Molecular mechanism of hypoxia-inducible factor 1alpha -p300 interaction. A leucine-rich interface regulated by a single cysteine.
about
Cloning and expression analysis of two distinct HIF-alpha isoforms--gcHIF-1alpha and gcHIF-4alpha--from the hypoxia-tolerant grass carp, Ctenopharyngodon idellusFIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factorModulation of p300 binding by posttranslational modifications of the C-terminal activation domain of hypoxia-inducible factor-1alphaThe phosphorylation status of PAS-B distinguishes HIF-1alpha from HIF-2alpha in NBS1 repressionStructural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alphaSuppression of hypoxia-inducible factor 1alpha (HIF-1alpha) transcriptional activity by the HIF prolyl hydroxylase EGLN1Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway.Hypoxia upregulates the expression of the NDRG1 gene leading to its overexpression in various human cancersKATs in cancer: functions and therapiesStructural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response.Exploration of the HIF-1α/p300 interface using peptide and Adhiron phage display technologiesCarboxyl-terminal transactivation activity of hypoxia-inducible factor 1 alpha is governed by a von Hippel-Lindau protein-independent, hydroxylation-regulated association with p300/CBP.Identification of recurring protein structure microenvironments and discovery of novel functional sites around CYS residuesModeling disordered protein interactions from biophysical principlesComplex regulation of the transactivation function of hypoxia-inducible factor-1 alpha by direct interaction with two distinct domains of the CREB-binding protein/p300.HIF-1alpha induces cell cycle arrest by functionally counteracting Myc.MnTE-2-PyP reduces prostate cancer growth and metastasis by suppressing p300 activity and p300/HIF-1/CREB binding to the promoter region of the PAI-1 gene.MAPK signaling up-regulates the activity of hypoxia-inducible factors by its effects on p300HIF-1α confers aggressive malignant traits on human tumor cells independent of its canonical transcriptional functionInhibition of the HIF1α-p300 interaction by quinone- and indandione-mediated ejection of structural Zn(II).Disrupting the CH1 domain structure in the acetyltransferases CBP and p300 results in lean mice with increased metabolic controlHypoxia-induced and stress-specific changes in chromatin structure and function.Synthesis of highly functionalized oligobenzamide proteomimetic foldamers by late stage introduction of sensitive groups.Petri net-based approach to modeling and analysis of selected aspects of the molecular regulation of angiogenesis.Mucosal protection by hypoxia-inducible factor prolyl hydroxylase inhibition.Cytoplasmic location of factor-inhibiting hypoxia-inducible factor is associated with an enhanced hypoxic response and a shorter survival in invasive breast cancerMechanisms of hypoxic signal transduction regulated by reactive nitrogen species.Molecular basis of coiled coil coactivator recruitment by the aryl hydrocarbon receptor nuclear translocator (ARNT).Protein domain mimetics as in vivo modulators of hypoxia-inducible factor signaling.Trichostatin A, a histone deacetylase inhibitor suppresses NADPH Oxidase 4-Derived Redox Signalling and AngiogenesisComplex role of HIF in cancer: the known, the unknown, and the unexpected.The molecular basis for impaired hypoxia-induced VEGF expression in diabetic tissues.Direct inhibition of hypoxia-inducible transcription factor complex with designed dimeric epidithiodiketopiperazine.Activity of hypoxia-inducible factor 2alpha is regulated by association with the NF-kappaB essential modulator.Proteasomal inhibition attenuates transcriptional activity of hypoxia-inducible factor 1 (HIF-1) via specific effect on the HIF-1alpha C-terminal activation domain.Hypoxia signalling manipulation for bone regeneration.Roles of p300 and cyclic adenosine monophosphate response element binding protein in high glucose-induced hypoxia-inducible factor 1α inactivation under hypoxic conditions.Transcriptional upregulation of HIF-1α by NF-κB/p65 and its associations with β-catenin/p300 complexes in endometrial carcinoma cells.Visualization of hypoxia-inducible factor 1α-p300 interactions in live cells by fluorescence resonance energy transfer.MnTE-2-PyP modulates thiol oxidation in a hydrogen peroxide-mediated manner in a human prostate cancer cell.
