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Items: 1 to 20 of 32

1.

Structures of mammalian ER α-glucosidase II capture the binding modes of broad-spectrum iminosugar antivirals.

Caputo AT, Alonzi DS, Marti L, Reca IB, Kiappes JL, Struwe WB, Cross A, Basu S, Lowe ED, Darlot B, Santino A, Roversi P, Zitzmann N.

Proc Natl Acad Sci U S A. 2016 Aug 9;113(32):E4630-8. doi: 10.1073/pnas.1604463113. Epub 2016 Jul 26.

PMID:
27462106
2.

Htm1p-Pdi1p is a folding-sensitive mannosidase that marks N-glycoproteins for ER-associated protein degradation.

Liu YC, Fujimori DG, Weissman JS.

Proc Natl Acad Sci U S A. 2016 Jul 12;113(28):E4015-24. doi: 10.1073/pnas.1608795113. Epub 2016 Jun 28.

PMID:
27357682
3.

Genetic dissection of mammalian ERAD through comparative haploid and CRISPR forward genetic screens.

Timms RT, Menzies SA, Tchasovnikarova IA, Christensen LC, Williamson JC, Antrobus R, Dougan G, Ellgaard L, Lehner PJ.

Nat Commun. 2016 Jun 10;7:11786. doi: 10.1038/ncomms11786.

4.

Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control.

Satoh T, Toshimori T, Yan G, Yamaguchi T, Kato K.

Sci Rep. 2016 Feb 5;6:20575. doi: 10.1038/srep20575.

5.

Thyroglobulin From Molecular and Cellular Biology to Clinical Endocrinology.

Di Jeso B, Arvan P.

Endocr Rev. 2016 Feb;37(1):2-36. doi: 10.1210/er.2015-1090. Epub 2015 Nov 23.

PMID:
26595189
6.

The UDP-glucose: glycoprotein glucosyltransferase (UGGT), a key enzyme in ER quality control, plays a significant role in plant growth as well as biotic and abiotic stress in Arabidopsis thaliana.

Blanco-Herrera F, Moreno AA, Tapia R, Reyes F, Araya M, D'Alessio C, Parodi A, Orellana A.

BMC Plant Biol. 2015 May 28;15:127. doi: 10.1186/s12870-015-0525-2.

7.

Transcriptional regulation of secretory capacity by bZip transcription factors.

Fox RM, Andrew DJ.

Front Biol (Beijing). 2015 Feb 1;10(1):28-51.

8.

Glucosidase II and MRH-domain containing proteins in the secretory pathway.

D'Alessio C, Dahms NM.

Curr Protein Pept Sci. 2015;16(1):31-48. Review.

9.

Effects of N-glycan precursor length diversity on quality control of protein folding and on protein glycosylation.

Samuelson J, Robbins PW.

Semin Cell Dev Biol. 2015 May;41:121-8. doi: 10.1016/j.semcdb.2014.11.008. Epub 2014 Dec 2. Review.

11.

Reglucosylation by UDP-glucose:glycoprotein glucosyltransferase 1 delays glycoprotein secretion but not degradation.

Tannous A, Patel N, Tamura T, Hebert DN.

Mol Biol Cell. 2015 Feb 1;26(3):390-405. doi: 10.1091/mbc.E14-08-1254. Epub 2014 Nov 26.

12.

A context-independent N-glycan signal targets the misfolded extracellular domain of Arabidopsis STRUBBELIG to endoplasmic-reticulum-associated degradation.

Hüttner S, Veit C, Vavra U, Schoberer J, Dicker M, Maresch D, Altmann F, Strasser R.

Biochem J. 2014 Dec 15;464(3):401-11. doi: 10.1042/BJ20141057.

13.

Novel roles for O-linked glycans in protein folding.

Vasudevan D, Haltiwanger RS.

Glycoconj J. 2014 Oct;31(6-7):417-26. doi: 10.1007/s10719-014-9556-4.

14.

Expression of α-subunit of α-glucosidase II in adult mouse brain regions and selected organs.

Anji A, Miller H, Raman C, Phillips M, Ciment G, Kumari M.

J Neurosci Res. 2015 Jan;93(1):82-93. doi: 10.1002/jnr.23470. Epub 2014 Aug 18.

15.

Endoplasmic reticulum-mediated protein quality control in Arabidopsis.

Liu Y, Li J.

Front Plant Sci. 2014 Apr 30;5:162. doi: 10.3389/fpls.2014.00162. eCollection 2014. Review.

16.

Glycoprotein folding and quality-control mechanisms in protein-folding diseases.

Ferris SP, Kodali VK, Kaufman RJ.

Dis Model Mech. 2014 Mar;7(3):331-41. doi: 10.1242/dmm.014589. Review.

17.

Structural basis for disparate sugar-binding specificities in the homologous cargo receptors ERGIC-53 and VIP36.

Satoh T, Suzuki K, Yamaguchi T, Kato K.

PLoS One. 2014 Feb 3;9(2):e87963. doi: 10.1371/journal.pone.0087963. eCollection 2014.

18.

Glycan-dependent and -independent interactions contribute to cellular substrate recruitment by calreticulin.

Wijeyesakere SJ, Rizvi SM, Raghavan M.

J Biol Chem. 2013 Dec 6;288(49):35104-16. doi: 10.1074/jbc.M113.507921. Epub 2013 Oct 7.

19.

UDP-glucose:glycoprotein glucosyltransferase (UGGT1) promotes substrate solubility in the endoplasmic reticulum.

Ferris SP, Jaber NS, Molinari M, Arvan P, Kaufman RJ.

Mol Biol Cell. 2013 Sep;24(17):2597-608. doi: 10.1091/mbc.E13-02-0101. Epub 2013 Jul 17.

20.

Structure of the lectin mannose 6-phosphate receptor homology (MRH) domain of glucosidase II, an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum.

Olson LJ, Orsi R, Alculumbre SG, Peterson FC, Stigliano ID, Parodi AJ, D'Alessio C, Dahms NM.

J Biol Chem. 2013 Jun 7;288(23):16460-75. doi: 10.1074/jbc.M113.450239. Epub 2013 Apr 22.

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