Comparative aspects of the molecular basis for thin-filament linked regulation of energy transduction in skeletal and smooth muscle-Reference-Cited by-同舟云学术

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Comparative aspects of the molecular basis for thin-filament linked regulation of energy transduction in skeletal and smooth muscle

Published:1989-10-01 Issue:5 Volume:17 Page:901-901
ISSN:0300-5127
Container-title:Biochemical Society Transactions
language:en
Short-container-title:

Author:

PATCHELL VALERIE B.¹,PERRY S. VICTOR¹,MOIR ARTHUR J. G.²,AUDEMARD ETIENNE³,MORNET DOMINIQUE³,LEVINE BARRY A.⁴

Affiliation:

1. Department of Physiology, Birmingham University, Birmingham B15 2TJ, U.K.

2. Department of Biochemistry, Sheffield University, Sheffield S10 2TN, U.K.

3. Centre de Biochimie Macromoleculaire, CNRS, 34033 Montpellier, France

4. Inorganic Chemistry Laboratory, Oxford University, Oxford OX1 3QR, U.K.

Publisher

Portland Press Ltd.

Subject

Biochemistry

Link

https://portlandpress.com/biochemsoctrans/article-pdf/17/5/901/504821/bst0170901.pdf

Cited by 11 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Cross-bridge binding to actin and force generation in skinned fibers of the rabbit psoas muscle in the presence of antibody fragments against the N-terminus of actin;Biophysical Journal;1996-01

2. Caldesmon, N-Terminal Yeast Actin Mutants, and the Regulation of Actomyosin Interactions;Biochemistry;1994-03-22

3. Interaction of caldesmon and myosin subfragment 1 with the C-terminus of actin;Biochemical and Biophysical Research Communications;1992-04

4. Actomyosin interactions in the presence of ATP and the N-terminal segment of actin;Biochemistry;1992-02-18

5. The importance of C-terminal amino acid residues of actin to the inhibition of actomyosin ATPase activity by caldesmon and troponin I;FEBS Letters;1992-02-10

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