Year |
Citation |
Score |
2020 |
Roscoe JM, Sevier CS. Pathways for Sensing and Responding to Hydrogen Peroxide at the Endoplasmic Reticulum. Cells. 9. PMID 33080949 DOI: 10.3390/cells9102314 |
0.395 |
|
2019 |
Nicklow EE, Sevier CS. Activity of the yeast cytoplasmic Hsp70 nucleotide exchange factor Fes1 is regulated by reversible methionine oxidation. The Journal of Biological Chemistry. PMID 31806703 DOI: 10.1074/Jbc.Ra119.010125 |
0.447 |
|
2019 |
Siegenthaler KD, Sevier CS. Working Together: Redox Signaling between the Endoplasmic Reticulum and Mitochondria. Chemical Research in Toxicology. PMID 30721036 DOI: 10.1021/Acs.Chemrestox.8B00379 |
0.31 |
|
2018 |
O'Donnell JP, Marsh HM, Sondermann H, Sevier C. Disrupted hydrogen bond network and impaired ATPase activity in an Hsc70 cysteine mutant. Biochemistry. PMID 29300467 DOI: 10.1021/Acs.Biochem.7B01005 |
0.4 |
|
2017 |
Ellgaard L, Sevier CS, Bulleid NJ. How Are Proteins Reduced in the Endoplasmic Reticulum? Trends in Biochemical Sciences. PMID 29153511 DOI: 10.1016/J.Tibs.2017.10.006 |
0.512 |
|
2017 |
Siegenthaler KD, Pareja KA, Wang J, Sevier CS. An unexpected role for the yeast nucleotide exchange factor Sil1 as a reductant acting on the molecular chaperone BiP. Elife. 6. PMID 28257000 DOI: 10.7554/Elife.24141 |
0.438 |
|
2016 |
Xu M, Marsh HM, Sevier CS. A Conserved Cysteine within the ATPase Domain of the Endoplasmic Reticulum Chaperone BiP is Necessary for a Complete Complement of BiP Activities. Journal of Molecular Biology. PMID 27543005 DOI: 10.1016/J.Jmb.2016.08.011 |
0.428 |
|
2016 |
Wang J, Sevier CS. Formation and Reversibility of BiP Cysteine Oxidation Facilitates Cell Survival During and Post Oxidative Stress. The Journal of Biological Chemistry. PMID 26865632 DOI: 10.1074/Jbc.M115.694810 |
0.409 |
|
2015 |
Sevier C. Redox signaling in the Endoplasmic Reticulum Free Radical Biology and Medicine. 87: S9. DOI: 10.1016/J.Freeradbiomed.2015.10.015 |
0.32 |
|
2014 |
Wang J, Pareja KA, Kaiser CA, Sevier CS. Redox signaling via the molecular chaperone BiP protects cells against endoplasmic reticulum-derived oxidative stress. Elife. 3: e03496. PMID 25053742 DOI: 10.7554/Elife.03496 |
0.424 |
|
2014 |
Loftus JP, Cavatorta D, Bushey JJ, Levine CB, Sevier CS, Wakshlag JJ. The 5-lipoxygenase inhibitor tepoxalin induces oxidative damage and altered PTEN status prior to apoptosis in canine osteosarcoma cell lines. Veterinary and Comparative Oncology. PMID 24813477 DOI: 10.1111/Vco.12094 |
0.316 |
|
2014 |
Wang J, Pareja KA, Kaiser CA, Sevier CS. Author response: Redox signaling via the molecular chaperone BiP protects cells against endoplasmic reticulum-derived oxidative stress Elife. DOI: 10.7554/Elife.03496.014 |
0.368 |
|
2012 |
Kim S, Sideris DP, Sevier CS, Kaiser CA. Balanced Ero1 activation and inactivation establishes ER redox homeostasis. The Journal of Cell Biology. 196: 713-25. PMID 22412017 DOI: 10.1083/Jcb.201110090 |
0.461 |
|
2012 |
Sevier CS. Erv2 and quiescin sulfhydryl oxidases: Erv-domain enzymes associated with the secretory pathway. Antioxidants & Redox Signaling. 16: 800-8. PMID 22142242 DOI: 10.1089/Ars.2011.4450 |
0.49 |
|
2010 |
Heldman N, Vonshak O, Sevier CS, Vitu E, Mehlman T, Fass D. Steps in reductive activation of the disulfide-generating enzyme Ero1p. Protein Science : a Publication of the Protein Society. 19: 1863-76. PMID 20669236 DOI: 10.1002/Pro.473 |
0.386 |
|
2010 |
