The long-range electrostatic interactions control tRNA-aminoacyl-tRNA synthetase complex formation.
about
The role of positively charged amino acids and electrostatic interactions in the complex of U1A protein and U1 hairpin II RNADiscovering RNA-protein interactome by using chemical context profiling of the RNA-protein interfaceInteraction of the influenza A virus polymerase PB2 C-terminal region with importin alpha isoforms provides insights into host adaptation and polymerase assembly.Kinetic and structural changes in HsmtPheRS, induced by pathogenic mutations in human FARS2.Idiosyncratic helix-turn-helix motif in Methanosarcina barkeri seryl-tRNA synthetase has a critical architectural role.Intra-protein compensatory mutations analysis highlights the tRNA recognition regions in aminoacyl-tRNA synthetases.
P2860
The long-range electrostatic interactions control tRNA-aminoacyl-tRNA synthetase complex formation.
description
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2003年の論文
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@zh-hant
2003年論文
@zh-hk
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name
The long-range electrostatic i ...... synthetase complex formation.
@en
type
label
The long-range electrostatic i ...... synthetase complex formation.
@en
prefLabel
The long-range electrostatic i ...... synthetase complex formation.
@en
P2860
P356
P1433
P1476
The long-range electrostatic i ...... A synthetase complex formation
@en
P2093
Mark Safro
P2860
P304
P356
10.1110/PS.0301203
P577
2003-06-01T00:00:00Z