Visualizing the formation of an RNA folding intermediate through a fast highly modular secondary structure switch (Q28830141)

1

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Brant Gracia

2

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Rick Russell

4

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Hashim M Al-Hashimi

Creative Commons Attribution 4.0 International

5

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language of work or name

English

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publication date

13 June 2016

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published in

Nature Communications

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volume

7

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page(s)

ncomms11768

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copyright license

start time

13 June 2016

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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Measuring Residual Dipolar Couplings in Excited Conformational States of Nucleic Acids by CEST NMR Spectroscopy

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Folding path of P5abc RNA involves direct coupling of secondary and tertiary structures

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Synthetic RNA switches as a tool for temporal and spatial control over gene expression

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Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion

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Multiple unfolding events during native folding of the Tetrahymena group I ribozyme

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Phi-value analysis for ultrafast folding proteins by NMR relaxation dispersion.

3 June 2018

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Extensive backbone dynamics in the GCAA RNA tetraloop analyzed using 13C NMR spin relaxation and specific isotope labeling

3 June 2018

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Exploring RNA folding one molecule at a time.

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RNA chaperones, RNA annealers and RNA helicases

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Probing invisible, low-populated States of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding

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An assembly landscape for the 30S ribosomal subunit

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3 June 2018

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Structural motifs in RNA.

3 June 2018

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Quantifying the energetic interplay of RNA tertiary and secondary structure interactions

3 June 2018

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3 June 2018

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RNA folding causes secondary structure rearrangement

3 June 2018

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Native secondary structure formation in RNA may be a slave to tertiary folding

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Coaxially stacked RNA helices in the catalytic center of the Tetrahymena ribozyme

3 June 2018

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RNA chaperones and the RNA folding problem

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Rearrangement of the secondary structure of the secondary structure of tryptophan sRNA in Escherichia coli

3 June 2018

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Alternative secondary structures in the 5' exon affect both forward and reverse self-splicing of the Tetrahymena intervening sequence RNA.

3 June 2018

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Concordant exploration of the kinetics of RNA folding from global and local perspectives.

3 June 2018

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The Fastest Global Events in RNA Folding: Electrostatic Relaxation and Tertiary Collapse of the Tetrahymena Ribozyme

21 January 2018

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Probing the folding landscape of the Tetrahymena ribozyme: commitment to form the native conformation is late in the folding pathway.

21 January 2018

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Probing transient Hoogsteen hydrogen bonds in canonical duplex DNA using NMR relaxation dispersion and single-atom substitution

21 January 2018

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Long-range interactions within a nonnative protein

21 January 2018

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HiTRACE: high-throughput robust analysis for capillary electrophoresis

21 January 2018

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RNA Folding at Millisecond Intervals by Synchrotron Hydroxyl Radical Footprinting

21 January 2018

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Conformational Dynamics of Bistable RNAs Studied by Time-Resolved NMR Spectroscopy

21 January 2018

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Extending the Range of Microsecond-to-Millisecond Chemical Exchange Detected in Labeled and Unlabeled Nucleic Acids by Selective Carbon R1ρNMR Spectroscopy

21 January 2018

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Kinetic intermediates in RNA folding

21 January 2018

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12 December 2020

Kinetic intermediates trapped by native interactions in RNA folding

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12 December 2020

Isolation of “Renaturable” Transfer Ribonucleic Acids

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12 December 2020

Hydrogen bonding effects on the (15)N and (1)H shielding tensors in nucleic acid base pairs

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12 December 2020

Intermediates and kinetic traps in the folding of a large ribozyme revealed by circular dichroism and UV absorbance spectroscopies and catalytic activity

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Conformational changes of transfer ribonucleic acid. Equilibrium phase diagrams

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Active site dynamics in the lead-dependent ribozyme

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Identifiers

DOI

10.1038/NCOMMS11768

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Dimensions Publication ID

ADS bibcode

2016NatCo...711768X

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1023992919

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1 reference

1 reference

PubMed publication ID

27292179

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