|
|
|
|
| LEADER |
01000caa a22002652 4500 |
| 001 |
NLM253025001 |
| 003 |
DE-627 |
| 005 |
20250219044450.0 |
| 007 |
cr uuu---uuuuu |
| 008 |
231224s2015 xx |||||o 00| ||eng c |
| 024 |
7 |
|
|a 10.1016/j.plantsci.2015.06.023
|2 doi
|
| 028 |
5 |
2 |
|a pubmed25n0843.xml
|
| 035 |
|
|
|a (DE-627)NLM253025001
|
| 035 |
|
|
|a (NLM)26398792
|
| 035 |
|
|
|a (PII)S0168-9452(15)30005-4
|
| 040 |
|
|
|a DE-627
|b ger
|c DE-627
|e rakwb
|
| 041 |
|
|
|a eng
|
| 100 |
1 |
|
|a Lannoo, Nausicaä
|e verfasserin
|4 aut
|
| 245 |
1 |
0 |
|a Review/N-glycans
|b The making of a varied toolbox
|
| 264 |
|
1 |
|c 2015
|
| 336 |
|
|
|a Text
|b txt
|2 rdacontent
|
| 337 |
|
|
|a ƒaComputermedien
|b c
|2 rdamedia
|
| 338 |
|
|
|a ƒa Online-Ressource
|b cr
|2 rdacarrier
|
| 500 |
|
|
|a Date Completed 12.07.2016
|
| 500 |
|
|
|a Date Revised 10.03.2022
|
| 500 |
|
|
|a published: Print-Electronic
|
| 500 |
|
|
|a Citation Status MEDLINE
|
| 520 |
|
|
|a Copyright © 2015 Elsevier Ireland Ltd. All rights reserved.
|
| 520 |
|
|
|a Asparagine (N)-linked protein glycosylation is one of the most crucial, prevalent, and complex co- and post-translational protein modifications. It plays a pivotal role in protein folding, quality control, and endoplasmic reticulum (ER)-associated degradation (ERAD) as well as in protein sorting, protein function, and in signal transduction. Furthermore, glycosylation modulates many important biological processes including growth, development, morphogenesis, and stress signaling processes. As a consequence, aberrant or altered N-glycosylation is often associated with reduced fitness, diseases, and disorders. The initial steps of N-glycan synthesis at the cytosolic side of the ER membrane and in the lumen of the ER are highly conserved. In contrast, the final N-glycan processing in the Golgi apparatus is organism-specific giving rise to a wide variety of carbohydrate structures. Despite our vast knowledge on N-glycans in yeast and mammals, the modus operandi of N-glycan signaling in plants is still largely unknown. This review will elaborate on the N-glycosylation biosynthesis pathway in plants but will also critically assess how N-glycans are involved in different signaling cascades, either active during normal development or upon abiotic and biotic stresses
|
| 650 |
|
4 |
|a Journal Article
|
| 650 |
|
4 |
|a Research Support, Non-U.S. Gov't
|
| 650 |
|
4 |
|a Review
|
| 650 |
|
4 |
|a Carbohydrate
|
| 650 |
|
4 |
|a ER
|
| 650 |
|
4 |
|a ERAD
|
| 650 |
|
4 |
|a Golgi
|
| 650 |
|
4 |
|a N-Glycan
|
| 650 |
|
4 |
|a Plant immunity
|
| 650 |
|
7 |
|a Polysaccharides
|2 NLM
|
| 700 |
1 |
|
|a Van Damme, Els J M
|e verfasserin
|4 aut
|
| 773 |
0 |
8 |
|i Enthalten in
|t Plant science : an international journal of experimental plant biology
|d 1985
|g 239(2015) vom: 20. Okt., Seite 67-83
|w (DE-627)NLM098174193
|x 1873-2259
|7 nnns
|
| 773 |
1 |
8 |
|g volume:239
|g year:2015
|g day:20
|g month:10
|g pages:67-83
|
| 856 |
4 |
0 |
|u http://dx.doi.org/10.1016/j.plantsci.2015.06.023
|3 Volltext
|
| 912 |
|
|
|a GBV_USEFLAG_A
|
| 912 |
|
|
|a SYSFLAG_A
|
| 912 |
|
|
|a GBV_NLM
|
| 912 |
|
|
|a GBV_ILN_350
|
| 951 |
|
|
|a AR
|
| 952 |
|
|
|d 239
|j 2015
|b 20
|c 10
|h 67-83
|