| Year |
Citation |
Score |
| 2024 |
Guerriero CJ, Brodsky JL. The HERCulean task of recognizing, ubiquitinating, and shielding misfolded integral membrane proteins. The Journal of Cell Biology. 223. PMID 38836811 DOI: 10.1083/jcb.202405160 |
0.358 |
|
| 2024 |
Mann MJ, Melendez-Suchi C, Vorndran HE, Sukhoplyasova M, Flory AR, Irvine MC, Iyer AR, Guerriero CJ, Brodsky JL, Hendershot LM, Buck TM. Loss of Grp170 results in catastrophic disruption of endoplasmic reticulum function. Molecular Biology of the Cell. mbcE24010012. PMID 38446639 DOI: 10.1091/mbc.E24-01-0012 |
0.345 |
|
| 2023 |
Hendershot LM, Buck TM, Brodsky JL. The Essential Functions of Molecular Chaperones and Folding Enzymes in Maintaining Endoplasmic Reticulum Homeostasis. Journal of Molecular Biology. 168418. PMID 38143019 DOI: 10.1016/j.jmb.2023.168418 |
0.422 |
|
| 2023 |
Daskivich GJ, Brodsky JL. The generation of detergent-insoluble clipped fragments from an ERAD substrate in mammalian cells. Scientific Reports. 13: 21508. PMID 38057493 DOI: 10.1038/s41598-023-48769-z |
0.427 |
|
| 2023 |
Mann MJ, Melendez-Suchi C, Sukhoplyasova M, Flory AR, Carson Irvine M, Iyer AR, Vorndran H, Guerriero CJ, Brodsky JL, Hendershot LM, Buck TM. Loss of Grp170 results in catastrophic disruption of endoplasmic reticulum functions. Biorxiv : the Preprint Server For Biology. PMID 37905119 DOI: 10.1101/2023.10.19.563191 |
0.344 |
|
| 2023 |
Sukhoplyasova M, Keith AM, Perrault EM, Vorndran HE, Jordahl AS, Yates ME, Pastor A, Li Z, Freaney ML, Deshpande RA, Adams DB, Guerriero C, Shi S, Kleyman TR, Kashlan O, ... Brodsky JL, et al. Lhs1 dependent ERAD is determined by transmembrane domain context. The Biochemical Journal. PMID 37702403 DOI: 10.1042/BCJ20230075 |
0.35 |
|
| 2022 |
Brodsky JL, Engelman DM, Hendershot LM, Piana-Agostinetti S, Sommer T. Taking out the trash: How misfolded proteins are removed from the endoplasmic reticulum. Faculty Reviews. 11: 29. PMID 36267301 DOI: 10.12703/r-01-0000018 |
0.412 |
|
| 2022 |
Nakatsukasa K, Wigge S, Takano Y, Kawarasaki T, Kamura T, Brodsky JL. A positive genetic selection for transmembrane domain mutations in HRD1 underscores the importance of Hrd1 complex integrity during ERAD. Current Genetics. PMID 35041076 DOI: 10.1007/s00294-022-01227-1 |
0.339 |
|
| 2021 |
Kumari D, Fisher EA, Brodsky JL. Hsp40s play distinct roles during the initial stages of apolipoprotein B biogenesis. Molecular Biology of the Cell. mbcE21090436. PMID 34910568 DOI: 10.1091/mbc.E21-09-0436 |
0.322 |
|
| 2021 |
Needham PG, Goeckeler-Fried JL, Zhang C, Sun Z, Wetzel AR, Bertrand CA, Brodsky JL. SLC26A9 is selected for endoplasmic reticulum associated degradation (ERAD) via Hsp70-dependent targeting of the soluble STAS domain. The Biochemical Journal. 478: 4203-4220. PMID 34821356 DOI: 10.1042/BCJ20210644 |
0.35 |
|
| 2021 |
Sun Z, Guerriero CJ, Brodsky JL. Substrate ubiquitination retains misfolded membrane proteins in the endoplasmic reticulum for degradation. Cell Reports. 36: 109717. PMID 34551305 DOI: 10.1016/j.celrep.2021.109717 |
0.476 |
|
| 2021 |
Kumari D, Brodsky JL. The Targeting of Native Proteins to the Endoplasmic Reticulum-Associated Degradation (ERAD) Pathway: An Expanding Repertoire of Regulated Substrates. Biomolecules. 11. PMID 34439852 DOI: 10.3390/biom11081185 |
0.428 |
|
| 2021 |
Burns GD, Hilal OE, Sun Z, Reutter KR, Preston GM, Augustine AA, Brodsky JL, Guerriero CJ. The characterization of distinct classes of misfolded proteins uncovers differential effects in yeast compromised for proteasome function. Febs Letters. PMID 34358326 DOI: 10.1002/1873-3468.14172 |
0.402 |
|
| 2021 |
Goeckeler-Fried JL, Aldrin Denny R, Joshi D, Hill C, Larsen MB, Chiang AN, Frizzell RA, Wipf P, Sorscher EJ, Brodsky JL. Improved correction of F508del-CFTR biogenesis with a folding facilitator and an inhibitor of protein ubiquitination. Bioorganic & Medicinal Chemistry Letters. 128243. PMID 34246753 DOI: 10.1016/j.bmcl.2021.128243 |
