Pardo, Luis A.

[["dc.bibliographiccitation.artnumber","e51825"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Valero, María Ll."],["dc.contributor.author","Mello de Queiroz, Fernanda"],["dc.contributor.author","Stühmer, Walter"],["dc.contributor.author","Viana, Félix"],["dc.contributor.author","Pardo, Luis A."],["dc.date.accessioned","2019-07-09T11:54:06Z"],["dc.date.available","2019-07-09T11:54:06Z"],["dc.date.issued","2012-12-14"],["dc.description.abstract","Overexpression of the cation-permeable channel TRPM8 in prostate cancers might represent a novel opportunity for their treatment. Inhibitors of TRPM8 reduce the growth of prostate cancer cells. We have used two recently described and highly specific blockers, AMTB and JNJ41876666, and RNAi to determine the relevance of TRPM8 expression in the proliferation of non-tumor and tumor cells. Inhibition of the expression or function of the channel reduces proliferation rates and proliferative fraction in all tumor cells tested, but not of non-tumor prostate cells. We observed no consistent acceleration of growth after stimulation of the channel with menthol or icilin, indicating that basal TRPM8 expression is enough to sustain growth of prostate cancer cells."],["dc.format.extent","12"],["dc.identifier.doi","10.1371/journal.pone.0051825"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8457"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60572"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","TRPM8 Ion Channels Differentially Modulate Proliferation and Cell Cycle Distribution of Normal and Cancer Prostate Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","1600253"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","BioEssays"],["dc.bibliographiccitation.volume","39"],["dc.contributor.author","Pedersen, Stine F."],["dc.contributor.author","Novak, Ivana"],["dc.contributor.author","Alves, Frauke"],["dc.contributor.author","Schwab, Albrecht"],["dc.contributor.author","Pardo, Luis A."],["dc.date.accessioned","2018-10-10T13:25:55Z"],["dc.date.available","2018-10-10T13:25:55Z"],["dc.date.issued","2017"],["dc.description.abstract","We present here the hypothesis that the unique microenvironmental pH landscape of acid-base transporting epithelia is an important factor in development of epithelial cancers, by rendering the epithelial and stromal cells pre-adapted to the heterogeneous extracellular pH (pHe ) in the tumor microenvironment. Cells residing in organs with net acid-base transporting epithelia such as the pancreatic ductal and gastric epithelia are exposed to very different, temporally highly variable pHe values apically and basolaterally. This translates into spatially and temporally non-uniform intracellular pH (pHi ) patterns. Disturbed pHe - and pHi -homeostasis contributes to essentially all hallmarks of cancer. Our hypothesis, that the physiological pHe microenvironment in acid-base secreting epithelia shapes cancers arising in these tissues, can be tested using novel imaging tools. The acidic tumor pHe in turn might be exploited therapeutically. Pancreatic cancers are used as our prime example, but we propose that this concept is also relevant for other cancers of acid-base transporting epithelia."],["dc.fs.pkfprnr","66887"],["dc.identifier.doi","10.1002/bies.201600253"],["dc.identifier.fs","631974"],["dc.identifier.pmid","28440551"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15964"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1521-1878"],["dc.title","Alternating pH landscapes shape epithelial cancer initiation and progression: Focus on pancreatic cancer"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Pharmacology"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Hartung, Franziska"],["dc.contributor.author","Krüwel, Thomas"],["dc.contributor.author","Shi, Xiaoyi"],["dc.contributor.author","Pfizenmaier, Klaus"],["dc.contributor.author","Kontermann, Roland"],["dc.contributor.author","Chames, Patrick"],["dc.contributor.author","Alves, Frauke"],["dc.contributor.author","Pardo, Luis A."],["dc.date.accessioned","2021-04-14T08:26:27Z"],["dc.date.available","2021-04-14T08:26:27Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.3389/fphar.2020.00686"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81946"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1663-9812"],["dc.title","A Novel Anti-Kv10.1 Nanobody Fused to Single-Chain TRAIL Enhances Apoptosis Induction in Cancer Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","589"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","American