Wichmann, Carolin

[["dc.bibliographiccitation.firstpage","7742"],["dc.bibliographiccitation.issue","37"],["dc.bibliographiccitation.journal","The Journal of Neuroscience"],["dc.bibliographiccitation.lastpage","7767"],["dc.bibliographiccitation.volume","41"],["dc.contributor.author","Butola, Tanvi"],["dc.contributor.author","Alvanos, Theocharis"],["dc.contributor.author","Hintze, Anika"],["dc.contributor.author","Koppensteiner, Peter"],["dc.contributor.author","Kleindienst, David"],["dc.contributor.author","Shigemoto, Ryuichi"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Moser, Tobias"],["dc.date.accessioned","2022-02-22T14:54:23Z"],["dc.date.available","2022-02-22T14:54:23Z"],["dc.date.issued","2021"],["dc.description.abstract","Rab-interacting molecule (RIM)-binding protein 2 (BP2) is a multidomain protein of the presynaptic active zone (AZ). By binding to RIM, bassoon (Bsn), and voltage-gated Ca2+ channels (CaV), it is considered to be a central organizer of the topography of CaV and release sites of synaptic vesicles (SVs) at the AZ. Here, we used RIM-BP2 knock-out (KO) mice and their wild-type (WT) littermates of either sex to investigate the role of RIM-BP2 at the endbulb of Held synapse of auditory nerve fibers (ANFs) with bushy cells (BCs) of the cochlear nucleus, a fast relay of the auditory pathway with high release probability. Disruption of RIM-BP2 lowered release probability altering short-term plasticity and reduced evoked EPSCs. Analysis of SV pool dynamics during high-frequency train stimulation indicated a reduction of SVs with high release probability but an overall normal size of the readily releasable SV pool (RRP). The Ca2+-dependent fast component of SV replenishment after RRP depletion was slowed. Ultrastructural analysis by superresolution light and electron microscopy revealed an impaired topography of presynaptic CaV and a reduction of docked and membrane-proximal SVs at the AZ. We conclude that RIM-BP2 organizes the topography of CaV, and promotes SV tethering and docking. This way RIM-BP2 is critical for establishing a high initial release probability as required to reliably signal sound onset information that we found to be degraded in BCs of RIM-BP2-deficient mice in vivo SIGNIFICANCE STATEMENT Rab-interacting molecule (RIM)-binding proteins (BPs) are key organizers of the active zone (AZ). Using a multidisciplinary approach to the calyceal endbulb of Held synapse that transmits auditory information at rates of up to hundreds of Hertz with submillisecond precision we demonstrate a requirement for RIM-BP2 for normal auditory signaling. Endbulb synapses lacking RIM-BP2 show a reduced release probability despite normal whole-terminal Ca2+ influx and abundance of the key priming protein Munc13-1, a reduced rate of SV replenishment, as well as an altered topography of voltage-gated (CaV)2.1 Ca2+ channels, and fewer docked and membrane proximal synaptic vesicles (SVs). This hampers transmission of sound onset information likely affecting downstream neural computations such as of sound localization."],["dc.identifier.doi","10.1523/JNEUROSCI.0586-21.2021"],["dc.identifier.pmid","34353898"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/100192"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/382"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/147"],["dc.language.iso","en"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A04: Aktivitätsabhängige morphologische Veränderungen am Endkolben von Held-Synapsen"],["dc.relation","SFB 1286 | B05: Quantitative molekulare Physiologie aktiver Zonen in Calyx-Synapsen"],["dc.relation.eissn","1529-2401"],["dc.relation.issn","0270-6474"],["dc.relation.workinggroup","RG Moser (Molecular Anatomy, Physiology and Pathology of Sound Encoding)"],["dc.relation.workinggroup","RG Wichmann (Molecular Architecture of Synapses)"],["dc.title","RIM-Binding Protein 2 Organizes Ca2+ Channel Topography and Regulates Release Probability and Vesicle Replenishment at a Fast Central Synapse"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","8474"],["dc.bibliographiccitation.issue","25"],["dc.bibliographiccitation.journal","Journal of Neuroscience"],["dc.bibliographiccitation.lastpage","8487"],["dc.bibliographiccitation.volume","34"],["dc.contributor.author","Li, L."],["dc.contributor.author","Tian, X."],["dc.contributor.author","Zhu, M."],["dc.contributor.author","Bulgari, D."],["dc.contributor.author","Bohme, M. A."],["dc.contributor.author","Goettfert, F."],["dc.contributor.author","Wichmann, C."],["dc.contributor.author","Sigrist, S. J."],["dc.contributor.author","Levitan, E. S."],["dc.contributor.author","Wu, C."],["dc.date.accessioned","2022-03-01T11:44:14Z"],["dc.date.available","2022-03-01T11:44:14Z"],["dc.date.issued","2014"],["dc.identifier.doi","10.1523/JNEUROSCI.0409-14.2014"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/102967"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1529-2401"],["dc.relation.issn","0270-6474"],["dc.title","Drosophila