0.393 |
|
| 2021 |
Honer J, Niemeyer KM, Fercher C, Diez Tissera AL, Jaberolansar N, Jafrani YMA, Zhou C, Caramelo JJ, Shewan AM, Schulz BL, Brodsky JL, Zacchi LF. TorsinA folding and N-linked glycosylation are sensitive to redox homeostasis. Biochimica Et Biophysica Acta. Molecular Cell Research. 119073. PMID 34062155 DOI: 10.1016/j.bbamcr.2021.119073 |
0.367 |
|
| 2021 |
Klionsky DJ, Abdel-Aziz AK, Abdelfatah S, Abdellatif M, Abdoli A, Abel S, Abeliovich H, Abildgaard MH, Abudu YP, Acevedo-Arozena A, Adamopoulos IE, Adeli K, Adolph TE, Adornetto A, Aflaki E, ... ... Brodsky JL, et al. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition). Autophagy. 1-382. PMID 33634751 DOI: 10.1080/15548627.2020.1797280 |
0.51 |
|
| 2021 |
Ferro-Novick S, Reggiori F, Brodsky JL. ER-Phagy, ER Homeostasis, and ER Quality Control: Implications for Disease. Trends in Biochemical Sciences. PMID 33509650 DOI: 10.1016/j.tibs.2020.12.013 |
0.579 |
|
| 2020 |
Singh A, Vashistha N, Heck J, Tang X, Wipf P, Brodsky JL, Hampton RY. Direct involvement of Hsp70 ATP hydrolysis in Ubr1-dependent quality control. Molecular Biology of the Cell. mbcE20080541. PMID 32966159 DOI: 10.1091/mbc.E20-08-0541 |
0.351 |
|
| 2020 |
Buck TM, Zeng X, Cantrell PS, Cattley RT, Hasanbasri Z, Yates ME, Nguyen D, Yates NA, Brodsky JL. The Capture of a Disabled Proteasome Identifies Erg25 as a Substrate for Endoplasmic Reticulum Associated Degradation. Molecular & Cellular Proteomics : McP. PMID 32868373 DOI: 10.1074/mcp.RA120.002050 |
0.325 |
|
| 2020 |
Estabrooks SK, Brodsky JL. Ubiquitination of disease-causing CFTR variants in a microsome-based assay. Analytical Biochemistry. 604: 113829. PMID 32621804 DOI: 10.1016/j.ab.2020.113829 |
0.426 |
|
| 2019 |
Sun Z, Brodsky JL. Protein quality control in the secretory pathway. The Journal of Cell Biology. PMID 31537714 DOI: 10.1083/jcb.201906047 |
0.399 |
|
| 2019 |
Cui Y, Parashar S, Zahoor M, Needham PG, Mari M, Zhu M, Chen S, Ho HC, Reggiori F, Farhan H, Brodsky JL, Ferro-Novick S. A COPII subunit acts with an autophagy receptor to target endoplasmic reticulum for degradation. Science (New York, N.Y.). 365: 53-60. PMID 31273116 DOI: 10.1126/Science.Aau9263 |
0.62 |
|
| 2019 |
Werner HM, Estabrooks SK, Preston GM, Brodsky JL, Horne WS. Exploring the Functional Consequences of Protein Backbone Alteration in Ubiquitin through Native Chemical Ligation. Chembiochem : a European Journal of Chemical Biology. PMID 31059184 DOI: 10.1002/Cbic.201900225 |
0.313 |
|
| 2019 |
Doonan LM, Guerriero CJ, Preston GM, Buck TM, Khazanov N, Fisher EA, Senderowitz H, Brodsky JL. Hsp104 Facilitates the Endoplasmic Reticulum Associated Degradation of Disease-Associated and Aggregation-Prone Substrates. Protein Science : a Publication of the Protein Society. PMID 31050848 DOI: 10.1002/Pro.3636 |
0.323 |
|
| 2019 |
Needham PG, Guerriero CJ, Brodsky JL. Chaperoning Endoplasmic Reticulum-Associated Degradation (ERAD) and Protein Conformational Diseases. Cold Spring Harbor Perspectives in Biology. PMID 30670468 DOI: 10.1101/Cshperspect.A033928 |
0.399 |
|
| 2018 |
Shurtleff MJ, Itzhak DN, Hussmann JA, Schirle Oakdale NT, Costa EA, Jonikas M, Weibezahn J, Popova KD, Jan CH, Sinitcyn P, Vembar SS, Hernandez H, Cox J, Burlingame AL, Brodsky J, et al. The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins. Elife. 7. PMID 29809151 DOI: 10.7554/Elife.37018 |
0.421 |
|
| 2018 |
Hager NA, Krasowski CJ, Mackie TD, Kolb AR, Needham PG, Augustine AA, Dempsey A, Szent-Gyorgyi C, Bruchez MP, Bain DJ, Kwiatkowski AV, O'Donnell AF, Brodsky JL. Select α-arrestins control cell-surface abundance of the mammalian Kir2.1 potassium channel in a yeast model. The Journal of Biological Chemistry. PMID 29784874 DOI: 10.1074/Jbc.Ra117.001293 |
