Characterization of Two-Pore Channel 2 by Nuclear Membrane Electrophysiology
Lysosomal calcium (Ca 2+ ) release mediated by NAADP triggers signalling cascades that regulate many cellular processes. The identification of two-pore channel 2 (TPC2) as the NAADP receptor advances our understanding of lysosomal Ca 2+ signalling, yet the lysosome is not amenable to traditional pat...
Gespeichert in:
| Veröffentlicht in: | Scientific reports 2016-02, Vol.6 (1), p.20282-20282, Article 20282 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 20282 |
|---|---|
| container_issue | 1 |
| container_start_page | 20282 |
| container_title | Scientific reports |
| container_volume | 6 |
| creator | Lee, Claire Shuk-Kwan Tong, Benjamin Chun-Kit Cheng, Cecily Wing-Hei Hung, Harry Chun-Hin Cheung, King-Ho |
| description | Lysosomal calcium (Ca
2+
) release mediated by NAADP triggers signalling cascades that regulate many cellular processes. The identification of two-pore channel 2 (TPC2) as the NAADP receptor advances our understanding of lysosomal Ca
2+
signalling, yet the lysosome is not amenable to traditional patch-clamp electrophysiology. Previous attempts to record TPC2 single-channel activity put TPC2 outside its native environment, which not reflect TPC2’s true physiological properties. To test the feasibility of using nuclear membrane electrophysiology for TPC2 channel characterization, we constructed a stable human TPC2-expressing DT40TKO cell line that lacks endogenous InsP
3
R and RyR (DT40TKO-hTPC2). Immunostaining revealed hTPC2 expression on the ER and nuclear envelope. Intracellular dialysis of NAADP into Fura-2-loaded DT40TKO-hTPC2 cells elicited cytosolic Ca
2+
transients, suggesting that hTPC2 was functionally active. Using nuclear membrane electrophysiology, we detected a ~220 pS single-channel current activated by NAADP with K
+
as the permeant ion. The detected single-channel recordings displayed a linear current-voltage relationship, were sensitive to Ned-19 inhibition, were biphasically regulated by NAADP concentration and regulated by PKA phosphorylation. In summary, we developed a cell model for the characterization of the TPC2 channel and the nuclear membrane patch-clamp technique provided an alternative approach to rigorously investigate the electrophysiological properties of TPC2 with minimal manipulation. |
| doi_str_mv | 10.1038/srep20282 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4738322</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1762678262</sourcerecordid><originalsourceid>FETCH-LOGICAL-c504t-eb81586a9783dbfac0713eb5f6f1813bbd66afdcf4748dae87d79fa6f62b97593</originalsourceid><addsrcrecordid>eNplkV1r2zAUhsVoWUubi_2BYuhNW_AmybY-bgYlpO0g7XaRXQtJPkpcHCuT7A7v108lWcha3RzB-_CejxehTwR_JrgQX2KADcVU0A_olOKyymlB6dHB_wRNYnzG6VVUlkR-RCeUiUJQVp6i-XSlg7Y9hOaP7hvfZd5li98-_-EDZEnsOmgzmpkxexpsCzpkj7A2QXeQzVqwffCb1Rgb3_rleI6OnW4jTHb1DP28my2mD_n8-_236e08txUu-xyMIJVgWnJR1MZpizkpwFSOOSJIYUzNmHa1dSUvRa1B8JpLp5lj1EheyeIMfd36bgazhtpC1wfdqk1o1jqMyutG_a90zUot_YsqeSHSRZLB1c4g-F8DxF6tm2ihbdNafoiKcEYZTxd6RS_foM9-CF1aTxEhJSasklWirreUDT6mRNx-GILVa0xqH1NiLw6n35P_QknAzRaISeqWEA5avnP7CwUVnM8</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1899016595</pqid></control><display><type>article</type><title>Characterization of Two-Pore Channel 2 by Nuclear Membrane Electrophysiology</title><source>MEDLINE</source><source>Nature Free</source><source>DOAJ Directory of Open Access Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><source>Springer Nature OA Free Journals</source><creator>Lee, Claire Shuk-Kwan ; Tong, Benjamin Chun-Kit ; Cheng, Cecily Wing-Hei ; Hung, Harry Chun-Hin ; Cheung, King-Ho</creator><creatorcontrib>Lee, Claire Shuk-Kwan ; Tong, Benjamin Chun-Kit ; Cheng, Cecily Wing-Hei ; Hung, Harry Chun-Hin ; Cheung, King-Ho</creatorcontrib><description>Lysosomal calcium (Ca
2+
) release mediated by NAADP triggers signalling cascades that regulate many cellular processes. The identification of two-pore channel 2 (TPC2) as the NAADP receptor advances our understanding of lysosomal Ca
2+
