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Developmental regulation of protein O-GlcNAcylation, O-GlcNAc transferase, and O-GlcNAcase in mammalian brain
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scholarly article
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stated in
PubMed
PubMed ID
22928023
retrieved
31 January 2017
title
Developmental regulation of protein O-GlcNAcylation, O-GlcNAc transferase, and O-GlcNAcase in mammalian brain
(English)
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PubMed
PubMed ID
22928023
retrieved
31 January 2017
main subject
brain
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author
Inge Grundke-Iqbal
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9
object named as
Inge Grundke-Iqbal
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PubMed
PubMed ID
22928023
retrieved
31 January 2017
Cheng-Xin Gong
series ordinal
12
object named as
Cheng-Xin Gong
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PubMed
PubMed ID
22928023
retrieved
31 January 2017
author name string
Ying Liu
series ordinal
1
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PubMed
PubMed ID
22928023
retrieved
31 January 2017
Xiaojing Li
series ordinal
2
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stated in
PubMed
PubMed ID
22928023
retrieved
31 January 2017
Yang Yu
series ordinal
3
1 reference
stated in
PubMed
PubMed ID
22928023
retrieved
31 January 2017
Jianhua Shi
series ordinal
4
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PubMed
PubMed ID
22928023
retrieved
31 January 2017
Zhihou Liang
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5
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PubMed
PubMed ID
22928023
retrieved
31 January 2017
Xiaoqin Run
series ordinal
6
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stated in
PubMed
PubMed ID
22928023
retrieved
31 January 2017
Yi Li
series ordinal
7
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PubMed
PubMed ID
22928023
retrieved
31 January 2017
Chun-ling Dai
series ordinal
8
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PubMed
PubMed ID
22928023
retrieved
31 January 2017
Khalid Iqbal
series ordinal
10
1 reference
stated in
PubMed
PubMed ID
22928023
retrieved
31 January 2017
Fei Liu
series ordinal
11
1 reference
stated in
PubMed
PubMed ID
22928023
retrieved
31 January 2017
language of work or name
English
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publication date
1 January 2012
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stated in
PubMed
PubMed ID
22928023
retrieved
31 January 2017
published in
PLOS One
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stated in
PubMed
PubMed ID
22928023
retrieved
31 January 2017
volume
7
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stated in
PubMed
PubMed ID
22928023
retrieved
31 January 2017
issue
8
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stated in
PubMed
PubMed ID
22928023
retrieved
31 January 2017
page(s)
e43724
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stated in
PubMed
PubMed ID
22928023
retrieved
31 January 2017
copyright license
Creative Commons Attribution 4.0 International
start time
22 August 2012
1 reference
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April 2022 Public Data File from Crossref
copyright status
copyrighted
0 references
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Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-modified proteins from the brain
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Aberrant glycosylation modulates phosphorylation of tau by protein kinase A and dephosphorylation of tau by protein phosphatase 2A and 5
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Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain
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The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny
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Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity
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Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats
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Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats
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Glycosylation of mammalian neurofilaments. Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M
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Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets
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The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways
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Dysregulation of the nutrient/stress sensor O-GlcNAcylation is involved in the etiology of cardiovascular disorders, type-2 diabetes and Alzheimer's disease.
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Brain glucose transporters, O-GlcNAcylation and phosphorylation of tau in diabetes and Alzheimer's disease
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The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine
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29 September 2017
Cross-talk between GlcNAcylation and phosphorylation: site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc
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29 September 2017
Murine platelets are not regulated by O-linked beta-N-acetylglucosamine
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29 September 2017
Regulation between O-GlcNAcylation and phosphorylation of neurofilament-M and their dysregulation in Alzheimer disease
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Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation
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29 September 2017
O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease
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Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability
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3 June 2018
Direct in-gel fluorescence detection and cellular imaging of O-GlcNAc-modified proteins
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3 June 2018
Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation.
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27 November 2018
Human Alzheimer's disease synaptic O-GlcNAc site mapping and iTRAQ expression proteomics with ion trap mass spectrometry
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27 November 2018
Enzymatic characterization and inhibition of the nuclear variant of human O-GlcNAcase
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27 November 2018
Alloxan is an inhibitor of O-GlcNAc-selective N-acetyl-beta-D-glucosaminidase.
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Concurrent alterations of O-GlcNAcylation and phosphorylation of tau in mouse brains during fasting.
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27 November 2018
Parallel identification of O-GlcNAc-modified proteins from cell lysates
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27 November 2018
UDP-N-acetylglucosaminyl transferase (OGT) in brain tissue: temperature sensitivity and subcellular distribution of cytosolic and nuclear enzyme
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27 November 2018
Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene
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27 November 2018
O-GlcNAc expression in developing and ageing mouse brain
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27 November 2018
O-linked N-acetylglucosamine levels in cerebellar neurons respond reciprocally to pertubations of phosphorylation.
1 reference
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27 November 2018
Assay of proteins in the presence of interfering materials
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/22928023
retrieved
12 December 2020
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inferred from PubMed ID database lookup
Identifiers
DOI
10.1371/JOURNAL.PONE.0043724
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2477944
ADS bibcode
2012PLoSO...743724L
0 references
OpenCitations bibliographic resource ID
2477944
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2477944
PMCID
3425547
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2477944
PubMed ID
22928023
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2477944
ResearchGate publication ID
230749464
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