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Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates.

Rosenbaum JC, Fredrickson EK, Oeser ML, Garrett-Engele CM, Locke MN, Richardson LA, Nelson ZW, Hetrick ED, Milac TI, Gottschling DE, Gardner RG.

Mol Cell. 2011 Jan 7;41(1):93-106. doi: 10.1016/j.molcel.2010.12.004.


Molecular chaperones and substrate ubiquitination control the efficiency of endoplasmic reticulum-associated degradation.

Goeckeler JL, Brodsky JL.

Diabetes Obes Metab. 2010 Oct;12 Suppl 2:32-8. doi: 10.1111/j.1463-1326.2010.01273.x. Review.


Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms.

Buchberger A, Bukau B, Sommer T.

Mol Cell. 2010 Oct 22;40(2):238-52. doi: 10.1016/j.molcel.2010.10.001. Review.


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.


Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1.

Heck JW, Cheung SK, Hampton RY.

Proc Natl Acad Sci U S A. 2010 Jan 19;107(3):1106-11. doi: 10.1073/pnas.0910591107. Epub 2009 Dec 28.


ANCHOR: web server for predicting protein binding regions in disordered proteins.

Dosztányi Z, Mészáros B, Simon I.

Bioinformatics. 2009 Oct 15;25(20):2745-6. doi: 10.1093/bioinformatics/btp518. Epub 2009 Aug 28.


Substrate binding site flexibility of the small heat shock protein molecular chaperones.

Jaya N, Garcia V, Vierling E.

Proc Natl Acad Sci U S A. 2009 Sep 15;106(37):15604-9. doi: 10.1073/pnas.0902177106. Epub 2009 Aug 26.


Intranuclear degradation of polyglutamine aggregates by the ubiquitin-proteasome system.

Iwata A, Nagashima Y, Matsumoto L, Suzuki T, Yamanaka T, Date H, Deoka K, Nukina N, Tsuji S.

J Biol Chem. 2009 Apr 10;284(15):9796-803. doi: 10.1074/jbc.M809739200. Epub 2009 Feb 13.


The unfoldomics decade: an update on intrinsically disordered proteins.

Dunker AK, Oldfield CJ, Meng J, Romero P, Yang JY, Chen JW, Vacic V, Obradovic Z, Uversky VN.

BMC Genomics. 2008 Sep 16;9 Suppl 2:S1. doi: 10.1186/1471-2164-9-S2-S1.


Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery.

Metzger MB, Maurer MJ, Dancy BM, Michaelis S.

J Biol Chem. 2008 Nov 21;283(47):32302-16. doi: 10.1074/jbc.M806424200. Epub 2008 Sep 23.


Abnormalities of the nucleus and nuclear inclusions in neurodegenerative disease: a work in progress.

Woulfe JM.

Neuropathol Appl Neurobiol. 2007 Feb;33(1):2-42. Review.


Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes.

Haynes C, Oldfield CJ, Ji F, Klitgord N, Cusick ME, Radivojac P, Uversky VN, Vidal M, Iakoucheva LM.

PLoS Comput Biol. 2006 Aug 4;2(8):e100. Epub 2006 Jun 23.


A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery.

Gauss R, Jarosch E, Sommer T, Hirsch C.

Nat Cell Biol. 2006 Aug;8(8):849-54. Epub 2006 Jul 16.


PML clastosomes prevent nuclear accumulation of mutant ataxin-7 and other polyglutamine proteins.

Janer A, Martin E, Muriel MP, Latouche M, Fujigasaki H, Ruberg M, Brice A, Trottier Y, Sittler A.

J Cell Biol. 2006 Jul 3;174(1):65-76.


The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment.

Gauss R, Sommer T, Jarosch E.

EMBO J. 2006 May 3;25(9):1827-35. Epub 2006 Apr 13.


Assessing protein disorder and induced folding.

Receveur-Bréchot V, Bourhis JM, Uversky VN, Canard B, Longhi S.

Proteins. 2006 Jan 1;62(1):24-45. Review.


Opinion: What is the role of protein aggregation in neurodegeneration?

Ross CA, Poirier MA.

Nat Rev Mol Cell Biol. 2005 Nov;6(11):891-8. Review.


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