Zobrazeno 1 - 10 of 68 pro vyhledávání: '"Richard D. Veenstra"'
1
Changes in cardiac Nav1.5 expression, function, and acetylation by pan-histone deacetylase inhibitors
Autor: Qin Xu, Xian Zhang, Richard D. Veenstra, Dakshesh Patel
Publikováno v: American Journal of Physiology-Heart and Circulatory Physiology. 311:H1139-H1149
Histone deacetylase (HDAC) inhibitors are small molecule anticancer therapeutics that exhibit limiting cardiotoxicities including QT interval prolongation and life-threatening cardiac arrhythmias. Because the molecular mechanisms for HDAC inhibitor-i
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f88d681b918a3a652e097567b19a5b6e
https://doi.org/10.1152/ajpheart.00156.2016
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2
Calcium-calmodulin gating of a pH-insensitive isoform of connexin43 gap junctions
Autor: Siyu Wei, Xianming Lin, Christian Cassara, Richard D. Veenstra
Publikováno v: The Biochemical journal. 476(7)
Intracellular protons and calcium ions are two major chemical factors that regulate connexin43 (Cx43) gap junction communication and the synergism or antagonism between pH and Ca2+ has been questioned for decades. To assess the ability of Ca2+ ions t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3df611ad23c675d32961e1ce21e3061
https://pubmed.ncbi.nlm.nih.gov/30910801
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3
Differences in Functional Expression of Connexin43 and NaV1.5 by Pan- and Class-Selective Histone Deacetylase Inhibition in Heart
Autor: Xian Zhang, Dakshesh Patel, Richard D. Veenstra, Qin Xu
Publikováno v: International Journal of Molecular Sciences, Vol 19, Iss 8, p 2288 (2018)
International Journal of Molecular Sciences
Volume 19
Issue 8
Class-selective histone deacetylase (HDAC) inhibitors were designed to improve safety profiles and therapeutic effectiveness in the treatment of multiple cancers relative to pan-HDAC inhibitors. However, the underlying mechanisms for their therapeuti
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be44228c7d74a81d166873d87ee8cb82
http://www.mdpi.com/1422-0067/19/8/2288
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6
Degradation of a connexin40 mutant linked to atrial fibrillation is accelerated
Autor: Dakshesh Patel, Eric C. Beyer, Richard D. Veenstra, Qin Xu, Adria R. Simon, Joanna Gemel, Arvydas Matiukas
Publikováno v: Journal of Molecular and Cellular Cardiology. 74:330-339
Several Cx40 mutants have been identified in patients with atrial fibrillation (AF). We have been working to identify physiological or cell biological abnormalities of several of these human mutants that might explain how they contribute to disease p
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f315aa71797c3cbbaf95c1c898183dbf
https://doi.org/10.1016/j.yjmcc.2014.06.010
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7
Gap junction regulation by calmodulin
Autor: Richard D. Veenstra, Jenny J. Yang, Juan Zou, Mani Salarian, Yanyi Chen, Charles F. Louis
Publikováno v: FEBS Letters. 588:1430-1438
Intracellular Ca2+ activated calmodulin (CaM) inhibits gap junction channels in the low nanomolar to high micromolar range of [Ca2+]i. This regulation plays an essential role in numerous cellular processes that include hearing, lens transparency, and
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf6a5c0652cbac861938726fe96e0558
https://doi.org/10.1016/j.febslet.2014.01.003
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8
Specificity of the connexin W3/4 locus for functional gap junction formation
Autor: Richard D. Veenstra, Qin Xu, Xian Zhang, Arvydas Matiukas, Xianming Lin
Publikováno v: Channels (Austin, Tex.). 10(6)
The N-terminal (NT) domain of the connexins forms an essential transjunctional voltage (Vj) sensor and pore-forming domain that when truncated, tagged, or mutated often leads to formation of a nonfunctional channel. The NT domain is relatively conser
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27da0adbc1e91d16dd4f1562cb00e088
https://pubmed.ncbi.nlm.nih.gov/27304225
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9
Establishment of the Dual Whole Cell Recording Patch Clamp Configuration for the Measurement of Gap Junction Conductance
Autor: Richard D, Veenstra
Publikováno v: Methods in molecular biology (Clifton, N.J.). 1437
The development of the patch clamp technique has enabled investigators to directly measure gap junction conductance between isolated pairs of small cells with resolution to the single channel level. The dual patch clamp recording technique requires s
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::72ee26cf21ec0b8d39cde1d9c256c2f9
https://pubmed.ncbi.nlm.nih.gov/27207298
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10
Gating of connexin 43 gap junctions by a cytoplasmic loop calmodulin binding domain
Autor: Qin Xu, Jenny J. Yang, Yanyi Chen, Richard D. Veenstra, Richard F. Kopp, Michael W. Roe
Publikováno v: American Journal of Physiology-Cell Physiology. 302:C1548-C1556
Calmodulin (CaM) binding sites were recently identified on the cytoplasmic loop (CL) of at least three α-subfamily connexins (Cx43, Cx44, Cx50), while Cx40 does not have this putative CaM binding domain. The purpose of this study was to examine the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9faace4205697384de95af1225539e9
https://doi.org/10.1152/ajpcell.00319.2011
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