Evidence map›Paper›PMID 21936556›Full record

ArticleJournal of the American Chemical Society2011

An active-site guanine participates in glmS ribozyme catalysis in its protonated state.

Júlia Viladoms, Lincoln G Scott, Martha J Fedor

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Assessing the Potential Effects of Active Site MgThe journal of physical chemistry letters · 2016
    Article
  7. Article
  8. Article
  9. Article
  10. Role of tautomerism in RNA biochemistry.RNA (New York, N.Y.) · 2015
    Review
  11. Synthesis of 2'-O-photocaged ribonucleoside phosphoramidites.Nucleosides, nucleotides & nucleic acids · 2015
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Towards Accurate Prediction of Protonation Equilibrium of Nucleic Acids.The journal of physical chemistry letters · 2013
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Júlia ViladomsDepartment of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, United States.
Lincoln G Scott
Martha J Fedor
Scripps Research Institute · USCassia (United States) · US

Funding

OPTIMIZATION OF INTERMOLECULAR HAIRPIN RNA CATALYSISR01GM046422 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI FEDOR, MARTHA J. · 1992 to 2010
$4.0M
NIGMS NIH HHS R01 GM046422
6 · The paper itself

Abstract

Active-site guanines that occupy similar positions have been proposed to serve as general base catalysts in hammerhead, hairpin, and glmS ribozymes, but no specific roles for these guanines have been demonstrated conclusively. Structural studies place G33(N1) of the glmS ribozyme of Bacillus anthracis within hydrogen-bonding distance of the 2'-OH nucleophile. Apparent pK(a) values determined from the pH dependence of cleavage kinetics for wild-type and mutant glmS ribozymes do not support a role for G33, or any other active-site guanine, in general base catalysis. Furthermore, discrepancies between apparent pK(a) values obtained from functional assays and microscopic pK(a) values obtained from pH-fluorescence profiles with ribozymes containing a fluorescent guanosine analogue, 8-azaguanosine, at position 33 suggest that the pH-dependent step in catalysis does not involve G33 deprotonation. These results point to an alternative model in which G33(N1) in its neutral, protonated form donates a hydrogen bond to stabilize the transition state.

Indexed as

Bacillus anthracisBiocatalysisCatalytic DomainGuanineModels, MolecularRNA, CatalyticGuanineRNA, Catalytic

Identifiers

PMID21936556
PMCPMC3212626
OpenAlexW1985401314

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.