The Azoarcus group I intron ribozyme misfolds and is accelerated for refolding by ATP-dependent RNA chaperone proteins.
about
RNA helicase proteins as chaperones and remodelersDEAD-box helicase proteins disrupt RNA tertiary structure through helix captureThe DEAD-box RNA helicase Dbp2 connects RNA quality control with repression of aberrant transcription.Evolutionary evidence for alternative structure in RNA sequence co-variationFolding pathways of the Tetrahymena ribozymeA kinetic and thermodynamic framework for the Azoarcus group I ribozyme reaction.Detecting riboSNitches with RNA folding algorithms: a genome-wide benchmark.Molecular crowding overcomes the destabilizing effects of mutations in a bacterial ribozyme.Secondary structure encodes a cooperative tertiary folding funnel in the Azoarcus ribozyme.Understanding the role of three-dimensional topology in determining the folding intermediates of group I introns.Increased ribozyme activity in crowded solutions.Structural dynamics of a mitochondrial tRNA possessing weak thermodynamic stability.Toward a molecular understanding of RNA remodeling by DEAD-box proteins.Mss116p: a DEAD-box protein facilitates RNA foldingBacterial group I introns: mobile RNA catalysts.Trans-splicing with the group I intron ribozyme from Azoarcus.RNA catalytic activity as a probe of chaperone-mediated RNA folding.RNA catalysis as a probe for chaperone activity of DEAD-box helicases.Formation of Tertiary Interactions during rRNA GTPase Center Folding.Nucleobases Undergo Dynamic Rearrangements during RNA Tertiary Folding.Negative Epistasis in Experimental RNA Fitness Landscapes.Molecular chaperones maximize the native state yield on biological times by driving substrates out of equilibrium.
P2860
Q27025517-40B696AD-3A98-4271-91DF-EC6C87E91213Q27313750-E06C9AE6-7F5F-4584-8398-81606413E622Q27939370-95323F65-7BA8-4B1A-AD6B-9F95B8F2E856Q28534841-7ACE5A34-3FC7-42BC-B975-4EC6476FD105Q34255755-AF843E36-B025-4683-8AE7-CE60EA40E7DEQ34363896-F7DE42A1-C056-4E75-BBAE-4AF12CF5D406Q35089028-039D2BF5-64D3-47E3-8DB9-C0359E3C2AF3Q35097979-0523ADD0-0D62-4D35-8D24-1839DFBA5C2CQ36443259-708DCCE5-1CE6-4501-A61B-DAAC044C2620Q36700154-545BC86C-C66D-4AC5-A748-6C78B9A429EDQ37536595-AC530DCD-7706-4427-8CF0-A1628086DC86Q37701405-3A4F1491-B8E7-41E1-A880-6302AAB07361Q38045141-4FE0F69A-86C7-4163-9A3A-31F10C74FE4CQ38051971-A663E62D-E45B-47EA-9101-E7DCC98E4068Q38722587-28F4274F-3FD0-46A9-BB1B-787E512A4084Q41878197-CCB8B1C1-D453-4657-AF60-97DCED4C5384Q41918015-6032546C-1A20-4ED0-9087-B0E76E0B1B73Q42097520-31A915A4-F6BB-4C41-84FB-11CD7393A285Q42104461-0E2C3805-30A0-402C-AE4A-2EDE174D89A9Q42837216-CAA0EB47-E66E-4EFC-AA80-C86A8364037DQ46812108-99582E3B-B8A9-4FA2-9179-76140E14AB35Q47317793-260783D6-AD26-44C5-9915-D19FF61BDDC9
P2860
The Azoarcus group I intron ribozyme misfolds and is accelerated for refolding by ATP-dependent RNA chaperone proteins.
description
2011 nî lūn-bûn
@nan
2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
The Azoarcus group I intron ri ...... endent RNA chaperone proteins.
@ast
The Azoarcus group I intron ri ...... endent RNA chaperone proteins.
@en
type
label
The Azoarcus group I intron ri ...... endent RNA chaperone proteins.
@ast
The Azoarcus group I intron ri ...... endent RNA chaperone proteins.
@en
prefLabel
The Azoarcus group I intron ri ...... endent RNA chaperone proteins.
@ast
The Azoarcus group I intron ri ...... endent RNA chaperone proteins.
@en
P2093
P2860
P921
P356
P1476
The Azoarcus group I intron ri ...... endent RNA chaperone proteins.
@en
P2093
Rick Russell
Selma Sinan
Xiaoyan Yuan
P2860
P304
37304-37312
P356
10.1074/JBC.M111.287706
P407
P577
2011-08-30T00:00:00Z