uniprot:Q9UFZ8 in citationmapping

8 results for uniprot:Q9UFZ8 in citationmapping

Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong alpha1-antitrypsin by human ER mannosidase I. Hosokawa N., Tremblay L.O., You Z., Herscovics A., Wada I., Nagata K. J. Biol. Chem. 278:26287-26294(2003) GeneRIF 11253 · Mapped (10) ER processing alpha1 2-mannosidase (ER ManI) has a role in ER-associated degradation of misfolded proteins GeneRIF 11253
Elucidation of the molecular logic by which misfolded alpha 1-antitrypsin is preferentially selected for degradation. Wu Y., Swulius M.T., Moremen K.W., Sifers R.N. Proc. Natl. Acad. Sci. U.S.A. 100:8229-8234(2003) GeneRIF 11253 · Mapped (15) Modification by endoplasmic reticulum mannosidase I (ERManI) contributes to the preferential selection of the misfolded AAT monomer for proteasomal degradation. GeneRIF 11253
Mechanism of class 1 (glycosylhydrolase family 47) {alpha}-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control. Karaveg K., Siriwardena A., Tempel W., Liu Z.J., Glushka J., Wang B.C., Moremen K.W. J. Biol. Chem. 280:16197-16207(2005) GeneRIF 11253 · Mapped (10) glycoside bond cleavage proceeds through a least motion conformational twist of a properly predisposed substrate GeneRIF 11253
Increased activity of lysosomal enzymes in the peritoneal fluid of patients with gynecologic cancers and pelvic inflammatory disease. Beratis N.G., Kaperonis A., Eliopoulou M.I., Kourounis G., Tzingounis V.A. J. Cancer Res. Clin. Oncol. 131:371-376(2005) GeneRIF 11253 · Mapped (16) Increased activity of alpha-mannosidase in the peritoneal fluid is associated with gynecologic cancers and pelvic inflammatory disease GeneRIF 11253
Stimulation of ERAD of misfolded null Hong Kong alpha1-antitrypsin by Golgi alpha1,2-mannosidases. Hosokawa N., You Z., Tremblay L.O., Nagata K., Herscovics A. Biochem. Biophys. Res. Commun. 362:626-632(2007) GeneRIF 11253 · Mapped (21) overexpression of Golgi alpha1 2-mannosidase IA IB and IC also accelerates ERAD of terminally misfolded human alpha1-antitrypsin variant null (Hong Kong) (NHK) and mannose trimming from the N-glycans on NHK in 293 cells GeneRIF 11253
Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation. Avezov E., Frenkel Z., Ehrlich M., Herscovics A., Lederkremer G.Z. Mol. Biol. Cell 19:216-225(2008) GeneRIF 11253 · Mapped (14) ERManI is required for trimming to Man(5-6)GlcNAc(2) and for endoplasmic reticulum associated degradation in cells in vivo. GeneRIF 11253
Theory and computation show that Asp463 is the catalytic proton donor in human endoplasmic reticulum alpha-(1-->2)-mannosidase I. Cantu D., Nerinckx W., Reilly P.J. Carbohydr. Res. 343:2235-2242(2008) GeneRIF 11253 · Mapped (10) the true catalytic proton donor is Asp463 in the human endoplasmic reticulum alpha-(1-->2)-mannosidase I GeneRIF 11253
Single nucleotide polymorphism-mediated translational suppression of endoplasmic reticulum mannosidase I modifies the onset of end-stage liver disease in alpha1-antitrypsin deficiency. Pan S., Huang L., McPherson J., Muzny D., Rouhani F., Brantly M., Gibbs R., Sifers R.N. Hepatology 50:275-281(2009) GeneRIF 11253 · Mapped (10) the identified single-nucleotide polymorphism can accelerate the onset of the end-stage liver disease associated with alpha1-antitrypsin deficiency and underscore the contribution of biosynthetic quality control as a modifier of genetic disease GeneRIF 11253