The kinetic folding pathway of the Tetrahymena ribozyme reveals possible similarities between RNA and protein folding (Q71031202)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8612073%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

title

The kinetic folding pathway of the Tetrahymena ribozyme reveals possible similarities between RNA and protein folding (English)

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15 October 2019

Zarrinkar PP

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15 October 2019

Williamson JR

series ordinal

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15 October 2019

publication date

1 May 1996

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Nature structural biology

15 October 2019

published in

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15 October 2019

volume

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15 October 2019

issue

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15 October 2019

page(s)

432-438

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15 October 2019

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RNA structure at high resolution

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The time dependence of chemical modification reveals slow steps in the folding of a group I ribozyme

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Ionic interactions and the global conformations of the hammerhead ribozyme

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Visualizing the higher order folding of a catalytic RNA molecule

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RNA chaperones and the RNA folding problem

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Monitoring of the cooperative unfolding of the sunY group I intron of bacteriophage T4. The active form of the sunY ribozyme is stabilized by multiple interactions with 3' terminal intron components

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Control of translation by mRNA secondary structure: the importance of the kinetics of structure formation

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Higher order folding and domain analysis of the ribozyme from Bacillus subtilis ribonuclease P.

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Protein facilitation of group I intron splicing by assembly of the catalytic core and the 5' splice site domain

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Assembly of a ribonucleoprotein catalyst by tertiary structure capture

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Kinetic intermediates in RNA folding

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The P9.1-P9.2 peripheral extension helps guide folding of the Tetrahymena ribozyme

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Modelling of the three-dimensional architecture of group I catalytic introns based on comparative sequence analysis

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An independently folding domain of RNA tertiary structure within the Tetrahymena ribozyme

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Visualization of a tertiary structural domain of the Tetrahymena group I intron by electron microscopy

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Role of conserved sequence elements 9L and 2 in self-splicing of the Tetrahymena ribosomal RNA precursor

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Phylogenetic and genetic evidence for base-triples in the catalytic domain of group I introns

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In vitro genetic analysis of the hinge region between helical elements P5-P4-P6 and P7-P3-P8 in the sunY group I self-splicing intron

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Nucleoside triples from the group I intron

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Catalysis of RNA cleavage by the Tetrahymena thermophila ribozyme. 1. Kinetic description of the reaction of an RNA substrate complementary to the active site

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Guanosine binding to the Tetrahymena ribozyme: thermodynamic coupling with oligonucleotide binding

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GAAA tetraloop and conserved bulge stabilize tertiary structure of a group I intron domain

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The neurospora CYT-18 protein suppresses defects in the phage T4 td intron by stabilizing the catalytically active structure of the intron core

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Cooperative binding of magnesium to transfer ribonucleic acid studied by a fluorescent probe

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Conformational changes of transfer RNA. The role of magnesium(II)

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Protein folding intermediates: native-state hydrogen exchange

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Finding the right fold

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Understanding how proteins fold: the lysozyme story so far.

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Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin

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Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2

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The folding of an enzyme. VI. The folding pathway of barnase: comparison with theoretical models

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Bipartite structure of the alpha-lactalbumin molten globule

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Sequence-specific endoribonuclease activity of the Tetrahymena ribozyme: enhanced cleavage of certain oligonucleotide substrates that form mismatched ribozyme-substrate complexes

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31 March 2020

Identifiers

DOI

10.1038/NSB0596-432

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8612073%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8612073%20AND%20SRC:MED&resulttype=core&format=json