Syd-1, Liprin- , and Protein Phosphatase 2A B' Subunit Wrd Function in a Linear Pathway to Prevent Ectopic Accumulation of Synaptic Materials in Distal Axons"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","95"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Cell and Tissue Research"],["dc.bibliographiccitation.lastpage","114"],["dc.bibliographiccitation.volume","361"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Moser, Tobias"],["dc.date.accessioned","2017-09-07T11:43:44Z"],["dc.date.available","2017-09-07T11:43:44Z"],["dc.date.issued","2015"],["dc.description.abstract","In the mammalian cochlea, sound is encoded at synapses between inner hair cells (IHCs) and type I spiral ganglion neurons (SGNs). Each SGN receives input from a single IHC ribbon-type active zone (AZ) and yet SGNs indefatigably spike up to hundreds of Hz to encode acoustic stimuli with submillisecond precision. Accumulating evidence indicates a highly specialized molecular composition and structure of the presynapse, adapted to suit these high functional demands. However, we are only beginning to understand key features such as stimulus-secretion coupling, exocytosis mechanisms, exo-endocytosis coupling, modes of endocytosis and vesicle reformation, as well as replenishment of the readily releasable pool. Relating structure and function has become an important avenue in addressing these points and has been applied to normal and genetically manipulated hair cell synapses. Here, we review some of the exciting new insights gained from recent studies of the molecular anatomy and physiology of IHC ribbon synapses."],["dc.identifier.doi","10.1007/s00441-014-2102-7"],["dc.identifier.gro","3141877"],["dc.identifier.isi","000357115200009"],["dc.identifier.pmid","25874597"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11594"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2067"],["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","Springer"],["dc.relation.eissn","1432-0878"],["dc.relation.issn","0302-766X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Relating structure and function of inner hair cell ribbon synapses"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","102282"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","iScience"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Hintze, Anika"],["dc.contributor.author","Gültas, Mehmet"],["dc.contributor.author","Semmelhack, Esther A."],["dc.contributor.author","Wichmann, Carolin"],["dc.date.accessioned","2021-06-01T09:41:21Z"],["dc.date.available","2021-06-01T09:41:21Z"],["dc.date.issued","2021"],["dc.description.abstract","Endbulbs of Held are located in the anteroventral cochlear nucleus and present the first central synapses of the auditory pathway. During development, endbulbs mature functionally to enable rapid and powerful synaptic transmission with high temporal precision. This process is accompanied by morphological changes of endbulb terminals. Loss of the hair cell-specific protein otoferlin (Otof) abolishes neurotransmission in the cochlea and results in the smaller endbulb of Held terminals. Thus, peripheral hearing impairment likely also leads to alterations in the morphological synaptic vesicle (SV) pool size at individual endbulb of Held active zones (AZs). Here, we investigated endbulb AZs in pre-hearing, young, and adult wild-type and Otof−/− mice. During maturation, SV numbers at endbulb AZs increased in wild-type mice but were found to be reduced in Otof−/− mice. The SV population at a distance of 0–15 nm was most strongly affected. Finally, overall SV diameters decreased in Otof−/− animals during maturation."],["dc.identifier.doi","10.1016/j.isci.2021.102282"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/84891"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/112"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A04: Aktivitätsabhängige morphologische Veränderungen am Endkolben von Held-Synapsen"],["dc.relation.issn","2589-0042"],["dc.relation.workinggroup","RG Wichmann (Molecular Architecture of Synapses)"],["dc.rights","CC BY-NC-ND 4.0"],["dc.title","Ultrastructural maturation of the endbulb of Held active zones comparing