Wenzel, Dirk

[["dc.bibliographiccitation.firstpage","395"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Clinical Cancer Research"],["dc.bibliographiccitation.lastpage","404"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Koch, Raphael"],["dc.contributor.author","Aung, Thiha"],["dc.contributor.author","Vogel, Daniel"],["dc.contributor.author","Chapuy, Björn"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Becker, Sabrina"],["dc.contributor.author","Sinzig, Ursula"],["dc.contributor.author","Venkataramani, Vivek"],["dc.contributor.author","von Mach, Tobias"],["dc.contributor.author","Jacob, Ralf"],["dc.contributor.author","Truemper, Lorenz H."],["dc.contributor.author","Wulf, Gerald G."],["dc.date.accessioned","2018-11-07T10:19:22Z"],["dc.date.available","2018-11-07T10:19:22Z"],["dc.date.issued","2016"],["dc.description.abstract","Purpose: Although R-CHOP-based immunochemotherapy cures significant proportions of patients with aggressive B-cell lymphoma, tumor cell susceptibility to chemotherapy varies, with mostly fatal outcome in cases of resistant disease. We and others have shown before that export of cytostatic drugs contributes to drug resistance. Now we provide a novel approach to overcome exosome-mediated drug resistance in aggressive B-cell lymphomas. Experimental Design: We used well-established centrifugation protocols to purify exosomes from DLBCL cell lines and detected anthracyclines using FACS and HPLC. We used shRNA knockdown of ABCA3 to determine ABCA3 dependence of chemotherapy susceptibility and monitored ABCA3 expression after indomethacin treatment using qPCR. Finally, we established an in vivo assay using a chorioallantoic membrane (CAM) assay to determine the synergy of anthracycline and indomethacin treatment. Results: We show increased efficacy of the anthracycline doxorubicin and the anthracenedione pixantrone by suppression of exosomal drug resistance with indomethacin. B-cell lymphoma cells in vitro efficiently extruded doxorubicin and pixantrone, in part compacted in exosomes. Exosomal biogenesis was critically dependent on the expression of the ATP-transporter A3 (ABCA3). Genetic or chemical depletion of ABCA3 augmented intracellular retention of both drugs and shifted the subcellular drug accumulation to prolonged nuclear retention. Indomethacin increased the cytostatic efficacy of both drugs against DLBCL cell lines in vitro and in vivo in a CAM assay. Conclusions: We propose pretreatment with indomethacin toward enhanced antitumor efficacy of anthracyclines and anthracenediones. (C) 2015 AACR."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft; University Medicine Goettingen"],["dc.identifier.doi","10.1158/1078-0432.CCR-15-0577"],["dc.identifier.isi","000369076500016"],["dc.identifier.pmid","26369630"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41643"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1557-3265"],["dc.relation.issn","1078-0432"],["dc.title","Nuclear Trapping through Inhibition of Exosomal Export by Indomethacin Increases Cytostatic Efficacy of Doxorubicin and Pixantrone"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","333"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","The Plant Cell"],["dc.bibliographiccitation.lastpage","350"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Orth, Travis"],["dc.contributor.author","Reumann, Sigrun"],["dc.contributor.author","Zhang, X."],["dc.contributor.author","Fan, Jilian"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Quan, Sheng"],["dc.contributor.author","Hu, Jianping"],["dc.date.accessioned","2018-11-07T11:07:27Z"],["dc.date.available","2018-11-07T11:07:27Z"],["dc.date.issued","2007"],["dc.description.abstract","PEROXIN11 ( PEX11) is a peroxisomal membrane protein in fungi and mammals and was proposed to play a major role in peroxisome proliferation. To begin understanding how peroxisomes proliferate in plants and how changes in peroxisome abundance affect plant development, we characterized the extended Arabidopsis thaliana PEX11 protein family, consisting of the three phylogenetically distinct subfamilies PEX11a, PEX11b, and PEX11c to PEX11e. All five Arabidopsis PEX11 proteins target to peroxisomes, as demonstrated for endogenous and cyan fluorescent protein fusion proteins by fluorescence microscopy and immunobiochemical analysis using highly purified leaf peroxisomes. PEX11a and PEX11c to PEX11e behave as integral proteins of the peroxisome membrane. Overexpression of At PEX11 genes in Arabidopsis induced peroxisome proliferation, whereas reduction in gene expression decreased peroxisome abundance. PEX11c and PEX11e, but not PEX11a, PEX11b, and PEX11d, complemented to significant degrees the growth phenotype of the Saccharomyces cerevisiae pex11 null mutant on oleic acid. Heterologous expression of PEX11e in the yeast mutant increased the number and reduced the size of the peroxisomes. We conclude that all five Arabidopsis PEX11 proteins promote peroxisome proliferation and that individual family members play specific roles in distinct peroxisomal subtypes and environmental conditions and possibly in different steps of peroxisome