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

Inhibition of mutant troponin C activity by an intra-domain disulphide bond.

Nature - 10 May 1990

Grabarek Z, Tan R Y, Wang J, Tao T, Gergely J

Abstract excerpt

Triggering of contraction in striated muscles involves a conformational transition in the N-terminal domain of troponin C, the calcium-binding component of thin filaments. We have designed a mutant troponin C in which the key conformational transition and the calcium-regulatory activity are reversibly blocked by the formation of a disulphide bridge. Our results may be applicable to other proteins of the same...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Calcium
Share to Fluorescent Dyes

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Conformation

Share to Rabbits

Share to Spectrometry, Fluorescence

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 2110625
DOI: 10.1038/345132a0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Inhibition of mutant troponin C activity by an intra-domain disulphide bond.PMID 2110625Read ↗

[Calcium regulation by troponin and its genetic disorder in striated muscle contraction].Semantic proximity Read ↗

Engineered troponin C constructs correct disease-related cardiac myofilament calcium sensitivity.Semantic proximity Read ↗

Mutations in the N- and D-helices of the N-domain of troponin C affect the C-domain and regulatory function.Semantic proximity Read ↗

Troponin-C mutants with increased calcium affinity.Semantic proximity Read ↗

Intramolecular interactions in the N-domain of cardiac troponin C are important determinants of calcium sensitivity of force development.Semantic proximity Read ↗

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

Probing the calcium-induced conformational transition of troponin C with site-directed mutants.Semantic proximity Read ↗

Designing calcium-sensitizing mutations in the regulatory domain of cardiac troponin C.Semantic proximity Read ↗

Ca2+-dependent interaction of the inhibitory region of troponin I with acidic residues in the N-terminal domain of troponin C.Semantic proximity Read ↗

Significance of troponin dynamics for Ca2+-mediated regulation of contraction and inherited cardiomyopathy.Semantic proximity Read ↗

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

Ca²+-binding properties and regulatory roles of lobster troponin C sites II and IV.Semantic proximity Read ↗

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