wild-type and otoferlin-deficient mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","jcs236737"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.volume","133"],["dc.contributor.author","Kroll, Jana"],["dc.contributor.author","Özçete, Özge Demet"],["dc.contributor.author","Jung, Sangyong"],["dc.contributor.author","Maritzen, Tanja"],["dc.contributor.author","Milosevic, Ira"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Moser, Tobias"],["dc.date.accessioned","2020-12-10T18:41:54Z"],["dc.date.available","2020-12-10T18:41:54Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1242/jcs.236737"],["dc.identifier.eissn","1477-9137"],["dc.identifier.issn","0021-9533"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77721"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","AP180 promotes release site clearance and clathrin-dependent vesicle reformation in mouse cochlear inner hair cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","2147"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","20"],["dc.contributor.affiliation","Chakrabarti, Rituparna; \t\t \r\n\t\t Molecular Architecture of Synapses Group, Institute for Auditory Neuroscience and InnerEarLab, University Medical Center Göttingen, 37075 Göttingen, Germany, rituparna.chakrabarti@med.uni-goettingen.de\t\t \r\n\t\t Center for Biostructural Imaging of Neurodegeneration, University Medical Center Göttingen, 37075 Göttingen, Germany, rituparna.chakrabarti@med.uni-goettingen.de\t\t \r\n\t\t Collaborative Research Center 889 “Cellular Mechanisms of Sensory Processing”, 37099 Göttingen, Germany, rituparna.chakrabarti@med.uni-goettingen.de"],["dc.contributor.affiliation","Wichmann, Carolin; \t\t \r\n\t\t Molecular Architecture of Synapses Group, Institute for Auditory Neuroscience and InnerEarLab, University Medical Center Göttingen, 37075 Göttingen, Germany, carolin.wichmann@med.uni-goettingen.de\t\t \r\n\t\t Center for Biostructural Imaging of Neurodegeneration, University Medical Center Göttingen, 37075 Göttingen, Germany, carolin.wichmann@med.uni-goettingen.de\t\t \r\n\t\t Collaborative Research Center 889 “Cellular Mechanisms of Sensory Processing”, 37099 Göttingen, Germany, carolin.wichmann@med.uni-goettingen.de\t\t \r\n\t\t Collaborative Research Center 1286 “Quantitative Synaptology”, 37099 Göttingen, Germany, carolin.wichmann@med.uni-goettingen.de\t\t \r\n\t\t Auditory Neuroscience Group, Max Planck Institute for Experimental Medicine, 37075 Göttingen, Germany, carolin.wichmann@med.uni-goettingen.de"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Chakrabarti, Rituparna"],["dc.date.accessioned","2019-07-09T11:51:18Z"],["dc.date.available","2019-07-09T11:51:18Z"],["dc.date.issued","2019"],["dc.date.updated","2022-09-06T05:26:16Z"],["dc.description.abstract","A critical aim in neuroscience is to obtain a comprehensive view of how regulated neurotransmission is achieved. Our current understanding of synapses relies mainly on data from electrophysiological recordings, imaging, and molecular biology. Based on these methodologies, proteins involved in a synaptic vesicle (SV) formation, mobility, and fusion at the active zone (AZ) membrane have been identified. In the last decade, electron tomography (ET) combined with a rapid freezing immobilization of neuronal samples opened a window for understanding the structural machinery with the highest spatial resolution in situ. ET provides significant insights into the molecular architecture of the AZ and the organelles within the presynaptic nerve terminal. The specialized sensory ribbon synapses exhibit a distinct architecture from neuronal synapses due to the presence of the electron-dense synaptic ribbon. However, both synapse types share the filamentous structures, also commonly termed as tethers that are proposed to contribute to different steps of SV recruitment and exocytosis. In this review, we discuss the emerging views on the role of filamentous structures in SV exocytosis gained from ultrastructural studies of excitatory, mainly central neuronal compared to ribbon-type synapses with a focus on inner hair cell (IHC) ribbon synapses. Moreover, we will speculate on the molecular entities that may be involved in filament formation and hence play a crucial role in the SV cycle."