New insights into translational regulation in the endoplasmic reticulum unfolded protein response.
about
Pharmacological brake-release of mRNA translation enhances cognitive memoryTranslational control by heme-regulated eIF2α kinase during erythropoiesisPrinciples of translational control: an overviewGRP78/BiP/HSPA5/Dna K is a universal therapeutic target for human diseaseAndrogen signaling promotes translation of TMEFF2 in prostate cancer cells via phosphorylation of the α subunit of the translation initiation factor 2CREBH determines the severity of sulpyrine-induced fatal shockALKBH1-Mediated tRNA Demethylation Regulates TranslationTranslational control during endoplasmic reticulum stress beyond phosphorylation of the translation initiation factor eIF2α.Global analysis of gene expression reveals mRNA superinduction is required for the inducible immune response to a bacterial pathogen.UPR-inducible miRNAs contribute to stressful situationsImpaired eukaryotic translation initiation factor 2B activity specifically in oligodendrocytes reproduces the pathology of vanishing white matter disease in mice.Regulation of OSU-03012 toxicity by ER stress proteins and ER stress-inducing drugs.The small molecule ISRIB reverses the effects of eIF2α phosphorylation on translation and stress granule assemblyApproaches to imaging unfolded secretory protein stress in living cells.Dissection of Ire1 functions reveals stress response mechanisms uniquely evolved in Candida glabrata.Combining valosin-containing protein (VCP) inhibition and suberanilohydroxamic acid (SAHA) treatment additively enhances the folding, trafficking, and function of epilepsy-associated γ-aminobutyric acid, type A (GABAA) receptorsHSPA5/Dna K may be a useful target for human disease therapies.Pancreatic endoplasmic reticulum kinase activation promotes medulloblastoma cell migration and invasion through induction of vascular endothelial growth factor ADNA Damage Regulates Translation through β-TRCP Targeting of CRePAn eIF2α-binding motif in protein phosphatase 1 subunit GADD34 and its viral orthologs is required to promote dephosphorylation of eIF2α.Inhibition of Mcl-1 with the pan-Bcl-2 family inhibitor (-)BI97D6 overcomes ABT-737 resistance in acute myeloid leukemia.IRE1α-Dependent Decay of CReP/Ppp1r15b mRNA Increases Eukaryotic Initiation Factor 2α Phosphorylation and Suppresses Protein SynthesisBaculovirus protein PK2 subverts eIF2α kinase function by mimicry of its kinase domain C-lobe.The unfolded protein response in fission yeast modulates stability of select mRNAs to maintain protein homeostasis.GRP78/Dna K Is a Target for Nexavar/Stivarga/Votrient in the Treatment of Human Malignancies, Viral Infections and Bacterial Diseases.Regulation of PERK-eIF2α signalling by tuberous sclerosis complex-1 controls homoeostasis and survival of myelinating oligodendrocytesIntermedin1-53 Protects Against Myocardial Fibrosis by Inhibiting Endoplasmic Reticulum Stress and Inflammation Induced by Homocysteine in Apolipoprotein E-Deficient Mice.Dual role of the integrated stress response in medulloblastoma tumorigenesis.Protein phosphatase PP1/GLC7 interaction domain in yeast eIF2γ bypasses targeting subunit requirement for eIF2α dephosphorylationRegulation of mRNA translation by signaling pathwaysTinkering with translation: protein synthesis in virus-infected cells.ER stress response mechanisms in the pathogenic yeast Candida glabrata and their roles in virulenceStress-induced remodeling of the bacterial proteome.The yeast peroxiredoxin Tsa1 protects against protein-aggregate-induced oxidative stressA new function and complexity for protein translation initiation factor eIF2BEndoplasmic reticulum stress and the unfolded protein response in disorders of myelinating gliaProtein kinase R(PKR)-like endoplasmic reticulum kinase (PERK) inhibitors: a patent review (2010-2015).Ghrelin's Effects on Proinflammatory Cytokine Mediated Apoptosis and Their Impact on β-Cell Functionality.EIF2S3 Mutations Associated with Severe X-Linked Intellectual Disability Syndrome MEHMO.Intermedin1-53 attenuates vascular smooth muscle cell calcification by inhibiting endoplasmic reticulum stress via cyclic adenosine monophosphate/protein kinase A pathway.
