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

The GTPase Rab4 interacts with Chlamydia trachomatis inclusion membrane protein CT229.

Infection and immunity - 1 Sept 2006

Rzomp K A, Moorhead A R, Scidmore M A

Abstract excerpt

Chlamydiae, which are obligate intracellular bacteria, replicate in a nonlysosomal vacuole, termed an inclusion. Although neither the host nor the chlamydial proteins that mediate the intracellular trafficking of the inclusion have been clearly identified, several enhanced green fluorescent protein (GFP)-tagged Rab GTPases, including Rab4A, are recruited to chlamydial inclusions. GFP-Rab4A associates with...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Chlamydia Infections
Share to Chlamydia trachomatis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Green Fluorescent Proteins

Share to Guanosine Triphosphate

Share to HeLa Cells

Share to Intracellular Membranes

Share to Membrane Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 16926431
DOI: 10.1128/IAI.00539-06
PMCID: PMC1594829

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

The GTPase Rab4 interacts with Chlamydia trachomatis inclusion membrane protein CT229.PMID 16926431Read ↗

Multiple Host Proteins That Function in Phosphatidylinositol-4-Phosphate Metabolism Are Recruited to the Chlamydial InclusionSemantic proximity Read ↗

The inclusion membrane protein IncS is critical for initiation of the Chlamydia intracellular developmental cycleSemantic proximity Read ↗

The Loss of Expression of a Single Type 3 Effector (CT622) Strongly Reduces Chlamydia trachomatis Infectivity and GrowthSemantic proximity Read ↗

The <i>Chlamydia</i> protein CpoS modulates the inclusion microenvironment and restricts the interferon response by acting on Rab35Semantic proximity Read ↗

Homologues of the Chlamydia trachomatis and Chlamydia muridarum Inclusion Membrane Protein IncS Are Interchangeable for Early Development but Not for Inclusion Stability in the Late Developmental CycleSemantic proximity Read ↗

Identification of a Family of Effectors Secreted by the Type III Secretion System That Are Conserved in Pathogenic ChlamydiaeSemantic proximity Read ↗

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

Absence of Specific Chlamydia trachomatis Inclusion Membrane Proteins Triggers Premature Inclusion Membrane Lysis and Host Cell Death.Semantic proximity Read ↗

A Functional Core of IncA Is Required for Chlamydia trachomatis Inclusion Fusion.Semantic proximity Read ↗

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

Hijacking host cell vesicular transport: New insights into the nutrient acquisition mechanism of ChlamydiaSemantic proximity Read ↗

Inclusion Membrane Proteins ofProtochlamydia amoebophilaUWE25 Reveal a Conserved Mechanism for Host Cell Interaction among theChlamydiaeSemantic proximity Read ↗

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