about
The human HDV-like CPEB3 ribozyme is intrinsically fast-reactingDEAD-box proteins as RNA helicases and chaperonesRNA helicase proteins as chaperones and remodelersDEAD-box helicase proteins disrupt RNA tertiary structure through helix captureThe Thermus thermophilus DEAD box helicase Hera contains a modified RNA recognition motif domain loosely connected to the helicase coreStructure of the RNA Binding Domain of a DEAD-Box Helicase Bound to Its Ribosomal RNA Target Reveals a Novel Mode of Recognition by an RNA Recognition MotifA ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesisNondenaturing purification of co-transcriptionally folded RNA avoids common folding heterogeneityVisualizing the formation of an RNA folding intermediate through a fast highly modular secondary structure switchRNA chaperones buffer deleterious mutations in E. coli.mRNA secondary structures fold sequentially but exchange rapidly in vivo.Protein roles in group I intron RNA folding: the tyrosyl-tRNA synthetase CYT-18 stabilizes the native state relative to a long-lived misfolded structure without compromising folding kinetics.Laser-assisted single-molecule refolding (LASR).Predicting RNA structure by multiple template homology modeling.Nonhierarchical ribonucleoprotein assembly suggests a strain-propagation model for protein-facilitated RNA folding.Fast flexible modeling of RNA structure using internal coordinates.Evaluating target silencing by short hairpin RNA mediated by the group I intron in cultured mammalian cellsDEAD-box protein CYT-19 is activated by exposed helices in a group I intron RNA.Multiple unfolding events during native folding of the Tetrahymena group I ribozymeNegative correlation between expression level and evolutionary rate of long intergenic noncoding RNAs.Single-molecule derivation of salt dependent base-pair free energies in DNAFolding pathways of the Tetrahymena ribozymeRoles of DEAD-box proteins in RNA and RNP Folding.The structural and functional diversity of metabolite-binding riboswitchesSolution structure of RNase P RNA.RNA structure and the mechanisms of alternative splicing.Single-molecule force spectroscopy of the add adenine riboswitch relates folding to regulatory mechanismThe Azoarcus group I intron ribozyme misfolds and is accelerated for refolding by ATP-dependent RNA chaperone proteins.Rapid RNA-ligand interaction analysis through high-information content conformational and stability landscapes.An active site rearrangement within the Tetrahymena group I ribozyme releases nonproductive interactions and allows formation of catalytic interactions.Secondary structure encodes a cooperative tertiary folding funnel in the Azoarcus ribozyme.A DEAD-box RNA helicase promotes thermodynamic equilibration of kinetically trapped RNA structures in vivoRNA dynamics: it is about time.The long-range P3 helix of the Tetrahymena ribozyme is disrupted during folding between the native and misfolded conformationsKinetic and thermodynamic framework for P4-P6 RNA reveals tertiary motif modularity and modulation of the folding preferred pathway.Raman crystallography of RNA.Biochemical and structural insights into RNA binding by Ssh10b, a member of the highly conserved Sac10b protein family in Archaea.Taming free energy landscapes with RNA chaperones.Understanding the transcriptome through RNA structure.Toward a molecular understanding of RNA remodeling by DEAD-box proteins.
P2860
Q24630713-D403B364-0781-47F0-ACD3-26B70B381CBCQ24631331-3D311BA7-731C-4C63-8472-AC0658DF2C70Q27025517-0CBF6838-DFFE-4AEA-AC42-F2912EB69603Q27313750-27840554-D927-4033-86D0-2F5DD86E990EQ27657196-FF18B552-9882-44E4-BBDD-C5D6229B5489Q27663709-2C2CD3FC-5A0B-4E87-B7A1-F5136AC184BBQ27931602-399B0FE7-342B-4012-8C12-B287CC682E70Q28475571-94D41060-63E2-4E57-835A-DA5F7D029910Q28830141-8D341902-D70E-486A-BE33-A8DDF54678A5Q30373007-AF33D430-1587-48C8-98A8-14ABFB2403BEQ33531744-1D9A0A43-0B1D-4EC8-8B3F-5BDBB8FD6410Q33618172-75378425-BBAB-4584-9E89-3A4F282EF62EQ33698740-717B37FC-278E-4BB6-9820-D8908ACCD5F1Q33861849-A3D866D2-6BED-4B5B-9492-ABB1ECD4A6EAQ33949652-8398C825-B4E9-4138-8D93-0A35421A2EBBQ33967798-95465771-D873-4674-9CC4-574161BC5E3FQ33969033-DE768C83-AF18-4441-99C1-F2E03C9E8F38Q33971823-D3E8E9D9-677C-4742-972F-66CE1AD7C9A6Q34001156-43986782-E8A9-4BC3-B600-5D1AD5D3A120Q34071155-A0F4E901-9DDE-41B7-AEC0-C0D8BA634152Q34100246-F258E078-DE88-4881-BAF9-990AE018A9A4Q34255755-33B7E1F7-061D-400F-A0DB-24A0E1AE3624Q34775640-D6557C4C-9642-4EAC-B303-1C22224CB7CAQ34965135-BA43D250-AA6C-4C2F-8BBB-C7E89AB67C44Q34985827-064EC739-78DF-49CC-BF79-407113AC841DQ35146258-79795AB1-944C-4C1A-831B-34A994A4E4E4Q35224302-42A5BA11-8CF1-4267-BC64-09C35ADEF5DFQ35423608-A02A79CE-6DA0-4F07-AAC9-CB11A6AB1F16Q36392455-CAAF0860-3476-49B9-92D2-A32333145E95Q36406303-98DCF40B-7812-4FBE-A8D8-318052A001AFQ36443259-766CDDE3-90C0-4769-A1F2-F3A8276D461DQ36566607-B1B00610-EBF7-4583-A0AC-BC01E1ACE968Q36967162-BB020E6B-ABCE-43E0-B0F5-F9FBFF73F07AQ36997306-37446251-0621-478B-9589-18ABC67ADCABQ37213759-F4AB1B76-B027-418C-BD73-72768C9D864EQ37366827-91332502-D6FE-4F22-B4F7-225E27DAB218Q37488472-79F6E19F-0663-4670-B16A-475875C5C154Q37806521-DA354BC8-F8B8-4711-A4B4-AAA6DF159B73Q37919342-4B2082EB-8134-4252-8864-656DEFD9E72FQ38045141-35156F00-B897-46EA-852A-32E53EF9AF56
P2860
description
2008 nî lūn-bûn
@nan
2008 թուականին հրատարակուած գիտական յօդուած
@hyw
2008 թվականին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
RNA misfolding and the action of chaperones
@ast
RNA misfolding and the action of chaperones
@en
RNA misfolding and the action of chaperones
@nl
type
label
RNA misfolding and the action of chaperones
@ast
RNA misfolding and the action of chaperones
@en
RNA misfolding and the action of chaperones
@nl
prefLabel
RNA misfolding and the action of chaperones
@ast
RNA misfolding and the action of chaperones
@en
RNA misfolding and the action of chaperones
@nl
P2860
P3181
P356
P1476
RNA misfolding and the action of chaperones
@en
P2093
Rick Russell
P2860
P3181
P356
10.2741/2557
P407
P577
2008-01-01T00:00:00Z