@article{
 title = {Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox},
 type = {article},
 year = {2013},
 identifiers = {[object Object]},
 pages = {337-349},
 volume = {201},
 websites = {http://www.ncbi.nlm.nih.gov/pubmed/23589496,http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=PMC3628511},
 month = {4},
 publisher = {Rockefeller Univ Press},
 day = {15},
 id = {1956dfe8-df8a-3386-8a44-fe9ec6af7721},
 created = {2016-04-13T17:21:29.000Z},
 accessed = {2016-04-13},
 file_attached = {false},
 profile_id = {9b1c14de-b75a-3e23-a406-ef006d6fed26},
 group_id = {f13cbab9-4ed3-3161-a244-dc1e9b314eef},
 last_modified = {2016-04-13T17:21:30.000Z},
 read = {false},
 starred = {false},
 authored = {true},
 confirmed = {true},
 hidden = {false},
 citation_key = {avezov2013lifetime},
 source_type = {article},
 abstract = {Interfering with disulfide bond formation impedes pro- tein folding and promotes endoplasmic reticulum (ER) stress. Due to limitations in measurement techniques, the relationships of altered thiol redox and ER stress have been difficult to assess. We report that fluorescent lifetime measurements circumvented the crippling dimness of an ER-tuned fluorescent redox-responsive probe (roGFPiE), faithfully tracking the activity of the major ER-localized protein disulfide isomerase, PDI. In vivo lifetime imag- ing by time-correlated single-photon counting (TCSPC) re- corded subtle changes in ER redox poise induced by exposure of mammalian cells to a reducing environment but revealed an unanticipated stability of redox to fluc- tuations in unfolded protein load. By contrast, TCSPC of roGFPiE uncovered a hitherto unsuspected reductive shift in the mammalian ER upon loss of luminal calcium, whether induced by pharmacological inhibition of calcium reup- take into the ER or by physiological activation of release channels. These findings recommend fluorescent lifetime imaging as a sensitive method to track ER redox homeo- stasis in mammalian cells.},
 bibtype = {article},
 author = {Avezov, Edward and Cross, Benedict C S and Schierle, Gabriele S Kaminski and Winters, Mikael and Harding, Heather P. and Melo, Eduardo Pinho and Kaminski, Clemens F. and Ron, David},
 journal = {Journal of Cell Biology},
 number = {2}
}

{"_id":"DwEaGteLRxt3LLXPh","bibbaseid":"avezov-cross-schierle-winters-harding-melo-kaminski-ron-lifetimeimagingofafluorescentproteinsensorrevealssurprisingstabilityoferthiolredox-2013","downloads":0,"creationDate":"2016-04-13T17:18:12.854Z","title":"Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox","author_short":["Avezov, E.","Cross, B., C., S.","Schierle, G., S., K.","Winters, M.","Harding, H., P.","Melo, E., P.","Kaminski, C., F.","Ron, D."],"year":2013,"bibtype":"article","biburl":null,"bibdata":{"title":"Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox","type":"article","year":"2013","identifiers":"[object Object]","pages":"337-349","volume":"201","websites":"http://www.ncbi.nlm.nih.gov/pubmed/23589496,http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=PMC3628511","month":"4","publisher":"Rockefeller Univ Press","day":"15","id":"1956dfe8-df8a-3386-8a44-fe9ec6af7721","created":"2016-04-13T17:21:29.000Z","accessed":"2016-04-13","file_attached":false,"profile_id":"9b1c14de-b75a-3e23-a406-ef006d6fed26","group_id":"f13cbab9-4ed3-3161-a244-dc1e9b314eef","last_modified":"2016-04-13T17:21:30.000Z","read":false,"starred":false,"authored":"true","confirmed":"true","hidden":false,"citation_key":"avezov2013lifetime","source_type":"article","abstract":"Interfering with disulfide bond formation impedes pro- tein folding and promotes endoplasmic reticulum (ER) stress. Due to limitations in measurement techniques, the relationships of altered thiol redox and ER stress have been difficult to assess. We report that fluorescent lifetime measurements circumvented the crippling dimness of an ER-tuned fluorescent redox-responsive probe (roGFPiE), faithfully tracking the activity of the