Journal Of Pathology"],["dc.bibliographiccitation.lastpage","598"],["dc.bibliographiccitation.volume","171"],["dc.contributor.author","Herrero-Herranz, Eva"],["dc.contributor.author","Pardo, Luis A."],["dc.contributor.author","Bunt, Gertrude"],["dc.contributor.author","Gold, Ralf"],["dc.contributor.author","Stühmer, Walter"],["dc.contributor.author","Linker, Ralf A."],["dc.date.accessioned","2018-11-07T10:59:44Z"],["dc.date.available","2018-11-07T10:59:44Z"],["dc.date.issued","2007"],["dc.description.abstract","Mechanisms of lesion repair in multiple sclerosis are incompletely understood. To some degree, remyelination can occur, associated with an increase of proliferating oligodendroglial cells. Recently, the expression of potassium channels has been implicated in the control of oligodendrocyte precursor cell proliferation in vitro. We investigated the expression of Kv1.4 potassium channels in myelin oligodendrocyte glycoprotein-induced experimental autoimmune encephalomyelitis, a model of multiple sclerosis. Confocal microscopy revealed expression of Kv1.4 in AN2-positive oligodendrocyte precursor cells and pre-myelinating oligodendrocytes in vitro but neither in mature oligodendrocytes nor in the spinal cords of healthy adult mice. After induction of myelin oligodendrocyte glycoprotein-induced experimental autoimmune encephalomyelitis, Kv1.4 immunoreactivity was detected in or around lesions already during disease onset with a peak early and a subsequent decrease in the late phase of the disease. Kv1.4 expression was confined to 2',3'-cyclic nucleotide 3'-phosphodiesterase-positive oligodendroglial cells, which were actively proliferating and ensheathed naked axons. After a demyelinating episode, the number of Kv1.4 and 2',3'-cyclic nucleotide 3'-phosphodiesterase double-positive cells was greatly reduced in ciliary neurotrophic factor knockout mice, a model with impaired lesion repair. in summary, the re-expression of an oligodendroglial potassium channel may have a functional implication on oligodendroglial cell cycle progression, thus influencing tissue repair in experimental autoimmune encephalomyelitis and multiple sclerosis."],["dc.identifier.doi","10.2353/ajpath.2007.061241"],["dc.identifier.isi","000248496300022"],["dc.identifier.pmid","17600124"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/50766"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","0002-9440"],["dc.title","Re-expression of a developmentally restricted potassium channel in autoimmune demyelination - Kv1.4 is implicated in oligodendroglial proliferation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","181"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","The Journal of Physiology"],["dc.bibliographiccitation.lastpage","196"],["dc.bibliographiccitation.volume","593"],["dc.contributor.author","Mortensen, Lena Sünke"],["dc.contributor.author","Schmidt, Hartmut"],["dc.contributor.author","Farsi, Zohreh"],["dc.contributor.author","Barrantes-Freer, Alonso"],["dc.contributor.author","Rubio, María E."],["dc.contributor.author","Ufartes, Roser"],["dc.contributor.author","Eilers, Jens"],["dc.contributor.author","Sakaba, Takeshi"],["dc.contributor.author","Stühmer, Walter"],["dc.contributor.author","Pardo, Luis A."],["dc.date.accessioned","2019-07-09T11:42:47Z"],["dc.date.available","2019-07-09T11:42:47Z"],["dc.date.issued","2014"],["dc.description.abstract","The voltage-gated potassium channel KV10.1 (Eag1) is widely expressed in the mammalian brain, but its physiological function is not yet understood. Previous studies revealed highest expression levels in hippocampus and cerebellumand suggested a synaptic localization of the channel. The distinct activation kinetics of KV10.1 indicate a role during repetitive activity of the cell.Here, we confirmthe synaptic localization of KV10.1 both biochemically and functionally and that the channel is sufficiently fast at physiological temperature to take part in repolarization of the action potential (AP).We studied the role of the channel in cerebellar physiology using patch clamp and two-photon Ca2+ imaging in KV10.1-deficient and wild-type mice. The excitability and action potential waveformrecorded at granule cell somata was unchanged, while Ca2+ influx into axonal boutons was enhanced in mutants in response to stimulation with three APs, but not after a single AP. Furthermore, mutants exhibited a frequency-dependent increase in facilitation at the parallel fibre–Purkinje cell synapse at high