Use of binding energy by an RNA enzyme for catalysis by positioning and substrate destabilization.
about
Ras-catalyzed hydrolysis of GTP: a new perspective from model studiesA relaxed active site after exon ligation by the group I intronNMR Localization of Divalent Cations at the Active Site of the Neurospora VS Ribozyme Provides Insights into RNA–Metal-Ion InteractionsThree metal ions at the active site of the Tetrahymena group I ribozymeEnergetic contribution of non-essential 5' sequence to catalysis in a hepatitis delta virus ribozymeMetal ion catalysis during group II intron self-splicing: parallels with the spliceosomeInsight into the functional versatility of RNA through model-making with applications to data fitting.An unconventional origin of metal-ion rescue and inhibition in the Tetrahymena group I ribozyme reaction.A kinetic and thermodynamic framework for the Azoarcus group I ribozyme reaction.Recognition of the 5' leader of pre-tRNA substrates by the active site of ribonuclease P.Extraordinarily slow binding of guanosine to the Tetrahymena group I ribozyme: implications for RNA preorganization and functionDetermining the catalytic role of remote substrate binding interactions in ketosteroid isomerase.Nonspecific binding to structured RNA and preferential unwinding of an exposed helix by the CYT-19 protein, a DEAD-box RNA chaperone.Structure-function analysis from the outside in: long-range tertiary contacts in RNA exhibit distinct catalytic roles.Ribozyme catalysis: not different, just worse.An active site rearrangement within the Tetrahymena group I ribozyme releases nonproductive interactions and allows formation of catalytic interactions.Ground state destabilization from a positioned general base in the ketosteroid isomerase active site.Thermodynamic evidence for negative charge stabilization by a catalytic metal ion within an RNA active siteThe change in hydrogen bond strength accompanying charge rearrangement: implications for enzymatic catalysis.Why nature really chose phosphate.Metal ion catalysis during the exon-ligation step of nuclear pre-mRNA splicing: extending the parallels between the spliceosome and group II intronsProbing the role of a secondary structure element at the 5'- and 3'-splice sites in group I intron self-splicing: the tetrahymena L-16 ScaI ribozyme reveals a new role of the G.U pair in self-splicingRNA catalytic activity as a probe of chaperone-mediated RNA folding.Tightening of active site interactions en route to the transition state revealed by single-atom substitution in the guanosine-binding site of the Tetrahymena group I ribozyme.A base triple in the Tetrahymena group I core affects the reaction equilibrium via a threshold effect.Kinetic characterization of the first step of the ribozyme-catalyzed trans excision-splicing reaction.Metal ion catalysis during splicing of premessenger RNA
P2860
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P2860
Use of binding energy by an RNA enzyme for catalysis by positioning and substrate destabilization.
description
1995 nî lūn-bûn
@nan
1995 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Use of binding energy by an RN ...... and substrate destabilization.
@ast
Use of binding energy by an RN ...... and substrate destabilization.
@en
Use of binding energy by an RN ...... and substrate destabilization.
@nl
type
label
Use of binding energy by an RN ...... and substrate destabilization.
@ast
Use of binding energy by an RN ...... and substrate destabilization.
@en
Use of binding energy by an RN ...... and substrate destabilization.
@nl
prefLabel
Use of binding energy by an RN ...... and substrate destabilization.
@ast
Use of binding energy by an RN ...... and substrate destabilization.
@en
Use of binding energy by an RN ...... and substrate destabilization.
@nl
P2093
P2860
P356
P1476
Use of binding energy by an RN ...... and substrate destabilization.
@en
P2093
D Herschlag
G J Narlikar
T S McConnell
V Gopalakrishnan
P2860
P304
P356
10.1073/PNAS.92.9.3668
P407
P577
1995-04-01T00:00:00Z