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

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

The Journal of membrane biology - 1 Apr 1990

Preston R R, Wallen-Friedman M A, Saimi Y, Kung C

Abstract excerpt

Two behavioral mutants of Paramecium tetraurelia, pantophobiacs A1 and A2, have single amino acid defects in the structure of calmodulin. The mutants exhibit several major ion current defects under voltage clamp: (i) the Ca2(+)-dependent K+ current activated upon depolarization of Paramecium is greatly reduced or missing in both mutants, (ii) both mutants lack a Ca2(+)-dependent K+ current activated upon...

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 Calcium
Share to Membrane Potentials

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

Share to Molecular Sequence Data

Share to Mutation

Share to Potassium Channels

Share to Sodium

Share to Sodium Channels

Source

Identifiers

PMID: 2159520
DOI: 10.1007/BF01869105

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

Calmodulin defects cause the loss of Ca2(+)-dependent K+ currents in two pantophobiac mutants of Paramecium tetraurelia.PMID 2159520Read ↗

Interactions between mutants with defects in two Ca2(+)-dependent K+ currents 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 ↗

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

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

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

Isolation and characterization of paramecium mutants defective in their response to magnesium.Semantic proximity Read ↗

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

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

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

The cloning and molecular analysis of pawn-B in Paramecium tetraurelia.Semantic proximity Read ↗

Paramecium calmodulin mutants defective in ion channel regulation associate with melittin in the absence of calcium but require it for tertiary collapse.Semantic proximity Read ↗

Ca(2+) current-deficient pawn mutants are promoted to queens during chronic depolarization of Paramecium tetraurelia.Semantic proximity Read ↗

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