Search Results - "PEMRICK, S. M"

The retinoid receptors by Pemrick, S M, Lucas, D A, Grippo, J F

“…The retinoid receptors belong to a large superfamily of ligand-inducible transcription factors that include the steroid, vitamin D and thyroid hormone…”
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Characterization of the chimeric retinoic acid receptor RARα/VDR by PEMRICK, S. M, ABARZUA, P, KRATZEISEN, C, MARKS, M. S, MEDIN, J. A, OZATO, K, GRIPPO, J. F

“…The chimeric receptor, RARα/VDR, contains the DNA-binding domain of the retinoic acid receptor (RARα) and the ligand-binding domain of the vitamin D receptor…”
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The phosphorylated L2 light chain of skeletal myosin is a modifier of the actomyosin ATPase by Pemrick, S M

“…Incubation of rabbit skeletal myosin with an extract of light chain kinase plus ATP phosphorylated the L2 light chain and modified the steady state kinetics of…”
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ATP, uncomplexed by divalent cations, and the LC2 light chain are interdependent modifiers of the skeletal actomyosin MgATPase activity by PEMRICK, S. M, MARTINEZ, P. A

“…In the absence of troponin and tropomyosin, skeletal actomyosin MgATPase activity can be altered by 2-3-fold by divalent cations. The 'sign' of this effect…”
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Qualitative Analysis of Skeletal Myosin as Substrate of Ca2+-Activated Neutral Protease: Comparison of Filamentous and Soluble, Native, and L2-Deficient Myosin by Pemrick, S. M., Grebenau, R. C.

“…Ca2+-activated neutral protease (CAF) was capable of degrading myosin over a 200-fold range of protease concentrations. CAF selected the heavy chain of myosin,…”
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LC2 involvement in the assembly of skeletal myosin filaments by Chowrashi, P K, Pemrick, S M, Pepe, F A

“…The assembly of LC2-deficient myosin was studied under conditions where control and LC2-reassociated myosin assemble around the native length of about 1.5…”
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The retinoid receptors by Pemrick, S M, Lucas, D A, Grippo, J F

“…The retinoid receptors belong to a large superfamily of ligand-inducible transcription factors that include the steroid, vitamin D and thyroid hormone…”
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The effect of treatment with 5,5'-dithiobis-(2-nitrobenzoic acid) on the initial rapid proton liberation during hydrolysis of adenosine triphosphate by myosin by Pemrick, S M

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Common electrophoretic properties of the fat body, haemolymph, and oöcytes of adult Tenebrio molitor by Pemrick, S M, Butz, A

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RNA synthesis of the fat body of adult Tenebrio molitor by Pemrick, S M, Butz, A

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The myosin filament XV assembly: contributions of 195 residue segments of the myosin rod and the eight C-terminal residues by Chowrashi, P K, Pemrick, S M, Li, S, Yi, P, Clarke, T, Maguire, B, Ader, G, Saintigny, P, Mittal, B, Tewari, M, Stoeckert, C, Stedman, H H, Sylvester, J E, Pepe, F A

“…A mixture of two peptides of approximately M(r) 13000 has been isolated from a papain digest of LC2 deficient myosin. The peptides assemble into highly ordered…”
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Initial rapid proton liberation during hydrolysis of adenosine triphosphate by myosin subfragment I by Pemrick, S M, Walz, Jr, F G

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Differences in the charge distribution of glycerol-extracted muscle fibers in rigor, relaxation, and contraction by Pemrick, S M, Edwards, C

“…Glycerol-extracted rabbit psoas muscle fibers were impaled with KCl-filled glass microelectrodes. For fibers at rest-length, the potentials were significantly…”
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Characterization of the chimeric retinoic acid receptor RARalpha/VDR by Pemrick, S M, Abarzúa, P, Kratzeisen, C, Marks, M S, Medin, J A, Ozato, K, Grippo, J F

“…The chimeric receptor, RARalpha/VDR, contains the DNA-binding domain of the retinoic acid receptor (RARalpha) and the ligand-binding domain of the vitamin D…”
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Evidence that the actin site is impaired by Ca2+-activated degradation of the heavy chain of dystrophic myosin by Pemrick, S M

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Comparison of the calcium sensitivity of actomyosin from native and L-2-deficient myosin by Pemrick, S M

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Initial Rapid Proton Liberation During Hydrolysis of Adenosine Triphosphate by Myosin Subfragment 1 by Pemrick, S.M., Walz, F.G.

“…The rate of hydrogen ion liberation during the hydrolysis of ATP by Subfragment I was followed in a stopped flow spectrophotometer. At pH 8, 20°, and in the…”
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Comparison of the calcium sensitivity of actomyosin from native and L2-deficient myosin by Pemrick, Suzanne M

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