The C-terminal domain of Escherichia coli Hfq increases the stability of the hexamer.
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Hfq variant with altered RNA binding functionsThe Escherichia Coli Hfq Protein: An Unattended DNA-Transactions RegulatorStructure of Escherichia coli Hfq bound to polyriboadenylate RNAStructural analysis of full-length Hfq fromEscherichia coliHfq-bridged ternary complex is important for translation activation of rpoS by DsrAMapping Hfq-RNA interaction surfaces using tryptophan fluorescence quenchingEscherichia coli Hfq has distinct interaction surfaces for DsrA, rpoS and poly(A) RNAsBicaudal C and trailer hitch have similar roles in gurken mRNA localization and cytoskeletal organization.Compaction and condensation of DNA mediated by the C-terminal domain of HfqClostridium difficile Hfq can replace Escherichia coli Hfq for most of its functionE. coli DNA associated with isolated Hfq interacts with Hfq's distal surface and C-terminal domainStructural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq.Structural insights into the recognition of the internal A-rich linker from OxyS sRNA by Escherichia coli Hfq.Hfq plays important roles in virulence and stress adaptation in Cronobacter sakazakii ATCC 29544.New insight into the structure and function of Hfq C-terminus.Effects of Hfq on the conformation and compaction of DNA.Characterization of Vibrio cholerae Hfq provides novel insights into the role of the Hfq C-terminal region.Quality control of bacterial mRNA decoding and decay.The bacterial protein Hfq: much more than a mere RNA-binding factor.Structure and RNA-binding properties of the bacterial LSm protein Hfq.The C-terminal domain of Escherichia coli Hfq is required for regulation.Structural and dynamic properties of the C-terminal region of the Escherichia coli RNA chaperone Hfq: integrative experimental and computational studies.Muscleblind-like 1 interacts with RNA hairpins in splicing target and pathogenic RNAs.RNAs actively cycle on the Sm-like protein Hfq.Membrane association of the bacterial riboregulator Hfq and functional perspectives.Acidic C-terminal domains autoregulate the RNA chaperone HfqHexamer to monomer equilibrium of E. coli Hfq in solution and its impact on RNA annealing.Conformational transition of DNA bound to Hfq probed by infrared spectroscopy.Hfq chaperone brings speed dating to bacterial sRNA
P2860
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P2860
The C-terminal domain of Escherichia coli Hfq increases the stability of the hexamer.
description
2004 nî lūn-bûn
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2004 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2004年の論文
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2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
The C-terminal domain of Escherichia coli Hfq increases the stability of the hexamer.
@ast
The C-terminal domain of Escherichia coli Hfq increases the stability of the hexamer.
@en
type
label
The C-terminal domain of Escherichia coli Hfq increases the stability of the hexamer.
@ast
The C-terminal domain of Escherichia coli Hfq increases the stability of the hexamer.
@en
prefLabel
The C-terminal domain of Escherichia coli Hfq increases the stability of the hexamer.
@ast
The C-terminal domain of Escherichia coli Hfq increases the stability of the hexamer.
@en
P2093
P1433
P1476
The C-terminal domain of Escherichia coli Hfq increases the stability of the hexamer
@en
P2093
Jérôme Seguin
Marc Folichon
Olivier Pellegrini
Philippe Derreumaux
Philippe Regnier
Sergio Marco
P2860
P304
P356
10.1111/J.1432-1033.2004.04026.X
P407
P577
2004-04-01T00:00:00Z