proliferation."],["dc.identifier.doi","10.1105/tpc.106.045831"],["dc.identifier.isi","000244757400027"],["dc.identifier.pmid","17220199"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52566"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Plant Biologists"],["dc.relation.issn","1040-4651"],["dc.title","The PEROXIN11 protein family controls peroxisome proliferation in Arabidopsis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","937"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","948"],["dc.bibliographiccitation.volume","172"],["dc.contributor.author","Trajkovic, K."],["dc.contributor.author","Dhaunchak, A. S."],["dc.contributor.author","Goncalves, J. T."],["dc.contributor.author","Wenzel, D."],["dc.contributor.author","Schneider, Anja"],["dc.contributor.author","Bunt, Gertrude"],["dc.contributor.author","Nave, K. A."],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2018-11-07T10:06:22Z"],["dc.date.available","2018-11-07T10:06:22Z"],["dc.date.issued","2006"],["dc.description.abstract","During vertebrate brain development, axons are enwrapped by myelin, an insulating membrane produced by oligodendrocytes. Neuron-derived signaling molecules are temporally and spatially required to coordinate oligodendrocyte differentiation. In this study, we show that neurons regulate myelin membrane trafficking in oligodendrocytes. In the absence of neurons, the major myelin membrane protein, the proteolipid protein (PLP), is internalized and stored in late endosomes/lysosomes (LEs/Ls) by a cholesterol-dependent and clathrin-independent endocytosis pathway that requires actin and the RhoA guanosine triphosphatase. Upon maturation, the rate of endocytosis is reduced, and a cAMP-dependent neuronal signal triggers the transport of PLP from LEs/Ls to the plasma membrane. These findings reveal a fundamental and novel role of LEs/Ls in oligodendrocytes: to store and release PLP in a regulated fashion. The release of myelin membrane from LEs/Ls by neuronal signals may represent a mechanism to control myelin membrane growth."],["dc.identifier.doi","10.1083/jcb.200509022"],["dc.identifier.isi","000235971900018"],["dc.identifier.pmid","16520383"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39080"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Rockefeller Univ Press"],["dc.relation.issn","0021-9525"],["dc.title","Neuron to glia signaling triggers myelin membrane exocytosis from endosomal storage sites"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","251"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","265"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Studencka, Maja"],["dc.contributor.author","Konzer, Anne"],["dc.contributor.author","Moneron, Gael"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Opitz, Lennart"],["dc.contributor.author","Salinas-Riester, Gabriela"],["dc.contributor.author","Bedet, Cecile"],["dc.contributor.author","Krüger, Marcus"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Wisniewski, Jacek R."],["dc.contributor.author","Schmidt, Henning"],["dc.contributor.author","Palladino, Francesca"],["dc.contributor.author","Schulze, Ekkehard"],["dc.contributor.author","Jedrusik-Bode, Monika"],["dc.date.accessioned","2017-09-07T11:43:14Z"],["dc.date.available","2017-09-07T11:43:14Z"],["dc.date.issued","2012"],["dc.description.abstract","Linker histone (H1) and heterochromatin protein 1 (HP1) are essential components of heterochromatin which contribute to the transcriptional repression of genes. It has been shown that the methylation mark of vertebrate histone HI is specifically recognized by the chromodomain of HP1. However, the exact biological role of linker histone binding to HP1 has not been determined. Here, we investigate the function of the Caenorhabditis elegans H1 variant HIS-24 and the HP1-like proteins HPL-1 and HPL-2 in the cooperative transcriptional regulation of immune-relevant genes. We provide the first evidence that HPL-1 interacts with HIS-24 monomethylated at lysine 14 (HIS-24KI4me1) and associates in vivo with promoters of genes involved in antimicrobial response. We also report an increase in overall cellular levels and alterations in the distribution of HIS-24K14me1 after infection with pathogenic bacteria. HIS-24K14me1 localization changes from being mostly nuclear to both nuclear and cytoplasmic in the intestinal cells of infected animals. Our results highlight an antimicrobial role of HIS-24K14me1 and suggest a functional link between epigenetic regulation by an HP1/H1 complex and the innate immune system in C. elegans."],["dc.identifier.doi","10.1128/MCB.05229-11"],["dc.identifier.gro","3142612"],["dc.identifier.isi","000299020100002"],["dc.identifier.pmid","22083954"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35"],["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","Novel Roles of Caenorhabditis elegans Heterochromatin Protein HP1 and Linker Histone in the Regulation of Innate Immune Gene Expression"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","121"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Traffic"],["dc.bibliographiccitation.lastpage","132"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Medigeshi, Guruprasad