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

IC97 is a novel intermediate chain of I1 dynein that interacts with tubulin and regulates interdoublet sliding.

Molecular biology of the cell - 1 Jul 2009

Wirschell Maureen, Yang Chun, Yang Pinfen, Fox Laura, Yanagisawa Haru-aki, Kamiya Ritsu, Witman George B, Porter Mary E, Sale Winfield S

Abstract excerpt

Our goal is to understand the assembly and regulation of flagellar dyneins, particularly the Chlamydomonas inner arm dynein called I1 dynein. Here, we focus on the uncharacterized I1-dynein IC IC97. The IC97 gene encodes a novel IC without notable structural domains. IC97 shares homology with the...

Read the complete abstract on PubMed

Topics

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

Share to Algal Proteins
Share to Axoneme
Share to Chlamydomonas reinhardtii

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dyneins

Share to Immunoprecipitation

Share to Microtubules

Share to Protein Subunits

Share to Tubulin

Source

Open in PubMed Open full text

Identifiers

PMID: 19420136
DOI: 10.1091/mbc.e09-04-0276
PMCID: PMC2704156

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19420136-2026-09-02.2. 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

IC97 is a novel intermediate chain of I1 dynein that interacts with tubulin and regulates interdoublet sliding.PMID 19420136Read ↗

IC138 defines a subdomain at the base of the I1 dynein that regulates microtubule sliding and flagellar motility.Semantic proximity Read ↗

Structural organization of the intermediate and light chain complex of Chlamydomonas ciliary I1 dynein.Semantic proximity Read ↗

Chlamydomonas IC97, an intermediate chain of the flagellar dynein f/I1, is required for normal flagellar and cellular motility.Semantic proximity Read ↗

The Chlamydomonas IDA7 locus encodes a 140-kDa dynein intermediate chain required to assemble the I1 inner arm complex.Semantic proximity Read ↗

Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein.Semantic proximity Read ↗

Insights into the structural organization of the I1 inner arm dynein from a domain analysis of the 1beta dynein heavy chain.Semantic proximity Read ↗

bop5 Mutations reveal new roles for the IC138 phosphoprotein in the regulation of flagellar motility and asymmetric waveforms.Semantic proximity Read ↗

Chlamydomonas DYX1C1/PF23 is essential for axonemal assembly and proper morphology of inner dynein arms.Semantic proximity Read ↗

IC138 is a WD-repeat dynein intermediate chain required for light chain assembly and regulation of flagellar bending.Semantic proximity Read ↗

Lis1 relieves cytoplasmic dynein-1 auto-inhibition by acting as a molecular wedgeSemantic proximity Read ↗

Lis1 relieves cytoplasmic dynein-1 autoinhibition by acting as a molecular wedgeSemantic proximity Read ↗

Pac1/LIS1 promotes an uninhibited conformation of dynein that coordinates its localization and activitySemantic proximity Read ↗

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