Wouters, Fred Silvester

[["dc.bibliographiccitation.firstpage","521"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Neurobiology of Disease"],["dc.bibliographiccitation.lastpage","531"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Esposito, Alessandro"],["dc.contributor.author","Dohm, Christoph P."],["dc.contributor.author","Kermer, Pawel"],["dc.contributor.author","Bähr, Mathias"],["dc.contributor.author","Wouters, Fred S."],["dc.date.accessioned","2017-09-07T11:49:47Z"],["dc.date.available","2017-09-07T11:49:47Z"],["dc.date.issued","2007"],["dc.description.abstract","alpha-Synuclein is a primarily neuronal protein that is enriched at the presynapse. alpha-Synuclein and the microtubule binding protein tau have been implicated in neurodegenerative diseases. alpha-Synuclein is known to associate with phospholipid vesicles, regulates dopamine metabolism and exhibits chaperone activity, but its main role remains largely unknown. Furthermore, knowledge on its interactions and posttranslational modifications is essential for a molecular understanding of alpha-synucleinopathies. We investigated alpha-synuclein mutations, causative for autosomal dominant forms of Parkinson's disease (A30P, A53T and E46K), and phosphorylation mutants at serine 129 (S129A and S129D) using fluorescently labelled alpha-synuclein, actin and tau. The investigation of colocalizafion, and protein-protein interactions by Forster resonance energy transfer and fluorescence lifetime imaging showed that alpha-synuclein associates with the actin cytoskeleton and interacts with tau. The A30P mutation and cytoskeletal destabilization decreased this interaction. Given the concurrent loss of membrane binding by this mutation, we propose a membrane- bound functional complex with tau that might involve the actin cytoskeleton. (c) 2007 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.nbd.2007.01.014"],["dc.identifier.gro","3143496"],["dc.identifier.isi","000247146400003"],["dc.identifier.pmid","17408955"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1017"],["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","0969-9961"],["dc.title","Alpha-synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeleton"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["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","1"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Molecular Neuroscience"],["dc.bibliographiccitation.lastpage","8"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Dohm, Christoph P."],["dc.contributor.author","Siedenberg, Sandra"],["dc.contributor.author","Liman, Jan"],["dc.contributor.author","Esposito, Alessandro"],["dc.contributor.author","Wouters, Fred S."],["dc.contributor.author","Reed, John C."],["dc.contributor.author","Bähr, Mathias"],["dc.contributor.author","Kermer, Pawel"],["dc.date.accessioned","2017-09-07T11:53:38Z"],["dc.date.available","2017-09-07T11:53:38Z"],["dc.date.issued","2006"],["dc.description.abstract","Bax ihibitor-1 (BI-1) has been characterized as an inhibitor of Bax-induced cell death in plants and various mammalian cell systems. To explore the function of BI-1 in neurons, we overexpressed BI-1 tagged to HA or GFP in rat nigral CSM14.1 and human SH-SY5Y neuroblastoma cells. Stable BI-1 expression proved marked protection from cell death induced by thapsigargine, a stress agent blocking the Call-ATPase of the endoplasmic reticulum (ER) but failed to inhibit cell death induced by staurosporine, a kinase inhibitor initiating mitochondria-dependent apoptosis. Moreover, BI-1 was neuroprotective in a paradigm mimicking ischemia, namely oxygen-glucose as well as serum deprivation. Examination of the subcellular distribution revealed that BI-1 predominantly locates to the ER and nuclear envelope but not mitochondria. Taken together, BI-1 overexpression in the ER is protective in neurons, making BI-1 an interesting target for future studies aiming at the inhibition of neuronal cell death during neurodegenerative diseases and stroke."],["dc.identifier.doi","10.1385/JMN:29:1:1"],["dc.identifier.gro","3143760"],["dc.identifier.isi","000237933400001"],["dc.identifier.pmid","16757804"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1309"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: NCI NIH HHS [CA67329]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0895-8696"],["dc.title","Bax inhibitor-1 protects neurons from oxygen-glucose deprivation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13115"],["dc.bibliographiccitation.issue","49"],["dc.bibliographiccitation.journal","Biochemistry"],["dc.bibliographiccitation.lastpage","13126"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Esposito, Alessandro"],["dc.contributor.author","Gralle, Matthias"],["dc.contributor.author","Dani, Maria Angela C."],["dc.contributor.author","Lange, Dirk"],["dc.contributor.author","Wouters, Fred S."],["dc.date.accessioned","2018-11-07T11:08:03Z"],["dc.date.available","2018-11-07T11:08:03Z"],["dc.date.issued","2008"],["dc.description.abstract","Intracellular pH is an important indicator for cellular metabolism and pathogenesis. pH sensing in living cells has been achieved using a number of synthetic organic dyes and genetically expressible sensor proteins, even allowing the specific targeting of intracellular organelles. Ideally, a class of genetically encodeable sensors need to cover relevant cellular pH ranges. We present a FRET-based pH sensor platform, based on the pH modulation of YFP acceptor fluorophores in a fusion construct with ECFP. The concurrent loss of the overlap integral upon acidification results in a proportionally reduced FRET coupling. The readout of FRET over the sensitized YFP fluorescence lifetime yields a highly sensitive and robust pH measurement that is self-calibrated. The principle is demonstrated in the existing high-efficiency FRET fusion Cyl 1.5, and tunability of the platform design is demonstrated by genetic alteration of the pH sensitivity of the acceptor moiety."],["dc.identifier.doi","10.1021/bi8009482"],["dc.identifier.isi","000261335400020"],["dc.identifier.pmid","19007185"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52703"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","0006-2960"],["dc.title","pHlameleons: A Family of FRET-Based Protein Sensors for Quantitative pH Imaging"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Henschel, Volker"],["dc.contributor.author","Esposito, Alessandro"],["dc.contributor.author","Butkevich, Eugenia"],["dc.contributor.author","Schmidt, Christoph F."],["dc.contributor.author","Wouters, Fred S."],["dc.contributor.author","Klopfenstein, Dieter Robert"],["dc.date.accessioned","2018-11-07T08:53:35Z"],["dc.date.available","2018-11-07T08:53:35Z"],["dc.date.issued","2011"],["dc.format.extent","150"],["dc.identifier.isi","000293637300385"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22451"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.eventlocation","Budapest, HUNGARY"],["dc.relation.issn","0175-7571"],["dc.title","Detecting protein conformational states in C. elegans in vivo by confocal fluorescence anisotropy"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","HFSP JOURNAL"],["dc.bibliographiccitation.lastpage","11"],["dc.bibliographiccitation.volume","2"],["dc.contributor.author","Wouters, Fred S."],["dc.contributor.author","Esposito, Alessandro"],["dc.date.accessioned","2018-11-07T11:18:35Z"],["dc.date.available","2018-11-07T11:18:35Z"],["dc.date.issued","2008"],["dc.description.abstract","Fluorescence lifetime imaging is a valuable and versatile tool for the investigation of the molecular environment of fluorophores in living cells. It is ideally suited and is therefore increasingly used-for the quantification of the occurrence of Forster Resonance Energy Transfer, a powerful microscopy method for the detection of subnanometer conformational changes, protein-protein interactions, and protein biochemical status. However, careful quantitative analysis is required for the correct and meaningful interpretation of fluorescence lifetime data. This can be a daunting task to the nonexpert user, and is the source for many avoidable errors and unsound interpretations. Digman and colleagues, Digman et al., 2007, Biophys. J. 94, L14-6. present an analysis technique that avoids data fitting in favor of a simple graphical polar data representation. In this \"phasor\" space, the physics