A two-faced cysteine residue modulates skeletal muscle contraction. Focus on “S-nitrosylation and S-glutathionylation of Cys134 on troponin I have opposing competitive actions on Ca2+ sensitivity in rat fast-twitch muscle fibers | Zendy

Josine M. de Winter | Zendy; Coen A. C. Ottenheijm | Zendy

Open Access

A two-faced cysteine residue modulates skeletal muscle contraction. Focus on “S-nitrosylation and S-glutathionylation of Cys134 on troponin I have opposing competitive actions on Ca²⁺ sensitivity in rat fast-twitch muscle fibers

Author(s) -

Josine M. de Winter,

Coen A. C. Ottenheijm

Publication year - 2017

Publication title -

ajp cell physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.432

H-Index - 181

eISSN - 1522-1563

pISSN - 0363-6143

DOI - 10.1152/ajpcell.00009.2017

Subject(s) - actin , skeletal muscle , tropomyosin , sarcomere , muscle contraction , myosin , troponin , chemistry , endoplasmic reticulum , troponin c , myocyte , calcium , biophysics , biochemistry , microbiology and biotechnology , biology , anatomy , medicine , organic chemistry , myocardial infarction

the contraction of skeletal muscle involves a cascade of events, starting in the central nervous system. Action potentials in motor neurons are transmitted at neuromuscular junctions to the plasma membranes of muscle fibers. The action potentials in plasma membranes propagate into so-called T-tubule

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