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

Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA – Implications for the catalytic mechanism of parvulins

24 Mar 2009

Abstract excerpt

BACKGROUND: Staphylococcus aureus is a Gram-positive pathogenic bacterium causing many kinds of infections from mild respiratory tract infections to life-threatening states as sepsis. Recent emergence of S. aureus strains resistant to numerous antibiotics has created a need for new antimicrobial agents and novel drug targets. S. aureus PrsA is a membrane associated extra-cytoplasmic lipoprotein which contains a...

Read the complete abstract on PubMed

Topics

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

Share to Histone Deacetylase Inhibitors Research
Share to Peptidase Inhibition and Analysis
Share to Signaling Pathways in Disease

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 19309529
DOI: 10.1186/1472-6807-9-17

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA – Implications for the catalytic mechanism of parvulinsPMID 19309529Read ↗

The Posttranslocational Chaperone Lipoprotein PrsA Is Involved in both Glycopeptide and Oxacillin Resistance in Staphylococcus aureusSemantic proximity Read ↗

Investigation of cross-opsonic effect leads to the discovery of PPIase- domain containing protein vaccine target to prevent infections by Gram-positive ESKAPE pathogensSemantic proximity Read ↗

An Intracellular Peptidyl-Prolyl cis/trans Isomerase Is Required for Folding and Activity of the Staphylococcus aureus Secreted Virulence Factor Nuclease.Semantic proximity Read ↗

Microbial Peptidyl-Prolyl <i>cis</i> / <i>trans</i> Isomerases (PPIases): Virulence Factors and Potential Alternative Drug TargetsSemantic proximity Read ↗

Targeting Protein Folding: A Novel Approach for the Treatment of Pathogenic BacteriaSemantic proximity Read ↗

The Peptidyl-Prolyl Isomerase Motif Is Lacking in PmpA, the PrsA-Like Protein Involved in the Secretion Machinery of Lactococcus lactisSemantic proximity Read ↗

Molecular basis of β-lactam antibiotic resistance of ESKAPE bacterium E. faecium Penicillin Binding Protein PBP5Semantic proximity Read ↗

Characterisation of SEQ0694 (PrsA/PrtM) of Streptococcus equi as a functional peptidyl-prolyl isomerase affecting multiple secreted protein substrates.Semantic proximity Read ↗

A de novo-designed antimicrobial peptide with activity against multiresistant Staphylococcus aureus acting on RsbW kinase.Semantic proximity Read ↗

Divergent LD-transpeptidase-independent effects of peptidoglycan carboxypeptidases on intrinsic β-lactam and vancomycin resistanceSemantic proximity Read ↗

The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.Semantic proximity Read ↗

Chlamydomonas Immunophilins and Parvulins: Survey and Critical Assessment of Gene ModelsSemantic proximity Read ↗

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