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

Biochemical and structural insights into microtubule perturbation by CopN from Chlamydia pneumoniae.

The Journal of biological chemistry - 5 Sept 2014

Nawrotek Agata, Guimarães Beatriz G, Velours Christophe, Subtil Agathe, Knossow Marcel, Gigant Benoît

Abstract excerpt

Although the actin network is commonly hijacked by pathogens, there are few reports of parasites targeting microtubules. The proposed member of the LcrE protein family from some Chlamydia species (e.g. pCopN from C. pneumoniae) binds tubulin and inhibits microtubule assembly in vitro. From the pCopN structure and its similarity with that of MxiC from Shigella, we definitively confirm CopN as the Chlamydia homolog...

Read the complete abstract on PubMed

Topics

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

Share to Chlamydophila pneumoniae
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microtubules

Share to Protein Structure, Secondary

Share to Sequence Homology, Amino Acid

Share to Spectrometry, Fluorescence

Share to Tubulin

Source

Open in PubMed Open full text

Identifiers

PMID: 25056950
DOI: 10.1074/jbc.M114.568436
PMCID: PMC4155683

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Biochemical and structural insights into microtubule perturbation by CopN from Chlamydia pneumoniae.PMID 25056950Read ↗

Taking control: reorganization of the host cytoskeleton by ChlamydiaSemantic proximity Read ↗

Chlamydia trachomatis Causes Centrosomal Defects Resulting in Chromosomal Segregation AbnormalitiesSemantic proximity Read ↗

A new role for Chlamydia trachomatis serology?Semantic proximity Read ↗

Pathogenic Puppetry: Manipulation of the Host Actin Cytoskeleton by Chlamydia trachomatisSemantic proximity Read ↗

The Proteome of the Isolated Chlamydia trachomatis Containing Vacuole Reveals a Complex Trafficking Platform Enriched for Retromer ComponentsSemantic proximity Read ↗

Pathogenicity and virulence of Chlamydia trachomatis : Insights into host interactions, immune evasion, and intracellular survivalSemantic proximity Read ↗

New Frontiers in Type III Secretion Biology: the Chlamydia PerspectiveSemantic proximity Read ↗

<i>Chlamydia trachomatis</i> Infection Causes Mitotic Spindle Pole Defects Independently from its Effects on Centrosome AmplificationSemantic proximity Read ↗

Molecular pathogenesis of Chlamydia trachomatisSemantic proximity Read ↗

A secondary structure motif predictive of protein localization to the chlamydial inclusion membraneSemantic proximity Read ↗

Initial Characterization of the Two ClpP Paralogs of <i>Chlamydia trachomatis</i> Suggests Unique Functionality for EachSemantic proximity Read ↗

The chlamydial OTU domain-containing proteinChlaOTU is an early type III secretion effector targeting ubiquitin and NDP52Semantic proximity Read ↗

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