Rehling, Peter

[["dc.bibliographiccitation.firstpage","2642"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","2649"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Hutu, Dana P."],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","Becker, Dorothea"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","van der Laan, Martin"],["dc.date.accessioned","2017-09-07T11:48:16Z"],["dc.date.available","2017-09-07T11:48:16Z"],["dc.date.issued","2008"],["dc.description.abstract","The presequence translocase of the mitochondrial inner membrane (TIM23 complex) mediates the import of preproteins with amino-terminal presequences. To drive matrix translocation the TIM23 complex recruits the presequence translocase-associated motor (PAM) with the matrix heat shock protein 70 (mtHsp70) as central subunit. Activity and localization of mtHsp70 are regulated by four membrane-associated cochaperones: the adaptor protein Tim44, the stimulatory J-complex Pam18/Pam16, and Pam17. It has been proposed that Tim44 serves as molecular platform to localize mtHsp70 and the J-complex at the TIM23 complex, but it is unknown how Pam17 interacts with the translocase. We generated conditional tim44 yeast mutants and selected a mutant allele, which differentially affects the association of PAM modules with TIM23. In tim44-804 mitochondria, the interaction of the J-complex with the TIM23 complex is impaired, whereas unexpectedly the binding of Pam17 is increased. Pam17 interacts with the channel protein Tim23, revealing a new interaction site between TIM23 and PAM. Thus, the motor PAM is composed of functional modules that bind to different sites of the translocase. We suggest that Tim44 is not simply a scaffold for binding of motor subunits but plays a differential role in the recruitment of PAM modules to the inner membrane translocase."],["dc.identifier.doi","10.1091/mbc.E07-12-1226"],["dc.identifier.gro","3143286"],["dc.identifier.isi","000259155200028"],["dc.identifier.pmid","18400944"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/783"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1939-4586"],["dc.relation.issn","1059-1524"],["dc.title","Mitochondrial protein import motor: Differential role of Tim44 in the recruitment of Pam17 and J-complex to the presequence translocase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Bioenergetics"],["dc.bibliographiccitation.volume","1777"],["dc.contributor.author","Wagner, Karina"],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Brandner, Katrin"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2018-11-07T11:12:55Z"],["dc.date.available","2018-11-07T11:12:55Z"],["dc.date.issued","2008"],["dc.format.extent","S42"],["dc.identifier.doi","10.1016/j.bbabio.2008.05.168"],["dc.identifier.isi","000258037700158"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53773"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.publisher.place","Amsterdam"],["dc.relation.conference","15th European Bioenergetic Conference"],["dc.relation.eventlocation","Trinity Coll, Dublin, IRELAND"],["dc.relation.issn","0005-2728"],["dc.title","Biogenesis of the mitochondrial carrier translocase"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","643"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","656"],["dc.bibliographiccitation.volume","195"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Melin, Jonathan"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:43:19Z"],["dc.date.available","2017-09-07T11:43:19Z"],["dc.date.issued","2011"],["dc.description.abstract","N-terminal targeting signals (presequences) direct proteins across the TOM complex in the outer mitochondrial membrane and the TIM23 complex in the inner mitochondrial membrane. Presequences provide directionality to the transport process and regulate the transport machineries during translocation. However, surprisingly little is known about how presequence receptors interact with the signals and what role these interactions play during preprotein transport. Here, we identify signal-binding sites of presequence receptors through photo-affinity labeling. Using engineered presequence probes, photo cross-linking sites on mitochondrial proteins were mapped mass spectrometrically, thereby defining a presequence-binding domain of Tim50, a core subunit of the TIM23 complex that is essential for mitochondrial protein import. Our results establish Tim50 as the primary presequence receptor at the inner membrane and show that targeting signals and Tim50 regulate the Tim23 channel in an antagonistic manner."],["dc.identifier.doi","10.1083/jcb.201105098"],["dc.identifier.gro","3142630"],["dc.identifier.isi","000297206400012"],["dc.identifier.pmid","22065641"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8033"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Rockefeller Univ Press"],["dc.relation.issn","0021-9525"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Tim50's presequence receptor domain is essential