Pangršič Vilfan, Tina

[["dc.bibliographiccitation.firstpage","411"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Nature Neuroscience"],["dc.bibliographiccitation.lastpage","413"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Nouvian, Régis"],["dc.contributor.author","Neef, Jakob"],["dc.contributor.author","Bulankina, Anna V"],["dc.contributor.author","Reisinger, Ellen"],["dc.contributor.author","Pangršič, Tina"],["dc.contributor.author","Frank, Thomas"],["dc.contributor.author","Sikorra, Stefan"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Binz, Thomas"],["dc.contributor.author","Moser, Tobias"],["dc.date.accessioned","2017-09-07T11:44:19Z"],["dc.date.available","2017-09-07T11:44:19Z"],["dc.date.issued","2011"],["dc.description.abstract","SNARE proteins mediate membrane fusion. Neurosecretion depends on neuronal soluble NSF attachment protein receptors ( SNAREs; SNAP-25, syntaxin-1, and synaptobrevin-1 or synaptobrevin-2) and is blocked by neurotoxin-mediated cleavage or genetic ablation. We found that exocytosis in mouse inner hair cells (IHCs) was insensitive to neurotoxins and genetic ablation of neuronal SNAREs. mRNA, but no synaptically localized protein, of neuronal SNAREs was present in IHCs. Thus, IHC exocytosis is unconventional and may operate independently of neuronal SNAREs."],["dc.identifier.doi","10.1038/nn.2774"],["dc.identifier.gro","3142757"],["dc.identifier.isi","000288849400007"],["dc.identifier.pmid","21378973"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/196"],["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","1097-6256"],["dc.title","Exocytosis at the hair cell ribbon synapse apparently operates without neuronal SNARE proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","671"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Trends in Neurosciences"],["dc.bibliographiccitation.lastpage","680"],["dc.bibliographiccitation.volume","35"],["dc.contributor.author","Pangršič, Tina"],["dc.contributor.author","Reisinger, Ellen"],["dc.contributor.author","Moser, Tobias"],["dc.date.accessioned","2017-09-07T11:48:22Z"],["dc.date.available","2017-09-07T11:48:22Z"],["dc.date.issued","2012"],["dc.description.abstract","Sound is encoded at synapses between cochlear inner hair cells and the auditory nerve. These synapses are anatomically and functionally specialized to transmit acoustic information with high fidelity over a lifetime. The molecular mechanisms of hair-cell transmitter release have recently attracted substantial interest. Here we review progress toward understanding otoferlin, a multi-C-2 domain protein identified a decade ago by genetic analysis of human deafness. Otoferlin functions in hair-cell exocytosis. Several otoferlin C-2 domains bind to Ca2+, phospholipids, and proteins. Current research reveals requirements for otoferlin in priming and fusion of synaptic vesicles during sound encoding. Understanding the molecular mechanisms through which otoferlin functions also has important implications for understanding the disease mechanisms that lead to deafness."],["dc.identifier.doi","10.1016/j.tins.2012.08.002"],["dc.identifier.gro","3142445"],["dc.identifier.isi","000311177000003"],["dc.identifier.pmid","22959777"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8363"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Elsevier Science London"],["dc.relation.issn","0166-2236"],["dc.title","Otoferlin: a multi-C-2 domain protein essential for hearing"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","102"],["dc.contributor.author","Pangrsic, Tina"],["dc.contributor.author","Strenzke, Nicola"],["dc.contributor.author","Schwaller, Beat"],["dc.contributor.author","Moser, Tobias"],["dc.date.accessioned","2018-11-07T09:14:14Z"],["dc.date.available","2018-11-07T09:14:14Z"],["dc.date.issued","2012"],["dc.format.extent","319A"],["dc.identifier.doi","10.1016/j.bpj.2011.11.1752"],["dc.identifier.isi","000321561202199"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27359"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.eventlocation","San Diego, CA"],["dc.relation.issn","0006-3495"],["dc.title","The Role of Mobile Calcium Buffers in Synaptic Transmission at the Inner Hair Cell Ribbon Synapse"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","247"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","264"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Wong, Aaron B."],["dc.contributor.author","Rutherford, Mark A."],["dc.contributor.author","Gabrielaitis, Mantas"],["dc.contributor.author","Pangršič, Tina"],["dc.contributor.author","Göttfert, Fabian"],["dc.contributor.author","Frank, Thomas"],["dc.contributor.author","Michanski, Susann"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Wolf, Fred"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Moser, Tobias"],["dc.date.accessioned","2017-09-07T11:46:33Z"],["dc.date.available","2017-09-07T11:46:33Z"],["dc.date.issued","2014"],["dc.description.abstract","Cochlear inner hair cells (IHCs) develop from pre-sensory pacemaker to sound