O-linked N-acetylglucosamine transferase (OGT) is overexpressed and promotes O-linked protein glycosylation in esophageal squamous cell carcinoma (Q36682124)

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scientific article published on 25 June 2012

Language	Label	Description	Also known as
English	O-linked N-acetylglucosamine transferase (OGT) is overexpressed and promotes O-linked protein glycosylation in esophageal squamous cell carcinoma	scientific article published on 25 June 2012

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scholarly article

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27 February 2020

O-linked N-acetylglucosamine transferase (OGT) is overexpressed and promotes O-linked protein glycosylation in esophageal squamous cell carcinoma (English)

1 reference

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27 February 2020

1 reference

based on heuristic

inferred from title

1 reference

based on heuristic

inferred from title

esophageal squamous cell carcinoma

1 reference

based on heuristic

inferred from title

8

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27 February 2020

author name string

Zhe Qiao

1

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27 February 2020

Chengxue Dang

2

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27 February 2020

Bin Zhou

3

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27 February 2020

Shaomin Li

4

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27 February 2020

Wei Zhang

5

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27 February 2020

Jiantao Jiang

6

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27 February 2020

Jin Zhang

7

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27 February 2020

Yuefeng Ma

9

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27 February 2020

publication date

25 June 2012

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27 February 2020

Journal of biomedical research

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27 February 2020

26

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27 February 2020

268-273

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27 February 2020

4

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27 February 2020

O-GlcNAcylation plays a role in tumor recurrence of hepatocellular carcinoma following liver transplantation

1 reference

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O-GlcNAcylation is a novel regulator of lung and colon cancer malignancy

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GlcNAcylation plays an essential role in breast cancer metastasis

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Nutrient sensor O-GlcNAc transferase regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1.

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The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways

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O-GlcNAc modulation at Akt1 Ser473 correlates with apoptosis of murine pancreatic beta cells

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O-GlcNAc regulates FoxO activation in response to glucose

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Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins

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Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability

1 reference

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30 September 2017

Identification of Asp174 and Asp175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants

1 reference

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The hexosamine signaling pathway: deciphering the "O-GlcNAc code"

1 reference

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Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes

1 reference

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30 September 2017

Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain

1 reference

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Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol.

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Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine

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1 reference

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1 reference

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1 reference

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1 reference

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12 December 2020

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Identifiers

10.7555/JBR.26.20110121

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27 February 2020

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27 February 2020

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27 February 2020

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