for signal driven transport across the TIM23 complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","4028"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Schendzielorz, Alexander Benjamin"],["dc.contributor.author","Bragoszewski, Piotr"],["dc.contributor.author","Naumenko, Nataliia"],["dc.contributor.author","Gomkale, Ridhima"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2020-04-29T13:50:43Z"],["dc.date.available","2020-04-29T13:50:43Z"],["dc.date.issued","2018"],["dc.description.abstract","The presequence translocase of the mitochondrial inner membrane (TIM23 complex) facilitates anterograde precursor transport into the matrix and lateral release of precursors with stop-transfer signal into the membrane (sorting). Sorting requires precursor exit from the translocation channel into the lipid phase through the lateral gate of the TIM23 complex. How the two transport modes are regulated and balanced against each other is unknown. Here we show that the import motor J-protein Pam18, which is essential for matrix import, controls lateral protein release into the lipid bilayer. Constitutively translocase-associated Pam18 obstructs lateral precursor transport. Concomitantly, Mgr2, implicated in precursor quality control, is displaced from the translocase. We conclude that during motor-dependent matrix protein transport, the transmembrane segment of Pam18 closes the lateral gate to promote anterograde polypeptide movement. This finding explains why a motor-free form of the translocase facilitates the lateral movement of precursors with a stop-transfer signal."],["dc.identifier.doi","10.1038/s41467-018-06492-8"],["dc.identifier.pmid","30279421"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15610"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/64487"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.eissn","2041-1723"],["dc.relation.issn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Motor recruitment to the TIM23 channel's lateral gate restricts polypeptide release into the inner membrane"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7780"],["dc.bibliographiccitation.issue","22"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","7789"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Truscott, Kaye N."],["dc.contributor.author","Wiedemann, Nils"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Muller, H"],["dc.contributor.author","Meisinger, Chris"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Guiard, Bernard"],["dc.date.accessioned","2017-09-07T11:45:14Z"],["dc.date.available","2017-09-07T11:45:14Z"],["dc.date.issued","2002"],["dc.description.abstract","The mitochondrial intermembrane space contains a protein complex essential for cell viability, the Tim9-Tim10 complex. This complex is required for the import of hydrophobic membrane proteins, such as the ADP/ATP carrier (AAC), into the inner membrane. Different views exist about the role played by the Tim9-Tim10 complex in translocation of the AAC precursor across the outer membrane. For this report we have generated a new tim10 yeast mutant that leads to a strong defect in AAC import into mitochondria. Thereby, for the first time, authentic AAC is stably arrested in the translocase complex of the outer membrane (TOM), as shown by antibody shift blue native electrophoresis. Surprisingly, AAC is still associated with the receptors Tom70 and Tom20 when the function of Tim10 is impaired. The nonessential Tim8-Tim13 complex of the intermembrane space is not involved in the transfer of AAC across the outer membrane. These results define a two-step mechanism for translocation of AAC across the outer membrane. The initial insertion of AAC into the import channel is independent of the function of Tim9-Tim10; however, completion of translocation across the outer membrane, including release from the TOM complex, requires a functional Tim9-Tim10 complex."],["dc.identifier.doi","10.1128/MCB.22.22.7780-7789.2002"],["dc.identifier.gro","3144157"],["dc.identifier.isi","000178953700006"],["dc.identifier.pmid","12391147"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1750"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1098-5549"],["dc.relation.issn","0270-7306"],["dc.title","Mitochondrial import of the ADP/ATP carrier: The essential TIM complex of the intermembrane space is required for precursor release from the TOM complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","38047"],["dc.bibliographiccitation.issue","36"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","38054"],["dc.bibliographiccitation.volume","279"],["dc.contributor.author","Li, Yanfeng"],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Voos, Wolfgang"],["dc.date.accessioned","2017-09-07T11:43:13Z"],["dc.date.available","2017-09-07T11:43:13Z"],["dc.date.issued","2004"],["dc.description.abstract","Transport of preproteins into the mitochondrial matrix requires the presequence translocase of the inner membrane (TIM23 