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Items: 1 to 20 of 135

1.

A network of ubiquitin ligases is important for the dynamics of misfolded protein aggregates in yeast.

Theodoraki MA, Nillegoda NB, Saini J, Caplan AJ.

J Biol Chem. 2012 Jul 6;287(28):23911-22. doi: 10.1074/jbc.M112.341164. Epub 2012 May 16.

2.

The Type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein.

Summers DW, Wolfe KJ, Ren HY, Cyr DM.

PLoS One. 2013;8(1):e52099. doi: 10.1371/journal.pone.0052099. Epub 2013 Jan 16.

3.

Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1.

Eisele F, Wolf DH.

FEBS Lett. 2008 Dec 24;582(30):4143-6. doi: 10.1016/j.febslet.2008.11.015. Epub 2008 Nov 27.

4.

Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins.

Nillegoda NB, Theodoraki MA, Mandal AK, Mayo KJ, Ren HY, Sultana R, Wu K, Johnson J, Cyr DM, Caplan AJ.

Mol Biol Cell. 2010 Jul 1;21(13):2102-16. doi: 10.1091/mbc.E10-02-0098. Epub 2010 May 12.

5.

The E3 ubiquitin ligase UBE3C enhances proteasome processivity by ubiquitinating partially proteolyzed substrates.

Chu BW, Kovary KM, Guillaume J, Chen LC, Teruel MN, Wandless TJ.

J Biol Chem. 2013 Nov 29;288(48):34575-87. doi: 10.1074/jbc.M113.499350. Epub 2013 Oct 24.

6.

UBR1 promotes protein kinase quality control and sensitizes cells to Hsp90 inhibition.

Sultana R, Theodoraki MA, Caplan AJ.

Exp Cell Res. 2012 Jan 1;318(1):53-60. doi: 10.1016/j.yexcr.2011.09.010. Epub 2011 Sep 29.

7.

Molecular mass as a determinant for nuclear San1-dependent targeting of misfolded cytosolic proteins to proteasomal degradation.

Amm I, Wolf DH.

FEBS Lett. 2016 Jun;590(12):1765-75. doi: 10.1002/1873-3468.12213. Epub 2016 May 25.

PMID:
27173001
8.

Elevated proteasome capacity extends replicative lifespan in Saccharomyces cerevisiae.

Kruegel U, Robison B, Dange T, Kahlert G, Delaney JR, Kotireddy S, Tsuchiya M, Tsuchiyama S, Murakami CJ, Schleit J, Sutphin G, Carr D, Tar K, Dittmar G, Kaeberlein M, Kennedy BK, Schmidt M.

PLoS Genet. 2011 Sep;7(9):e1002253. doi: 10.1371/journal.pgen.1002253. Epub 2011 Sep 8.

9.

Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.

Wang L, Mao X, Ju D, Xie Y.

J Biol Chem. 2004 Dec 31;279(53):55218-23. Epub 2004 Oct 25.

10.

Chaperone-mediated 26S proteasome remodeling facilitates free K63 ubiquitin chain production and aggresome clearance.

Nanduri P, Hao R, Fitzpatrick T, Yao TP.

J Biol Chem. 2015 Apr 10;290(15):9455-64. doi: 10.1074/jbc.M114.627950. Epub 2015 Feb 24.

11.

Hsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligase.

Guerriero CJ, Weiberth KF, Brodsky JL.

J Biol Chem. 2013 Jun 21;288(25):18506-20. doi: 10.1074/jbc.M113.475905. Epub 2013 May 7.

12.

Prefoldin Promotes Proteasomal Degradation of Cytosolic Proteins with Missense Mutations by Maintaining Substrate Solubility.

Comyn SA, Young BP, Loewen CJ, Mayor T.

PLoS Genet. 2016 Jul 22;12(7):e1006184. doi: 10.1371/journal.pgen.1006184. eCollection 2016 Jul.

13.

Rqc1 and Ltn1 Prevent C-terminal Alanine-Threonine Tail (CAT-tail)-induced Protein Aggregation by Efficient Recruitment of Cdc48 on Stalled 60S Subunits.

Defenouillère Q, Zhang E, Namane A, Mouaikel J, Jacquier A, Fromont-Racine M.

J Biol Chem. 2016 Jun 3;291(23):12245-53. doi: 10.1074/jbc.M116.722264. Epub 2016 Apr 18.

PMID:
27129255
14.

Genome-wide analysis identifies MYND-domain protein Mub1 as an essential factor for Rpn4 ubiquitylation.

Ju D, Wang X, Xu H, Xie Y.

Mol Cell Biol. 2008 Feb;28(4):1404-12. Epub 2007 Dec 10.

15.

Exposed hydrophobicity is a key determinant of nuclear quality control degradation.

Fredrickson EK, Rosenbaum JC, Locke MN, Milac TI, Gardner RG.

Mol Biol Cell. 2011 Jul 1;22(13):2384-95. doi: 10.1091/mbc.E11-03-0256. Epub 2011 May 5.

16.

Triad3A regulates ubiquitination and proteasomal degradation of RIP1 following disruption of Hsp90 binding.

Fearns C, Pan Q, Mathison JC, Chuang TH.

J Biol Chem. 2006 Nov 10;281(45):34592-600. Epub 2006 Sep 12.

17.

Hul5 ubiquitin ligase: good riddance to bad proteins.

Fang NN, Mayor T.

Prion. 2012 Jul 1;6(3):240-4. doi: 10.4161/pri.19929. Epub 2012 Jul 1. Review.

18.

Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting.

Shiber A, Breuer W, Brandeis M, Ravid T.

Mol Biol Cell. 2013 Jul;24(13):2076-87. doi: 10.1091/mbc.E13-01-0010. Epub 2013 May 1.

19.

The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system.

Park SH, Bolender N, Eisele F, Kostova Z, Takeuchi J, Coffino P, Wolf DH.

Mol Biol Cell. 2007 Jan;18(1):153-65. Epub 2006 Oct 25.

20.

The San1 Ubiquitin Ligase Functions Preferentially with Ubiquitin-conjugating Enzyme Ubc1 during Protein Quality Control.

Ibarra R, Sandoval D, Fredrickson EK, Gardner RG, Kleiger G.

J Biol Chem. 2016 Sep 2;291(36):18778-90. doi: 10.1074/jbc.M116.737619. Epub 2016 Jul 12.

PMID:
27405755

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