Probing the mechanisms of DEAD-box proteins as general RNA chaperones: the C-terminal domain of CYT-19 mediates general recognition of RNA.
about
DEAD-box proteins as RNA helicases and chaperonesRNA misfolding and the action of chaperonesRNA helicase proteins as chaperones and remodelersDEAD-box helicase proteins disrupt RNA tertiary structure through helix captureA novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibilityThe Thermus thermophilus DEAD box helicase Hera contains a modified RNA recognition motif domain loosely connected to the helicase coreStructure of the Yeast DEAD Box Protein Mss116p Reveals Two Wedges that Crimp RNAChanging nucleotide specificity of the DEAD-box helicase Hera abrogates communication between the Q-motif and the P-loopHigh-Throughput Genetic Identification of Functionally Important Regions of the Yeast DEAD-Box Protein Mss116pRecognition of two distinct elements in the RNA substrate by the RNA-binding domain of the T. thermophilus DEAD box helicase HeraDEAD-box protein CYT-19 is activated by exposed helices in a group I intron RNA.Roles of DEAD-box proteins in RNA and RNP Folding.Solution structures of DEAD-box RNA chaperones reveal conformational changes and nucleic acid tethering by a basic tailThe Azoarcus group I intron ribozyme misfolds and is accelerated for refolding by ATP-dependent RNA chaperone proteins.The DEAD-box helicase eIF4A: paradigm or the odd one out?The putative RNase P motif in the DEAD box helicase Hera is dispensable for efficient interaction with RNA and helicase activity.Unwinding RNA's secrets: advances in the biology, physics, and modeling of complex RNAs.Kinetic redistribution of native and misfolded RNAs by a DEAD-box chaperone.DEAD-box proteins can completely separate an RNA duplex using a single ATP.Superfamily 2 helicasesCrystallization and preliminary X-ray diffraction of the DEAD-box protein Mss116p complexed with an RNA oligonucleotide and AMP-PNP.The mechanism of ATP-dependent RNA unwinding by DEAD box proteins.RNA folding in living cells.Single-molecule FRET reveals nucleotide-driven conformational changes in molecular machines and their link to RNA unwinding and DNA supercoiling.Toward a molecular understanding of RNA remodeling by DEAD-box proteins.Mss116p: a DEAD-box protein facilitates RNA foldingThe Ded1/DDX3 subfamily of DEAD-box RNA helicases.When core competence is not enough: functional interplay of the DEAD-box helicase core with ancillary domains and auxiliary factors in RNA binding and unwinding.Do DEAD-box proteins promote group II intron splicing without unwinding RNA?Role of the amino terminal RHAU-specific motif in the recognition and resolution of guanine quadruplex-RNA by the DEAH-box RNA helicase RHAUFunction of the C-terminal domain of the DEAD-box protein Mss116p analyzed in vivo and in vitro.Unwinding by local strand separation is critical for the function of DEAD-box proteins as RNA chaperones.Allosteric activation of the ATPase activity of the Escherichia coli RhlB RNA helicase.Distinct RNA-unwinding mechanisms of DEAD-box and DEAH-box RNA helicase proteins in remodeling structured RNAs and RNPs.A ribonuclease III domain protein functions in group II intron splicing in maize chloroplasts.The DEAD-Box Protein CYT-19 Uses Arginine Residues in Its C-Tail To Tether RNA Substrates.The DEAD-box protein DDX43 (HAGE) is a dual RNA-DNA helicase and has a K-homology domain required for full nucleic acid unwinding activity.
P2860
Q24631331-4C5BE327-44BB-42F3-AA23-0A9C88379812Q24656891-371E3081-1DFE-4FC5-844C-AB06B831F699Q27025517-75D4EEA0-56FF-4F7F-AD72-751E86216587Q27313750-C08EF403-F70E-428E-B9C4-692E20089B96Q27653023-6514979D-427E-49D9-8863-3A4CAD39E2B6Q27657196-8A137CC4-39B0-4620-B902-DF1BFBA9565BQ27657414-33CDF2C9-5AE6-4771-A013-C0269DB508FCQ27666921-07F5E10F-F321-4DCF-BC03-2B95B1DFAB74Q27674440-D2D7CD09-07B3-4177-AACD-78993C92AFAAQ27677838-D3C9FC57-2ED6-488C-BF21-E4A4295E2F55Q33971823-C795EF1F-DAFB-4944-8DD6-7C8BE8EA0EEFQ34775640-FC1748D6-05E6-4E28-AD0D-921C30453AE4Q35134012-A2821950-E558-4263-AE88-4292A298996CQ35423608-37947532-E812-4C93-8F93-824EE071D791Q36662305-54AB8B4B-E3CA-4958-963C-C36FFB0BE657Q36935407-0DC9F546-AE41-4B39-B089-9A209D668929Q36953513-0718473E-11CC-42BD-AEF0-334F4CCAFF53Q36969447-8E61E9F1-91EC-4373-AD59-D436EF1006B8Q37068571-D2F5E8F1-B942-4E96-903F-23969613219BQ37178493-A37806CA-714F-48BC-B0BF-DCFBC4078B1AQ37287838-47618611-2503-4D3C-81C4-8B6606C18357Q37595518-C285119A-F4E0-487A-82A6-9681FFC60CA5Q37806517-0D7E967F-C0F4-49CE-B006-7B1C464222B6Q37856414-F055E738-0FD9-4DFB-9143-C50780AC42FCQ38045141-34313A35-310D-454E-8FC3-992C94F8D780Q38051971-B20FF152-A491-41BB-8BCF-A9F700E2856DQ38231370-3B128773-A32B-4E99-ACC1-7028DF22975BQ38365540-D041456D-029C-47C2-9529-3B2ECC5E87DBQ39694970-5EFC6B2A-6432-4E52-A07A-01943344781CQ39703515-3C6817E4-B60A-4737-BA76-381332D2A3E3Q41807822-E167363E-56F8-42C2-B452-B6E2246C6B57Q42103595-1D80EADD-5971-4DBA-AA80-518C78FB8555Q46828491-6214AA88-B924-47A3-B7FB-90AE638BFF7CQ47390153-689E36C1-DD0E-43C3-836A-40775B0E31C5Q48078203-AD64DEF6-C14E-4564-8419-E17A23F9D489Q48223275-97FA668E-FEDC-4D7C-A38D-26CD368CD53FQ51022151-2EA27CDA-4FCB-4270-83F9-9EE578CFBD0C
P2860
Probing the mechanisms of DEAD-box proteins as general RNA chaperones: the C-terminal domain of CYT-19 mediates general recognition of RNA.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Probing the mechanisms of DEAD ...... es general recognition of RNA.
@en
type
label
Probing the mechanisms of DEAD ...... es general recognition of RNA.
@en
prefLabel
Probing the mechanisms of DEAD ...... es general recognition of RNA.
@en
P2093
P2860
P356
P1433
P1476
Probing the mechanisms of DEAD ...... es general recognition of RNA.
@en
P2093
Alan M Lambowitz
Hari Bhaskaran
Jacob K Grohman
Mark Del Campo
Pilar Tijerina
Rick Russell
P2860
P304
P356
10.1021/BI0619472
P407
P577
2007-02-21T00:00:00Z