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

Mycobacterium tuberculosis Rv0198c, a putative matrix metalloprotease is involved in pathogenicity.

Tuberculosis (Edinburgh, Scotland) - 1 Mar 2011

Muttucumaru D G Niranjala, Smith Debbie A, McMinn Elizabeth J, Reese Valerie, Coler Rhea N, Parish Tanya

Abstract excerpt

We are interested in the role of proteases in the biology of the global human pathogen, Mycobacterium tuberculosis. We have focused on a putative matrix metalloprotease, Rv0198c. In order to investigate its role we constructed an unmarked chromosomal deletion of the gene and analysed the phenotype of the resulting mutant. No differences in growth in axenic culture were seen and there was no measurable change in...

Read the complete abstract on PubMed

Topics

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

Share to Chromosome Deletion
Share to Lung

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Macrophages

Share to Matrix Metalloproteinases

Share to Mice, SCID

Share to Mycobacterium tuberculosis

Share to Spleen

Share to Tuberculosis

Source

Identifiers

PMID: 21216669
DOI: 10.1016/j.tube.2010.11.010

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

Mycobacterium tuberculosis Rv0198c, a putative matrix metalloprotease is involved in pathogenicity.PMID 21216669Read ↗

Expression of a unique M. tuberculosis DNA MTase Rv1509 in M. smegmatis alters the gene expression pattern and enhances virulenceSemantic proximity Read ↗

Characterisation of a putative M23-domain containing protein in Mycobacterium tuberculosis.Semantic proximity Read ↗

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

Secretory protein Rv1987, a ‘probable chitinase’ from <i>Mycobacterium tuberculosis</i> is a novel chitin and cellulose binding protein lacking enzymatic functionSemantic proximity Read ↗

Rv2231c, a unique histidinol phosphate aminotransferase from Mycobacterium tuberculosis, supports virulence by inhibiting host-directed defenseSemantic proximity Read ↗

Proteomic analysis of <i>Mycobacterium tuberculosis</i> lacking a putative short-chain dehydrogenase (Rv0148)Semantic proximity Read ↗

Unveiling the Significance of LysE in Survival and Virulence of Mycobacterium Tuberculosis: A Comprehensive Review reveals it as a potential Drug Target, Diagnostic Marker, and a Vaccine CandidateSemantic proximity Read ↗

ClpP Protease, a Promising Antimicrobial TargetSemantic proximity Read ↗

Cutinase‐like proteins of <i>Mycobacterium tuberculosis</i> : characterization of their variable enzymatic functions and active site identificationSemantic proximity Read ↗

Identification of Quantitative Proteomic Differences between Mycobacterium tuberculosis Lineages with Altered VirulenceSemantic proximity Read ↗

N-terminomics identifies widespread endoproteolysis and novel methionine excision in a genome-reduced bacterial pathogenSemantic proximity Read ↗

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

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