OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha
about
IOP1, a novel hydrogenase-like protein that modulates hypoxia-inducible factor-1alpha activityPosttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)The MRH protein Erlectin is a member of the endoplasmic reticulum synexpression group and functions in N-glycan recognitionOS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERADHuman XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiPA dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposalMyeloid translocation gene-16 co-repressor promotes degradation of hypoxia-inducible factor 1The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF).Suppression of hypoxia-inducible factor 1alpha (HIF-1alpha) transcriptional activity by the HIF prolyl hydroxylase EGLN1BMI-1 promotes ewing sarcoma tumorigenicity independent of CDKN2A repressionIdentification of an alternative mechanism of degradation of the hypoxia-inducible factor-1alphaStudies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assayHypoxia-inducible factor-1alpha polymorphisms and TSC1/2 mutations are complementary in head and neck cancersLncRNAs in pancreatic cancerHypoxia and Integrin-Mediated Epithelial Restitution during Mucosal InflammationPHD2: from hypoxia regulation to disease progressionSubstrate-Trapped Interactors of PHD3 and FIH Cluster in Distinct Signaling PathwaysRegulation of immune cells by local-tissue oxygen tension: HIF1 alpha and adenosine receptorsMolecular mechanisms of action and therapeutic uses of pharmacological inhibitors of HIF-prolyl 4-hydroxylases for treatment of ischemic diseasesReducing Tumour Hypoxia via Oral Administration of Oxygen NanobubblesHypoxia-inducible factor prolyl-hydroxylase 2 senses high-salt intake to increase hypoxia inducible factor 1alpha levels in the renal medullaLive cell imaging of protein dislocation from the endoplasmic reticulum.Increased prolyl 4-hydroxylase domain proteins compensate for decreased oxygen levels. Evidence for an autoregulatory oxygen-sensing system.Phosphorylation of cold shock domain/Y-box proteins by ERK2 and GSK3beta and repression of the human VEGF promoter.Bcl-2 regulates HIF-1alpha protein stabilization in hypoxic melanoma cells via the molecular chaperone HSP90.The function of hypoxia-inducible factor (HIF) is independent of the endoplasmic reticulum protein OS-9Coordinate regulation of the oxygen-dependent degradation domains of hypoxia-inducible factor 1 alpha.Identification of cellular proteins interacting with equine infectious anemia virus S2 protein.Targeted genes and interacting proteins of hypoxia inducible factor-1.The hypoxia-inducible-factor hydroxylases bring fresh air into hypoxia signalling.Spermidine/spermine-N1-acetyltransferase 2 is an essential component of the ubiquitin ligase complex that regulates hypoxia-inducible factor 1alpha.Activation of the epithelial sodium channel by the metalloprotease meprin β subunit.Loss of PHD3 allows tumours to overcome hypoxic growth inhibition and sustain proliferation through EGFR.Spermidine/spermine N(1)-acetyltransferase-1 binds to hypoxia-inducible factor-1alpha (HIF-1alpha) and RACK1 and promotes ubiquitination and degradation of HIF-1alpha.Hypoxia increases sirtuin 1 expression in a hypoxia-inducible factor-dependent manner.Conserved syntenic clusters of protein coding genes are missing in birds.Hypoxia-inducible factor-1α contributes to the profibrotic action of angiotensin II in renal medullary interstitial cellsPhospholipase D1 protein coordinates dynamic assembly of HIF-1α-PHD-VHL to regulate HIF-1α stabilityVillin and actin in the mouse kidney brush-border membrane bind to and are degraded by meprins, an interaction that contributes to injury in ischemia-reperfusionA Novel Role of OS-9 in the Maintenance of Intestinal Barrier Function from Hypoxia-induced Injury via p38-dependent Pathway.
