Comment on “The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation”

10.1371/journal.pone.0180005

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Main Authors:	Bard F., Chia J.
Other Authors:	BIOCHEMISTRY
Format:	Article
Published:	Public Library of Science 2020
Subjects:	epidermal growth factor mitogen activated protein kinase 1 mitogen activated protein kinase 3 n acetylgalactosamine n acetylgalactosaminyltransferase n acetylgalactosaminyltransferase 1 n acetylgalactosaminyltransferase 2 n acetylgalactosaminyltransferase 3 n acetylgalactosaminyltransferase 4 n acetylgalactosaminyltransferase 6 platelet derived growth factor protein tyrosine kinase Tn antigen unclassified drug glycopeptide mucin carbohydrate metabolism catalysis endoplasmic reticulum enzyme activation enzyme activity enzyme localization gene expression Golgi complex n acetylgalactosamine T activation pathway Note protein glycosylation signal transduction glycosylation human Glycopeptides Glycosylation Humans Mucins N-Acetylgalactosaminyltransferases
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/165786
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1657862024-11-09T05:16:16Z Comment on “The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation” Bard F. Chia J. BIOCHEMISTRY epidermal growth factor mitogen activated protein kinase 1 mitogen activated protein kinase 3 n acetylgalactosamine n acetylgalactosaminyltransferase n acetylgalactosaminyltransferase 1 n acetylgalactosaminyltransferase 2 n acetylgalactosaminyltransferase 3 n acetylgalactosaminyltransferase 4 n acetylgalactosaminyltransferase 6 platelet derived growth factor protein tyrosine kinase Tn antigen unclassified drug glycopeptide mucin n acetylgalactosaminyltransferase carbohydrate metabolism catalysis endoplasmic reticulum enzyme activation enzyme activity enzyme localization gene expression Golgi complex n acetylgalactosamine T activation pathway Note protein glycosylation signal transduction glycosylation human Glycopeptides Glycosylation Humans Mucins N-Acetylgalactosaminyltransferases 10.1371/journal.pone.0180005 PLoS ONE 12 7 e0180005 2020-03-19T09:01:38Z 2020-03-19T09:01:38Z 2017 Article Bard F., Chia J. (2017). Comment on “The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation”. PLoS ONE 12 (7) : e0180005. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0180005 1932-6203 https://scholarbank.nus.edu.sg/handle/10635/165786 Public Library of Science Unpaywall 20200320
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	epidermal growth factor mitogen activated protein kinase 1 mitogen activated protein kinase 3 n acetylgalactosamine n acetylgalactosaminyltransferase n acetylgalactosaminyltransferase 1 n acetylgalactosaminyltransferase 2 n acetylgalactosaminyltransferase 3 n acetylgalactosaminyltransferase 4 n acetylgalactosaminyltransferase 6 platelet derived growth factor protein tyrosine kinase Tn antigen unclassified drug glycopeptide mucin n acetylgalactosaminyltransferase carbohydrate metabolism catalysis endoplasmic reticulum enzyme activation enzyme activity enzyme localization gene expression Golgi complex n acetylgalactosamine T activation pathway Note protein glycosylation signal transduction glycosylation human Glycopeptides Glycosylation Humans Mucins N-Acetylgalactosaminyltransferases
spellingShingle	epidermal growth factor mitogen activated protein kinase 1 mitogen activated protein kinase 3 n acetylgalactosamine n acetylgalactosaminyltransferase n acetylgalactosaminyltransferase 1 n acetylgalactosaminyltransferase 2 n acetylgalactosaminyltransferase 3 n acetylgalactosaminyltransferase 4 n acetylgalactosaminyltransferase 6 platelet derived growth factor protein tyrosine kinase Tn antigen unclassified drug glycopeptide mucin n acetylgalactosaminyltransferase carbohydrate metabolism catalysis endoplasmic reticulum enzyme activation enzyme activity enzyme localization gene expression Golgi complex n acetylgalactosamine T activation pathway Note protein glycosylation signal transduction glycosylation human Glycopeptides Glycosylation Humans Mucins N-Acetylgalactosaminyltransferases Bard F. Chia J. Comment on “The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation”
description	10.1371/journal.pone.0180005
author2	BIOCHEMISTRY
author_facet	BIOCHEMISTRY Bard F. Chia J.
format	Article
author	Bard F. Chia J.
author_sort	Bard F.
title	Comment on “The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation”
title_short	Comment on “The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation”
title_full	Comment on “The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation”
title_fullStr	Comment on “The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation”
title_full_unstemmed	Comment on “The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation”
title_sort	comment on “the galnac-t activation pathway (gala) is not a general mechanism for regulating mucin-type o-glycosylation”
publisher	Public Library of Science
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/165786
_version_	1821221374261198848

Comment on “The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation”

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