0.305 |
|
| 2018 |
Sun Z, Brodsky JL. The degradation pathway of a model misfolded protein is determined by aggregation propensity. Molecular Biology of the Cell. mbcE18020117. PMID 29688814 DOI: 10.1091/mbc.E18-02-0117 |
0.444 |
|
| 2018 |
Preston GM, Guerriero CJ, Metzger MB, Michaelis S, Brodsky JL. Substrate Insolubility Dictates Hsp104-Dependent Endoplasmic-Reticulum-Associated Degradation. Molecular Cell. 70: 242-253.e6. PMID 29677492 DOI: 10.1016/J.Molcel.2018.03.016 |
0.387 |
|
| 2018 |
Shurtleff MJ, Itzhak DN, Hussmann JA, Oakdale NTS, Costa EA, Jonikas M, Weibezahn J, Popova KD, Jan CH, Sinitcyn P, Vembar SS, Hernandez H, Cox J, Burlingame AL, Brodsky JL, et al. Author response: The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins Elife. DOI: 10.7554/Elife.37018.023 |
0.374 |
|
| 2017 |
Nakasone MA, Lewis TA, Walker O, Thakur A, Mansour W, Castañeda CA, Goeckeler-Fried JL, Parlati F, Chou TF, Hayat O, Zhang D, Camara CM, Bonn SM, Nowicka UK, Krueger S, ... ... Brodsky JL, et al. Structural Basis for the Inhibitory Effects of Ubistatins in the Ubiquitin-Proteasome Pathway. Structure (London, England : 1993). PMID 29153505 DOI: 10.1016/J.Str.2017.10.007 |
0.502 |
|
| 2017 |
Sun Z, Brodsky JL. Guardians of the ERAD Galaxy. Cell. 171: 267-268. PMID 28985557 DOI: 10.1016/j.cell.2017.09.023 |
0.308 |
|
| 2017 |
Zacchi LF, Dittmar JC, Mihalevic MJ, Shewan AM, Schulz BL, Brodsky JL, Bernstein KA. A novel high-throughput yeast genetic screen for factors modifying protein levels of the Early-Onset Torsion Dystonia-associated variant torsinAΔE. Disease Models & Mechanisms. PMID 28768697 DOI: 10.1242/Dmm.029926 |
0.334 |
|
| 2017 |
O'Donnell BM, Mackie TD, Subramanya AR, Brodsky JL. Endoplasmic Reticulum-Associated Degradation of the Renal Potassium Channel, ROMK, Leads to Type II Bartter Syndrome. The Journal of Biological Chemistry. PMID 28630040 DOI: 10.1074/Jbc.M117.786376 |
0.312 |
|
| 2017 |
Guerriero CJ, Reutter KR, Augustine AA, Preston GM, Weiberth KF, Mackie TD, Cleveland-Rubeor HC, Bethel NP, Callenberg KM, Nakatsukasa K, Grabe M, Brodsky JL. Transmembrane helix hydrophobicity is an energetic barrier during the retrotranslocation of integral membrane ERAD substrates. Molecular Biology of the Cell. PMID 28539401 DOI: 10.1091/Mbc.E17-03-0184 |
0.357 |
|
| 2017 |
Preston GM, Brodsky JL. The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation. The Biochemical Journal. 474: 445-469. PMID 28159894 DOI: 10.1042/BCJ20160582 |
0.416 |
|
| 2016 |
Buck TM, Jordahl AS, Yates ME, Preston M, Cook E, Kleyman TR, Brodsky JL. Interactions Between Intersubunit Transmembrane Domains Regulate the Chaperone Dependent Degradation of an Oligomeric Membrane Protein. The Biochemical Journal. PMID 27903760 DOI: 10.1042/BCJ20160760 |
0.315 |
|
| 2016 |
McClure ML, Barnes S, Brodsky JL, Sorscher EJ. Trafficking and Function of the Cystic Fibrosis Transmembrane Conductance Regulator: A Complex Network of Post-Translational Modifications. American Journal of Physiology. Lung Cellular and Molecular Physiology. ajplung.00431.2015. PMID 27474090 DOI: 10.1152/ajplung.00431.2015 |
0.311 |
|
| 2016 |
Manos-Turvey A, Brodsky JL, Wipf P. The effect of structure and mechanism of the Hsp70 chaperone on the ability to identify chemical modulators and therapeutics Topics in Medicinal Chemistry. 19: 81-129. DOI: 10.1007/7355_2015_90 |
0.31 |
|
| 2015 |
Prosser DC, Pannunzio AE, Brodsky JL, Thorner J, Wendland B, O'Donnell AF. Alpha-arrestins participate in cargo selection for both clathrin-independent and clathrin-mediated endocytosis. Journal of Cell Science. PMID 26459639 DOI: 10.1242/Jcs.175372 |
0.318 |
|
| 2015 |
Needham PG, Patel HJ, Chiosis G, Thibodeau PH, Brodsky JL. Mutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions. Journal of Molecular Biology. PMID 25913688 DOI: 10.1016/J.Jmb.2015.04.010 |
0.324 |