transducer. Here, we report that this involves changes in structure and function of the ribbon synapses between IHCs and spiral ganglion neurons (SGNs) around hearing onset in mice. As synapses matured they changed from holding several small presynaptic active zones (AZs) and apposed postsynaptic densities (PSDs) to one large AZ/PSD complex per SGN bouton. After the onset of hearing (i) IHCs had fewer and larger ribbons; (ii) Ca(V)1.3 channels formed stripe-like clusters rather than the smaller and round clusters at immature AZs; (iii) extrasynaptic Ca(V)1.3-channels were selectively reduced, (iv) the intrinsic Ca2+ dependence of fast exocytosis probed by Ca2+ uncaging remained unchanged but (v) the apparent Ca2+ dependence of exocytosis linearized, when assessed by progressive dihydropyridine block of Ca2+ influx. Biophysical modeling of exocytosis at mature and immature AZ topographies suggests that Ca2+ influx through an individual channel dominates the [Ca2+] driving exocytosis at each mature release site. We conclude that IHC synapses undergo major developmental refinements, resulting in tighter spatial coupling between Ca2+ influx and exocytosis."],["dc.identifier.doi","10.1002/embj.201387110"],["dc.identifier.gro","3142187"],["dc.identifier.isi","000331394400008"],["dc.identifier.pmid","24442635"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5499"],["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","Developmental refinement of hair cell synapses tightens the coupling of Ca2+ influx to exocytosis"],["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","4"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.lastpage","738"],["dc.bibliographiccitation.volume","68"],["dc.contributor.author","Frank, Thomas"],["dc.contributor.author","Rutherford, Mark A."],["dc.contributor.author","Strenzke, Nicola"],["dc.contributor.author","Neef, Andreas"],["dc.contributor.author","Pangrsic, Tina"],["dc.contributor.author","Khimich, Darina"],["dc.contributor.author","Fetjova, Anna"],["dc.contributor.author","Gundelfinger, Eckart D."],["dc.contributor.author","Liberman, M. Charles"],["dc.contributor.author","Harke, Benjamin"],["dc.contributor.author","Bryan, Keith E."],["dc.contributor.author","Lee, Amy"],["dc.contributor.author","Egner, Alexander"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Moser, Tobias"],["dc.date.accessioned","2017-09-07T11:45:13Z"],["dc.date.available","2017-09-07T11:45:13Z"],["dc.date.issued","2010"],["dc.description.abstract","At the presynaptic active zone, Ca2+ influx triggers fusion of synaptic vesicles. It is not well understood how Ca2+ channel clustering and synaptic vesicle docking are organized. Here, we studied structure and function of hair cell ribbon synapses following genetic disruption of the presynaptic scaffold protein Bassoon. Mutant synapses-mostly lacking the ribbon-showed a reduction in membrane-proximal vesicles, with ribbonless synapses affected more than ribbon-occupied synapses. Ca2+ channels were also fewer at mutant synapses and appeared in abnormally shaped clusters. Ribbon absence reduced Ca2+ channel numbers at mutant and wildtype synapses. Fast and sustained exocytosis was reduced, notwithstanding normal coupling of the remaining Ca2+ channels to exocytosis. In vitro recordings revealed a slight impairment of vesicle replenishment. Mechanistic modeling of the in vivo data independently supported morphological and functional in vitro findings. We conclude that Bassoon and the ribbon (1) create a large number of release sites by organizing Ca2+ channels and vesicles, and (2) promote vesicle replenishment."],["dc.identifier.doi","10.1016/j.neuron.2010.10.027"],["dc.identifier.gro","3142827"],["dc.identifier.isi","000285079500011"],["dc.identifier.pmid","21092861"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/274"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Cell Press"],["dc.relation.issn","0896-6273"],["dc.title","Bassoon and the Synaptic Ribbon Organize Ca2+ Channels and Vesicles to Add Release Sites and Promote Refilling"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Jean, Philippe"],["dc.contributor.author","Anttonen, Tommi"],["dc.contributor.author","Michanski, Susann"],["dc.contributor.author","de Diego, Antonio M. G."],["dc.contributor.author","Steyer, Anna M."],["dc.contributor.author","Neef, Andreas"],["dc.contributor.author","Oestreicher, David"],["dc.contributor.author","Kroll, Jana"],["dc.contributor.author","Nardis, Christos"],["dc.contributor.author","Pangršič, Tina"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Ashmore, Jonathan"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Moser, Tobias"],["dc.date.accessioned","2021-04-14T08:25:48Z"],["dc.date.available","2021-04-14T08:25:48Z"],["dc.date.issued","2020"],["dc.description.abstract","Inner hair cells (IHCs) are the primary receptors for hearing. They are housed in the cochlea and convey sound information to the brain via synapses with the auditory nerve. IHCs have been thought to be electrically and metabolically independent from each other. We report that, upon developmental maturation, in mice 30% of the IHCs are electrochemically coupled in ‘mini-syncytia’. This coupling permits transfer of fluorescently-labeled metabolites and macromolecular tracers. The membrane capacitance, Ca2+-current, and resting current increase with the number of dye-coupled IHCs. Dual voltage-clamp experiments substantiate low resistance electrical coupling. Pharmacology and tracer permeability rule out coupling by gap junctions and purinoceptors. 