signalling, yet the lysosome is not amenable to traditional patch-clamp electrophysiology. Previous attempts to record TPC2 single-channel activity put TPC2 outside its native environment, which not reflect TPC2’s true physiological properties. To test the feasibility of using nuclear membrane electrophysiology for TPC2 channel characterization, we constructed a stable human TPC2-expressing DT40TKO cell line that lacks endogenous InsP
3
R and RyR (DT40TKO-hTPC2). Immunostaining revealed hTPC2 expression on the ER and nuclear envelope. Intracellular dialysis of NAADP into Fura-2-loaded DT40TKO-hTPC2 cells elicited cytosolic Ca
2+
transients, suggesting that hTPC2 was functionally active. Using nuclear membrane electrophysiology, we detected a ~220 pS single-channel current activated by NAADP with K
+
as the permeant ion. The detected single-channel recordings displayed a linear current-voltage relationship, were sensitive to Ned-19 inhibition, were biphasically regulated by NAADP concentration and regulated by PKA phosphorylation. In summary, we developed a cell model for the characterization of the TPC2 channel and the nuclear membrane patch-clamp technique provided an alternative approach to rigorously investigate the electrophysiological properties of TPC2 with minimal manipulation.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep20282</identifier><identifier>PMID: 26838264</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>13 ; 14/34 ; 631/443 ; 631/80 ; Animals ; Calcium - metabolism ; Calcium Channels - genetics ; Calcium Channels - metabolism ; Calcium Signaling - physiology ; Calcium signalling ; Cell Line ; Channel gating ; Chickens ; Cyclic AMP-Dependent Protein Kinases - metabolism ; Dialysis ; Electrophysiological Phenomena ; Electrophysiology ; Endoplasmic Reticulum - metabolism ; Fura-2 ; Gene Expression Regulation ; HEK293 Cells ; Humanities and Social Sciences ; Humans ; Lipids ; Lysosomes - metabolism ; Membranes ; Models, Biological ; multidisciplinary ; NAADP ; NADP - analogs & derivatives ; NADP - metabolism ; Nuclear Envelope - physiology ; Patch-Clamp Techniques ; Phosphorylation ; Protein kinase A ; Ryanodine receptors ; Science</subject><ispartof>Scientific reports, 2016-02, Vol.6 (1), p.20282-20282, Article 20282</ispartof><rights>The Author(s) 2016</rights><rights>Copyright Nature Publishing Group Feb 2016</rights><rights>Copyright © 2016, Macmillan Publishers Limited 2016 Macmillan Publishers Limited</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c504t-eb81586a9783dbfac0713eb5f6f1813bbd66afdcf4748dae87d79fa6f62b97593</citedby><cites>FETCH-LOGICAL-c504t-eb81586a9783dbfac0713eb5f6f1813bbd66afdcf4748dae87d79fa6f62b97593</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4738322/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4738322/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26838264$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Claire Shuk-Kwan</creatorcontrib><creatorcontrib>Tong, Benjamin Chun-Kit</creatorcontrib><creatorcontrib>Cheng, Cecily Wing-Hei</creatorcontrib><creatorcontrib>Hung, Harry Chun-Hin</creatorcontrib><creatorcontrib>Cheung, King-Ho</creatorcontrib><title>Characterization of Two-Pore Channel 2 by Nuclear Membrane Electrophysiology</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Lysosomal calcium (Ca
2+
) release mediated by NAADP triggers signalling cascades that regulate many cellular processes. The identification of two-pore channel 2 (TPC2) as the NAADP receptor advances our understanding of lysosomal Ca
2+
signalling, yet the lysosome is not amenable to traditional patch-clamp electrophysiology. Previous attempts to record TPC2 single-channel activity put TPC2 outside its native environment, which not reflect TPC2’s true physiological properties. To test the feasibility of using nuclear membrane electrophysiology for TPC2 channel characterization, we constructed a stable human TPC2-expressing DT40TKO cell line that lacks endogenous InsP
3
R and RyR (DT40TKO-hTPC2). Immunostaining revealed hTPC2 expression on the ER and nuclear envelope. Intracellular dialysis of NAADP into Fura-2-loaded DT40TKO-hTPC2 cells elicited cytosolic Ca
2+
transients, suggesting that hTPC2 was functionally active. Using nuclear membrane electrophysiology, we detected a ~220 pS single-channel current activated by NAADP with K
+