|
| 2015 |
Buck TM, Jordan R, Lyons-Weiler J, Adelman JL, Needham PG, Kleyman TR, Brodsky JL. Expression of three topologically distinct membrane proteins elicits unique stress response pathways in the yeast Saccharomyces cerevisiae. Physiological Genomics. 47: 198-214. PMID 25759377 DOI: 10.1152/Physiolgenomics.00101.2014 |
0.397 |
|
| 2014 |
Li H, Wu HC, Liu Z, Zacchi LF, Brodsky JL, Zolkiewski M. Intracellular complexes of the early-onset torsion dystonia-associated AAA+ ATPase TorsinA. Springerplus. 3: 743. PMID 25674472 DOI: 10.1186/2193-1801-3-743 |
0.351 |
|
| 2014 |
Brodsky JL, Clark PL. Protein folding in the cell, from atom to organism. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 28: 5034-8. PMID 25451678 DOI: 10.1096/Fj.14-1202Ufm |
0.358 |
|
| 2014 |
Nakatsukasa K, Kamura T, Brodsky JL. Recent technical developments in the study of ER-associated degradation. Current Opinion in Cell Biology. 29: 82-91. PMID 24867671 DOI: 10.1016/J.Ceb.2014.04.008 |
0.348 |
|
| 2014 |
Alvaro CG, O'Donnell AF, Prosser DC, Augustine AA, Goldman A, Brodsky JL, Cyert MS, Wendland B, Thorner J. Specific α-arrestins negatively regulate Saccharomyces cerevisiae pheromone response by down-modulating the G-protein-coupled receptor Ste2. Molecular and Cellular Biology. 34: 2660-81. PMID 24820415 DOI: 10.1128/Mcb.00230-14 |
0.307 |
|
| 2014 |
Brodsky JL, Merz A, Serio T. Organelle and proteome quality control mechanisms: how cells are able to keep calm and carry on. Molecular Biology of the Cell. 25: 733-4. PMID 24626847 DOI: 10.1091/Mbc.E13-11-0672 |
0.394 |
|
| 2014 |
Brodsky JL. The threads that tie protein-folding diseases. Disease Models & Mechanisms. 7: 3-4. PMID 24396147 DOI: 10.1242/dmm.014985 |
0.332 |
|
| 2014 |
Tran JR, Brodsky JL. The Cdc48-Vms1 complex maintains 26S proteasome architecture. The Biochemical Journal. 458: 459-67. PMID 24351022 DOI: 10.1042/BJ20131161 |
0.331 |
|
| 2013 |
Brodsky JL. Just a trim, please: refining ER degradation through deubiquitination. Cell. 154: 479-81. PMID 23890819 DOI: 10.1016/j.cell.2013.07.008 |
0.365 |
|
| 2013 |
Hecht KA, Wytiaz VA, Ast T, Schuldiner M, Brodsky JL. Characterization of an M28 metalloprotease family member residing in the yeast vacuole. Fems Yeast Research. 13: 471-84. PMID 23679341 DOI: 10.1111/1567-1364.12050 |
0.321 |
|
| 2013 |
Guerriero CJ, Weiberth KF, Brodsky JL. Hsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligase. The Journal of Biological Chemistry. 288: 18506-20. PMID 23653356 DOI: 10.1074/Jbc.M113.475905 |
0.428 |
|
| 2013 |
Buck TM, Plavchak L, Roy A, Donnelly BF, Kashlan OB, Kleyman TR, Subramanya AR, Brodsky JL. The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channel. The Journal of Biological Chemistry. 288: 18366-80. PMID 23645669 DOI: 10.1074/Jbc.M113.469882 |
0.381 |
|
| 2013 |
Needham PG, Brodsky JL. How early studies on secreted and membrane protein quality control gave rise to the ER associated degradation (ERAD) pathway: the early history of ERAD. Biochimica Et Biophysica Acta. 1833: 2447-57. PMID 23557783 DOI: 10.1016/J.Bbamcr.2013.03.018 |
0.385 |
|
| 2013 |
Donnelly BF, Needham PG, Snyder AC, Roy A, Khadem S, Brodsky JL, Subramanya AR. Hsp70 and Hsp90 multichaperone complexes sequentially regulate thiazide-sensitive cotransporter endoplasmic reticulum-associated degradation and biogenesis. The Journal of Biological Chemistry. 288: 13124-35. PMID 23482560 DOI: 10.1074/Jbc.M113.455394 |
0.317 |
|
| 2012 |
Brodsky JL. Cleaning up: ER-associated degradation to the rescue. Cell. 151: 1163-7. PMID 23217703 DOI: 10.1016/j.cell.2012.11.012 |
0.3 |
|
| 2012 |
Guerriero CJ, Brodsky JL. The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology. Physiological Reviews. 92: 537-76. PMID 22535891 DOI: 10.1152/Physrev.00027.2011 |
0.366 |
|
| 2012 |
