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

The dilated cardiomyopathy G159D mutation in cardiac troponin C weakens the anchoring interaction with troponin I.

Biochemistry - 14 Oct 2008

Baryshnikova Olga K, Robertson Ian M, Mercier Pascal, Sykes Brian D

Abstract excerpt

NMR spectroscopy has been employed to elucidate the molecular consequences of the DCM G159D mutation on the structure and dynamics of troponin C, and its interaction with troponin I (TnI). Since the molecular effects of human mutations are often subtle, all NMR experiments were conducted as direc...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Cardiomyopathy, Dilated
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Binding

Share to Troponin C

Share to Troponin I

Source

Identifiers

PMID: 18803402
DOI: 10.1021/bi801165c

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18803402-2026-09-02.2. 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

The dilated cardiomyopathy G159D mutation in cardiac troponin C weakens the anchoring interaction with troponin I.PMID 18803402Read ↗

The cardiac-specific N-terminal region of troponin I positions the regulatory domain of troponin C.Semantic proximity Read ↗

Molecular Effects of cTnC DCM Mutations on Calcium Sensitivity and Myofilament Activation-An Integrated Multiscale Modeling Study.Semantic proximity Read ↗

The troponin C G159D mutation blunts myofilament desensitization induced by troponin I Ser23/24 phosphorylation.Semantic proximity Read ↗

Challenging current paradigms related to cardiomyopathies. Are changes in the Ca2+ sensitivity of myofilaments containing cardiac troponin C mutations (G159D and L29Q) good predictors of the phenotypic outcomes?Semantic proximity Read ↗

Arg92Leu-cTnT Alters the cTnC-cTnI Interface Disrupting PKA-Mediated Relaxation.Semantic proximity Read ↗

Functional analysis of a unique troponin c mutation, GLY159ASP, that causes familial dilated cardiomyopathy, studied in explanted heart muscle.Semantic proximity Read ↗

Modulation of Structure and Dynamics of Cardiac Troponin by Phosphorylation and Mutations Revealed by Molecular Dynamics Simulations.Semantic proximity Read ↗

Structural kinetics of cardiac troponin C mutants linked to familial hypertrophic and dilated cardiomyopathy in troponin complexes.Semantic proximity Read ↗

Structural and functional consequences of cardiac troponin C L57Q and I61Q Ca(2+)-desensitizing variants.Semantic proximity Read ↗

Amide hydrogens reveal a temperature-dependent structural transition that enhances site-II Ca2+-binding affinity in a C-domain mutant of cardiac troponin C.Semantic proximity Read ↗

Drastic Ca2+ sensitization of myofilament associated with a small structural change in troponin I in inherited restrictive cardiomyopathy.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 ↗

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