P2860
Q21128794-311BFA1D-EEC0-4550-A7FA-811684CAD8D9Q26865758-BB3EF9F8-BEF1-4292-9941-6CED5A4F2ECDQ26995200-1CEBEA84-85C2-4242-8CFF-D4262F8B5D7FQ28254667-FA5B2E03-1E73-4F3F-BDDA-A6767103E6ABQ28486024-C73490B2-7125-4F97-A5C9-E4777DAC1566Q28486047-B7D0E190-D55E-44A1-900E-4FF76D92CC67Q28590996-76D409F2-819F-4C6E-962F-C80FCA27544AQ33556172-45415967-D943-4201-9E4E-7B6BAF498519Q33611060-34B84387-F8A1-4015-ACA4-979533912F8EQ33752232-89551BD7-10EA-4D67-8D9C-54DF09B4EC9AQ34123857-7F2DD788-A8BA-400B-84E6-F7773C757699Q34289307-ED9CA414-DCE1-459B-BC9C-894587E7D9C3Q34464670-FFACA20C-F2E0-46EE-B1AA-D702D0DCF649Q34546956-1914569E-8101-471C-8B2C-9A4BCF399366Q34574891-F24FCB6F-D663-4977-86EE-969C7FCA10A2Q34801457-AE6FAFA7-CDCA-4F00-8BF6-D879E1B29B4BQ35110761-165C9E0E-7604-4AA2-B9AF-AF36141F36C2Q35582746-FD562644-89C2-4075-AD5B-9A31D4EAD95BQ35668793-8964E37A-596B-4588-81D9-119C7DD1B8B0Q35845921-B0FFF16D-A92E-43A8-A1D9-4C9AF266BE9CQ35859229-09C00D20-C375-40D6-8BC3-11EC3C5CF932Q35868391-C1FE3BE7-AAC2-49D0-96C1-19CFFF9AE520Q35961375-990B6446-31C6-4683-83CB-C7193C60BCE2Q36314567-55D27C6E-4225-49AE-90B4-CE61EC34A384Q36830763-DD67A4D1-5155-499B-806C-CE301AFF2088Q37099475-D40FE685-7E99-46DB-A7FD-CA710E43804FQ37420506-11EDA8F2-C518-4ADA-8679-09EF6737C05BQ37665597-3DD3D40F-B955-4BB9-9573-41C0C87ED030Q37701984-267452CE-F7D3-4505-B5B2-1D6CDAF34FC3Q38034202-719064CF-5C5E-46BA-B4B9-4684FF6F3D9EQ38064834-A04490CD-9E44-40F7-B6ED-921AB79C0A70Q38171052-A2BC9C6C-69E8-47F2-9789-CA9CE36BA9D5Q38213227-B1B7999C-B36E-4A84-91E6-47648139909EQ38271105-66846BD8-8D5C-4C1F-A07C-180403EDCA1FQ38285158-BB10CF31-7FD9-497E-854B-D6E8F525A108Q38801191-AB573A74-E078-4D35-9626-6F3F8E2F0540Q38819666-8A4BDBF0-C980-43F9-97A4-A8580E238092Q38844959-1846A554-56DE-46C8-9EFC-67F582AD456AQ41921225-2E8A19E7-7680-4D9D-B4FC-AF4A5CFCE4CBQ46493701-8A548CB0-2C63-46D3-A557-3DD0644AC7A7
P2860
New insights into translational regulation in the endoplasmic reticulum unfolded protein response.
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
New insights into translationa ...... lum unfolded protein response.
@en
type
label
New insights into translationa ...... lum unfolded protein response.
@en
prefLabel
New insights into translationa ...... lum unfolded protein response.
@en
P2860
P1476
New insights into translationa ...... lum unfolded protein response.
@en
P2860
P356
10.1101/CSHPERSPECT.A012278
P577
2012-06-01T00:00:00Z