Tran JR, Brodsky JL. Assays to measure ER-associated degradation in yeast. Methods in Molecular Biology (Clifton, N.J.). 832: 505-18. PMID 22350909 DOI: 10.1007/978-1-61779-474-2_36 |
0.32 |
|
| 2012 |
Grubb S, Guo L, Fisher EA, Brodsky JL. Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates. Molecular Biology of the Cell. 23: 520-32. PMID 22190736 DOI: 10.1091/mbc.E11-08-0704 |
0.311 |
|
| 2011 |
Needham PG, Mikoluk K, Dhakarwal P, Khadem S, Snyder AC, Subramanya AR, Brodsky JL. The thiazide-sensitive NaCl cotransporter is targeted for chaperone-dependent endoplasmic reticulum-associated degradation. The Journal of Biological Chemistry. 286: 43611-21. PMID 22027832 DOI: 10.1074/Jbc.M111.288928 |
0.393 |
|
| 2011 |
Brodsky JL, Skach WR. Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems. Current Opinion in Cell Biology. 23: 464-75. PMID 21664808 DOI: 10.1016/j.ceb.2011.05.004 |
0.43 |
|
| 2011 |
Bell SL, Chiang AN, Brodsky JL. Expression of a malarial Hsp70 improves defects in chaperone-dependent activities in ssa1 mutant yeast. Plos One. 6: e20047. PMID 21625512 DOI: 10.1371/journal.pone.0020047 |
0.301 |
|
| 2011 |
Falcone D, Henderson MP, Nieuwland H, Coughlan CM, Brodsky JL, Andrews DW. Stability and function of the Sec61 translocation complex depends on the Sss1p tail-anchor sequence. The Biochemical Journal. 436: 291-303. PMID 21355855 DOI: 10.1042/Bj20101865 |
0.335 |
|
| 2011 |
Tran JR, Tomsic LR, Brodsky JL. A Cdc48p-associated factor modulates endoplasmic reticulum-associated degradation, cell stress, and ubiquitinated protein homeostasis. The Journal of Biological Chemistry. 286: 5744-55. PMID 21148305 DOI: 10.1074/jbc.M110.179259 |
0.461 |
|
| 2010 |
Goeckeler JL, Brodsky JL. Molecular chaperones and substrate ubiquitination control the efficiency of endoplasmic reticulum-associated degradation. Diabetes, Obesity & Metabolism. 12: 32-8. PMID 21029298 DOI: 10.1111/j.1463-1326.2010.01273.x |
0.431 |
|
| 2010 |
Brodsky JL. The use of in vitro assays to measure endoplasmic reticulum-associated degradation. Methods in Enzymology. 470: 661-79. PMID 20946830 DOI: 10.1016/S0076-6879(10)70027-6 |
0.425 |
|
| 2010 |
Nakatsukasa K, Brodsky JL. in vitro reconstitution of the selection, ubiquitination, and membrane extraction of a polytopic ERAD substrate. Methods in Molecular Biology (Clifton, N.J.). 619: 365-76. PMID 20419421 DOI: 10.1007/978-1-60327-412-8_21 |
0.457 |
|
| 2009 |
Vembar SS, Jin Y, Brodsky JL, Hendershot LM. The mammalian Hsp40 ERdj3 requires its Hsp70 interaction and substrate-binding properties to complement various yeast Hsp40-dependent functions. The Journal of Biological Chemistry. 284: 32462-71. PMID 19748898 DOI: 10.1074/Jbc.M109.000729 |
0.312 |
|
| 2009 |
Brodsky JL, Wojcikiewicz RJ. Substrate-specific mediators of ER associated degradation (ERAD). Current Opinion in Cell Biology. 21: 516-21. PMID 19443192 DOI: 10.1016/j.ceb.2009.04.006 |
0.385 |
|
| 2008 |
Vembar SS, Brodsky JL. One step at a time: endoplasmic reticulum-associated degradation. Nature Reviews. Molecular Cell Biology. 9: 944-57. PMID 19002207 DOI: 10.1038/nrm2546 |
0.395 |
|
| 2008 |
Rabu C, Wipf P, Brodsky JL, High S. A precursor-specific role for Hsp40/Hsc70 during tail-anchored protein integration at the endoplasmic reticulum. The Journal of Biological Chemistry. 283: 27504-13. PMID 18667436 DOI: 10.1074/Jbc.M804591200 |
0.443 |
|
| 2008 |
Kang Y, Taldone T, Clement CC, Fewell SW, Aguirre J, Brodsky JL, Chiosis G. Design of a fluorescence polarization assay platform for the study of human Hsp70. Bioorganic & Medicinal Chemistry Letters. 18: 3749-51. PMID 18515098 DOI: 10.1016/J.Bmcl.2008.05.046 |
0.311 |
|
| 2008 |
Nakatsukasa K, Brodsky JL. The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum. Traffic (Copenhagen, Denmark). 9: 861-70. PMID 18315532 DOI: 10.1111/j.1600-0854.2008.00729.x |
0.401 |
|
| 2008 |
