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

An intragenic suppressor of a calmodulin mutation in Paramecium: genetic and biochemical characterization.

Genetics - 1 Nov 1991

Hinrichsen R D, Pollock M, Hennessey T, Russell C

Abstract excerpt

We describe a suppressor of the calmodulin mutant cam1 in Paramecium tetraurelia. The cam1 mutant, which has a SER----PHE change at residue 101 of the third calcium-binding domain, inhibits the activity of the Ca(2+)-dependent K+ current and causes exaggerated behavioral responses to most stimuli. An enrichment scheme, based on an increased sensitivity to Ba2+ in cam1 cells, was used to isolate suppressors. One...

Topics

Animals
Behavior, Animal
Calcium
Calmodulin
Calmodulin-Binding Proteins
DNA Mutational Analysis
Enzyme Activation
Mutation
Paramecium
Phosphoric Diester Hydrolases
Potassium Channels

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Binding

Source

Open in PubMed Open full text

Identifiers

PMID: 1661255
DOI: 10.1093/genetics/129.3.717
PMCID: PMC1204739

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1661255-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An intragenic suppressor of a calmodulin mutation in Paramecium: genetic and biochemical characterization.PMID 1661255Read ↗

Primary mutations in calmodulin prevent activation of the Ca(++)-dependent Na+ channel in Paramecium.Semantic proximity Read ↗

New non-lethal calmodulin mutations in Paramecium. A structural and functional bipartition hypothesis.Semantic proximity Read ↗

Efficient transformation of cam2, a behavioral mutant of Paramecium tetraurelia, with the calmodulin gene.Semantic proximity Read ↗

In vivo Paramecium mutants show that calmodulin orchestrates membrane responses to stimuli.Semantic proximity Read ↗

Paramecium calmodulin mutants defective in ion channel regulation can bind calcium and undergo calcium-induced conformational switching.Semantic proximity Read ↗

Calmodulin defects cause the loss of Ca2(+)-dependent K+ currents in two pantophobiac mutants of Paramecium tetraurelia.Semantic proximity Read ↗

Mutations in paramecium calmodulin indicate functional differences between the C-terminal and N-terminal lobes in vivo.Semantic proximity Read ↗

Genetic dissection of Ca2(+)-dependent ion channel function in Paramecium.Semantic proximity Read ↗

Calcium binding to calmodulin mutants having domain-specific effects on the regulation of ion channels.Semantic proximity Read ↗

Calmodulin mutants and Ca2(+)-dependent channels in Paramecium.Semantic proximity Read ↗

Interactions between mutants with defects in two Ca2(+)-dependent K+ currents of Paramecium tetraurelia.Semantic proximity Read ↗

Phenylalanine fluorescence studies of calcium binding to N-domain fragments of Paramecium calmodulin mutants show increased calcium affinity correlates with increased disorder.Semantic proximity Read ↗

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