Peptidyl-prolyl isomerases: functionality and potential therapeutic targets in cardiovascular disease.

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Multiple Growth Factors, But Not VEGF, Stimulate Glycosaminoglycan Hyperelongation in Retinal Choroidal Endothelial Cells.The Essential Role of Pin1 via NF-κB Signaling in Vascular Inflammation and Atherosclerosis in ApoE-/- Mice.

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Peptidyl-prolyl isomerases: functionality and potential therapeutic targets in cardiovascular disease.

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http://www.wikidata.org/entity/Q38265843

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2015 nî lūn-bûn

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2015年の論文

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2015年学术文章

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Peptidyl-prolyl isomerases: fu ...... ets in cardiovascular disease.

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Peptidyl-prolyl isomerases: fu ...... ets in cardiovascular disease.

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Peptidyl-prolyl isomerases: fu ...... ets in cardiovascular disease.

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Peptidyl-prolyl isomerases: fu ...... ets in cardiovascular disease.

@en

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Hossein B Rezaei

http://www.w3.org/2001/XMLSchema#string

Narin Osman

http://www.w3.org/2001/XMLSchema#string

Wenhua Zheng

http://www.w3.org/2001/XMLSchema#string

P2860

Pin1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC

A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase

Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12

Pin1 down-regulates transforming growth factor-beta (TGF-beta) signaling by inducing degradation of Smad proteins

Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin

Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1.

Pin1 prolyl isomerase regulates endothelial nitric oxide synthase

Structure-based design of novel human Pin1 inhibitors (II)

Discovery of cell-active phenyl-imidazole Pin1 inhibitors by structure-guided fragment evolution

A Smad action turnover switch operated by WW domain readers of a phosphoserine code

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117-124

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scholarly article

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10.1111/1440-1681.12335

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

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Peter J Little

Terrence Piva

Danielle Kamato

Muhamad Ashraf Rostam

P577

2015-02-01T00:00:00Z

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P5875

267875386

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25377120

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Peptidyl-prolyl isomerases: functionality and potential therapeutic targets in cardiovascular disease.

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P2860

P2860

Peptidyl-prolyl isomerases: functionality and potential therapeutic targets in cardiovascular disease.

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P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

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P1433

P1476

P2093

P2860

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P31

P356

P433

P478

P50

P577

P5875

P698