Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Switch action of troponin on muscle thin filament as revealed by spin labeling and pulsed EPR.

The Journal of biological chemistry - 2 Apr 2010

Aihara Tomoki, Nakamura Motoyoshi, Ueki Shoji, Hara Hideyuki, Miki Masao, Arata Toshiaki

Abstract excerpt

We have used pulsed electron-electron double resonance (PELDOR) spectroscopy to measure the distance between spin labels at Cys(133) of the regulatory region of TnI (TnI133) and a native or genetically substituted cysteine of TnC (TnC44, TnC61, or TnC98). In the +Ca(2+) state, the TnC44-TnI133-T...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Chickens
Share to Cysteine
Share to Electron Spin Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Muscle Fibers, Skeletal

Share to Rabbits

Share to Spin Labels

Share to Troponin C

Share to Troponin I

Source

Open in PubMed Open full text

Identifiers

PMID: 20139080
DOI: 10.1074/jbc.M109.082925
PMCID: PMC2856275

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20139080-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Switch action of troponin on muscle thin filament as revealed by spin labeling and pulsed EPR.PMID 20139080Read ↗

Structure of the troponin complex. Implications of photocross-linking of troponin I to troponin C thiol mutants.Semantic proximity Read ↗

Proximity relationships between residue 117 of rabbit skeletal troponin-I and residues in troponin-C and actin.Semantic proximity Read ↗

Ca(2+) induces an extended conformation of the inhibitory region of troponin I in cardiac muscle troponin.Semantic proximity Read ↗

Structural and functional studies on Troponin I and Troponin C interactions.Semantic proximity Read ↗

Structure of the inhibitory region of troponin by site directed spin labeling electron paramagnetic resonance.Semantic proximity Read ↗

Ca(2+)- and S1-induced movement of troponin T on reconstituted skeletal muscle thin filaments observed by fluorescence energy transfer spectroscopy.Semantic proximity Read ↗

Allosteric Transmission along a Loosely Structured Backbone Allows a Cardiac Troponin C Mutant to Function with Only One Ca2+ Ion.Semantic proximity Read ↗

Conformation of the regulatory domain of cardiac muscle troponin C in its complex with cardiac troponin I.Semantic proximity Read ↗

Dynamics of the C-terminal region of TnI in the troponin complex in solution.Semantic proximity Read ↗

NMR structure of a bifunctional rhodamine labeled N-domain of troponin C complexed with the regulatory "switch" peptide from troponin I: implications for in situ fluorescence studies in muscle fibers.Semantic proximity Read ↗

Mutations of hydrophobic residues in the N-terminal domain of troponin C affect calcium binding and exchange with the troponin C-troponin I96-148 complex and muscle force production.Semantic proximity Read ↗

Structural and kinetic effects of hypertrophic cardiomyopathy related mutations R146G/Q and R163W on the regulatory switching activity of rat cardiac troponin I.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.