R."],["dc.contributor.author","Krikunova, Maria"],["dc.contributor.author","Radhakrishnan, Karthikeyan"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Klingauf, Juergen"],["dc.contributor.author","Schu, Peter"],["dc.date.accessioned","2018-11-07T11:20:52Z"],["dc.date.available","2018-11-07T11:20:52Z"],["dc.date.issued","2008"],["dc.description.abstract","The adaptor protein complex AP-1 mediates vesicular protein sorting between the trans Golgi network and endosomes. AP-1 recycles between membranes and the cytoplasm together with clathrin during transport vesicle formation and vesicle uncoating. AP-1 recycles independent of clathrin, indicating binding to unproductive membrane domains and premature termination of vesicle budding. Membrane recruitment requires ADP ribosylation factor-1-GTP, a transmembrane protein containing an AP-1-binding motif and phosphatidyl-inositol phosphate (PI-4-P). Little is known about the regulation of AP-1 membrane-cytoplasm recycling. We identified the N-terminal domain of mu 1A-adaptin as being involved in the regulation of AP-1 membrane-cytoplasm recycling by constructing chimeras of mu 1A and its homologue mu 2. The AP-1 complex containing this mu 2-mu 1A chimera had slowed down recycling kinetics, resulting in missorting of mannose 6-phosphate receptors. The N-terminal domain is only accessible from the cytoplasmic AP-1 surface. None of the proteins known to influence AP-1 membrane recycling bound to this mu 1A domain, indicating the regulation of AP-1 membrane-cytoplasm recycling by an yet unidentified cytoplasmic protein."],["dc.identifier.doi","10.1111/j.1600-0854.2007.00672.x"],["dc.identifier.isi","000251588300011"],["dc.identifier.pmid","17988225"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55638"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Publishing"],["dc.relation.issn","1398-9219"],["dc.title","AP-1 membrane-cytoplasm recycling regulated by mu 1A-adaptin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","650"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Experimental Dermatology"],["dc.bibliographiccitation.lastpage","655"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Kotzerke, Kristina"],["dc.contributor.author","Mempel, Martin"],["dc.contributor.author","Aung, Thiha"],["dc.contributor.author","Wulf, Gerald G."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Schoen, Michael Peter"],["dc.contributor.author","Braun, Andrea"],["dc.date.accessioned","2018-11-07T09:19:28Z"],["dc.date.available","2018-11-07T09:19:28Z"],["dc.date.issued","2013"],["dc.description.abstract","It has long been known that keratinocytes influence cutaneous immunity through secretion of soluble factors. Exosomes, small membrane vesicles of endocytotic origin, have been implicated in intercellular communication processes such as the transfer of tumor cell antigens and the activation of recipient dendritic cells (DC). However, little is known about immunomodulatory functions of keratinocyte-derived exosomes. To address this question, we analysed exosome secretion of the murine keratinocyte cell line MPEK under steady state as well as inflammatory conditions (+/- IFN). These exosomes were readily taken up by bone marrow-derived DC (BMDC) in vitro resulting in a matured phenotype, as evidenced by increased CD40 expression as well as by the production of large amounts of IL-6, IL-10 and IL-12. When the transfer of antigen-specific information through exosomes was investigated, it was found that keratinocytes took up antigen (ovalbumin) and transferred it to their exosomes. However, these antigen-harbouring exosomes failed to induce antigen-specific T cell responses via BMDC. Together, this novel biological function suggests that keratinocytes are able to direct unspecific immune processes but do not elicit specific immune responses."],["dc.identifier.doi","10.1111/exd.12230"],["dc.identifier.isi","000325008600005"],["dc.identifier.pmid","24079734"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28641"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0906-6705"],["dc.title","Immunostimulatory activity of murine keratinocyte-derived exosomes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Journal of Cell Biology"],["dc.bibliographiccitation.volume","85"],["dc.contributor.author","Wagner, Oliver"],["dc.contributor.author","Esposito, Alessandro"],["dc.contributor.author","Shen, K."],["dc.contributor.author","Wenzel, D."],["dc.contributor.author","Kohler, B."],["dc.contributor.author","Wouters, Fred S."],["dc.contributor.author","Klopfenstein, D. R."],["dc.date.accessioned","2018-11-07T10:11:06Z"],["dc.date.available","2018-11-07T10:11:06Z"],["dc.date.issued","2006"],["dc.format.extent","23"],["dc.identifier.isi","000237127500036"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39980"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Gmbh, Urban & Fischer Verlag"],["dc.publisher.place","Jena"],["dc.relation.conference","29th Annual Meeting of the German Society for Cell Biology"],["dc.relation.eventlocation","Braunschweig, GERMANY"],["dc.relation.issn","0171-9335"],["dc.title","How the LAR-interacting protein SYD-2 both clusters and regulates motor activity