bridging the gap between glycosylation and vesicle traffic

Clicks: 202
ID: 258695
2016
Free PDF
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal
Steady

Ranked #47 of 54 articles by views in autonomous agents and multi-agent systems

Most read Least read

Bar heights use a square-root scale.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Sign in to mint
Abstract
Glycosylation is recognised as a vitally important posttranslational modification. The structure of glycans that decorate proteins and lipids is largely dictated by biosynthetic reactions occurring in the Golgi apparatus. This biosynthesis relies on the relative distribution of glycosyltransferases and glycosidases, which is maintained by retrograde vesicle traffic between Golgi cisternae. Tethering of vesicles at the Golgi apparatus prior to fusion is regulated by Rab GTPases, coiled-coil tethers termed golgins and the multisubunit tethering complex known as the conserved oligomeric Golgi (COG) complex. In this review we discuss the mechanisms involved in vesicle tethering at the Golgi apparatus and highlight the importance of tethering in the context of glycan biosynthesis and a set of diseases known as congenital disorders of glycosylation.
Reference Key
eungar2016frontiersbridging Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Daniel eUngar;Peter eFisher
Journal autonomous agents and multi-agent systems
Year 2016
DOI
10.3389/fcell.2016.00015
URL
http://journal.frontiersin.org/Journal/10.3389/fcell.2016.00015/full
Keywords
golgi apparatus congenital disorders of glycosylation

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

Comments

No comments yet. Be the first to comment on this article.