of lifetime imaging becomes more intuitive and accessible also to the inexperienced user. The cumulated information from image pixels, even over different cells, describes patterns and trajectories that can be visually interpreted in physically meaningful ways. Its usefulness is demonstrated in the study of the dimerization of the uPAR receptor (Caiolfa et al., 2007, J. Cell Biol. 179, 1067-1082)."],["dc.identifier.doi","10.2976/1.2833600"],["dc.identifier.isi","000258367100002"],["dc.identifier.pmid","19404448"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55073"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Hfsp Publishing"],["dc.relation.issn","1955-2068"],["dc.title","Quantitative analysis of fluorescence lifetime imaging made easy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","19605"],["dc.bibliographiccitation.issue","46"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","19610"],["dc.bibliographiccitation.volume","106"],["dc.contributor.author","Wagner, Oliver"],["dc.contributor.author","Esposito, Alessandro"],["dc.contributor.author","Koehler, Barbara"],["dc.contributor.author","Chen, Chih-Wei"],["dc.contributor.author","Shen, Che-Piao"],["dc.contributor.author","Wu, Gong-Her"],["dc.contributor.author","Butkevich, Eugenia"],["dc.contributor.author","Mandalapu, Sailaja"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Wouters, Fred S."],["dc.contributor.author","Klopfenstein, Dieter Robert"],["dc.date.accessioned","2018-11-07T11:22:00Z"],["dc.date.available","2018-11-07T11:22:00Z"],["dc.date.issued","2009"],["dc.description.abstract","Kinesin-3 motor UNC-104/KIF1A is essential for transporting synaptic precursors to synapses. Although the mechanism of cargo binding is well understood, little is known how motor activity is regulated. We mapped functional interaction domains between SYD-2 and UNC-104 by using yeast 2-hybrid and pull-down assays and by using FRET/fluorescence lifetime imaging microscopy to image the binding of SYD-2 to UNC-104 in living Caenorhabditis elegans. We found that UNC-104 forms SYD-2-dependent axonal clusters (appearing during the transition from L2 to L3 larval stages), which behave in FRAP experiments as dynamic aggregates. High-resolution microscopy reveals that these clusters contain UNC-104 and synaptic precursors (synaptobrevin-1). Analysis of motor motility indicates bi-directional movement of UNC-104, whereas in syd-2 mutants, loss of SYD-2 binding reduces net anterograde movement and velocity (similar after deleting UNC-104's liprin-binding domain), switching to retrograde transport characteristics when no role of SYD-2 on dynein and conventional kinesin UNC-116 motility was found. These data present a kinesin scaffolding protein that controls both motor clustering along axons and motor motility, resulting in reduced cargo transport efficiency upon loss of interaction."],["dc.identifier.doi","10.1073/pnas.0902949106"],["dc.identifier.isi","000271907400068"],["dc.identifier.pmid","19880746"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55905"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Synaptic scaffolding protein SYD-2 clusters and activates kinesin-3 UNC-104 in C. elegans"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Neural Transmission"],["dc.bibliographiccitation.volume","114"],["dc.contributor.author","Dohm, C. P."],["dc.contributor.author","Esposito, Alessandro"],["dc.contributor.author","Liman, Jan"],["dc.contributor.author","Reed, J. C."],["dc.contributor.author","Wouters, Fred S."],["dc.contributor.author","Baehr, M."],["dc.contributor.author","Kermer, Pawel"],["dc.date.accessioned","2018-11-07T11:04:36Z"],["dc.date.available","2018-11-07T11:04:36Z"],["dc.date.issued","2007"],["dc.format.extent","X"],["dc.identifier.isi","000244485200047"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/51879"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Wien"],["dc.relation.conference","5th Congress Deutsche-Parkinson-Gesellschaft"],["dc.relation.eventlocation","Ulm, GERMANY"],["dc.relation.issn","0300-9564"],["dc.title","Molecular mechanisms and neuroprotection in cellular models of Parkinson's disease"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]