major ER-localized protein disulfide isomerase, PDI. In vivo lifetime imag- ing by time-correlated single-photon counting (TCSPC) re- corded subtle changes in ER redox poise induced by exposure of mammalian cells to a reducing environment but revealed an unanticipated stability of redox to fluc- tuations in unfolded protein load. By contrast, TCSPC of roGFPiE uncovered a hitherto unsuspected reductive shift in the mammalian ER upon loss of luminal calcium, whether induced by pharmacological inhibition of calcium reup- take into the ER or by physiological activation of release channels. These findings recommend fluorescent lifetime imaging as a sensitive method to track ER redox homeo- stasis in mammalian cells.","bibtype":"article","author":"Avezov, Edward and Cross, Benedict C S and Schierle, Gabriele S Kaminski and Winters, Mikael and Harding, Heather P. and Melo, Eduardo Pinho and Kaminski, Clemens F. and Ron, David","journal":"Journal of Cell Biology","number":"2","bibtex":"@article{\n title = {Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox},\n type = {article},\n year = {2013},\n identifiers = {[object Object]},\n pages = {337-349},\n volume = {201},\n websites = {http://www.ncbi.nlm.nih.gov/pubmed/23589496,http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=PMC3628511},\n month = {4},\n publisher = {Rockefeller Univ Press},\n day = {15},\n id = {1956dfe8-df8a-3386-8a44-fe9ec6af7721},\n created = {2016-04-13T17:21:29.000Z},\n accessed = {2016-04-13},\n file_attached = {false},\n profile_id = {9b1c14de-b75a-3e23-a406-ef006d6fed26},\n group_id = {f13cbab9-4ed3-3161-a244-dc1e9b314eef},\n last_modified = {2016-04-13T17:21:30.000Z},\n read = {false},\n starred = {false},\n authored = {true},\n confirmed = {true},\n hidden = {false},\n citation_key = {avezov2013lifetime},\n source_type = {article},\n abstract = {Interfering with disulfide bond formation impedes pro- tein folding and promotes endoplasmic reticulum (ER) stress. Due to limitations in measurement techniques, the relationships of altered thiol redox and ER stress have been difficult to assess. We report that fluorescent lifetime measurements circumvented the crippling dimness of an ER-tuned fluorescent redox-responsive probe (roGFPiE), faithfully tracking the activity of the major ER-localized protein disulfide isomerase, PDI. In vivo lifetime imag- ing by time-correlated single-photon counting (TCSPC) re- corded subtle changes in ER redox poise induced by exposure of mammalian cells to a reducing environment but revealed an unanticipated stability of redox to fluc- tuations in unfolded protein load. By contrast, TCSPC of roGFPiE uncovered a hitherto unsuspected reductive shift in the mammalian ER upon loss of luminal calcium, whether induced by pharmacological inhibition of calcium reup- take into the ER or by physiological activation of release channels. These findings recommend fluorescent lifetime imaging as a sensitive method to track ER redox homeo- stasis in mammalian cells.},\n bibtype = {article},\n author = {Avezov, Edward and Cross, Benedict C S and Schierle, Gabriele S Kaminski and Winters, Mikael and Harding, Heather P. and Melo, Eduardo Pinho and Kaminski, Clemens F. and Ron, David},\n journal = {Journal of Cell Biology},\n number = {2}\n}","author_short":["Avezov, E.","Cross, B., C., S.","Schierle, G., S., K.","Winters, M.","Harding, H., P.","Melo, E., P.","Kaminski, C., F.","Ron, D."],"urls":{"Website":"http://www.ncbi.nlm.nih.gov/pubmed/23589496,http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=PMC3628511"},"bibbaseid":"avezov-cross-schierle-winters-harding-melo-kaminski-ron-lifetimeimagingofafluorescentproteinsensorrevealssurprisingstabilityoferthiolredox-2013","role":"author","downloads":0},"search_terms":["lifetime","imaging","fluorescent","protein","sensor","reveals","surprising","stability","thiol","redox","avezov","cross","schierle","winters","harding","melo","kaminski","ron"],"keywords":[],"authorIDs":[]}