D
Dale W. Laird
Researcher at University of Western Ontario
Publications - 184
Citations - 15654
Dale W. Laird is an academic researcher from University of Western Ontario. The author has contributed to research in topics: Connexin & Pannexin. The author has an hindex of 64, co-authored 181 publications receiving 14438 citations. Previous affiliations of Dale W. Laird include University of Minnesota & California Institute of Technology.
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Journal ArticleDOI
Pannexin 1 channels mediate ‘find-me’ signal release and membrane permeability during apoptosis
Faraaz B. Chekeni,Michael R. Elliott,Michael R. Elliott,Joanna K. Sandilos,Scott F. Walk,Scott F. Walk,Jason M. Kinchen,Jason M. Kinchen,Eduardo R. Lazarowski,Allison Armstrong,Allison Armstrong,Silvia Penuela,Dale W. Laird,Guy S. Salvesen,Brant E. Isakson,Douglas A. Bayliss,Kodi S. Ravichandran,Kodi S. Ravichandran +17 more
TL;DR: PANX1 is identified as a plasma membrane channel mediating the regulated release of find-me signals and selective plasma membrane permeability during apoptosis, and a new mechanism of PANX1 activation by caspases is identified.
Journal ArticleDOI
Multicolor and Electron Microscopic Imaging of Connexin Trafficking
Guido M. Gaietta,Thomas J. Deerinck,Stephen R. Adams,James C. Bouwer,Oded Tour,Dale W. Laird,Gina E. Sosinsky,Roger Y. Tsien,Mark H. Ellisman +8 more
TL;DR: This approach was used to show that newly synthesized connexin43 was transported predominantly in 100- to 150-nanometer vesicles to the plasma membrane and incorporated at the periphery of existing gap junctions, whereas older connexins were removed from the center of the plaques into pleiomorphic vesicle of widely varying sizes.
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Life cycle of connexins in health and disease
TL;DR: This review will assess the current understanding of wild-type and selected disease-linked mutant connexin transport through the secretory pathway, gap-junction assembly at the cell surface, internalization and degradation.
Journal ArticleDOI
Turnover and phosphorylation dynamics of connexin43 gap junction protein in cultured cardiac myocytes.
TL;DR: It is postulate that the rapid turnover of Cx43 and its multiple sites of phosphorylation play important roles in the regulation of cell-cell communication via gap junctions and the turnover rate of phosphate groups was found to be experimentally defined by the half-life of the protein.
Journal ArticleDOI
Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins
Silvia Penuela,Ruchi Bhalla,Xiang-Qun Gong,Kyle N. Cowan,Steven J. Celetti,Bryce Cowan,Donglin Bai,Qing Shao,Dale W. Laird +8 more
TL;DR: Functional assays in cultured cells transiently expressing Panx1 and Panx3 were incapable of forming intercellular channels, but assembled into functional cell surface channels, showing that these proteins probably play an important biological role as single membrane channels.