firing rates. We propose that KV10.1 acts as a modulator of local AP shape specifically during high-frequency burst firing when other potassium channels suffer cumulative inactivation."],["dc.identifier.doi","10.1113/jphysiol.2014.281600"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13714"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58742"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","0022-3751"],["dc.rights","CC BY-NC-ND 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/3.0"],["dc.title","KV 10.1 opposes activity-dependent increase in Ca2+ influx into the presynaptic terminal of the parallel fibre-Purkinje cell synapse"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","201"],["dc.bibliographiccitation.journal","Frontiers in physiology"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Herrmann, Solveig"],["dc.contributor.author","Ninkovic, Milena"],["dc.contributor.author","Kohl, Tobias"],["dc.contributor.author","Pardo, Luis A."],["dc.date.accessioned","2019-07-09T11:40:08Z"],["dc.date.available","2019-07-09T11:40:08Z"],["dc.date.issued","2013"],["dc.description.abstract","Although crucial for their correct function, the mechanisms controlling surface expression of ion channels are poorly understood. In the case of the voltage-gated potassium channel KV10.1, this is determinant not only for its physiological function in brain, but also for its pathophysiology in tumors and possible use as a therapeutic target. The Golgi resident protein PIST binds several membrane proteins, thereby modulating their expression. Here we describe a PDZ domain-mediated interaction of KV10.1 and PIST, which enhances surface levels of KV10.1. The functional, but not the physical interaction of both proteins is dependent on the coiled-coil and PDZ domains of PIST; insertion of eight amino acids in the coiled-coil domain to render the neural form of PIST (nPIST) and the corresponding short isoform in an as-of-yet unknown form abolishes the effect. In addition, two new isoforms of PIST (sPIST and nsPIST) lacking nearly the complete PDZ domain were cloned and shown to be ubiquitously expressed. PIST and KV10.1 co-precipitate from native and expression systems. nPIST also showed interaction, but did not alter the functional expression of the channel. We could not document physical interaction between KV10.1 and sPIST, but it reduced KV10.1 functional expression in a dominant-negative manner. nsPIST showed weak physical interaction and no functional effect on KV10.1. We propose these isoforms to work as modulators of PIST function via regulating the binding on interaction partners."],["dc.identifier.doi","10.3389/fphys.2013.00201"],["dc.identifier.fs","604131"],["dc.identifier.pmid","23966943"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10690"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58100"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1664-042X"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","PIST (GOPC) modulates the oncogenic voltage-gated potassium channel KV10.1."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","42"],["dc.bibliographiccitation.firstpage","42-1"],["dc.bibliographiccitation.journal","Molecular Cancer"],["dc.bibliographiccitation.lastpage","42-10"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Mello de Queiroz, Fernanda"],["dc.contributor.author","Suarez-Kurtz, Guilherme"],["dc.contributor.author","Stühmer, Walter"],["dc.contributor.author","Pardo, Luis A."],["dc.date.accessioned","2019-07-09T11:54:22Z"],["dc.date.available","2019-07-09T11:54:22Z"],["dc.date.issued","2006"],["dc.description.abstract","Background: The expression of the human Eag1 potassium channel (Kv10.1) is normally restricted to the adult brain, but it has been detected in both tumour cell lines and primary tumours. Our purpose was to determine the frequency of expression of Eag1 in soft tissue sarcoma and its potential clinical implications. Results: We used specific monoclonal antibodies to determine the expression levels of Eag1 in soft tissue sarcomas from 210 patients by immunohistochemistry. Eag1 was expressed in 71% of all tumours, with frequencies ranging from 56% (liposarcoma) to 82% (rhabdomyosarcoma). We detected differences in expression levels depending on the histological type, but no association was seen between expression of this protein and sex, age, grade or tumour size. Four cell lines derived from relevant sarcoma histological types (fibrosarcoma and rhabdomyosarcoma) were tested for Eag1 expression by