P2860
Q24301670-D74C4301-F56C-41B1-834E-3A93CF69FF12Q24304828-DA3AC36D-A9D5-465B-ACF6-693C7B4DB8AAQ24307679-166AF7CF-94A4-4681-860C-11A8CBED769AQ24312778-379FAA09-4B12-41CA-B6CC-2D1919CCC585Q24316328-F8FC0B36-454E-4EA1-8CBF-AAA988C4B134Q24322193-15FCD158-2F5A-4DB1-B1C6-FDCC6EC9E2ACQ24337524-4E984FE1-B169-4DB9-B166-595AB423E231Q24529065-A6AE1707-0A04-432D-8AAA-D2F895BB2C34Q24538799-FAAF0897-5538-4996-998B-7E49DDAA24F8Q24650619-D5871B2B-F5DE-49A8-AB92-CA9A3FF7A959Q24651502-93F10F2C-CB12-4C21-B927-CD490C27D68BQ24671869-A5EE4727-1799-46F7-90E8-85E510549BFAQ25255621-F5082BAF-3359-4A3A-A690-BC6BDBE95E50Q26739965-0A6C72B2-411F-4021-90BC-49F9F90AE225Q26995631-4DCEE184-D62A-48DF-A386-3A46D3CEEA99Q28069316-96E71DE6-D424-4E36-9392-CC29B32DAD42Q28116317-A97696E3-D933-4D7B-9340-3B31EADDD943Q28268052-3ADA2C66-8137-433E-9334-477F6AE01BB7Q28297656-00926297-0206-4D80-9E86-7EEE65668024Q28468506-843D4638-1470-45DA-A2D9-6FE797BA8974Q28567251-07A17E7A-1ED7-409C-9F26-54CF319B40C0Q30524630-23C098D0-6B87-4534-89E8-AA7EA2CF89EAQ33247514-0A114541-3679-415A-9049-8172589949A3Q33292543-AA5BEB9C-C06A-40A7-8AFD-CAF86B138E69Q33644391-332517FE-BF87-4B38-A716-481A14BE7CAAQ33895152-94AA48CB-31C2-440E-9740-27284B1D0F13Q33925239-6506BF79-BFC7-429B-A2A1-327B2C0B7F94Q33965217-734E1995-B05A-4456-AAAA-FD86667BF8C9Q34286796-C7DF98D6-D349-471E-9C8A-C58984BF2457Q34360746-BBECCA86-E4BF-4281-B7C8-7E3D244C7A24Q34635842-C8ACF706-65B4-4E89-BF00-C1CC8933C89BQ34639469-22DF4FB8-33E9-48DD-9007-D34B89AB97D9Q34677727-9D31495B-A8E3-4016-BA00-F327A019234DQ34688845-82C0F9DE-4437-4BFB-A941-4E67218D77A6Q34799862-32CA1219-DF25-41B9-9B1B-7CB180200BBAQ34908315-E2115493-0D37-4B7B-B7E8-8E20119FE3BEQ35022857-85DB42F0-C046-4B51-BA64-CEF84CA5D158Q35068054-6D97BF8C-5741-4FEE-A089-9C4FA3233EE2Q35326081-297F4266-BBBF-4898-8754-2D94A16BF4E1Q35632726-C4AC57D0-AC9B-40B6-8ACA-7CAEE11E68FB
P2860
OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha
description
2005 nî lūn-bûn
@nan
2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
OS-9 interacts with hypoxia-in ...... dent degradation of HIF-1alpha
@ast
OS-9 interacts with hypoxia-in ...... dent degradation of HIF-1alpha
@en
OS-9 interacts with hypoxia-in ...... dent degradation of HIF-1alpha
@en-gb
OS-9 interacts with hypoxia-in ...... dent degradation of HIF-1alpha
@nl
type
label
OS-9 interacts with hypoxia-in ...... dent degradation of HIF-1alpha
@ast
OS-9 interacts with hypoxia-in ...... dent degradation of HIF-1alpha
@en
OS-9 interacts with hypoxia-in ...... dent degradation of HIF-1alpha
@en-gb
OS-9 interacts with hypoxia-in ...... dent degradation of HIF-1alpha
@nl
prefLabel
OS-9 interacts with hypoxia-in ...... dent degradation of HIF-1alpha
@ast
OS-9 interacts with hypoxia-in ...... dent degradation of HIF-1alpha
@en
OS-9 interacts with hypoxia-in ...... dent degradation of HIF-1alpha
@en-gb
OS-9 interacts with hypoxia-in ...... dent degradation of HIF-1alpha
@nl
P2093
P3181
P1433
P1476
OS-9 interacts with hypoxia-in ...... dent degradation of HIF-1alpha
@en
P2093
Amato J Giaccia
Balaji Krishnamachary
Brian Kelly
Denise A Chan
Jin Hyen Baek
Mia Pearson
Patrick C Mahon
P304
P3181
P356
10.1016/J.MOLCEL.2005.01.011
P407
P577
2005-02-18T00:00:00Z