Membrane chaperoning by members of the PspA/IM30 protein family.

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dc.identifier.uri Thurotte, Adrien Brüser, Thomas Mascher, Thorsten Schneider, Dirk 2019-06-26T12:21:09Z 2019-06-26T12:21:09Z 2017
dc.identifier.citation Thurotte, Adrien; Brüser, Thomas; Mascher, Thorsten; Schneider, Dirk: Membrane chaperoning by members of the PspA/IM30 protein family. In: Communicative & Integrative Biology 10 (2017), Nr. 1, e1264546. DOI:
dc.description.abstract PspA, IM30 (Vipp1) and LiaH, which all belong to the PspA/IM30 protein family, form high molecular weight oligomeric structures. For all proteins membrane binding and protection of the membrane structure and integrity has been shown or postulated. Here we discuss the possible membrane chaperoning activity of PspA, IM30 and LiaH and propose that larger oligomeric structures bind to stressed membrane regions, followed by oligomer disassembly and membrane stabilization by protein monomers or smaller/different oligomeric scaffolds. eng
dc.language.iso eng
dc.publisher London : Informa UK Limited
dc.relation.ispartofseries Communicative & Integrative Biology 10 (2017), Nr. 1
dc.rights CC BY-NC-ND 4.0 Unported
dc.subject Monomer eng
dc.subject Protein family eng
dc.subject Oligomer eng
dc.subject Membrane structure eng
dc.subject Membrane eng
dc.subject Biochemistry eng
dc.subject Biology eng
dc.subject.ddc 570 | Biowissenschaften, Biologie ger
dc.title Membrane chaperoning by members of the PspA/IM30 protein family.
dc.type article
dc.type Text
dc.relation.issn 1942-0889
dc.bibliographicCitation.issue 1
dc.bibliographicCitation.volume 10
dc.bibliographicCitation.firstPage e1264546
dc.description.version publishedVersion
tib.accessRights frei zug�nglich

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