Nakatsukasa K, Huyer G, Michaelis S, Brodsky JL. Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell. 132: 101-12. PMID 18191224 DOI: 10.1016/J.Cell.2007.11.023 |
0.458 |
|
| 2007 |
Buck TM, Wright CM, Brodsky JL. The activities and function of molecular chaperones in the endoplasmic reticulum. Seminars in Cell & Developmental Biology. 18: 751-61. PMID 17964199 DOI: 10.1016/j.semcdb.2007.09.001 |
0.367 |
|
| 2007 |
Hrizo SL, Gusarova V, Habiel DM, Goeckeler JL, Fisher EA, Brodsky JL. The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-associated degradation (ERAD). The Journal of Biological Chemistry. 282: 32665-75. PMID 17823116 DOI: 10.1074/Jbc.M705216200 |
0.306 |
|
| 2007 |
Brodsky JL, Scott CM. Tipping the delicate balance: defining how proteasome maturation affects the degradation of a substrate for autophagy and endoplasmic reticulum associated degradation (ERAD). Autophagy. 3: 623-5. PMID 17786020 |
0.32 |
|
| 2007 |
Feng D, Zhao X, Soromani C, Toikkanen J, Römisch K, Vembar SS, Brodsky JL, Keränen S, Jäntti J. The transmembrane domain is sufficient for Sbh1p function, its association with the Sec61 complex, and interaction with Rtn1p. The Journal of Biological Chemistry. 282: 30618-28. PMID 17699516 DOI: 10.1074/jbc.M701840200 |
0.386 |
|
| 2007 |
Kashlan OB, Mueller GM, Qamar MZ, Poland PA, Ahner A, Rubenstein RC, Hughey RP, Brodsky JL, Kleyman TR. Small heat shock protein alphaA-crystallin regulates epithelial sodium channel expression. The Journal of Biological Chemistry. 282: 28149-56. PMID 17664274 DOI: 10.1074/jbc.M703409200 |
0.353 |
|
| 2007 |
Scott CM, Kruse KB, Schmidt BZ, Perlmutter DH, McCracken AA, Brodsky JL. ADD66, a gene involved in the endoplasmic reticulum-associated degradation of alpha-1-antitrypsin-Z in yeast, facilitates proteasome activity and assembly. Molecular Biology of the Cell. 18: 3776-87. PMID 17634286 DOI: 10.1091/Mbc.E07-01-0034 |
0.323 |
|
| 2007 |
Brodsky JL. The protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulum-associated degradation). The Biochemical Journal. 404: 353-63. PMID 17521290 DOI: 10.1042/BJ20061890 |
0.448 |
|
| 2007 |
Ahner A, Nakatsukasa K, Zhang H, Frizzell RA, Brodsky JL. Small heat-shock proteins select deltaF508-CFTR for endoplasmic reticulum-associated degradation. Molecular Biology of the Cell. 18: 806-14. PMID 17182856 DOI: 10.1091/Mbc.E06-05-0458 |
0.398 |
|
| 2007 |
Nakatsukasa K, Brodsky JL. The Role of BiP/Kar2p in the Translocation of Proteins Across the ER Membrane Enzymes. 25: 245-273. DOI: 10.1016/S1874-6047(07)25010-3 |
0.484 |
|
| 2006 |
Kruse KB, Brodsky JL, McCracken AA. Autophagy: an ER protein quality control process. Autophagy. 2: 135-7. PMID 16874086 DOI: 10.4161/Auto.2.2.2388 |
0.402 |
|
| 2006 |
Brodsky JL, Chiosis G. Hsp70 molecular chaperones: emerging roles in human disease and identification of small molecule modulators. Current Topics in Medicinal Chemistry. 6: 1215-25. PMID 16842158 DOI: 10.2174/156802606777811997 |
0.31 |
|
| 2006 |
McCracken AA, Brodsky JL. Recognition and delivery of ERAD substrates to the proteasome and alternative paths for cell survival Current Topics in Microbiology and Immunology. 300: 17-40. PMID 16573235 |
0.375 |
|
| 2006 |
Kruse KB, Brodsky JL, McCracken AA. Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: one for soluble Z variant of human alpha-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ. Molecular Biology of the Cell. 17: 203-12. PMID 16267277 DOI: 10.1091/Mbc.E04-09-0779 |
0.331 |
|
| 2005 |
Nishikawa S, Brodsky JL, Nakatsukasa K. Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). Journal of Biochemistry. 137: 551-5. PMID 15944407 DOI: 10.1093/jb/mvi068 |
0.439 |
|
| 2005 |
Lee RJ, McCracken AA, Brodsky JL. Reconstitution of endoplasmic reticulum-associated degradation using yeast membranes and cytosol. Methods in Molecular Biology (Clifton, N.J.). 301: 175-84. PMID 15917632 DOI: 10.1385/1-59259-895-1:175 |
