The structure of the ARE-binding domains of Hu antigen R (HuR) undergoes conformational changes during RNA binding
about
A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteinsStructural analysis of Dis3l2, an exosome-independent exonuclease from Schizosaccharomyces pombeThe fungal natural product azaphilone-9 binds to HuR and inhibits HuR-RNA interaction in vitro.A 1536-well fluorescence polarization assay to screen for modulators of the MUSASHI family of RNA-binding proteins.Post-transcriptional regulation of programmed cell death 4 (PDCD4) mRNA by the RNA-binding proteins human antigen R (HuR) and T-cell intracellular antigen 1 (TIA1)Identification of Small-Molecule Inhibitors of the HuR/RNA Interaction Using a Fluorescence Polarization Screening Assay Followed by NMR ValidationIdentification of novel proteins binding the AU-rich element of α-prothymosin mRNA through the selection of open reading frames (RIDome).Evidence for cooperative tandem binding of hnRNP C RRMs in mRNA processing.A targeted genome association study examining transient receptor potential ion channels, acetylcholine receptors, and adrenergic receptors in Chronic Fatigue Syndrome/Myalgic Encephalomyelitis.The C-terminal RNA binding motif of HuR is a multi-functional domain leading to HuR oligomerization and binding to U-rich RNA targets.Dihydrotanshinone-I interferes with the RNA-binding activity of HuR affecting its post-transcriptional function.Discriminating between HuR and TTP binding sites using the k-spectrum kernel method.Structural study of the Fox-1 RRM protein hydration reveals a role for key water molecules in RRM-RNA recognition.Can we observe changes in mRNA "state"? Overview of methods to study mRNA interactions with regulatory proteins relevant in cancer related processes.Crystal Structure of the N-Terminal RNA Recognition Motif of mRNA Decay Regulator AUF1.Post-transcriptional controls by ribonucleoprotein complexes in the acquisition of drug resistance.Assembly of functional ribonucleoprotein complexes by AU-rich element RNA-binding protein 1 (AUF1) requires base-dependent and -independent RNA contacts.Impact of HuR inhibition by the small molecule MS-444 on colorectal cancer cell tumorigenesis.Regulation of ELAV/Hu RNA-binding proteins by phosphorylation.Hu Antigen R (HuR) multimerization contributes to glioma disease progression.Musashi RNA-Binding Proteins as Cancer Drivers and Novel Therapeutic Targets.Posttranscriptional control of airway inflammation.Regulation of HuR structure and function by dihydrotanshinone-I.Molecular basis for the specific and multivariant recognitions of RNA substrates by human hnRNP A2/B1.Exploration of ligand binding modes towards the identification of compounds targeting HuR: a combined STD-NMR and Molecular Modelling approach
P2860
Q27684537-A8EDAD92-383A-45CB-BD3B-638CBDE9AE4EQ27700982-320692D8-760D-4945-A12B-18A21A366C60Q33570640-7FB54A34-1FB2-43CD-AC51-ACF258ED0C09Q34054941-3E8FDDB2-82E9-4C0F-A0D9-04CF6B2C6890Q35055533-E6CCE7D3-2393-4CA7-9F98-26640C2A6E00Q35781852-D062C60F-A029-46C7-8975-6FC671FFA296Q35825902-F59F5F65-C146-4139-A2D6-627B1A928CFAQ36158569-519BFACE-F50E-4D1A-BF69-75C751FBE718Q36190203-E8138561-3495-491D-9F22-CCEE3E631AB5Q36191766-A7F2FE1A-E005-40C4-BD0B-E93C102476CEQ36265691-0BAEEC16-6769-44C9-8866-052594252135Q36319763-B8FA2C32-C8A1-492A-B156-44565369BD9CQ36372186-9C5C605D-E996-4D9D-B0F3-58EA8407DE0BQ36431066-5832B96D-BC99-4DB9-9299-534F147FB8DDQ37089106-36F4BBEE-61F0-4423-9490-ACE25B16D4C5Q37139289-8ADD0034-50CB-45A3-869F-D23A10D65E03Q37201249-3FF8E894-8160-4C9F-863A-8005DA423115Q37687521-5E2BD648-19E9-4D4D-BA8C-31E8BB585FF3Q38238671-D2B6068D-1959-4501-9E75-8C7BD4BD48DBQ38633256-6DBD1805-6136-4CBB-AD90-203995794D7CQ39112430-F60A7ACB-98E4-4F2E-AF09-D89EFB6A3F8AQ47601835-12AF043D-415D-4ED1-8F85-D8816117A657Q47766837-C044AABE-BD5F-44E6-974D-5A134603CF24Q48147488-09F61F73-1A59-4552-9941-029D663AB89CQ58743732-16525DB0-7F58-46D0-9717-9708A289C725
P2860
The structure of the ARE-binding domains of Hu antigen R (HuR) undergoes conformational changes during RNA binding
description
2013 nî lūn-bûn
@nan
2013 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի մարտին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年学术文章
@wuu
2013年学术文章
@zh-cn
2013年学术文章
@zh-hans
2013年学术文章
@zh-my
2013年学术文章
@zh-sg
2013年學術文章
@yue
name
The structure of the ARE-bindi ...... nal changes during RNA binding
@ast
The structure of the ARE-bindi ...... nal changes during RNA binding
@en
The structure of the ARE-bindi ...... nal changes during RNA binding
@nl
type
label
The structure of the ARE-bindi ...... nal changes during RNA binding
@ast
The structure of the ARE-bindi ...... nal changes during RNA binding
@en
The structure of the ARE-bindi ...... nal changes during RNA binding
@nl
prefLabel
The structure of the ARE-bindi ...... nal changes during RNA binding
@ast
The structure of the ARE-bindi ...... nal changes during RNA binding
@en
The structure of the ARE-bindi ...... nal changes during RNA binding
@nl
P2093
P2860
P3181
P1476
The structure of the ARE-bindi ...... nal changes during RNA binding
@en
P2093
Fuxing Zeng
Huihui Liu
Maikun Teng
Zexian Liu
P2860
P304
P3181
P356
10.1107/S0907444912047828
P50
P577
2013-03-01T00:00:00Z