Salubrinal attenuated retinal neovascularization by inhibiting CHOP-HIF1α-VEGF pathways.

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Salubrinal attenuated retinal neovascularization by inhibiting CHOP-HIF1α-VEGF pathways.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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2017年學術文章

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name

Salubrinal attenuated retinal neovascularization by inhibiting CHOP-HIF1α-VEGF pathways.

@en

Salubrinal attenuated retinal neovascularization by inhibiting CHOP-HIF1α-VEGF pathways.

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Item

label

Salubrinal attenuated retinal neovascularization by inhibiting CHOP-HIF1α-VEGF pathways.

@en

Salubrinal attenuated retinal neovascularization by inhibiting CHOP-HIF1α-VEGF pathways.

@nl

prefLabel

Salubrinal attenuated retinal neovascularization by inhibiting CHOP-HIF1α-VEGF pathways.

@en

Salubrinal attenuated retinal neovascularization by inhibiting CHOP-HIF1α-VEGF pathways.

@nl

P1476

Salubrinal attenuated retinal neovascularization by inhibiting CHOP-HIF1α-VEGF pathways.

@en

P2093

Boyu Yang

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

Ching-Kit Tsui

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

Dan Ye

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Jingjing Huang

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

Lin Lu

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

Qiaochu Cheng

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

Shanshan Yu

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

Xi Lu

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

Xiaoling Liang

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Yaguang Hu

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P2860

The oxidative stressor arsenite activates vascular endothelial growth factor mRNA transcription by an ATF4-dependent mechanism

Efficacy of intravitreal bevacizumab for stage 3+ retinopathy of prematurity

Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway

Angiogenesis in cancer and other diseases

Induction of HIF-1alpha in response to hypoxia is instantaneous

Purification and characterization of hypoxia-inducible factor 1

Angiogenesis in cancer, vascular, rheumatoid and other disease

Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes

Unfolded protein response regulation in keloid cells.

Transcriptional regulation of VEGF-A by the unfolded protein response pathway.

P304

77219-77232

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P31

scholarly article

P356

10.18632/ONCOTARGET.20431

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P407

English

P433

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

P478

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

P577

2017-08-24T00:00:00Z

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P698

29100382

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P921

neovascularization

P932

5652775

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