complex) and the presequence translocase-associated motor (PAM). The motor consists of five essential subunits, the mitochondrial heat shock protein 70 (mtHsp70) and four cochaperones, the nucleotide exchange-factor Mge1, the translocase-associated fulcrum Tim44, the J-protein Pam18, and Pam16. Pam16 forms a complex with Pam18 and displays similarity to J-proteins but lacks the canonical tripeptide motif His-Pro-Asp (HPD). We report that Pam16 does not function as a typical J-domain protein but, rather, antagonizes the function of Pam18. Pam16 specifically inhibits the Pam18-mediated stimulation of the ATPase activity of mtHsp70. The inclusion of the HPD motif in Pam16 does not confer the ability to stimulate mtHsp70 activity. Pam16-HPD fully substitutes for wild-type Pam16 in vitro and in vivo but is not able to replace Pam18. Pam16 represents a new type of cochaperone that controls the stimulatory effect of the J-protein Pam18 and regulates the interaction of mtHsp70 with precursor proteins during import into mitochondria."],["dc.identifier.doi","10.1074/jbc.M404319200"],["dc.identifier.gro","3143946"],["dc.identifier.isi","000223554600099"],["dc.identifier.pmid","15218029"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1516"],["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","0021-9258"],["dc.title","The presequence translocase-associated protein import motor of mitochondria"],["dc.title.subtitle","Pam16 functions in an antagonistic manner to Pam18"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","363"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Molecular Cell"],["dc.bibliographiccitation.lastpage","373"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Kovermann, P."],["dc.contributor.author","Truscott, Kaye N."],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Sepuri, N. B."],["dc.contributor.author","Müller, H."],["dc.contributor.author","Jensen, R. E."],["dc.contributor.author","Wagner, Richard"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.date.accessioned","2017-09-07T11:45:56Z"],["dc.date.available","2017-09-07T11:45:56Z"],["dc.date.issued","2002"],["dc.description.abstract","The protein insertion complex of the mitochondrial inner membrane is crucial for import of the numerous multitopic membrane proteins with internal targeting signals. Little is known about the molecular mechanism of this complex, including whether it forms a real channel or merely acts as scaffold for protein insertion. We report the unexpected observation that Tim22 is the only essential membrane-integrated subunit of the complex. Reconstituted Tim22 forms a hydrophilic, high-conductance channel with distinct opening states and pore diameters. The channel is voltage-activated and specifically responds to an internal targeting signal, but not to presequences. Thus, a protein insertion complex can combine three essential functions, signal recognition, channel formation, and energy transduction, in one central component."],["dc.identifier.doi","10.1016/S1097-2765(02)00446-X"],["dc.identifier.gro","3144222"],["dc.identifier.isi","000173927000019"],["dc.identifier.pmid","11864609"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1822"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: NIGMS NIH HHS [R01-GM46803]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1097-2765"],["dc.title","Tim22, the essential core of the mitochondrial protein insertion complex, forms a voltage-activated and signal-gated channel"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","817"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","829"],["dc.bibliographiccitation.volume","120"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","Lind, Maria"],["dc.contributor.author","Frazier, Ann E."],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Meisinger, Chris"],["dc.contributor.author","Geissler, Andreas"],["dc.contributor.author","Sickmann, Albert"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Truscott, Kaye N."],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:54:31Z"],["dc.date.available","2017-09-07T11:54:31Z"],["dc.date.issued","2005"],["dc.description.abstract","The presequence translocase of the inner mitochondrial membrane (TIM23 complex) operates at a central junction of protein import. It accepts preproteins from the outer membrane TOM complex and directs them to inner membrane insertion or, in cooperation with the presequence translocase-associated motor (PAM), to the matrix. Little is known of how the TIM23 complex coordinates these tasks. We have identified Tim21 (YGR033c) that interacts with the TOM complex. Tim21 is specific for a TIM23 form that cooperates with TOM and promotes inner membrane insertion. Protein translocation into the matrix requires a switch to a Tim21-free, PAM bound presequence translocase. Tim17 is crucial for the switch by performing two separable functions: promotion of inner membrane insertion and binding of Pam18 to form the functional