0.455 |
|
| 2005 |
Brodsky JL. An in vitro assay for the selective endoplasmic reticulum associated degradation of an unglycosylated secreted protein Methods. 35: 354-359. PMID 15804607 DOI: 10.1016/j.ymeth.2004.10.007 |
0.406 |
|
| 2005 |
Ahner A, Whyte FM, Brodsky JL. Distinct but overlapping functions of Hsp70, Hsp90, and an Hsp70 nucleotide exchange factor during protein biogenesis in yeast Archives of Biochemistry and Biophysics. 435: 32-41. PMID 15680904 DOI: 10.1016/j.abb.2004.11.005 |
0.332 |
|
| 2004 |
Ahner A, Brodsky JL. Checkpoints in ER-associated degradation: Excuse me, which way to the proteasome? Trends in Cell Biology. 14: 474-478. PMID 15350974 DOI: 10.1016/j.tcb.2004.07.013 |
0.373 |
|
| 2004 |
Youker RT, Walsh P, Beilharz T, Lithgow T, Brodsky JL. Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast Molecular Biology of the Cell. 15: 4787-4797. PMID 15342786 DOI: 10.1091/mbc.E04-07-0584 |
0.324 |
|
| 2004 |
Huyer G, Piluek WF, Fansler Z, Kreft SG, Hochstrasser M, Brodsky JL, Michaelis S. Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein. The Journal of Biological Chemistry. 279: 38369-78. PMID 15252059 DOI: 10.1074/Jbc.M402468200 |
0.478 |
|
| 2004 |
Lee RJ, Liu CW, Harty C, McCracken AA, Latterich M, Römisch K, DeMartino GN, Thomas PJ, Brodsky JL. Uncoupling retro-translocation and degradation in the ER-associated degradation of a soluble protein. The Embo Journal. 23: 2206-15. PMID 15152188 DOI: 10.1038/Sj.Emboj.7600232 |
0.4 |
|
| 2004 |
Coughlan CM, Walker JL, Cochran JC, Wittrup KD, Brodsky JL. Degradation of mutated bovine pancreatic trypsin inhibitor in the yeast vacuole suggests post-endoplasmic reticulum protein quality control. The Journal of Biological Chemistry. 279: 15289-97. PMID 14744871 DOI: 10.1074/Jbc.M309673200 |
0.398 |
|
| 2003 |
McCracken AA, Brodsky JL. Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD). Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 25: 868-77. PMID 12938176 DOI: 10.1002/Bies.10320 |
0.36 |
|
| 2003 |
Kabani M, Kelley SS, Morrow MW, Montgomery DL, Sivendran R, Rose MD, Gierasch LM, Brodsky JL. Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP. Molecular Biology of the Cell. 14: 3437-48. PMID 12925775 DOI: 10.1091/Mbc.E02-12-0847 |
0.304 |
|
| 2003 |
Palmer EA, Kruse KB, Fewell SW, Buchanan SM, Brodsky JL, McCracken AA. Differential requirements of novel A1PiZ degradation deficient (ADD) genes in ER-associated protein degradation. Journal of Cell Science. 116: 2361-73. PMID 12711700 DOI: 10.1242/Jcs.00439 |
0.402 |
|
| 2003 |
Sullivan ML, Youker RT, Watkins SC, Brodsky JL. Localization of the BiP molecular chaperone with respect to endoplasmic reticulum foci containing the cystic fibrosis transmembrane conductance regulator in yeast. The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society. 51: 545-8. PMID 12642634 DOI: 10.1177/002215540305100417 |
0.428 |
|
| 2003 |
Kabani M, Beckerich JM, Brodsky JL. The yeast Sls1p and Fes1p proteins define a new family of Hsp70 nucleotide exchange factors Current Genomics. 4: 465-473. DOI: 10.2174/1389202033490268 |
0.331 |
|
| 2002 |
Goeckeler JL, Stephens A, Lee P, Caplan AJ, Brodsky JL. Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity. Molecular Biology of the Cell. 13: 2760-70. PMID 12181344 DOI: 10.1091/Mbc.02-04-0051 |
0.322 |
|
| 2002 |
Kabani M, Beckerich JM, Brodsky JL. Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p Molecular and Cellular Biology. 22: 4677-4689. PMID 12052876 DOI: 10.1128/MCB.22.13.4677-4689.2002 |
0.38 |
|
| 2001 |
Fewell SW, Travers KJ, Weissman JS, Brodsky JL. The action of molecular chaperones in the early secretory pathway. Annual Review of Genetics. 35: 149-91. PMID 11700281 DOI: 10.1146/Annurev.Genet.35.102401.090313 |
0.433 |
|
| 2001 |
