Work Done by Titin Protein Folding Assists Muscle Contraction-Reference-Cited by-同舟云学术

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Work Done by Titin Protein Folding Assists Muscle Contraction

Published:2016-02 Issue:6 Volume:14 Page:1339-1347
ISSN:2211-1247
Container-title:Cell Reports
language:en
Short-container-title:Cell Reports

Author:

Rivas-Pardo Jaime Andrés,Eckels Edward C.,Popa Ionel,Kosuri Pallav,Linke Wolfgang A.,Fernández Julio M.

Publisher

Elsevier BV

Subject

General Biochemistry, Genetics and Molecular Biology

Reference29 articles.

1. Single molecule force spectroscopy on titin implicates immunoglobulin domain stability as a cardiac disease mechanism;Anderson;J. Biol. Chem.,2013

2. Muscle cross-section measurement by magnetic resonance imaging;Beneke;Eur. J. Appl. Physiol. Occup. Physiol.,1991

3. Dynamics of equilibrium folding and unfolding transitions of titin immunoglobulin domain under constant forces;Chen;J. Am. Chem. Soc.,2015

4. Force-clamp spectroscopy monitors the folding trajectory of a single protein;Fernandez;Science,2004

5. Single myosin molecule mechanics: piconewton forces and nanometre steps;Finer;Nature,1994

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1. Investigation of Structural Peculiarities of Smooth Muscle Titin Aggregates, Formed under Different In Vitro Conditions, by Small-Angle X-Ray Scattering and Fourier Transform Infrared Spectroscopy;Bulletin of Experimental Biology and Medicine;2024-09-12

2. Force re-development after shortening reveals a role for titin in stretch–shortening performance enhancement in skinned muscle fibres;Journal of Experimental Biology;2024-09-01

3. Fatiguing exercise reduces cellular passive Young's modulus in human vastus lateralis muscle;Experimental Physiology;2024-08-20

4. Autoinhibition of cMyBP-C by its middle domains;2024-07-22

5. Force‐regulated chaperone activity of BiP/ERdj3 is opposite to their homologs DnaK/DnaJ;Protein Science;2024-06-12

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