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

Nuclear trafficking, histone cleavage and induction of apoptosis by the meningococcal App and MspA autotransporters

20 Jan 2015

Abstract excerpt

Neisseria meningitidis, a major cause of bacterial meningitis and septicaemia, secretes multiple virulence factors, including the adhesion and penetration protein (App) and meningococcal serine protease A (MspA). Both are conserved, immunogenic, type Va autotransporters harbouring S6-family serine endopeptidase domains. Previous work suggested that both could mediate adherence to human cells, but their precise...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Genetics and Biotechnology
Share to Bacterial Infections and Vaccines
Share to Peptidase Inhibition and Analysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 25600171
DOI: 10.1111/cmi.12417

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Nuclear trafficking, histone cleavage and induction of apoptosis by the meningococcal App and MspA autotransportersPMID 25600171Read ↗

Identification and characterization of App: an immunogenic autotransporter protein of Neisseria meningitidis.Semantic proximity Read ↗

Characterization of MspA, an Immunogenic Autotransporter Protein That Mediates Adhesion to Epithelial and Endothelial Cells in <i>Neisseria meningitidis</i>Semantic proximity Read ↗

CD46 accelerates macrophage-mediated host susceptibility to meningococcal sepsis in a murine model.Semantic proximity Read ↗

GP96 drives exacerbation of secondary bacterial pneumonia following influenza A virus infectionSemantic proximity Read ↗

A Neisserial autotransporter NalP modulating the processing of other autotransporters.Semantic proximity Read ↗

CD46 in Meningococcal DiseaseSemantic proximity Read ↗

Type VII Secretion Substrates of Pathogenic Mycobacteria Are Processed by a Surface ProteaseSemantic proximity Read ↗

Proteomic and bioinformatic pipeline to screen the ligands of S. pneumoniae interacting with human brain microvascular endothelial cellsSemantic proximity Read ↗

The putative proteinase maturation protein A of Streptococcus pneumoniae is a conserved surface protein with potential to elicit protective immune responses.Semantic proximity Read ↗

The AmiC/NlpD pathway dominates peptidoglycan breakdown in <i>Neisseria meningitidis</i> and affects cell separation, NOD1 agonist production, and infectionSemantic proximity Read ↗

Staphylococcus aureus protein A mediates invasion across airway epithelial cells through activation of RhoA GTPase signaling and proteolytic activity.Semantic proximity Read ↗

ADAM17 targeting by human cytomegalovirus remodels the cell surface proteome to simultaneously regulate multiple immune pathwaysSemantic proximity Read ↗

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