as the permeant ion. The detected single-channel recordings displayed a linear current-voltage relationship, were sensitive to Ned-19 inhibition, were biphasically regulated by NAADP concentration and regulated by PKA phosphorylation. In summary, we developed a cell model for the characterization of the TPC2 channel and the nuclear membrane patch-clamp technique provided an alternative approach to rigorously investigate the electrophysiological properties of TPC2 with minimal manipulation.</description><subject>13</subject><subject>14/34</subject><subject>631/443</subject><subject>631/80</subject><subject>Animals</subject><subject>Calcium - metabolism</subject><subject>Calcium Channels - genetics</subject><subject>Calcium Channels - metabolism</subject><subject>Calcium Signaling - physiology</subject><subject>Calcium signalling</subject><subject>Cell Line</subject><subject>Channel gating</subject><subject>Chickens</subject><subject>Cyclic AMP-Dependent Protein Kinases - metabolism</subject><subject>Dialysis</subject><subject>Electrophysiological Phenomena</subject><subject>Electrophysiology</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Fura-2</subject><subject>Gene Expression Regulation</subject><subject>HEK293 Cells</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Lipids</subject><subject>Lysosomes - metabolism</subject><subject>Membranes</subject><subject>Models, Biological</subject><subject>multidisciplinary</subject><subject>NAADP</subject><subject>NADP - analogs & derivatives</subject><subject>NADP - metabolism</subject><subject>Nuclear Envelope - physiology</subject><subject>Patch-Clamp Techniques</subject><subject>Phosphorylation</subject><subject>Protein kinase A</subject><subject>Ryanodine receptors</subject><subject>Science</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNplkV1r2zAUhsVoWUubi_2BYuhNW_AmybY-bgYlpO0g7XaRXQtJPkpcHCuT7A7v108lWcha3RzB-_CejxehTwR_JrgQX2KADcVU0A_olOKyymlB6dHB_wRNYnzG6VVUlkR-RCeUiUJQVp6i-XSlg7Y9hOaP7hvfZd5li98-_-EDZEnsOmgzmpkxexpsCzpkj7A2QXeQzVqwffCb1Rgb3_rleI6OnW4jTHb1DP28my2mD_n8-_236e08txUu-xyMIJVgWnJR1MZpizkpwFSOOSJIYUzNmHa1dSUvRa1B8JpLp5lj1EheyeIMfd36bgazhtpC1wfdqk1o1jqMyutG_a90zUot_YsqeSHSRZLB1c4g-F8DxF6tm2ihbdNafoiKcEYZTxd6RS_foM9-CF1aTxEhJSasklWirreUDT6mRNx-GILVa0xqH1NiLw6n35P_QknAzRaISeqWEA5avnP7CwUVnM8</recordid><startdate>20160203</startdate><enddate>20160203</enddate><creator>Lee, Claire Shuk-Kwan</creator><creator>Tong, Benjamin Chun-Kit</creator><creator>Cheng, Cecily Wing-Hei</creator><creator>Hung, Harry Chun-Hin</creator><creator>Cheung, King-Ho</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PIMPY</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20160203</creationdate><title>Characterization of Two-Pore Channel 2 by Nuclear Membrane Electrophysiology</title><author>Lee, Claire Shuk-Kwan ; Tong, Benjamin Chun-Kit ; Cheng, Cecily Wing-Hei ; Hung, Harry Chun-Hin ; Cheung, King-Ho</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c504t-eb81586a9783dbfac0713eb5f6f1813bbd66afdcf4748dae87d79fa6f62b97593</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>13</topic><topic>14/34</topic><topic>631/443</topic><topic>631/80</topic><topic>Animals</topic><topic>Calcium - metabolism</topic><topic>Calcium Channels - genetics</topic><topic>Calcium Channels - metabolism</topic><topic>Calcium Signaling - physiology</topic><topic>Calcium signalling</topic><topic>Cell Line</topic><topic>Channel gating</topic><topic>Chickens</topic><topic>Cyclic AMP-Dependent Protein Kinases - metabolism</topic><topic>Dialysis</topic><topic>Electrophysiological Phenomena</topic><topic>Electrophysiology</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Fura-2</topic><topic>Gene Expression Regulation</topic><topic>HEK293 Cells</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>Lipids</topic><topic>Lysosomes - metabolism</topic><topic>Membranes</topic><topic>Models, Biological</topic><topic>multidisciplinary</topic><topic>NAADP</topic><topic>NADP - analogs & derivatives</topic><topic>NADP - metabolism</topic><topic>Nuclear Envelope - physiology</topic><topic>Patch-Clamp Techniques</topic><topic>Phosphorylation</topic><topic>Protein kinase A</topic><topic>Ryanodine receptors</topic><topic>Science</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, Claire Shuk-Kwan</creatorcontrib><creatorcontrib>Tong, Benjamin Chun-Kit</creatorcontrib><creatorcontrib>Cheng, Cecily