FKBPs in bacterial infections

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dc.contributor.authorÜnal, Can Murat
dc.contributor.authorSteinert, Michael
dc.date.accessioned2021-01-08T21:51:28Z
dc.date.available2021-01-08T21:51:28Z
dc.date.issued2015
dc.departmentTAÜ, Fen Fakültesi, Moleküler Biyoteknoloji Bölümüen_US
dc.descriptionUnal, Can/0000-0003-4710-9567en_US
dc.descriptionWOS:000361263700015en_US
dc.descriptionPubMed: 25529296en_US
dc.description.abstractBackground: FK506-binding proteins (FKBPs) contain a domain with peptidyl-prolyl-cis/trans-isomerase (PPlase) activity and bind the immunosuppressive drugs FK506 and rapamycin. FKBPs belong to the immunophilin family and are found in eukaryotes and bacteria. Scope of review: In this review we describe two major groups of bacterial virulence-associated FKBPs, the trigger factor and Mip-like PPIases. Moreover, we discuss the contribution of host FKBPs in bacterial infection processes. Major conclusions: Since PPIases are regarded as alternative antiinfective drug targets we highlight current research strategies utilizing pipecolinic acid and cycloheximide derivatives as well as substrate based inhibitors. General significance: The current research strategies suggest a beneficial synergism of drug development and basic research. This article is part of a Special Issue entitled Proline-directed Foldases: Cell Signaling Catalysts and Drug Targets. (C) 2014 Elsevier B.V. All rights reserved.
dc.description.sponsorshipTUBITAKTurkiye Bilimsel ve Teknolojik Arastirma Kurumu (TUBITAK) [2219 (2012/2. term)]; State of Lower Saxony, Niedersachsisches Vorab [VWZN2889]; DFGGerman Research Foundation (DFG) [STE838/8-1]
dc.description.sponsorshipCan M. Unal is supported by a 2219 (2012/2. term) grant from TUBITAK, and the State of Lower Saxony, Niedersachsisches Vorab (VWZN2889) within the joint research project "CDiff: Epidemiology and systems biology of the bacterial pathogen Clostridium difficile". Michael Steinert is funded by the DFG grant STE838/8-1.
dc.identifier.doi10.1016/j.bbagen.2014.12.018
dc.identifier.endpage2102en_US
dc.identifier.issn0304-4165
dc.identifier.issn1872-8006
dc.identifier.issue10en_US
dc.identifier.scopus2-s2.0-84940597104
dc.identifier.scopusqualityQ1
dc.identifier.startpage2096en_US
dc.identifier.urihttp://doi.org/10.1016/j.bbagen.2014.12.018
dc.identifier.urihttps://hdl.handle.net/20.500.12846/285
dc.identifier.volume1850en_US
dc.identifier.wosWOS:000361263700015
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.institutionauthorÜnal, Can Murat
dc.language.isoen
dc.publisherElsevier Science Bv
dc.relation.ispartofBiochimica Et Biophysica Acta-General Subjects
dc.relation.publicationcategoryother
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectFk506-Binding Proteinen_US
dc.subjectMacrophage Infectivity Potentiator (Mip)en_US
dc.subjectBacteriaen_US
dc.subjectPathogenen_US
dc.subjectInfectionen_US
dc.subjectDrug Targeten_US
dc.titleFKBPs in bacterial infections
dc.typeReview Article

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