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

Prediction of Extracellular Proteases of the Human Pathogen Helicobacter pylori Reveals Proteolytic Activity of the Hp1018/19 Protein HtrA

22 Oct 2008

Abstract excerpt

Exported proteases of Helicobacter pylori (H. pylori) are potentially involved in pathogen-associated disorders leading to gastric inflammation and neoplasia. By comprehensive sequence screening of the H. pylori proteome for predicted secreted proteases, we retrieved several candidate genes. We detected caseinolytic activities of several such proteases, which are released independently from the H. pylori type IV...

Read the complete abstract on PubMed

Topics

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

Share to Enzyme Production and Characterization
Share to Galectins and Cancer Biology
Share to Helicobacter pylori-related gastroenterology studies

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 18946507
DOI: 10.1371/journal.pone.0003510

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Prediction of Extracellular Proteases of the Human Pathogen Helicobacter pylori Reveals Proteolytic Activity of the Hp1018/19 Protein HtrAPMID 18946507Read ↗

Characterisation of worldwide Helicobacter pylori strains reveals genetic conservation and essentiality of serine protease HtrA.Semantic proximity Read ↗

Proteolytic Landscapes in Gastric Pathology and CancerogenesisSemantic proximity Read ↗

Trimer stability of Helicobacter pylori HtrA is regulated by a natural mutation in the protease domain.Semantic proximity Read ↗

Importance of two PDZ domains for the proteolytic and chaperone activities of Helicobacter pylori serine protease HtrA.Semantic proximity Read ↗

Bacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulence.Semantic proximity Read ↗

Proteome Analysis of Secreted Proteins of the Gastric Pathogen <i>Helicobacter pylori</i>Semantic proximity Read ↗

HtrA Protease Family as Therapeutic TargetsSemantic proximity Read ↗

HtrA-mediated E-cadherin cleavage is limited to DegP and DegQ homologs expressed by gram-negative pathogensSemantic proximity Read ↗

Establishment of serine protease htrA mutants in Helicobacter pylori is associated with secA mutationsSemantic proximity Read ↗

Helicobacter pylori CagA and Cag type IV secretion system activity have key roles in triggering gastric transcriptional and proteomic alterationsSemantic proximity Read ↗

More than Just Protein Degradation: The Regulatory Roles and Moonlighting Functions of Extracellular Proteases Produced by Fungi Pathogenic for HumansSemantic proximity Read ↗

Protease propeptide structures, mechanisms of activation, and functions.Semantic proximity Read ↗

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