Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium
about
Structural basis for DNA-mediated allosteric regulation facilitated by the AAA+ module of Lon proteaseAnalytical Ultracentrifugation as a Tool to Study Nonspecific Protein-DNA InteractionsThe crystal structure and small-angle X-ray analysis of CsdL/TcdA reveal a new tRNA binding motif in the MoeB/E1 superfamilyIn vivo kinetics of U4/U6·U5 tri-snRNP formation in Cajal bodies.Using Lamm-Equation modeling of sedimentation velocity data to determine the kinetic and thermodynamic properties of macromolecular interactions.Analysis of PKR activation using analytical ultracentrifugationMeCP2 binds cooperatively to its substrate and competes with histone H1 for chromatin binding sitesIonic interactions between PRNA and P protein in Bacillus subtilis RNase P characterized using a magnetocapture-based assayThe role of human Dicer-dsRBD in processing small regulatory RNAsDetermination of protein complex stoichiometry through multisignal sedimentation velocity experiments.Disconnected Interacting Protein 1 binds with high affinity to pre-tRNA and ADAT.Analysis of high-affinity binding of protein kinase R to double-stranded RNAMechanism of PKR Activation by dsRNA.Domain stabilities in protein kinase R (PKR): evidence for weak interdomain interactionsRNA dimerization promotes PKR dimerization and activation.Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.Histidine-tag-directed chromophores for tracer analyses in the analytical ultracentrifugeAnalysis of PKR-RNA interactions by sedimentation velocity5'-triphosphate-dependent activation of PKR by RNAs with short stem-loops.Resolving the contributions of two cooperative mechanisms to the DNA binding of AGT.Electrophoretic mobility shift assay (EMSA) for detecting protein-nucleic acid interactions.Interaction of PKR with single-stranded RNAFunctional energetic landscape in the allosteric regulation of muscle pyruvate kinase. 1. Calorimetric studyFunctional energetic landscape in the allosteric regulation of muscle pyruvate kinase. 2. Fluorescence study.
P2860
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P2860
Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium
description
2004 nî lūn-bûn
@nan
2004 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մարտին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
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
Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium
@ast
Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium
@en
Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium
@nl
type
label
Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium
@ast
Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium
@en
Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium
@nl
prefLabel
Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium
@ast
Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium
@en
Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium
@nl
P2860
P1476
Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium
@en
P2093
James L Cole
Jason W Ucci
P2860
P304
P356
10.1016/J.BPC.2003.10.033
P577
2004-03-01T00:00:00Z