TIM-PAM complex. Thus, the presequence translocase is not a static complex but switches between TOM tethering and PAM binding in a reaction cycle involving Tim21 and Tim17."],["dc.identifier.doi","10.1016/j.cell.2005.01.011"],["dc.identifier.gro","3143878"],["dc.identifier.isi","000228067500011"],["dc.identifier.pmid","15797382"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1440"],["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","0092-8674"],["dc.title","Mitochondrial presequence translocase: Switching between TOM tethering and motor recruitment involves Tim21 and Tim17"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","226"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","233"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Frazier, Ann E."],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Voos, W."],["dc.contributor.author","Li, Y. F."],["dc.contributor.author","Lind, Maria"],["dc.contributor.author","Meisinger, Chris"],["dc.contributor.author","Geissler, A."],["dc.contributor.author","Sickmann, Albert"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Bilanchone, V."],["dc.contributor.author","Cumsky, M. G."],["dc.contributor.author","Truscott, Kaye N."],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:43:59Z"],["dc.date.available","2017-09-07T11:43:59Z"],["dc.date.issued","2004"],["dc.description.abstract","Mitochondrial preproteins destined for the matrix are translocated by two channel-forming transport machineries, the translocase of the outer membrane and the presequence translocase of the inner membrane. The presequence translocase-associated protein import motor (PAM) contains four essential subunits: the matrix heat shock protein 70 (mtHsp70) and its three cochaperones Mge1, Tim44 and Pam18. Here we report that the PAM contains a fifth essential subunit, Pam16 ( encoded by Saccharomyces cerevisiae YJL104W), which is selectively required for preprotein translocation into the matrix, but not for protein insertion into the inner membrane. Pam16 interacts with Pam18 and is needed for the association of Pam18 with the presequence translocase and for formation of a mtHsp70 Tim44 complex. Thus, Pam16 is a newly identified type of motor subunit and is required to promote a functional PAM reaction cycle, thereby driving preprotein import into the matrix."],["dc.identifier.doi","10.1038/nsmb735"],["dc.identifier.gro","3144008"],["dc.identifier.isi","000220281100012"],["dc.identifier.pmid","14981507"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1585"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: NIGMS NIH HHS [GM 57017]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1545-9985"],["dc.title","Pam16 has an essential role in the mitochondrial protein import motor"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7449"],["dc.bibliographiccitation.issue","17"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","7458"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","Lind, Maria"],["dc.contributor.author","Perschil, Inge"],["dc.contributor.author","Sickmann, Albert"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Meisinger, Chris"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:54:18Z"],["dc.date.available","2017-09-07T11:54:18Z"],["dc.date.issued","2005"],["dc.description.abstract","Import of mitochondrial matrix proteins involves the general translocase of the outer membrane and the presequence translocase of the inner membrane. The presequence translocase-associated motor (PAM) drives the completion of preprotein translocation into the matrix. Five subunits of PAM are known: the preprotein-binding matrix heat shock protein 70 (mtHsp70), the nucleotide exchange factor Mge1, Tim44 that directs mtHsp70 to the inner membrane, and the membrane-bound complex of Pam16-Pam18 that regulates the ATPase activity of mtHsp70. We have identified a sixth motor subunit. Pam17 (encoded by the open reading frame YKR065c) is anchored in the inner membrane and exposed to the matrix. Mitochondria lacking Pam17 are selectively impaired in the import of matrix proteins and the generation of an import-driving activity of PAM. Pam17 is required for formation of a stable complex between the cochaperones Pam16 and Pam18 and promotes the association of Pam16-Pam18 with the presequence translocase. Our findings suggest that Pam17 is required for the correct organization of the Pam16-Pam18 complex and thus contributes to regulation of mtHsp70 activity at the inner membrane translocation site."],["dc.identifier.doi","10.1128/MCB.25.17.7449-7458.2005"],["dc.identifier.gro","3143811"],["dc.identifier.isi","000231329300006"],["dc.identifier.pmid","16107694"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1366"],["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","0270-7306"],["dc.title","Pam17 is required for architecture and translocation activity of the mitochondrial protein import motor"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]