real-time RT-PCR. We found all four lines to be positive for Eag1. In these cell lines, blockage of Eag1 by RNA interference led to a decrease in proliferation. Conclusion: Eag1 is aberrantly expressed in over 70% sarcomas. In sarcoma cell lines, inhibition of Eag1 expression and/or function leads to reduced proliferation. The high frequency of expression of Eag1 in primary tumours and the restriction of normal expression of the channel to the brain, suggests the application of this protein for diagnostic or therapeutic purposes."],["dc.identifier.doi","10.1186/1476-4598-5-42"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60643"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Ether à go-go potassium channel expression in soft tissue sarcoma patients"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e26329"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","PLOS ONE"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Kohl, Tobias"],["dc.contributor.author","Lörinczi, Eva"],["dc.contributor.author","Pardo, Luis A."],["dc.contributor.author","Stühmer, Walter"],["dc.date.accessioned","2018-11-07T08:50:44Z"],["dc.date.available","2018-11-07T08:50:44Z"],["dc.date.issued","2011"],["dc.description.abstract","K(V)10.1 is a mammalian brain voltage-gated potassium channel whose ectopic expression outside of the brain has been proven relevant for tumor biology. Promotion of cancer cell proliferation by K(V)10.1 depends largely on ion flow, but some oncogenic properties remain in the absence of ion permeation. Additionally, K(V)10.1 surface populations are small compared to large intracellular pools. Control of protein turnover within cells is key to both cellular plasticity and homeostasis, and therefore we set out to analyze how endocytic trafficking participates in controlling K(V)10.1 intracellular distribution and life cycle. To follow plasma membrane K(V)10.1 selectively, we generated a modified channel of displaying an extracellular affinity tag for surface labeling by alpha-bungarotoxin. This modification only minimally affected K(V)10.1 electrophysiological properties. Using a combination of microscopy and biochemistry techniques, we show that K(V)10.1 is constitutively internalized involving at least two distinct pathways of endocytosis and mainly sorted to lysosomes. This occurs at a relatively fast rate. Simultaneously, recycling seems to contribute to maintain basal K(V)10.1 surface levels. Brief K(V)10.1 surface half-life and rapid lysosomal targeting is a relevant factor to be taken into account for potential drug delivery and targeting strategies directed against K(V)10.1 on tumor cells."],["dc.identifier.doi","10.1371/journal.pone.0026329"],["dc.identifier.isi","000295976000098"],["dc.identifier.pmid","22022602"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8343"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21761"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","Najko"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","Rapid Internalization of the Oncogenic K+ Channel K(V)10.1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","721"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.lastpage","733"],["dc.bibliographiccitation.volume","45"],["dc.contributor.author","Napp, Joanna"],["dc.contributor.author","Pardo, Luis A."],["dc.contributor.author","Hartung, Franziska"],["dc.contributor.author","Tietze, Lutz Friedjan"],["dc.contributor.author","Stühmer, Walter"],["dc.contributor.author","Alves, Frauke"],["dc.date.accessioned","2018-11-07T10:07:59Z"],["dc.date.available","2018-11-07T10:07:59Z"],["dc.date.issued","2016"],["dc.description.abstract","The K(v)10.1 (Eag1) voltage-gated potassium channel represents a promising molecular target for novel cancer therapies or diagnostic purposes. Physiologically, it is only expressed in the brain, but it was found overexpressed in more than 70 % of tumours of diverse origin. Furthermore, as a plasma membrane protein, it is easily accessible to extracellular interventions. In this study we analysed the feasibility of the anti-K(v)10.1 monoclonal antibody mAb62 to target tumour cells in vitro and in vivo and to deliver therapeutics to the tumour. Using time-domain near infrared fluorescence (NIRF) imaging in a subcutaneous MDA-MB-435S tumour model in nude mice, we showed that mAb62-Cy5.5 specifically accumulates at the tumour for at least 1 week in vivo with a maximum intensity at 48 h. Blocking experiments with an excess of unlabelled mAb62 and application of the free Cy5.5 