Wing-Hei</creatorcontrib><creatorcontrib>Hung, Harry Chun-Hin</creatorcontrib><creatorcontrib>Cheung, King-Ho</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest Health & Medical Research Collection</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Health & Nursing</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Applied & Life Sciences</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, Claire Shuk-Kwan</au><au>Tong, Benjamin Chun-Kit</au><au>Cheng, Cecily Wing-Hei</au><au>Hung, Harry Chun-Hin</au><au>Cheung, King-Ho</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of Two-Pore Channel 2 by Nuclear Membrane Electrophysiology</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2016-02-03</date><risdate>2016</risdate><volume>6</volume><issue>1</issue><spage>20282</spage><epage>20282</epage><pages>20282-20282</pages><artnum>20282</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Lysosomal calcium (Ca
2+
) release mediated by NAADP triggers signalling cascades that regulate many cellular processes. The identification of two-pore channel 2 (TPC2) as the NAADP receptor advances our understanding of lysosomal Ca
2+
signalling, yet the lysosome is not amenable to traditional patch-clamp electrophysiology. Previous attempts to record TPC2 single-channel activity put TPC2 outside its native environment, which not reflect TPC2’s true physiological properties. To test the feasibility of using nuclear membrane electrophysiology for TPC2 channel characterization, we constructed a stable human TPC2-expressing DT40TKO cell line that lacks endogenous InsP
3
R and RyR (DT40TKO-hTPC2). Immunostaining revealed hTPC2 expression on the ER and nuclear envelope. Intracellular dialysis of NAADP into Fura-2-loaded DT40TKO-hTPC2 cells elicited cytosolic Ca
2+
transients, suggesting that hTPC2 was functionally active. Using nuclear membrane electrophysiology, we detected a ~220 pS single-channel current activated by NAADP with K
+
as the permeant ion. The detected single-channel recordings displayed a linear current-voltage relationship, were sensitive to Ned-19 inhibition, were biphasically regulated by NAADP concentration and regulated by PKA phosphorylation. In summary, we developed a cell model for the characterization of the TPC2 channel and the nuclear membrane patch-clamp technique provided an alternative approach to rigorously investigate the electrophysiological properties of TPC2 with minimal manipulation.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>26838264</pmid><doi>10.1038/srep20282</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 2045-2322 |
| ispartof | Scientific reports, 2016-02, Vol.6 (1), p.20282-20282, Article 20282 |
| issn | 2045-2322 2045-2322 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4738322 |
| source | MEDLINE; Nature Free; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry; Springer Nature OA Free Journals |
| subjects | 13 14/34 631/443 631/80 Animals Calcium - metabolism Calcium Channels - genetics Calcium Channels - metabolism Calcium Signaling - physiology Calcium signalling Cell Line Channel gating Chickens Cyclic AMP-Dependent Protein Kinases - metabolism Dialysis Electrophysiological Phenomena Electrophysiology Endoplasmic Reticulum - metabolism Fura-2 Gene Expression Regulation HEK293 Cells Humanities and Social Sciences Humans Lipids Lysosomes - metabolism Membranes Models, Biological multidisciplinary NAADP NADP - analogs & derivatives NADP - metabolism Nuclear Envelope - physiology Patch-Clamp Techniques Phosphorylation Protein kinase A Ryanodine receptors Science |
| title | Characterization of Two-Pore Channel 2 by Nuclear Membrane Electrophysiology |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-21T08%3A18%3A52IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Characterization%20of%20Two-Pore%20Channel%202%20by%20Nuclear%20Membrane%20Electrophysiology&rft.jtitle=Scientific%20reports&rft.au=Lee,%20Claire%20Shuk-Kwan&rft.date=2016-02-03&rft.volume=6&rft.issue=1&rft.spage=20282&rft.epage=20282&rft.pages=20282-20282&rft.artnum=20282&rft.issn=2045-2322&rft.eissn=2045-2322&rft_id=info:doi/10.1038/srep20282&rft_dat=%3Cproquest_pubme%3E1762678262%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1899016595&rft_id=info:pmid/26838264&rfr_iscdi=true |