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

Vaccine potential of bacterial macrophage infectivity potentiator (MIP)-like peptidyl prolylcis/transisomerase (PPIase) proteins

15 Oct 2015

Abstract excerpt

Peptidyl prolyl cis/trans isomerases (PPIases) are a superfamily of proteins ubiquitously distributed among living organisms, which function primarily to assist the folding and structuring of unfolded and partially folded polypeptide chains and proteins. In this review, we focus specifically on the Macrophage Infectivity Potentiator (MIP)-like PPIases, which are members of the immunophilin family of FK506-binding...

Read the complete abstract on PubMed

Topics

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

Share to Peptidase Inhibition and Analysis
Share to Signaling Pathways in Disease
Share to Toxin Mechanisms and Immunotoxins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 26468663
DOI: 10.1586/14760584.2015.1095638

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

Vaccine potential of bacterial macrophage infectivity potentiator (MIP)-like peptidyl prolylcis/transisomerase (PPIase) proteinsPMID 26468663Read ↗

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

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

A Burkholderia pseudomallei Macrophage Infectivity Potentiator-Like Protein Has Rapamycin-Inhibitable Peptidylprolyl Isomerase Activity and Pleiotropic Effects on VirulenceSemantic proximity Read ↗

Mip protein of Legionella pneumophila exhibits peptidyl‐prolyl‐cis/trans isomerase (PPIase) activitySemantic proximity Read ↗

Ng‐MIP, a surface‐exposed lipoprotein of Neisseria gonorrhoeae, has a peptidyl‐prolyl cis/trans isomerase (PPIase) activity and is involved in persistence in macrophagesSemantic proximity Read ↗

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

Biochemical and functional analyses of the Mip protein: influence of the N-terminal half and of peptidylprolyl isomerase activity on the virulence of Legionella pneumophila.Semantic proximity Read ↗

In Silico Analysis of Conformational Changes Induced by Normal and Mutation of Macrophage Infectivity Potentiator Catalytic Residues and its Interactions with Rapamycin.Semantic proximity Read ↗

Molecular cloning of a Coxiella burnetii gene encoding a macrophage infectivity potentiator (Mip) analogueSemantic proximity Read ↗

M.tb-Rv2462c of Mycobacterium tuberculosis Shows Chaperone-like Activity and Plays a Role in Stress Adaptation and ImmunomodulationSemantic proximity Read ↗

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

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