fluorophore demonstrate specific binding to the tumour. Ex vivo NIRF imaging of whole tumours as well as NIRF imaging and microscopy of tumour slices confirmed the accumulation of the mAb62-Cy5.5 in tumours but not in brain tissue. Moreover, mAb62 was conjugated to the prodrug-activating enzyme beta-D-galactosidase (beta-gal; mAb62-beta-gal). The beta-gal activity of the mAb62-beta-gal conjugate was analysed in vitro on K(v)10.1-expressing MDAMB-435S cells in comparison to control AsPC-1 cells. We show that the mAb62-beta-gal conjugate possesses high beta-gal activity when bound to K(v)10.1-expressing MDA-MB-435S cells. Moreover, using the beta-gal activatable NIRF probe DDAOG, we detected mAb62-beta-gal activity in vivo over the tumour area. In summary, we could show that the anti-K(v)10.1 antibody is a promising tool for the development of novel concepts of targeted cancer therapy."],["dc.identifier.doi","10.1007/s00249-016-1152-z"],["dc.identifier.isi","000384822200012"],["dc.identifier.pmid","27444284"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13779"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39387"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","Najko"],["dc.relation.issn","1432-1017"],["dc.relation.issn","0175-7571"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","In vivo imaging of tumour xenografts with an antibody targeting the potassium channel K(v)10.1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","309"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","EMBO Molecular Medicine"],["dc.bibliographiccitation.lastpage","319"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Grube, Sabrina"],["dc.contributor.author","Gerchen, Martin F."],["dc.contributor.author","Adamcio, Bartosz"],["dc.contributor.author","Pardo, Luis A."],["dc.contributor.author","Martin, Sabine"],["dc.contributor.author","Malzahn, Dörthe"],["dc.contributor.author","Papiol, Sergi"],["dc.contributor.author","Begemann, Martin"],["dc.contributor.author","Ribbe, Katja"],["dc.contributor.author","Friedrichs, Heidi"],["dc.contributor.author","Radyushkin, Konstantin A."],["dc.contributor.author","Müller, Michael"],["dc.contributor.author","Benseler, Fritz"],["dc.contributor.author","Riggert, Joachim"],["dc.contributor.author","Falkai, Peter"],["dc.contributor.author","Bickeböller, Heike"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Stühmer, Walter"],["dc.contributor.author","Ehrenreich, Hannelore"],["dc.date.accessioned","2017-09-07T11:44:13Z"],["dc.date.available","2017-09-07T11:44:13Z"],["dc.date.issued","2011"],["dc.description.abstract","KCNN3, encoding the small conductance calcium-activated potassium channel SK3, harbours a polymorphic CAG repeat in the amino-terminal coding region with yet unproven function. Hypothesizing that KCNN3 genotypes do not influence susceptibility to schizophrenia but modify its phenotype, we explored their contribution to specific schizophrenic symptoms. Using the Gottingen Research Association for Schizophrenia (GRAS) data collection of schizophrenic patients (n=1074), we performed a phenotype-based genetic association study (PGAS) of KCNN3. We show that long CAG repeats in the schizophrenic sample are specifically associated with better performance in higher cognitive tasks, comprising the capacity to discriminate, select and execute (p<0.0001). Long repeats reduce SK3 channel function, as we demonstrate by patch-clamping of transfected HEK293 cells. In contrast, modelling the opposite in mice, i.e. KCNN3 overexpression/channel hyperfunction, leads to selective deficits in higher brain functions comparable to those influenced by SK3 conductance in humans. To conclude, KCNN3 genotypes modify cognitive performance, shown here in a large sample of schizophrenic patients. Reduction of SK3 function may constitute a pharmacological target to improve cognition in schizophrenia and other conditions with cognitive impairment."],["dc.identifier.doi","10.1002/emmm.201100135"],["dc.identifier.gro","3142723"],["dc.identifier.isi","000292277600003"],["dc.identifier.pmid","21433290"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8179"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/159"],["dc.language.iso","en"],["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.relation.issn","1757-4676"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","A CAG repeat polymorphism of KCNN3 predicts SK3 channel function and cognitive performance in schizophrenia"],["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"]]