Vitu E, Kim S, Sevier CS, Lutzky O, Heldman N, Bentzur M, Unger T, Yona M, Kaiser CA, Fass D. Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum. The Journal of Biological Chemistry. 285: 18155-65. PMID 20348090 DOI: 10.1074/Jbc.M109.064931 |
0.521 |
|
2010 |
Sevier CS. New insights into oxidative folding. The Journal of Cell Biology. 188: 757-8. PMID 20308423 DOI: 10.1083/Jcb.201002114 |
0.348 |
|
2008 |
Vitu E, Gross E, Greenblatt HM, Sevier CS, Kaiser CA, Fass D. Yeast Mpd1p reveals the structural diversity of the protein disulfide isomerase family. Journal of Molecular Biology. 384: 631-40. PMID 18845159 DOI: 10.1016/J.Jmb.2008.09.052 |
0.406 |
|
2008 |
Sevier CS, Kaiser CA. Ero1 and redox homeostasis in the endoplasmic reticulum. Biochimica Et Biophysica Acta. 1783: 549-56. PMID 18191641 DOI: 10.1016/J.Bbamcr.2007.12.011 |
0.505 |
|
2007 |
Sevier CS, Qu H, Heldman N, Gross E, Fass D, Kaiser CA. Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1. Cell. 129: 333-44. PMID 17448992 DOI: 10.1016/J.Cell.2007.02.039 |
0.474 |
|
2006 |
Sevier CS, Kaiser CA. Conservation and diversity of the cellular disulfide bond formation pathways. Antioxidants & Redox Signaling. 8: 797-811. PMID 16771671 DOI: 10.1089/Ars.2006.8.797 |
0.527 |
|
2006 |
Sevier CS, Kaiser CA. Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1. Molecular Biology of the Cell. 17: 2256-66. PMID 16495342 DOI: 10.1091/Mbc.E05-05-0417 |
0.48 |
|
2006 |
Gross E, Sevier CS, Heldman N, Vitu E, Bentzur M, Kaiser CA, Thorpe C, Fass D. Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. Proceedings of the National Academy of Sciences of the United States of America. 103: 299-304. PMID 16407158 DOI: 10.1073/Pnas.0506448103 |
0.322 |
|
2005 |
Vala A, Sevier CS, Kaiser CA. Structural determinants of substrate access to the disulfide oxidase Erv2p. Journal of Molecular Biology. 354: 952-66. PMID 16288914 DOI: 10.1016/J.Jmb.2005.09.076 |
0.369 |
|
2005 |
Sevier CS, Kadokura H, Tam VC, Beckwith J, Fass D, Kaiser CA. The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases. Protein Science : a Publication of the Protein Society. 14: 1630-42. PMID 15930008 DOI: 10.1110/Ps.051355705 |
0.482 |
|
2002 |
Sevier CS, Kaiser CA. Formation and transfer of disulphide bonds in living cells. Nature Reviews. Molecular Cell Biology. 3: 836-47. PMID 12415301 DOI: 10.1038/Nrm954 |
0.459 |
|
2002 |
Gross E, Sevier CS, Vala A, Kaiser CA, Fass D. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nature Structural Biology. 9: 61-7. PMID 11740506 DOI: 10.1038/Nsb740 |
0.464 |
|
2001 |
Sevier CS, Cuozzo JW, Vala A, Åslund F, Kaiser CA. A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation Nature Cell Biology. 3: 874-882. PMID 11584268 DOI: 10.1038/Ncb1001-874 |
0.415 |
|
2001 |
Sevier CS, Machamer CE. p38: A novel protein that associates with the vesicular stomatitis virus glycoprotein. Biochemical and Biophysical Research Communications. 287: 574-82. PMID 11554768 DOI: 10.1006/Bbrc.2001.5621 |
0.61 |
|
2000 |
Sevier CS, Weisz OA, Davis M, Machamer CE. Efficient export of the vesicular stomatitis virus G protein from the endoplasmic reticulum requires a signal in the cytoplasmic tail that includes both tyrosine-based and di-acidic motifs. Molecular Biology of the Cell. 11: 13-22. PMID 10637287 DOI: 10.1091/Mbc.11.1.13 |
0.625 |
|
1998 |
Sevier CS, Machamer CE. Fragmentation of a Golgi-localized chimeric protein allows detergent solubilization and reveals an alternate conformation of the cytoplasmic domain. Biochemistry. 37: 185-92. PMID 9425038 DOI: 10.1021/Bi971782K |
0.623 |
|
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