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

Detection of Cytosolic Shigella flexneri via a C-Terminal Triple-Arginine Motif of GBP1 Inhibits Actin-Based Motility.

mBio - 12 Dec 2017

Piro Anthony S, Hernandez Dulcemaria, Luoma Sarah, Feeley Eric M, Finethy Ryan, Yirga Azeb, Frickel Eva M, Lesser Cammie F, Coers Jörn

Abstract excerpt

Dynamin-like guanylate binding proteins (GBPs) are gamma interferon (IFN-γ)-inducible host defense proteins that can associate with cytosol-invading bacterial pathogens. Mouse GBPs promote the lytic destruction of targeted bacteria in the host cell cytosol, but the antimicrobial function of human GBPs and the mechanism by which these proteins associate with cytosolic bacteria are poorly understood. Here, we...

Read the complete abstract on PubMed

Topics

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

Share to Antigens, Bacterial
Share to Burkholderia

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytosol

Share to GTP-Binding Proteins

Share to Lipopolysaccharides

Share to O Antigens

Share to Shigella flexneri

Share to Ubiquitination

Source

Open in PubMed Open full text

Identifiers

PMID: 29233899
DOI: 10.1128/mBio.01979-17
PMCID: PMC5727416

Genes

GBP1
GBP2
GBP3
GBP4
GBP6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Detection of Cytosolic Shigella flexneri via a C-Terminal Triple-Arginine Motif of GBP1 Inhibits Actin-Based Motility.PMID 29233899Read ↗

Detection of cytosolic <i>Shigella flexneri</i> via a C-terminal triple-arginine motif of GBP1 inhibits actin-based motilitySemantic proximity Read ↗

Human giant GTPase GVIN1 forms an antimicrobial coatomer around the intracellular bacterial pathogen <i>Burkholderia thailandensis</i>Semantic proximity Read ↗

GBP1 recruitment to actin-rich pedestals induced by extracellular Gram-negative bacteria promotes pyroptosisSemantic proximity Read ↗

Structural mechanism for guanylate-binding proteins (GBPs) targeting by the Shigella E3 ligase IpaH9.8Semantic proximity Read ↗

Interferon inducible GBPs restrict Burkholderia thailandensis motility induced cell-cell fusionSemantic proximity Read ↗

GBP2 aggregates LPS and activates the caspase-4 inflammasome independent of the bacterial encapsulation factor GBP1Semantic proximity Read ↗

Burkholderia pseudomallei BimC Is Required for Actin-Based Motility, Intracellular Survival, and VirulenceSemantic proximity Read ↗

A patatin-like phospholipase mediates <i>Rickettsia parkeri</i> escape from host membranesSemantic proximity Read ↗

Sweet host revenge: Galectins and GBPs join forces at broken membranesSemantic proximity Read ↗

A dual role for PGLYRP1 in host defense and immune regulation during <i>B. pertussis</i> infectionSemantic proximity Read ↗

Genome-wide protective response used by group A <i>Streptococcus</i> to evade destruction by human polymorphonuclear leukocytesSemantic proximity Read ↗

Shigella hijacks the exocyst to cluster macropinosomes for efficient vacuolar escapeSemantic proximity Read ↗

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