Zobrazeno 1 - 9 of 9 pro vyhledávání: '"Clarence A. Dunn"'
1
Phosphorylation of connexin43 at MAPK, PKC or CK1 sites each distinctly alter the kinetics of epidermal wound repair
Autor: Kristin J. Lastwika, Clarence A. Dunn, Paul D. Lampe, Joell L. Solan
Publikováno v: J Cell Sci
The gap junction protein connexin 43 (Cx43) is a key player in wound healing, and inhibitors of Cx43, which speed epidermal wound healing, are currently in clinical trials. Here, we provide direct in vivo evidence that specific phosphorylation events
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::842855b3eb4575bf2cea06b95e51bdd4
https://doi.org/10.1242/jcs.234633
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2
Connexin43 phosphorylation in brain, cardiac, endothelial and epithelial tissues
Autor: Rachael P. Norris, Lucrecia Márquez-Rosado, Clarence A. Dunn, Joell L. Solan, Paul D. Lampe
Publikováno v: Biochimica et Biophysica Acta (BBA) - Biomembranes. 1818(8):1985-1992
Gap junctions, composed of proteins from the connexin family, allow for intercellular communication between cells in essentially all tissues. There are 21 connexin genes in the human genome and different tissues express different connexin genes. Most
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1dcd357ffd9ab454e12e40263c0c8a1e
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3
Protein kinase C spatially and temporally regulates gap junctional communication during human wound repair via phosphorylation of connexin43 on serine368
Autor: Clarence A. Dunn, Marcia L. Usui, Paul D. Lampe, William G. Carter, Theresa S. Richards, John E. Olerud
Publikováno v: The Journal of Cell Biology
Phosphorylation of connexin43 (Cx43) on serine368 (S368) has been shown to decrease gap junctional communication via a reduction in unitary channel conductance. Examination of phosphoserine368 (pS368) in normal human skin tissue using a phosphorylati
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87bc1f0f7c7028f0c67ba5e234475211
https://doi.org/10.1083/jcb.200404142
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4
Adhesion or Plasmin Regulates Tyrosine Phosphorylation of a Novel Membrane Glycoprotein p80/gp140/CUB Domain-containing Protein 1 in Epithelia
Autor: Randy O. Sigle, Clarence A. Dunn, Tai Mei Yang, Tod Brown, William G. Carter, Yuping Xia, Beatrice S. Knudsen, Tatiana Zaitsevskaia
Publikováno v: Journal of Biological Chemistry. 279:14772-14783
Suspension of cultured human foreskin keratinocytes (HKs) with trypsin phosphorylates tyrosine residues on an 80-kDa membrane glycoprotein, p80 (Xia, Y., Gil, S. G., and Carter, W. G. (1996) J. Cell Biol. 132, 727-740). Readhesion dephosphorylates p8
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2941234ae09c20a89632aef4ef9cf014
https://doi.org/10.1074/jbc.m309678200
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5
Injury-triggered Akt phosphorylation of Cx43: a ZO-1-driven molecular switch that regulates gap junction size
Autor: Paul D. Lampe, Clarence A. Dunn
The proteins that form vertebrate gap junctions, the connexins, are highly regulated and have short (< 2 h) half-lives. Phosphorylation of connexin43 (Cx43) is generally known to affect gap junction assembly, channel gating and turnover. After findin
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0007c733c6b69686abcb54ed52e463a
https://europepmc.org/articles/PMC3889401/
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6
MAPK phosphorylation of connexin 43 promotes binding of cyclin E and smooth muscle cell proliferation
Autor: Paul D. Lampe, Leslie A. Mitchell, Cecilia W. Lo, Brant E. Isakson, Angela K. Best, Scott R. Johnstone, Yelena Peskova, Robert K. Nakamoto, Adam C. Straub, Brett M. Kroncke, Michael Koval, Linda Columbus, Clarence A. Dunn
Publikováno v: Circulation research. 111(2)
Rationale: Dedifferentiation of vascular smooth muscle cells (VSMC) leading to a proliferative cell phenotype significantly contributes to the development of atherosclerosis. Mitogen-activated protein kinase (MAPK) phosphorylation of proteins includi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9011c814c54cae4520e763383e9dde7
https://pubmed.ncbi.nlm.nih.gov/22652908
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7
The role of membrane microdomains in transmembrane signaling through the epithelial glycoprotein Gp140/CDCP1
Autor: Tod Brown, Stacy M. Alvares, William G. Carter, Clarence A. Dunn, Elizabeth E. Wayner
Publikováno v: Biochimica et biophysica acta. 1780(3)
Cell adhesion to the extracellular matrix (ECM) via integrin adhesion receptors initiates signaling cascades leading to changes in cell behavior. While integrin clustering is necessary to initiate cell attachment to the matrix, additional membrane co
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e32c2421a562c6ef115d3fe8a1d8318
https://pubmed.ncbi.nlm.nih.gov/18269919
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