Morrow MW, Brodsky JL. Yeast ribosomes bind to highly purified reconstituted Sec61p complex and to mammalian p180 Traffic. 2: 705-716. PMID 11576447 DOI: 10.1034/j.1600-0854.2001.21005.x |
0.302 |
|
| 2001 |
Nishikawa SI, Fewell SW, Kato Y, Brodsky JL, Endo T. Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation Journal of Cell Biology. 153: 1061-1069. PMID 11381090 DOI: 10.1083/jcb.153.5.1061 |
0.451 |
|
| 2001 |
Zhang Y, Nijbroek G, Sullivan ML, McCracken AA, Watkins SC, Michaelis S, Brodsky JL. Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast. Molecular Biology of the Cell. 12: 1303-14. PMID 11359923 DOI: 10.1091/Mbc.12.5.1303 |
0.469 |
|
| 1999 |
Brodsky JL, McCracken AA. ER protein quality control and proteasome-mediated protein degradation Seminars in Cell and Developmental Biology. 10: 507-513. PMID 10597633 DOI: 10.1006/scdb.1999.0321 |
0.43 |
|
| 1999 |
Coury LA, Zeidel ML, Brodsky JL. Use of yeast sec6 mutant for purification of vesicles containing recombinant membrane proteins Methods in Enzymology. 306: 169-186. PMID 10432454 DOI: 10.1016/S0076-6879(99)06012-7 |
0.366 |
|
| 1999 |
Brodsky JL, Werner ED, Dubas ME, Goeckeler JL, Kruse KB, McCracken AA. The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct. The Journal of Biological Chemistry. 274: 3453-60. PMID 9920890 DOI: 10.1074/Jbc.274.6.3453 |
0.405 |
|
| 1998 |
McClellan AJ, Endres JB, Vogel JP, Palazzi D, Rose MD, Brodsky JL. Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER. Molecular Biology of the Cell. 9: 3533-45. PMID 9843586 DOI: 10.1091/Mbc.9.12.3533 |
0.416 |
|
| 1998 |
Brodsky JL, Bäuerle M, Horst M, McClellan AJ. Mitochondrial Hsp70 cannot replace BiP in driving protein translocation into the yeast endoplasmic reticulum Febs Letters. 435: 183-186. PMID 9762904 DOI: 10.1016/S0014-5793(98)01065-5 |
0.386 |
|
| 1998 |
Brodsky JL. Translocation of Proteins across the Endoplasmic Reticulum Membrane International Review of Cytology. 178: 277-328. PMID 9348672 DOI: 10.1016/S0074-7696(08)62139-7 |
0.45 |
|
| 1998 |
McCracken AA, Werner ED, Brodsky JL. Endoplasmic Reticulum-Associated Protein degradation: An Unconventional Route to a Familiar Fate Advances in Molecular and Cell Biology. 27: 165-200. DOI: 10.1016/S1569-2558(08)60461-0 |
0.422 |
|
| 1997 |
Brodsky JL. Quantitation of membrane proteins in reconstituted vesicles prepared from yeast Analytical Biochemistry. 246: 262-263. PMID 9073366 DOI: 10.1006/abio.1997.2028 |
0.333 |
|
| 1997 |
Brodsky JL, McCracken AA. ER-associated and proteasome-mediated protein degradation: How two topologically restricted events came together Trends in Cell Biology. 7: 151-156. DOI: 10.1016/S0962-8924(97)01020-9 |
0.404 |
|
| 1996 |
Werner ED, Brodsky JL, McCracken AA. Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate. Proceedings of the National Academy of Sciences of the United States of America. 93: 13797-801. PMID 8943015 DOI: 10.1073/Pnas.93.24.13797 |
0.417 |
|
| 1995 |
Brodsky JL, Goeckeler J, Schekman R. BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum Proceedings of the National Academy of Sciences of the United States of America. 92: 9643-9646. PMID 7568189 DOI: 10.1073/Pnas.92.21.9643 |
0.586 |
|
| 1994 |
Brodsky JL, Schekman R. 4 Heat Shock Cognate Proteins and Polypeptide Translocation Across the Endoplasmic Reticulum Membrane Cold Spring Harbor Monograph Archive. 26: 85-109. DOI: 10.1101/087969427.26.85 |
0.583 |
|
| 1993 |
Brodsky JL, Hamamoto S, Feldheim D, Schekman R. Reconstitution of protein translocation from solubilized yeast membranes reveals topologically distinct roles for BiP and cytosolic Hsc70 Journal of Cell Biology. 120: 95-102. PMID 8416998 DOI: 10.1083/Jcb.120.1.95 |
0.635 |
|
| 1993 |
Brodsky JL, Schekman R. A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome Journal of Cell Biology. 123: 1355-1363. PMID 8253836 DOI: 10.1083/Jcb.123.6.1355 |
0.519 |
|
| Show low-probability matches. |
