Schendzielorz, Alexander Benjamin

[["dc.bibliographiccitation.firstpage","2464"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Cell Metabolism"],["dc.bibliographiccitation.lastpage","2483.e18"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Morgenstern, Marcel"],["dc.contributor.author","Peikert, Christian D."],["dc.contributor.author","Lübbert, Philipp"],["dc.contributor.author","Suppanz, Ida"],["dc.contributor.author","Klemm, Cinzia"],["dc.contributor.author","Alka, Oliver"],["dc.contributor.author","Steiert, Conny"],["dc.contributor.author","Naumenko, Nataliia"],["dc.contributor.author","Schendzielorz, Alexander"],["dc.contributor.author","Melchionda, Laura"],["dc.contributor.author","Warscheid, Bettina"],["dc.date.accessioned","2022-01-11T14:05:34Z"],["dc.date.available","2022-01-11T14:05:34Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1016/j.cmet.2021.11.001"],["dc.identifier.pii","S1550413121005295"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/97693"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-507"],["dc.relation.issn","1550-4131"],["dc.title","Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","265"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Trends in Cell Biology"],["dc.bibliographiccitation.lastpage","275"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Schendzielorz, Alexander Benjamin"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:44:25Z"],["dc.date.available","2017-09-07T11:44:25Z"],["dc.date.issued","2015"],["dc.description.abstract","Trans location of presequence-containing precursor proteins into the inner mitochondrial membrane and matrix is an essential process that is facilitated by the translocase of the outer membrane (TOM) together with the presequence translocase of the inner membrane (TIM23). After initial recognition by receptors of the TOM complex followed by transport across the outer membrane, the precursor emerges into the intermembrane space (IMS). Recognition of the presequence by Tim50 triggers rearrangements of the presequence translocase, priming it for inner membrane translocation. Subsequently, the precursor can be released into the membrane or translocated into the mitochondrial matrix aided by the import motor. This heat-shock protein 70 (Hsp70)-based motor drives precursor unfolding and translocation and is subject to dynamic remodelling. Here, we review recent advances in understanding of the mechanisms underlying protein transport along the. presequence pathway."],["dc.identifier.doi","10.1016/j.tcb.2014.12.001"],["dc.identifier.gro","3141912"],["dc.identifier.isi","000353863700002"],["dc.identifier.pmid","25542066"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2456"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0962-8924"],["dc.title","Unlocking the presequence import pathway"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","889"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Journal of Infectious Diseases"],["dc.bibliographiccitation.lastpage","897"],["dc.bibliographiccitation.volume","211"],["dc.contributor.author","Gierer, S."],["dc.contributor.author","Muller, M. A."],["dc.contributor.author","Heurich, A."],["dc.contributor.author","Ritz, D."],["dc.contributor.author","Springstein, B. L."],["dc.contributor.author","Karsten, C. B."],["dc.contributor.author","Schendzielorz, A."],["dc.contributor.author","Gnirss, K."],["dc.contributor.author","Drosten, C."],["dc.contributor.author","Pohlmann, S."],["dc.date.accessioned","2022-10-06T13:34:58Z"],["dc.date.available","2022-10-06T13:34:58Z"],["dc.date.issued","2014"],["dc.identifier.doi","10.1093/infdis/jiu407"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/116024"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.eissn","1537-6613"],["dc.relation.issn","0022-1899"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.title","Inhibition of Proprotein Convertases Abrogates Processing of the Middle Eastern Respiratory Syndrome Coronavirus Spike Protein in Infected Cells but Does Not Reduce Viral Infectivity"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1850"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.bibliographiccitation.lastpage","1859"],["dc.bibliographiccitation.volume","1853"],["dc.contributor.author","Melin, Jonathan"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Gomkale, Ridhima"],["dc.contributor.author","Schendzielorz, Alexander Benjamin"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Schulz, Christian"],["dc.date.accessioned","2017-09-07T11:43:40Z"],["dc.date.available","2017-09-07T11:43:40Z"],["dc.date.issued","2015"],["dc.description.abstract","The translocase of the outer mitochondrial membrane (TOM complex) is the general entry gate into mitochondria for almost all imported proteins. A variety of specific receptors allow the TOM complex to recognize targeting signals of various precursor proteins that are transported along different import pathways. Aside from the well-characterized presequence receptors Tom20 and Tom22 a third TOM receptor, Tom70, binds proteins of the carrier family containing multiple transmembrane segments. Here we demonstrate that Tom70 directly binds to presequence peptides using a dedicated groove. A single point mutation in the cavity of this pocket (M551R) reduces the presequence binding affinity of Tom70 ten-fold and selectively impairs import of the presequence-containing precursor Mdl1 but not the ADP/ATP carrier (MC). Hence Tom70 contributes to the presequence import pathway by recognition of the targeting signal of the Mdl1 precursor. (C) 2015 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbamcr.2015.04.021"],["dc.identifier.gro","3141858"],["dc.identifier.isi","000356209600009"],["dc.identifier.pmid","25958336"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1856"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","0006-3002"],["dc.relation.issn","0167-4889"],["dc.title","A presequence-binding groove in Tom70 supports import of Mdl1 into mitochondria"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]