Peptide blockade of HIFalpha degradation modulates cellular metabolism and angiogenesis - Wikidata - awgldk - TriplyDB

Peptide blockade of HIFalpha degradation modulates cellular metabolism and angiogenesis

Peptide blockade of HIFalpha degradation modulates cellular metabolism and angiogenesis

http://www.wikidata.org/entity/Q34074553

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Targeting Protein-Protein Interactions in the HIF System Hypoxia and fibrosis in chronic kidney disease: crossing at pericytes Small-Molecule Inhibitors of the Interaction between the E3 Ligase VHL and HIF1α Targeting the von Hippel–Lindau E3 Ubiquitin Ligase Using Small Molecules To Disrupt the VHL/HIF-1α Interaction Inhibition of 2-oxoglutarate dependent oxygenases Potent and selective chemical probe of hypoxic signalling downstream of HIF-α hydroxylation via VHL inhibition Natural product-derived small molecule activators of hypoxia-inducible factor-1 (HIF-1)Cell-type-specific regulation of degradation of hypoxia-inducible factor 1 alpha: role of subcellular compartmentalization.Manipulating angiogenesis in medicine.Hypoxia-inducible transcription factors stabilization in the thick ascending limb protects against ischemic acute kidney injury.Recent advances in the use of protein transduction domains for the delivery of peptides, proteins and nucleic acids in vivo.Activation of the hypoxia-inducible factor-1alpha pathway accelerates bone regeneration Hypoxia inducible factor prolyl 4-hydroxylase enzymes: center stage in the battle against hypoxia, metabolic compromise and oxidative stress.Hypoxia-inducible factor prolyl 4-hydroxylase inhibition. A target for neuroprotection in the central nervous system.HIF-prolyl hydroxylases in the rat kidney: physiologic expression patterns and regulation in acute kidney injury.Targeting carbonic anhydrase IX activity and expression.(2R)-[(4-Biphenylylsulfonyl)amino]-N-hydroxy-3-phenylpropionamide (BiPS), a matrix metalloprotease inhibitor, is a novel and potent activator of hypoxia-inducible factors.Tuning the strength of a bacterial N-end rule degradation signal Inhibition of endogenous HIF inactivation induces angiogenesis in ischaemic skeletal muscles of mice.Age-related cataracts: Role of unfolded protein response, Ca2+ mobilization, epigenetic DNA modifications, and loss of Nrf2/Keap1 dependent cytoprotection.Membrane-permeable Bcl-xL prevents MPTP-induced dopaminergic neuronal loss in the substantia nigra.

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P2860

Peptide blockade of HIFalpha degradation modulates cellular metabolism and angiogenesis

http://www.wikidata.org/entity/Q34074553

description

2002 nî lūn-bûn

@nan

2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Peptide blockade of HIFalpha degradation modulates cellular metabolism and angiogenesis

@ast

Peptide blockade of HIFalpha degradation modulates cellular metabolism and angiogenesis

@en

Peptide blockade of HIFalpha degradation modulates cellular metabolism and angiogenesis

@nl

type

label

Peptide blockade of HIFalpha degradation modulates cellular metabolism and angiogenesis

@ast

Peptide blockade of HIFalpha degradation modulates cellular metabolism and angiogenesis

@en

Peptide blockade of HIFalpha degradation modulates cellular metabolism and angiogenesis

@nl

prefLabel

Peptide blockade of HIFalpha degradation modulates cellular metabolism and angiogenesis

@ast

Peptide blockade of HIFalpha degradation modulates cellular metabolism and angiogenesis

@en

Peptide blockade of HIFalpha degradation modulates cellular metabolism and angiogenesis

@nl

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Peptide blockade of HIFalpha degradation modulates cellular metabolism and angiogenesis

@en

P2093

Carsten Willam

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

Christopher W Pugh

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

Kai-Uwe Eckardt

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

Michael I Wilson

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

Norma Masson

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Patrick H Maxwell

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

Roy Bicknell

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S Aleema Mahmood

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

P2860

The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis

HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing

C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation

A conserved family of prolyl-4-hydroxylases that modify HIF

FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity

Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling

Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL

Tetracycline-reversible silencing of eukaryotic promoters

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

Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation

P304

10423-10428

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scholarly article

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10.1073/PNAS.162119399

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16

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99

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Peter J. Ratcliffe

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2002-07-29T00:00:00Z

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11234194

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12149454

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124930

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