scholarly article | Q13442814 |
P6179 | Dimensions Publication ID | 1031807460 |
P356 | DOI | 10.1038/NSMB0204-108 |
P698 | PubMed publication ID | 14749767 |
P2093 | author name string | Richard N Sifers | |
P2860 | cites work | Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis | Q22010397 |
Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle | Q24296412 | ||
Checkpoints: controls that ensure the order of cell cycle events | Q28131705 | ||
EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin | Q28212764 | ||
Setting the standards: quality control in the secretory pathway | Q29620321 | ||
Elucidation of the molecular logic by which misfolded alpha 1-antitrypsin is preferentially selected for degradation. | Q30332997 | ||
Organizational diversity among distinct glycoprotein endoplasmic reticulum-associated degradation programs | Q33902839 | ||
Protein glucosylation and its role in protein folding | Q34019347 | ||
Glycopeptide specificity of the secretory protein folding sensor UDP-glucose glycoprotein:glucosyltransferase. | Q34236548 | ||
Dissecting glycoprotein quality control in the secretory pathway | Q34394333 | ||
The action of molecular chaperones in the early secretory pathway | Q34432209 | ||
Protein degradation in the endoplasmic reticulum | Q37947738 | ||
Conformation-independent binding of monoglucosylated ribonuclease B to calnexin | Q38349363 | ||
Quality control in the secretory pathway | Q40380586 | ||
The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation | Q47256575 | ||
Recognition of local glycoprotein misfolding by the ER folding sensor UDP-glucose:glycoprotein glucosyltransferase | Q73606685 | ||
Calnexin, calreticulin and the folding of glycoproteins | Q80818194 | ||
P433 | issue | 2 | |
P304 | page(s) | 108-109 | |
P577 | publication date | 2004-02-01 | |
P1433 | published in | Nature Structural & Molecular Biology | Q1071739 |
P1476 | title | Insights into checkpoint capacity | |
P478 | volume | 11 |
Q33761462 | Evasion of endoplasmic reticulum surveillance makes Wsc1p an obligate substrate of Golgi quality control |
Q91738942 | Mutually exclusive locales for N-linked glycans and disorder in human glycoproteins |
Q36438832 | Sequestration of mutated alpha1-antitrypsin into inclusion bodies is a cell-protective mechanism to maintain endoplasmic reticulum function. |
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