{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,14]],"date-time":"2026-09-14T13:05:29Z","timestamp":1789391129412,"version":"build-2803163510"},"reference-count":43,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,9,14]],"date-time":"2026-09-14T00:00:00Z","timestamp":1789344000000},"content-version":"am","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"},{"start":{"date-parts":[[2026,9,14]],"date-time":"2026-09-14T00:00:00Z","timestamp":1789344000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"},{"start":{"date-parts":[[2026,9,14]],"date-time":"2026-09-14T00:00:00Z","timestamp":1789344000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/100000015","name":"U.S. Department of Energy","doi-asserted-by":"publisher","award":["DE\u2010SC0026354"],"award-info":[{"award-number":["DE\u2010SC0026354"]}],"id":[{"id":"10.13039\/100000015","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Yeast"],"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Over the last three decades, blue native polyacrylamide gel electrophoresis (BN\u2010PAGE), a technique that allows the resolution of large protein complexes in their native conformations, has profoundly impacted the study of mitochondrial biology and our understanding of oxidative phosphorylation (OXPHOS) system's biogenesis and organization. However, while protein samples for BN\u2010PAGE can be prepared from permeabilized mammalian cells, the analysis of yeast OXPHOS complexes requires the prior isolation of mitochondria from whole yeast cells. This requirement limits high\u2010throughput studies and prevents short time\u2010course analyses. We therefore combined BN\u2010PAGE techniques with the cryogenic milling of snap\u2010frozen cells to develop cryoBN\u2010PAGE, which allows for the preparation of BN\u2010PAGE samples from whole\u2010cell yeast lysates and avoids the cost and time associated with mitochondrial isolation. Here, we show the optimization of the method and demonstrate that it can be efficiently paired with a number of downstream applications, such as immunoblots, second\u2010dimension SDS\u2010PAGE, and\n                    <jats:italic>in gel<\/jats:italic>\n                    enzymatic activity assays. Furthermore, by avoiding the time\u2010consuming mitochondrial isolation, cryoBN\u2010PAGE allows for precise time\u2010course assays and the investigation of rapid changes in the properties of the OXPHOS system in response to alterations in environmental conditions.\n                  <\/jats:p>","DOI":"10.1002\/yea.70043","type":"journal-article","created":{"date-parts":[[2026,9,14]],"date-time":"2026-09-14T12:34:31Z","timestamp":1789389271000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["CryoBN\u2010PAGE: A Rapid and Cost\u2010Effective Method for the Analysis of Yeast Respiratory Complexes and Their Dynamic Organization"],"prefix":"10.1002","author":[{"ORCID":"https:\/\/orcid.org\/0009-0000-4632-2599","authenticated-orcid":false,"given":"Lizeth J.","family":"Camacho Lopez","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Biology Miller School of Medicine, University of Miami Miami Florida USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8724-5999","authenticated-orcid":false,"given":"Mazzen H.","family":"Eldeeb","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology Miller School of Medicine, University of Miami Miami Florida USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elliana G.","family":"Mohrhardt","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology Miller School of Medicine, University of Miami Miami Florida USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0509-3835","authenticated-orcid":false,"given":"Flavia","family":"Fontanesi","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology Miller School of Medicine, University of Miami Miami Florida USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,9,14]]},"reference":[{"key":"e_1_2_9_2_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M113.525733"},{"key":"e_1_2_9_3_1","doi-asserted-by":"publisher","DOI":"10.15252\/embr.202051015"},{"key":"e_1_2_9_4_1","doi-asserted-by":"publisher","DOI":"10.3389\/fcell.2021.796128"},{"key":"e_1_2_9_5_1","doi-asserted-by":"publisher","DOI":"10.1080\/10715760701635082"},{"key":"e_1_2_9_6_1","doi-asserted-by":"publisher","DOI":"10.1002\/cpmb.41"},{"key":"e_1_2_9_7_1","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/18.19.5226"},{"issue":"24","key":"e_1_2_9_8_1","doi-asserted-by":"crossref","first-page":"18093","DOI":"10.1074\/jbc.M001901200","article-title":"The Cytochrome bc1 and Cytochrome c Oxidase Complexes Associate to Form a Single Supracomplex in Yeast Mitochondria","volume":"275","author":"Cruciat C. 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