The 17-residue transmembrane domain of β-galactoside α2,6-sialyltransferase is sufficient for golgi retention
Journal of Cell Biology
Saved in:
Main Authors: | Wong, S.H., Low, S.H., Hong, W. |
---|---|
Other Authors: | INSTITUTE OF MOLECULAR & CELL BIOLOGY |
Format: | Article |
Published: |
2014
|
Online Access: | http://scholarbank.nus.edu.sg/handle/10635/112102 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | National University of Singapore |
Similar Items
-
Golgi-localized β-galactoside α2,6-sialyltransferase in transfected CHO cells is redistributed into the endoplasmic reticulum by brefeldin A
by: Tang, B.L., et al.
Published: (2014) -
TARGETING SIGNAL(S) THAT MEDIATE LOCALIZATION OF [BETA]-GALACTOSIDE [ALPHA]2,6-SIALYLTRANSFERASE AND TGN38 TO THE GOLGI APPARATUS
by: WONG SIEW HENG
Published: (2020) -
The transmembrane domain of N-glucosaminyltransferase I contains a Golgi retention signal
by: Tang, B.L., et al.
Published: (2014) -
Cell type differences in Golgi retention signals for transmembrane proteins
by: Tang, B.L., et al.
Published: (2014) -
GPP130 stem region is necessary and sufficient for intra-Golgi cisternal rim localization of type II transmembrane proteins
by: Wong, Jing Xue
Published: (2023)