3D electron microscopy indicates instead that IHCs are coupled by membrane fusion sites. Consequently, depolarization of one IHC triggers presynaptic Ca2+-influx at active zones in the entire mini-syncytium. Based on our findings and modeling, we propose that IHC-mini-syncytia enhance sensitivity and reliability of cochlear sound encoding."],["dc.identifier.doi","10.1038/s41467-020-17003-z"],["dc.identifier.pmid","32587250"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81736"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/383"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","2041-1723"],["dc.relation.workinggroup","RG Moser (Molecular Anatomy, Physiology and Pathology of Sound Encoding)"],["dc.relation.workinggroup","RG Möbius"],["dc.relation.workinggroup","RG Pangršič Vilfan (Experimental Otology)"],["dc.relation.workinggroup","RG Wichmann (Molecular Architecture of Synapses)"],["dc.rights","CC BY 4.0"],["dc.title","Macromolecular and electrical coupling between inner hair cells in the rodent cochlea"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","The Journal of Physiological Sciences"],["dc.bibliographiccitation.volume","59"],["dc.contributor.author","Moser, Tobias"],["dc.contributor.author","Frank, Thomas"],["dc.contributor.author","Pangsric, Tina"],["dc.contributor.author","Neef, Jakob"],["dc.contributor.author","Brandt, Andreas"],["dc.contributor.author","Meyer, Alexander C."],["dc.contributor.author","Egner, Alexander"],["dc.contributor.author","Striessnig, Joerg"],["dc.contributor.author","Gregg, Ronald R."],["dc.contributor.author","Petit, Christine"],["dc.contributor.author","Schwaller, Beat"],["dc.contributor.author","Khimich, Darina"],["dc.date.accessioned","2018-11-07T08:34:55Z"],["dc.date.available","2018-11-07T08:34:55Z"],["dc.date.issued","2009"],["dc.format.extent","30"],["dc.identifier.isi","000271023100099"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17937"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Tokyo"],["dc.relation.issn","1880-6546"],["dc.title","Molecular Physiology Of The Hair Cell Ribbon Synapse"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.contributor.author","Chakrabarti, Rituparna"],["dc.contributor.author","Jaime Tobon, Lina Maria"],["dc.contributor.author","Slitin, Loujin"],["dc.contributor.author","Redondo-Canales, Magdalena"],["dc.contributor.author","Hoch, Gerhard"],["dc.contributor.author","Slashcheva, Marina"],["dc.contributor.author","Fritsch, Elisabeth"],["dc.contributor.author","Bodensiek, Kai"],["dc.contributor.author","Özçete, Özge Demet"],["dc.contributor.author","Gültas, Mehmet"],["dc.contributor.author","Michanski, Susann"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Neef, Jakob"],["dc.contributor.author","Pangrsic, Tina"],["dc.contributor.author","Moser, Tobias"],["dc.contributor.author","Wichmann, Carolin"],["dc.date.accessioned","2022-08-24T05:56:10Z"],["dc.date.available","2022-08-24T05:56:10Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1101/2022.05.10.491334"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113153"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/483"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/164"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | Z04: Quantitative Visualisierung und Analyse synaptischer Proteine mit Hilfe von Nanobodies"],["dc.relation.workinggroup","RG Moser (Molecular Anatomy, Physiology and Pathology of Sound Encoding)"],["dc.relation.workinggroup","RG Pangršič Vilfan (Experimental Otology)"],["dc.relation.workinggroup","RG Wichmann (Molecular Architecture of Synapses)"],["dc.title","Optogenetics and electron tomography for structure-function analysis of cochlear ribbon synapses"],["dc.type","preprint"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Molecular Neuroscience"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Oestreicher, David"],["dc.contributor.author","Picher, Maria Magdalena"],["dc.contributor.author","Rankovic, Vladan"],["dc.contributor.author","Moser, Tobias"],["dc.contributor.author","Pangrsic, Tina"],["dc.date.accessioned","2021-10-01T09:58:18Z"],["dc.date.available","2021-10-01T09:58:18Z"],["dc.date.issued","2021"],["dc.description.abstract","Clinical management of auditory synaptopathies like other genetic hearing disorders is currently limited to the use of hearing aids or cochlear implants. However, future gene therapy promises restoration of hearing in selected forms of monogenic hearing impairment, in which cochlear morphology is preserved over a time