P2860
Q21263015-A17142A6-55DA-4A3A-8E1E-8D0256D872E1Q24300161-DF6EA0DE-9696-44FF-8A69-859AFFED6B28Q24300822-88DEC991-8EAF-4D1B-8D6E-7E7A70211011Q24306098-A32A8847-25D4-4048-A9F2-721440D6C8DFQ24534120-B3C46EC8-466F-4955-9247-94C538833C89Q24538799-A9636700-4FBF-496C-8396-168B330E2811Q24539006-011CB3E1-7CEF-4726-913C-453D8AF5B716Q24794324-0512B4A1-0E6A-44C1-BD5C-25DE1B2F1731Q26859355-5BB485A7-3DB0-4319-9160-C663DBE08039Q27638869-2C1FEA21-65E8-4BF3-808B-5EB8116ED45EQ27701444-F6276A9C-6240-4435-ACC0-D65B7E892F83Q28213770-CB1ACF60-A802-4882-9DFF-D953E940767DQ30385213-E3B83136-89EC-4CF8-AB0E-1DF9B287765AQ30400966-0F4BD418-D4A6-42BC-AF96-5292EAB0035DQ33593991-0ECBCBA0-3B98-46C6-9071-0501257DE6D0Q33705004-ACC5B65A-E069-4FDE-855A-0698FFE0DBB9Q33841634-88E0EE54-486D-4927-9899-977C704D7657Q34177495-DB3ADB25-217B-417F-9FA6-FB618F4238DBQ34586733-D9D51AEC-8AAE-44CD-841B-51BA8780A628Q34778239-310A6FE1-085F-419E-8AB3-87BBDE1660AAQ35185366-A57E552D-A762-4E49-AF9F-EA7A8ED81F08Q35901931-C500D916-2C46-4A16-9FEC-FAD0220659C3Q35966915-251C46D9-186E-4053-A369-1BAFE64700FBQ36295356-B40130C1-EF10-46E7-AE31-E1AF0389B58AQ36372667-3522F76B-6D9C-480A-BC61-1BFB84C062B0Q36465353-4E6E4A73-4EF7-45E5-A2E6-C6BD676D7046Q36795849-6A9EC44A-3C97-494F-B1FB-2DEE6F8FBC1CQ37200897-67D83B7D-881A-4053-8E74-9D8DFD29681EQ37203888-09A06966-BEB4-4F50-AED5-93FFB2111B09Q37251585-A649C4EB-A27A-42B7-AA1C-D19EBD4E3E0DQ37301016-BF7C0366-40AA-4155-BCA6-5E6D3BB615EEQ37304128-45640A7C-CEF2-423F-BC73-EFB8C7C6AA3BQ37486398-5C7A0945-A9F1-4714-B8E3-C2CD854C4E1EQ38331952-9D89D230-EDF1-410C-8EE1-E0C1A5C3E960Q38407792-E729EABD-77DE-4F5B-9E3A-43330E8ED354Q38434373-1FD9EFF2-4F07-4C33-9AF6-D7780EB18BA7Q38799649-B8B2026B-6EED-426F-AD60-9AE431E16019Q39094933-BEDD0B50-8D97-4FD6-A6ED-00223707CFAFQ39106982-05A66236-5DA5-4C99-A0E0-4AB78880DCF5Q39348469-529216BB-8DBB-4C93-B8C5-4372D9BF67A9
P2860
Molecular mechanism of hypoxia-inducible factor 1alpha -p300 interaction. A leucine-rich interface regulated by a single cysteine.
description
2000 nî lūn-bûn
@nan
2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Molecular mechanism of hypoxia ...... egulated by a single cysteine.
@ast
Molecular mechanism of hypoxia ...... egulated by a single cysteine.
@en
type
label
Molecular mechanism of hypoxia ...... egulated by a single cysteine.
@ast
Molecular mechanism of hypoxia ...... egulated by a single cysteine.
@en
prefLabel
Molecular mechanism of hypoxia ...... egulated by a single cysteine.
@ast
Molecular mechanism of hypoxia ...... egulated by a single cysteine.
@en
P2093
P2860
P356
P1476
Molecular mechanism of hypoxia ...... egulated by a single cysteine.
@en
P2093
P2860
P304
P356
10.1074/JBC.M009522200
P407
P577
2000-11-03T00:00:00Z