Roles of N-linked glycans in the endoplasmic reticulum.

By Ari Helenius, M. Aebi. Annual Review of Biochemistry, 2004

2,077 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology, Organic Chemistry

View Paper: https://www.semanticscholar.org/paper/08f7204dcf7f5ca4fe7d013aec71d0a4bbd9cec7

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. S. Marciniak
2. A. Varki
3. Jerry Eichler
4. J. Marth
5. M. Molinari
6. D. Ron
7. D. Hebert
8. M. Aebi

In Molecular Biology

1. A. Varki
2. S. Marciniak
3. Jerry Eichler
4. J. Marth
5. Michael W. W. Adams
6. M. Molinari
7. Dihua Yu
8. D. Ron

In Organic Chemistry

1. A. Varki
2. Jerry Eichler
3. J. Marth
4. M. Aebi

Citations in the corpus

• Endoplasmic reticulum stress signaling in disease. (2006, background): “In addition, other catalysts directly promote correct folding by the addition of carbohydrates (63), cis-trans isomerization about peptide bonds (166), and the creation and rearrangement of disulfide bonds (189).”
• Posttranslational Protein Modification in Archaea (2005, background): “If, as proposed (46, 157), the elaborate process responsible”
• Glycosylation and stabilization of programmed death ligand-1 suppresses T-cell activity (2016, positive): “N -glycosylation affects a number of biological processes, including the modulation of protein–protein interactions 12 .”
• Glycosylation in cellular mechanisms of health and disease. (2006, background): “Both lectin binding by chaperones and steric effects of glycans contribute substantially to protein folding prior to trafficking to the Golgi and beyond by reducing protein aggregation and retaining nascent unfolded glycoproteins in the endoplasmic reticulum (Parodi, 2000; Helenius and Aebi, 2004).”
• In and out of the ER: protein folding, quality control, degradation, and related human diseases. (2007, background): “2) and generally slows the folding reaction helping to increase its overall efficiency (145).”
• N-linked protein glycosylation in the ER. (2013, background): “In addition, this shift in the temporal order of maturation events is a prerequisite for using N-linked glycans as “universal signals” to modulate and control N-glycoprotein folding [6]: N-linked glycans can direct the folding machinery to defined regions of the polypeptide and the differentially pr”
• ERAD: the long road to destruction (2005, background): “For example, in mammalian cells, the lectin-type chaperones calnexin/calreticulin (CNX/CRT) retain immature glycoproteins in the ER and assist their foldin”
• Molecular chaperones and protein quality control. (2006, neutral): “Review”
• Biological roles of glycans (2016, background): “However, even after the last glucose residue has been permanently removed, there are further steps of recognition of the oligomannose type N-glycans that have been partially processed by ER mannosidases (879) (880) (881) (882) (883) (884) .”