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft"],["dc.identifier.doi","10.3390/ijms20092147"],["dc.identifier.pmid","31052288"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16099"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59921"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/29"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A04: Aktivitätsabhängige morphologische Veränderungen am Endkolben von Held-Synapsen"],["dc.relation.eissn","1422-0067"],["dc.relation.workinggroup","RG Wichmann (Molecular Architecture of Synapses)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","Nanomachinery Organizing Release at Neuronal and Ribbon Synapses"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2686"],["dc.bibliographiccitation.issue","21"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","2702"],["dc.bibliographiccitation.volume","34"],["dc.contributor.author","Jung, SangYong"],["dc.contributor.author","Maritzen, Tanja"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Jing, Zhizi"],["dc.contributor.author","Neef, Andreas"],["dc.contributor.author","Revelo, Natalia H."],["dc.contributor.author","Al-Moyed, Hanan"],["dc.contributor.author","Meese, Sandra"],["dc.contributor.author","Wojcik, Sonja M."],["dc.contributor.author","Panou, Iliana"],["dc.contributor.author","Bulut, Haydar"],["dc.contributor.author","Schu, Peter"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Reisinger, Ellen"],["dc.contributor.author","Rizzoli, Silvio"],["dc.contributor.author","Neef, Jakob"],["dc.contributor.author","Strenzke, Nicola"],["dc.contributor.author","Haucke, Volker"],["dc.contributor.author","Moser, Tobias"],["dc.date.accessioned","2017-09-07T11:54:53Z"],["dc.date.available","2017-09-07T11:54:53Z"],["dc.date.issued","2015"],["dc.description.abstract","Active zones (AZs) of inner hair cells (IHCs) indefatigably release hundreds of vesicles per second, requiring each release site to reload vesicles at tens per second. Here, we report that the endocytic adaptor protein 2 (AP-2) is required for release site replenishment and hearing. We show that hair cell-specific disruption of AP-2 slows IHC exocytosis immediately after fusion of the readily releasable pool of vesicles, despite normal abundance of membrane-proximal vesicles and intact endocytic membrane retrieval. Sound-driven postsynaptic spiking was reduced in a use-dependent manner, and the altered interspike interval statistics suggested a slowed reloading of release sites. Sustained strong stimulation led to accumulation of endosome-like vacuoles, fewer clathrin-coated endocytic intermediates, andvesicle depletion of the membrane-distal synaptic ribbon in AP-2-deficient IHCs, indicating a further role of AP-2 in clathrin-dependent vesicle reformation on a timescale of many seconds. Finally, we show that AP-2 sorts its IHC-cargo otoferlin. We propose that binding of AP-2 to otoferlin facilitates replenishment of release sites, for example, via speeding AZ clearance of exocytosed material, in addition to a role of AP-2 in synaptic vesicle reformation."],["dc.identifier.doi","10.15252/embj.201591885"],["dc.identifier.gro","3141791"],["dc.identifier.isi","000364337100008"],["dc.identifier.pmid","26446278"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1112"],["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","1460-2075"],["dc.relation.issn","0261-4189"],["dc.title","Disruption of adaptor protein 2μ (AP‐2μ) in cochlear hair cells impairs vesicle reloading of synaptic release sites and hearing"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","724"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.lastpage","738"],["dc.bibliographiccitation.volume","66"],["dc.contributor.author","Banovic, Daniel"],["dc.contributor.author","Khorramshahi, Omid"],["dc.contributor.author","Owald, David"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Riedt, Tamara"],["dc.contributor.author","Fouquet, Wernher"],["dc.contributor.author","Tian, Rui"],["dc.contributor.author","Sigrist, Stephan J."],["dc.contributor.author","Aberle, Hermann"],["dc.date.accessioned","2022-03-01T11:45:20Z"],["dc.date.available","2022-03-01T11:45:20Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.1016/j.neuron.2010.05.020"],["dc.identifier.pii","S0896627310004162"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103292"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0896-6273"],["dc.title","Drosophila Neuroligin 1 Promotes Growth and Postsynaptic Differentiation at Glutamatergic Neuromuscular Junctions"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","843"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","855"],["dc.bibliographiccitation.volume","177"],["dc.contributor.author","Besse, Florence"],["dc.contributor.author","Mertel, Sara"],["dc.contributor.author","Kittel, Robert J."],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Rasse, Tobias M."],["dc.contributor.author","Sigrist, Stephan