of KIF1A/UNC-104 in C. elegans"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","239"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Craniofacial Surgery"],["dc.bibliographiccitation.lastpage","243"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Wiltfang, J."],["dc.contributor.author","Merten, Hans-Albert"],["dc.contributor.author","Schultze-Mosgau, S."],["dc.contributor.author","Schrell, U."],["dc.contributor.author","Wenzel, D."],["dc.contributor.author","Kessler, P."],["dc.date.accessioned","2018-11-07T10:54:00Z"],["dc.date.available","2018-11-07T10:54:00Z"],["dc.date.issued","2000"],["dc.description.abstract","Metallic plates are known for their passive intraosseous transmission in the growing skull. To avoid plate removal, resorbable material with strength comparable to that of metallic plates and predictable resorption would be desirable. This should be accomplished without causing inflammatory complications and foreign body reactions often seen with highly crystalline poly-L-lactic acid or pure polyglycolic acid implants. In an animal experiment in four young Gottingen minipigs, the resorbable poly-L-lactic acid/polyglycolic acid copolymer LactoSorb was tested previously. In addition to testing the mechanical properties, the process of degradation and sub- versus epi- or supraperiosteal application of the miniplate device LactoSorb was evaluated using a frontal cranioosteoplasty model. Furthermore, LactoSorb was used in 10 patients with craniosynostosis or craniofacial trauma. During degradation, the absorbable poly-L-lactic acid/polyglycolic acid miniplates acted like metal plates because they also displayed passive intraosseous transmission in the growing animal model. Degradation took 12 to 18 months and was not delayed by bony incorporation. Their mechanical properties proved to be sufficient in craniofacial surgery. Epiperiosteal plating prolonged the passive intraosseous transmission effect during the first 3 months after surgery. There were no major inflammatory reactions seen in the experimental and/or in the clinical study."],["dc.identifier.doi","10.1097/00001665-200011030-00006"],["dc.identifier.isi","000167444600007"],["dc.identifier.pmid","11314302"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49469"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Lippincott Williams & Wilkins"],["dc.relation.issn","1049-2275"],["dc.title","Biodegradable miniplates (LactoSorb): Long-term results in infant minipigs and clinical results"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3285"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","3290"],["dc.bibliographiccitation.volume","93"],["dc.contributor.author","Egner, Alexander"],["dc.contributor.author","Geisler, Claudia"],["dc.contributor.author","von Middendorff, Claas"],["dc.contributor.author","Bock, Hannes"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Medda, Rebecca"],["dc.contributor.author","Andresen, Martin"],["dc.contributor.author","Stiel, Andre C."],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Schoenle, Andreas"],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2017-09-07T11:49:23Z"],["dc.date.available","2017-09-07T11:49:23Z"],["dc.date.issued","2007"],["dc.description.abstract","We demonstrate nanoscale resolution in far-field fluorescence microscopy using reversible photoswitching and localization of individual fluorophores at comparatively fast recording speeds and from the interior of intact cells. These advancements have become possible by asynchronously recording the photon bursts of individual molecular switching cycles. We present images from the microtubular network of an intact mammalian cell with a resolution of 40 nm."],["dc.identifier.doi","10.1529/biophysj.107.112201"],["dc.identifier.gro","3143415"],["dc.identifier.isi","000250199300033"],["dc.identifier.pmid","17660318"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/927"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0006-3495"],["dc.title","Fluorescence nanoscopy in whole cells by asynchronous localization of photoswitching emitters"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2412"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","2421"],["dc.bibliographiccitation.volume","117"],["dc.contributor.author","Toth, Alexandra"],["dc.contributor.author","Meyrat, Axel"],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Santiago, Ricardo"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","von Ballmoos, Christoph"],["dc.contributor.author","Ott, Martin"],["dc.date.accessioned","2020-12-10T18:12:55Z"],["dc.date.available","2020-12-10T18:12:55Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1073/pnas.1917968117"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74534"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/42"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A05: Mitochondriale Heterogenität in Synapsen"],["dc.relation.workinggroup","RG Jakobs (Structure and Dynamics of Mitochondria)"],["dc.title","Kinetic coupling of the respiratory chain with ATP synthase, but not proton gradients, drives ATP production in cristae membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]