Mitochondrial permeability transition pore: Back to the drawing board

dc.contributor.author	Chinopoulos Christos
dc.date.accessioned	2022-06-30T07:53:21Z
dc.date.available	2022-06-30T07:53:21Z
dc.date.issued	2018
dc.identifier	85021161724
dc.identifier	85055086882
dc.identifier.citation	journalVolume=117;journalIssueNumber=SI;journalTitle=NEUROCHEMISTRY INTERNATIONAL;pagerange=49-54;journalAbbreviatedTitle=NEUROCHEM INT;
dc.identifier.uri	http://repo.lib.semmelweis.hu//handle/123456789/6676
dc.identifier.uri	doi:10.1016/j.neuint.2017.06.010
dc.description.abstract	Current models theorizing on what the mitochondrial permeability transition (mPT) pore is made of, implicate the c-subunit rings of ATP synthase complex. However, two very recent studies, one on atomistic simulations and in the other disrupting all genes coding for the c subunit disproved those models. As a consequence of this, the structural elements of the pore remain unknown. The purpose of the present short-review is to (i) briefly review the latest findings, (ii) serve as an index for more comprehensive reviews regarding mPT specifics, (iii) reiterate on the potential pitfalls while investigating mPT in conjunction to bioenergetics, and most importantly (iv) suggest to those in search of mPT pore identity, to also look elsewhere. © 2017 Elsevier Ltd.
dc.format.extent	49-54
dc.relation.ispartof	urn:issn:0197-0186
dc.title	Mitochondrial permeability transition pore: Back to the drawing board
dc.type	Journal Article
dc.date.updated	2019-01-23T10:03:32Z
dc.language.rfc3066	en
dc.rights.holder	NULL
dc.identifier.mtmt	3294518
dc.identifier.wos	000438660000006
dc.identifier.pubmed	28647376
dc.contributor.institution	MTA-SE Lendület Neurobiokémiai Munkacsoport
dc.contributor.institution	Orvosi Biokémiai Intézet
dc.contributor.institution	MTA-SE Neurobiokémiai és Molekuláris Élettani Kutatócsoport (2006-ig: MTA-SE Neurobiokémiai Kutatócsoport)
dc.mtmt.swordnote	Összes idézések száma a WoS-ban: 0