J."],["dc.contributor.author","Ephrussi, Anne"],["dc.date.accessioned","2022-03-01T11:46:32Z"],["dc.date.available","2022-03-01T11:46:32Z"],["dc.date.issued","2007"],["dc.description.abstract","Synapses can undergo rapid changes in size as well as in their vesicle release function during both plasticity processes and development. This fundamental property of neuronal cells requires the coordinated rearrangement of synaptic membranes and their associated cytoskeleton, yet remarkably little is known of how this coupling is achieved. In a GFP exon-trap screen, we identified Drosophila melanogaster Basigin (Bsg) as an immunoglobulin domain-containing transmembrane protein accumulating at periactive zones of neuromuscular junctions. Bsg is required pre- and postsynaptically to restrict synaptic bouton size, its juxtamembrane cytoplasmic residues being important for that function. Bsg controls different aspects of synaptic structure, including distribution of synaptic vesicles and organization of the presynaptic cortical actin cytoskeleton. Strikingly, bsg function is also required specifically within the presynaptic terminal to inhibit nonsynchronized evoked vesicle release. We thus propose that Bsg is part of a transsynaptic complex regulating synaptic compartmentalization and strength, and coordinating plasma membrane and cortical organization."],["dc.description.abstract","Synapses can undergo rapid changes in size as well as in their vesicle release function during both plasticity processes and development. This fundamental property of neuronal cells requires the coordinated rearrangement of synaptic membranes and their associated cytoskeleton, yet remarkably little is known of how this coupling is achieved. In a GFP exon-trap screen, we identified Drosophila melanogaster Basigin (Bsg) as an immunoglobulin domain-containing transmembrane protein accumulating at periactive zones of neuromuscular junctions. Bsg is required pre- and postsynaptically to restrict synaptic bouton size, its juxtamembrane cytoplasmic residues being important for that function. Bsg controls different aspects of synaptic structure, including distribution of synaptic vesicles and organization of the presynaptic cortical actin cytoskeleton. Strikingly, bsg function is also required specifically within the presynaptic terminal to inhibit nonsynchronized evoked vesicle release. We thus propose that Bsg is part of a transsynaptic complex regulating synaptic compartmentalization and strength, and coordinating plasma membrane and cortical organization."],["dc.identifier.doi","10.1083/jcb.200701111"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103706"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1540-8140"],["dc.relation.issn","0021-9525"],["dc.title","The Ig cell adhesion molecule Basigin controls compartmentalization and vesicle release at Drosophila melanogaster synapses"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1104"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Biochemical and Biophysical Research Communications"],["dc.bibliographiccitation.lastpage","1110"],["dc.bibliographiccitation.volume","310"],["dc.contributor.author","Wichmann, C."],["dc.contributor.author","Naumann, P. T."],["dc.contributor.author","Spangenberg, O."],["dc.contributor.author","Konrad, M."],["dc.contributor.author","Mayer, F."],["dc.contributor.author","Hoppert, M."],["dc.date.accessioned","2018-11-07T10:35:20Z"],["dc.date.available","2018-11-07T10:35:20Z"],["dc.date.issued","2003"],["dc.description.abstract","Modular systems for protein coupling have been applied for anchoring enzyme molecules on liposome surfaces. Two cytoplasmic model enzymes, alpha-amylase from Escherichia coli (EC. 3.2. 1. 1) and guanylate kinase from Saccharomyces cerevisiae (EC. 2.7.4.8), were directly coupled by a histidine-tag or indirectly via strep-tag and streptavidin or streptactin linker to a liposome membrane. Though the catalytic properties of the enzymes are generally maintained, stability and specific activity of the enzymes are modified after coupling and are especially influenced by the lipid used for the liposome assembly. (C) 2003 Elsevier Inc."],["dc.identifier.doi","10.1016/j.bbrc.2003.09.128"],["dc.identifier.isi","000186146200011"],["dc.identifier.pmid","14559229"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45074"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","0006-291X"],["dc.title","Liposomes for microcompartmentation of enzymes and their influence on catalytic activity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]