| Year |
Citation |
Score |
| 2022 |
Umano A, Fang K, Qu Z, Scaglione JB, Altinok S, Treadway CJ, Wick ET, Paulakonis E, Karunanayake C, Chou S, Bardakjian TM, Gonzalez-Alegre P, Page RC, Schisler JC, Brown NG, ... ... Scaglione KM, et al. The molecular basis of spinocerebellar ataxia type 48 caused by a de novo mutation in the ubiquitin ligase CHIP. The Journal of Biological Chemistry. 101899. PMID 35398354 DOI: 10.1016/j.jbc.2022.101899 |
0.363 |
|
| 2020 |
Kanack A, Vittal V, Haver H, Keppel T, Gundry RL, Klevit RE, Scaglione KM. UbcH5 interacts with substrates to participate in lysine selection with the E3 ubiquitin ligase CHIP. Biochemistry. PMID 32401531 DOI: 10.1021/Acs.Biochem.0C00084 |
0.453 |
|
| 2017 |
Wang B, Zeng L, Merillat SA, Ochaba J, Thompson LM, Barmada SJ, Scaglione KM, Paulson HL. The ubiquitin conjugating enzyme Ube2W regulates solubility of the Huntington's disease protein, huntingtin. Neurobiology of Disease. PMID 28986324 DOI: 10.1016/j.nbd.2017.10.002 |
0.327 |
|
| 2016 |
Lass A, Cocklin R, Scaglione KM, Skowyra M, Korolev S, Goebl M, Skowyra D. Erratum to: The loop-less (tm)Cdc34 E2 mutant defective polyubiquitination in vitro and in vivo supports yeast growth in a manner dependent on Ubp14 and Cka2. Cell Division. 11: 13. PMID 27761151 DOI: 10.1186/S13008-016-0018-1 |
0.653 |
|
| 2016 |
Ristic G, Tsou WL, Guzi E, Kanack AJ, Scaglione KM, Todi SV. USP5 is dispensable for mono-ubiquitin maintenance in Drosophila. The Journal of Biological Chemistry. PMID 26917723 DOI: 10.1074/jbc.M115.703504 |
0.319 |
|
| 2015 |
Faggiano S, Menon RP, Kelly GP, Todi SV, Scaglione KM, Konarev PV, Svergun DI, Paulson HL, Pastore A. Allosteric regulation of deubiquitylase activity through ubiquitination. Frontiers in Molecular Biosciences. 2: 2. PMID 25988170 DOI: 10.3389/fmolb.2015.00002 |
0.389 |
|
| 2015 |
Vittal V, Shi L, Wenzel DM, Scaglione KM, Duncan ED, Basrur V, Elenitoba-Johnson KS, Baker D, Paulson HL, Brzovic PS, Klevit RE. Intrinsic disorder drives N-terminal ubiquitination by Ube2w. Nature Chemical Biology. 11: 83-9. PMID 25436519 DOI: 10.1038/Nchembio.1700 |
0.356 |
|
| 2013 |
Faggiano S, Menon RP, Kelly GP, McCormick J, Todi SV, Scaglione KM, Paulson HL, Pastore A. Enzymatic production of mono-ubiquitinated proteins for structural studies: The example of the Josephin domain of ataxin-3. Febs Open Bio. 3: 453-8. PMID 24251111 DOI: 10.1016/j.fob.2013.10.005 |
0.358 |
|
| 2013 |
Tsou WL, Burr AA, Ouyang M, Blount JR, Scaglione KM, Todi SV. Ubiquitination regulates the neuroprotective function of the deubiquitinase ataxin-3 in vivo. The Journal of Biological Chemistry. 288: 34460-9. PMID 24106274 DOI: 10.1074/jbc.M113.513903 |
0.398 |
|
| 2013 |
Smith MC, Scaglione KM, Assimon VA, Patury S, Thompson AD, Dickey CA, Southworth DR, Paulson HL, Gestwicki JE, Zuiderweg ER. The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex. Biochemistry. 52: 5354-64. PMID 23865999 DOI: 10.1021/Bi4009209 |
0.308 |
|
| 2013 |
Scaglione KM, Basrur V, Ashraf NS, Konen JR, Elenitoba-Johnson KS, Todi SV, Paulson HL. The ubiquitin-conjugating enzyme (E2) Ube2w ubiquitinates the N terminus of substrates. The Journal of Biological Chemistry. 288: 18784-8. PMID 23696636 DOI: 10.1074/jbc.C113.477596 |
0.345 |
|
| 2011 |
Scaglione KM, Zavodszky E, Todi SV, Patury S, Xu P, RodrÃguez-Lebrón E, Fischer S, Konen J, Djarmati A, Peng J, Gestwicki JE, Paulson HL. Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP. Molecular Cell. 43: 599-612. PMID 21855799 DOI: 10.1016/J.Molcel.2011.05.036 |
0.438 |
|
| 2011 |
Lass A, Cocklin R, Scaglione KM, Skowyra M, Korolev S, Goebl M, Skowyra D. The loop-less tmCdc34 E2 mutant defective in polyubiquitination in vitro and in vivo supports yeast growth in a manner dependent on Ubp14 and Cka2. Cell Division. 6: 7. PMID 21453497 DOI: 10.1186/1747-1028-6-7 |
0.678 |
|
| 2010 |
Todi SV, Scaglione KM, Blount JR, Basrur V, Conlon KP, Pastore A, Elenitoba-Johnson K, Paulson HL. Activity and cellular functions of the deubiquitinating enzyme and polyglutamine disease protein ataxin-3 are regulated by ubiquitination at lysine 117. The Journal of Biological Chemistry. 285: 39303-13. PMID 20943656 DOI: 10.1074/jbc.M110.181610 |
0.368 |
|
| 2009 |
Todi SV, Winborn BJ, Scaglione KM, Blount JR, Travis SM, Paulson HL. Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3. The Embo Journal. 28: 372-82. PMID 19153604 DOI: 10.1038/emboj.2008.289 |
0.338 |
|
| 2008 |
Winborn BJ, Travis SM, Todi SV, Scaglione KM, Xu P, Williams AJ, Cohen RE, Peng J, Paulson HL. The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains. The Journal of Biological Chemistry. 283: 26436-43. PMID 18599482 DOI: 10.1074/Jbc.M803692200 |
0.364 |
|
| 2007 |
Scaglione KM, Bansal PK, Deffenbaugh AE, Kiss A, Moore JM, Korolev S, Cocklin R, Goebl M, Kitagawa K, Skowyra D. SCF E3-mediated autoubiquitination negatively regulates activity of Cdc34 E2 but plays a nonessential role in the catalytic cycle in vitro and in vivo. Molecular and Cellular Biology. 27: 5860-70. PMID 17562869 DOI: 10.1128/Mcb.01555-06 |
0.654 |
|
| 2007 |
Kim HT, Kim KP, Lledias F, Kisselev AF, Scaglione KM, Skowyra D, Gygi SP, Goldberg AL. Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages. The Journal of Biological Chemistry. 282: 17375-86. PMID 17426036 DOI: 10.1074/Jbc.M609659200 |
0.639 |
|
| 2003 |
Deffenbaugh AE, Scaglione KM, Zhang L, Moore JM, Buranda T, Sklar LA, Skowyra D. Release of ubiquitin-charged Cdc34-S - Ub from the RING domain is essential for ubiquitination of the SCF(Cdc4)-bound substrate Sic1. Cell. 114: 611-22. PMID 13678584 DOI: 10.1016/S0092-8674(03)00641-X |
0.651 |
|
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