Regulated phosphorylation of a major UDP-glucuronosyltransferase isozyme by tyrosine kinases dictates endogenous substrate selection for detoxification (Q34489142)

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English	Regulated phosphorylation of a major UDP-glucuronosyltransferase isozyme by tyrosine kinases dictates endogenous substrate selection for detoxification	scientific article

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scholarly article

1 reference

Europe PubMed Central

2 August 2017

Regulated phosphorylation of a major UDP-glucuronosyltransferase isozyme by tyrosine kinases dictates endogenous substrate selection for detoxification (English)

1 reference

Europe PubMed Central

2 August 2017

phosphorylation

1 reference

based on heuristic

inferred from title

author name string

Partha S Mitra

1

1 reference

Europe PubMed Central

2 August 2017

Nikhil K Basu

2

1 reference

Europe PubMed Central

2 August 2017

Mousumi Basu

3

1 reference

Europe PubMed Central

2 August 2017

Sunit Chakraborty

4

1 reference

Europe PubMed Central

2 August 2017

Tapas Saha

5

1 reference

Europe PubMed Central

2 August 2017

Ida S Owens

6

1 reference

Europe PubMed Central

2 August 2017

language of work or name

0 references

publication date

5 November 2010

1 reference

Europe PubMed Central

2 August 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

2 August 2017

286

1 reference

Europe PubMed Central

2 August 2017

2

1 reference

Europe PubMed Central

2 August 2017

1639-1648

1 reference

Europe PubMed Central

2 August 2017

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1 reference

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Src supports UDP-glucuronosyltransferase-2B7 detoxification of catechol estrogens associated with breast cancer

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The major chemical-detoxifying system of UDP-glucuronosyltransferases requires regulated phosphorylation supported by protein kinase C

1 reference

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Phosphorylation of a UDP-glucuronosyltransferase regulates substrate specificity

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Gastrointestinally distributed UDP-glucuronosyltransferase 1A10, which metabolizes estrogens and nonsteroidal anti-inflammatory drugs, depends upon phosphorylation

1 reference

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Glucuronidation and the UDP-glucuronosyltransferases in health and disease.

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Direct inhibitory effect of curcumin on Src and focal adhesion kinase activity

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Differential and Special Properties of the Major Human UGT1-encoded Gastrointestinal UDP-glucuronosyltransferases Enhance Potential to Control Chemical Uptake

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Expression of UGT2B7, a UDP-glucuronosyltransferase implicated in the metabolism of 4-hydroxyestrone and all-trans retinoic acid, in normal human breast parenchyma and in invasive and in situ breast cancers

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Activation of Src kinase in skeletal muscle cells by 1, 1,25-(OH(2))-vitamin D(3) correlates with tyrosine phosphorylation of the vitamin D receptor (VDR) and VDR-Src interaction

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Functional role of estrogen metabolism in target cells: review and perspectives

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1 reference

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1 reference

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1 reference

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Identifiers

10.1074/JBC.M110.165126

1 reference

Europe PubMed Central

2 August 2017

1 reference

Europe PubMed Central

2 August 2017

1 reference

Europe PubMed Central

2 August 2017

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