1984
Qualitative analysis of skeletal myosin as substrate of Ca2+-activated neutral protease: comparison of filamentous and soluble, native, and L2-deficient myosinS M Pemrick, R C Grebenau
The Biochemical Journal|November 15, 1991
ATP, uncomplexed by divalent cations, and the LC2 light chain are interdependent modifiers of the skeletal actomyosin MgATPase activityS M Pemrick, P A Martinez
The Journal of Biological Chemistry|May 10, 1972
Initial rapid proton liberation during hydrolysis of adenosine triphosphate by myosin subfragment IS M Pemrick, F G Walz
Pageof 2

Showing results (1-10 of 15) with videos related to

Sort By:
Pageof 2
Biochemical and Biophysical Research Communications|April 8, 1974
The effect of treatment with 5,5'-dithiobis-(2-nitrobenzoic acid) on the initial rapid proton liberation during hydrolysis of adenosine triphosphate by myosinS M Pemrick
Biochemical and Biophysical Research Communications|October 15, 1981
Evidence that the actin site is impaired by Ca2+-activated degradation of the heavy chain of dystrophic myosinS M Pemrick
The Journal of Biological Chemistry|September 25, 1980
The phosphorylated L2 light chain of skeletal myosin is a modifier of the actomyosin ATPaseS M Pemrick
Biochemistry|September 6, 1977
Comparison of the calcium sensitivity of actomyosin from native and L-2-deficient myosinS M Pemrick
Journal of Insect Physiology|June 1, 1970
RNA synthesis of the fat body of adult Tenebrio molitorS M Pemrick, A Butz
Journal of Insect Physiology|July 1, 1970
Common electrophoretic properties of the fat body, haemolymph, and oöcytes of adult Tenebrio molitorS M Pemrick, A Butz
The Journal of General Physiology|November 1, 1974
Differences in the charge distribution of glycerol-extracted muscle fibers in rigor, relaxation, and contractionS M Pemrick, C Edwards
The Journal of Cell Biology|December 1, 1984
Qualitative analysis of skeletal myosin as substrate of Ca2+-activated neutral protease: comparison of filamentous and soluble, native, and L2-deficient myosinS M Pemrick, R C Grebenau
The Biochemical Journal|November 15, 1991
ATP, uncomplexed by divalent cations, and the LC2 light chain are interdependent modifiers of the skeletal actomyosin MgATPase activityS M Pemrick, P A Martinez
The Journal of Biological Chemistry|May 10, 1972
Initial rapid proton liberation during hydrolysis of adenosine triphosphate by myosin subfragment IS M Pemrick, F G Walz
Pageof 2