Phosphorylation of transglutaminase 2 (TG2) at serine-216 has a role in TG2 mediated activation of nuclear factor-kappa B and in the downregulation of PTEN (Q34324624)

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English	Phosphorylation of transglutaminase 2 (TG2) at serine-216 has a role in TG2 mediated activation of nuclear factor-kappa B and in the downregulation of PTEN	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

Phosphorylation of transglutaminase 2 (TG2) at serine-216 has a role in TG2 mediated activation of nuclear factor-kappa B and in the downregulation of PTEN (English)

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

phosphorylation

1 reference

based on heuristic

inferred from title

author name string

Yi Wang

1

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

Sudharsana R Ande

2

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

Suresh Mishra

3

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Europe PubMed Central

PubMed publication ID

1 August 2017

language of work or name

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publication date

3 July 2012

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Europe PubMed Central

PubMed publication ID

1 August 2017

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Europe PubMed Central

PubMed publication ID

1 August 2017

12

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Europe PubMed Central

PubMed publication ID

1 August 2017

277

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

Overexpression of phospho mutant forms of transglutaminase 2 downregulates epidermal growth factor receptor

1 reference

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Non-genomic loss of PTEN function in cancer: not in my genes.

1 reference

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1 reference

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1 reference

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Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer

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Transglutaminase 2 kinase activity facilitates protein kinase A-induced phosphorylation of retinoblastoma protein

1 reference

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Tissue transglutaminase expression promotes cell attachment, invasion and survival in breast cancer cells

1 reference

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Overexpression of tissue transglutaminase leads to constitutive activation of nuclear factor-kappaB in cancer cells: delineation of a novel pathway

1 reference

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Mutation of a critical arginine in the GTP-binding site of transglutaminase 2 disinhibits intracellular cross-linking activity

1 reference

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Phosphorylation of histones by tissue transglutaminase.

1 reference

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Pim kinases phosphorylate multiple sites on Bad and promote 14-3-3 binding and dissociation from Bcl-XL

1 reference

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Tissue transglutaminase is a multifunctional BH3-only protein

1 reference

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Tissue transglutaminase has intrinsic kinase activity: identification of transglutaminase 2 as an insulin-like growth factor-binding protein-3 kinase

1 reference

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Insulin-like growth factor binding protein-3 interacts with autocrine motility factor/phosphoglucose isomerase (AMF/PGI) and inhibits the AMF/PGI function

1 reference

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Suppression of PTEN expression by NF-kappa B prevents apoptosis

1 reference

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Transglutaminase 2: an enigmatic enzyme with diverse functions

1 reference

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Phospholipase Cdelta1 is a guanine nucleotide exchanging factor for transglutaminase II (Galpha h) and promotes alpha 1B-adrenoreceptor-mediated GTP binding and intracellular calcium release

1 reference

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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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1 reference

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1 reference

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1 reference

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Phosphorylation of serine 276 is essential for p65 NF-kappaB subunit-dependent cellular responses

1 reference

https://api.crossref.org/works/10.1186%2F1471-2407-12-277

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A role for tissue transglutaminase in hepatic injury and fibrogenesis, and its regulation by NF-kappaB

1 reference

https://pubmed.ncbi.nlm.nih.gov/22759359

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based on heuristic

inferred from PubMed ID database lookup

The core domain of the tissue transglutaminase Gh hydrolyzes GTP and ATP

1 reference

https://pubmed.ncbi.nlm.nih.gov/22759359

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Phosphorylation of transglutaminase 2 by PKA at Ser216 creates 14-3-3 binding sites

1 reference

https://pubmed.ncbi.nlm.nih.gov/22759359

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Extracellular transglutaminase 2 has a role in cell adhesion, whereas intracellular transglutaminase 2 is involved in regulation of endothelial cell proliferation and apoptosis

1 reference

https://pubmed.ncbi.nlm.nih.gov/22759359

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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10.1186/1471-2407-12-277

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Europe PubMed Central

PubMed publication ID

1 August 2017

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PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

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