Evidence map›Paper›PMID 21108273›Full record

ArticleChembiochem : a European journal of chemical biology2010

Analysis of metal ion dependence in glmS ribozyme self-cleavage and coenzyme binding.

Kevin Klawuhn, Joshua A Jansen, Joshua Souchek, Garrett A Soukup, Juliane K Soukup

Open access · bronzeAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. A divalent cation-dependent variant of theRNA (New York, N.Y.) · 2017
    Article
  5. Assessing the Potential Effects of Active Site MgThe journal of physical chemistry letters · 2016
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Mechanism and distribution of glmS ribozymes.Methods in molecular biology (Clifton, N.J.) · 2012
    Article
  11. Article
  12. Review
  13. Article
  14. 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

5 authors at 1 institution in 1 country.

Kevin KlawuhnDepartment of Chemistry, Creighton University, 2500 California Plaza, Omaha, Nebraska 68178, USA.
Joshua A Jansen
Joshua Souchek
Garrett A Soukup
Juliane K Soukup
Creighton University · US

Funding

ZINC FINGER-INSPIRED FLUORESCENT CHEMOSENSORSP20RR016469 · NCRR · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI TURPEN, JAMES B · 2001 to 2011
$36.2M
Development of Artificial Agonists for a Bacterial RiboswitchR15GM083641 · NIGMS · CREIGHTON UNIVERSITY · PI STRAUSS-SOUKUP, JULIANE K · 2007 to 2010
$781k
NCRR NIH HHS P20 RR016469NCRR NIH HHS P20RR016469NIGMS NIH HHS R15 GM083641PHS HHS R15M083641
6 · The paper itself

Abstract

The bacterial glmS ribozyme is mechanistically unique among both riboswitches and RNA catalysts. Its self-cleavage activity is the basis of riboswitch regulation of glucosamine-6-phosphate (GlcN6P) production, and catalysis requires GlcN6P as a coenzyme. Previous work has shown that the coenzyme amine of GlcN6P is essential for glmS ribozyme self-cleavage, as is its protonation state. Metal ions are also essential within the glmS ribozyme core for both structure and function of the ribozyme. Although metal ions do not directly promote catalysis, we show that metal ion identity and the varying physicochemical properties of metal ions have an impact on the rate of glmS ribozyme self-cleavage. Specifically, these studies demonstrate that metal ion identity influences the overall apparent pK(a) of ribozyme self-cleavage, and metal ion binding largely reflects phosphate oxygen affinity. Results suggest that metal ions take alternative roles in supporting the mechanism of catalysis.

Indexed as

Bacillus cereusBacterial ProteinsCoenzymesGlucosamineGlucose-6-PhosphateGlutamine-Fructose-6-Phosphate Transaminase (Isomerizing)MetalsProtein BindingRNA, CatalyticBacterial ProteinsCoenzymescomponent S, glutamate mutase protein, BacteriaGlucosamineglucosamine 6-phosphateGlucose-6-PhosphateGlutamine-Fructose-6-Phosphate Transaminase (Isomerizing)MetalsRNA, Catalytic

Identifiers

PMID21108273
PMCPMC3251013
OpenAlexW1974732040

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.