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

Impact of methionine oxidation on calmodulin structural dynamics.

Biochemical and biophysical research communications - 9 Jan 2015

McCarthy Megan R, Thompson Andrew R, Nitu Florentin, Moen Rebecca J, Olenek Michael J, Klein Jennifer C, Thomas David D

Abstract excerpt

We have used electron paramagnetic resonance (EPR) to examine the structural impact of oxidizing specific methionine (M) side chains in calmodulin (CaM). It has been shown that oxidation of either M109 or M124 in CaM diminishes CaM regulation of the muscle calcium release channel, the ryanodine receptor (RyR), and that mutation of M to Q (glutamine) in either case produces functional effects identical to those of...

Read the complete abstract on PubMed

Topics

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

Share to Calmodulin
Share to Electron Spin Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glutamine

Share to Methionine

Share to Mutation

Share to Oxidation-Reduction

Share to Protein Structure, Secondary

Share to Spin Labels

Source

Open in PubMed Open full text

Identifiers

PMID: 25478640
DOI: 10.1016/j.bbrc.2014.11.091
PMCID: PMC4312012

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Impact of methionine oxidation on calmodulin structural dynamics.PMID 25478640Read ↗

Met125 is essential for maintaining the structural integrity of calmodulin's C-terminal domain.Semantic proximity Read ↗

Structural dynamics of calmodulin-ryanodine receptor interactions: electron paramagnetic resonance using stereospecific spin labels.Semantic proximity Read ↗

Chemical shift perturbations induced by residue specific mutations of CaM interacting with NOS peptides.Semantic proximity Read ↗

Structural Consequences of Calmodulin EF Hand Mutations.Semantic proximity Read ↗

Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant.Semantic proximity Read ↗

Activation of constitutive nitric oxide synthases by oxidized calmodulin mutants.Semantic proximity Read ↗

Chemical shift assignments of calmodulin constructs with EF hand mutations.Semantic proximity Read ↗

Sampling unfolding intermediates in calmodulin by single-molecule spectroscopy.Semantic proximity Read ↗

Oxidation of calmodulin alters activation and regulation of CaMKII.Semantic proximity Read ↗

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

Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations.Semantic proximity Read ↗

Structural Mechanism of Electron Shuttling in Inducible Nitric Oxide SynthaseSemantic proximity Read ↗

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