window that enables intervention. This includes non-syndromic autosomal recessive hearing impairment DFNB93, caused by defects in the CABP2 gene. Calcium-binding protein 2 (CaBP2) is a potent modulator of inner hair cell (IHC) voltage-gated calcium channels Ca V 1.3. Based on disease modeling in Cabp2 –/– mice, DFNB93 hearing impairment has been ascribed to enhanced steady-state inactivation of IHC Ca V 1.3 channels, effectively limiting their availability to trigger synaptic transmission. This, however, does not seem to interfere with cochlear development and does not cause early degeneration of hair cells or their synapses. Here, we studied the potential of a gene therapeutic approach for the treatment of DFNB93. We used AAV2/1 and AAV-PHP.eB viral vectors to deliver the Cabp2 coding sequence into IHCs of early postnatal Cabp2 –/– mice and assessed the level of restoration of hair cell function and hearing. Combining in vitro and in vivo approaches, we observed high transduction efficiency, and restoration of IHC Ca V 1.3 function resulting in improved hearing of Cabp2 –/– mice. These preclinical results prove the feasibility of DFNB93 gene therapy."],["dc.description.abstract","Clinical management of auditory synaptopathies like other genetic hearing disorders is currently limited to the use of hearing aids or cochlear implants. However, future gene therapy promises restoration of hearing in selected forms of monogenic hearing impairment, in which cochlear morphology is preserved over a time window that enables intervention. This includes non-syndromic autosomal recessive hearing impairment DFNB93, caused by defects in the CABP2 gene. Calcium-binding protein 2 (CaBP2) is a potent modulator of inner hair cell (IHC) voltage-gated calcium channels Ca V 1.3. Based on disease modeling in Cabp2 –/– mice, DFNB93 hearing impairment has been ascribed to enhanced steady-state inactivation of IHC Ca V 1.3 channels, effectively limiting their availability to trigger synaptic transmission. This, however, does not seem to interfere with cochlear development and does not cause early degeneration of hair cells or their synapses. Here, we studied the potential of a gene therapeutic approach for the treatment of DFNB93. We used AAV2/1 and AAV-PHP.eB viral vectors to deliver the Cabp2 coding sequence into IHCs of early postnatal Cabp2 –/– mice and assessed the level of restoration of hair cell function and hearing. Combining in vitro and in vivo approaches, we observed high transduction efficiency, and restoration of IHC Ca V 1.3 function resulting in improved hearing of Cabp2 –/– mice. These preclinical results prove the feasibility of DFNB93 gene therapy."],["dc.identifier.doi","10.3389/fnmol.2021.689415"],["dc.identifier.pmid","34489639"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/90035"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/418"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-469"],["dc.publisher","Frontiers Media S.A."],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1662-5099"],["dc.relation.workinggroup","RG Moser (Molecular Anatomy, Physiology and Pathology of Sound Encoding)"],["dc.relation.workinggroup","RG Pangršič Vilfan (Experimental Otology)"],["dc.rights","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Cabp2-Gene Therapy Restores Inner Hair Cell Calcium Currents and Improves Hearing in a DFNB93 Mouse Model"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","6843"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","The Journal of neuroscience"],["dc.bibliographiccitation.lastpage","6848"],["dc.bibliographiccitation.volume","34"],["dc.contributor.author","Weiler, Simon"],["dc.contributor.author","Krinner, Stefanie"],["dc.contributor.author","Wong, Aaron B."],["dc.contributor.author","Moser, Tobias"],["dc.contributor.author","Pangršič, Tina"],["dc.date.accessioned","2017-09-07T11:46:15Z"],["dc.date.available","2017-09-07T11:46:15Z"],["dc.date.issued","2014"],["dc.description.abstract","Sound encoding is mediated by Ca2+ influx-evoked release of glutamate at the ribbon synapse of inner hair cells. Here we studied the role of ATP in this process focusing on Ca2+ current through Ca(V)1.3 channels and Ca2+ homeostasis in mouse inner hair cells. Patch-clamp recordings and Ca2+ imaging demonstrate that hydrolyzable ATP is essential to maintain synaptic Ca2+ influx in inner hair cells via fueling Ca2+-ATPases to avoid an increase in cytosolic [Ca2+] and subsequent Ca2+/calmodulin-dependent inactivation of Ca(V)1.3 channels."],["dc.identifier.doi","10.1523/JNEUROSCI.4990-13.2014"],["dc.identifier.gro","3142124"],["dc.identifier.isi","000336895000012"],["dc.identifier.pmid","24828638"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4811"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Soc Neuroscience"],["dc.relation.issn","0270-6474"],["dc.title","ATP Hydrolysis Is Critically Required for Function of Ca(V)1.3 Channels in Cochlear Inner Hair Cells via Fueling Ca2+ Clearance"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]