ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism
about
A yeast two-hybrid system reconstituting substrate recognition of the von Hippel-Lindau tumor suppressor proteinMint3 enhances the activity of hypoxia-inducible factor-1 (HIF-1) in macrophages by suppressing the activity of factor inhibiting HIF-1MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH)Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factorFactor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domainsThe role of cullin 5-containing ubiquitin ligasesThe Role of Oxygen Sensors, Hydroxylases, and HIF in Cardiac Function and DiseaseAsparagine beta-hydroxylation stabilizes the ankyrin repeat domain foldSubstrate selectivity analyses of factor inhibiting hypoxia-inducible factorExpanding chemical biology of 2-oxoglutarate oxygenasesInhibition of 2-oxoglutarate dependent oxygenasesPotent and Selective Triazole-Based Inhibitors of the Hypoxia-Inducible Factor Prolyl-Hydroxylases with Activity in the Murine BrainConsequences of IkappaB alpha hydroxylation by the factor inhibiting HIF (FIH)ASB9 interacts with ubiquitous mitochondrial creatine kinase and inhibits mitochondrial functionGene expression analysis of embryonic stem cells expressing VE-cadherin (CD144) during endothelial differentiationAnalysis of transcription factors expressed at the anterior mouse limb bud.Sent to destroy: the ubiquitin proteasome system regulates cell signaling and protein quality control in cardiovascular development and disease.Hypoxia-dependent sequestration of an oxygen sensor by a widespread structural motif can shape the hypoxic response--a predictive kinetic model.Essential role for the d-Asb11 cul5 Box domain for proper notch signaling and neural cell fate decisions in vivo.The asparaginyl hydroxylase factor inhibiting HIF-1alpha is an essential regulator of metabolismExpression and DNA methylation levels of prolyl hydroxylases PHD1, PHD2, PHD3 and asparaginyl hydroxylase FIH in colorectal cancer.The ubiquitin ligase ASB4 promotes trophoblast differentiation through the degradation of ID2Quantitative mass spectrometry reveals dynamics of factor-inhibiting hypoxia-inducible factor-catalyzed hydroxylation.Ascorbic acid regulates osterix expression in osteoblasts by activation of prolyl hydroxylase and ubiquitination-mediated proteosomal degradation pathwayFactor inhibiting HIF (FIH) recognizes distinct molecular features within hypoxia-inducible factor-α (HIF-α) versus ankyrin repeat substratesTurn me on: regulating HIF transcriptional activity.Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.The role of HIF prolyl hydroxylases in tumour growth.Hypoxia. The role of hypoxia and HIF-dependent signalling events in rheumatoid arthritis.New Insights into Protein Hydroxylation and Its Important Role in Human Diseases.Regulation of ankyrin repeat and suppressor of cytokine signalling box protein 4 expression in the immortalized murine endothelial cell lines MS1 and SVR: a role for tumour necrosis factor alpha and oxygenFactor inhibiting HIF (FIH-1) promotes renal cancer cell survival by protecting cells from HIF-1α-mediated apoptosis.Onconeuronal cerebellar degeneration-related antigen, Cdr2, is strongly expressed in papillary renal cell carcinoma and leads to attenuated hypoxic response.Overexpression of factor inhibiting HIF-1 enhances vessel maturation and tumor growth via platelet-derived growth factor-C.Metabolic Phenotyping of Anks3 Depletion in mIMCD-3 cells - a Putative Nephronophthisis Candidate.Hypoxia Inducible Factor as a Central Regulator of Metabolism - Implications for the Development of Obesity
P2860
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P248
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P2860
ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism
description
2007 nî lūn-bûn
@nan
2007 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
ASB4 is a hydroxylation substr ...... an oxygen-dependent mechanism
@ast
ASB4 is a hydroxylation substr ...... an oxygen-dependent mechanism
@en
ASB4 is a hydroxylation substr ...... an oxygen-dependent mechanism
@en-gb
ASB4 is a hydroxylation substr ...... an oxygen-dependent mechanism
@nl
type
label
ASB4 is a hydroxylation substr ...... an oxygen-dependent mechanism
@ast
ASB4 is a hydroxylation substr ...... an oxygen-dependent mechanism
@en
ASB4 is a hydroxylation substr ...... an oxygen-dependent mechanism
@en-gb
ASB4 is a hydroxylation substr ...... an oxygen-dependent mechanism
@nl
prefLabel
ASB4 is a hydroxylation substr ...... an oxygen-dependent mechanism
@ast
ASB4 is a hydroxylation substr ...... an oxygen-dependent mechanism
@en
ASB4 is a hydroxylation substr ...... an oxygen-dependent mechanism
@en-gb
ASB4 is a hydroxylation substr ...... an oxygen-dependent mechanism
@nl
P2093
P2860
P921
P356
P1476
ASB4 is a hydroxylation substr ...... an oxygen-dependent mechanism
@en
P2093
James E Ferguson
Kevin Smith
Kyle Powers
Peter Charles
P2860
P304
P356
10.1128/MCB.00511-07
P407
P577
2007-09-01T00:00:00Z