Evidence map›Paper›PMID 27155231›Full record

ArticleFEBS letters2016

Inhibition of yeast ribonucleotide reductase by Sml1 depends on the allosteric state of the enzyme.

Tessianna A Misko, Sanath R Wijerathna, Tomas Radivoyevitch, Anthony J Berdis, Md Faiz Ahmad, Michael E Harris, Chris G Dealwis

Open access · greenAbstract readLetter
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 33% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Review
  3. 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

7 authors at 3 institutions in 1 country.

Tessianna A MiskoDepartment of Pharmacology, Case Western Reserve University, Cleveland, OH, USA.
Sanath R WijerathnaDepartment of Pharmacology, Case Western Reserve University, Cleveland, OH, USA.
Tomas RadivoyevitchDepartment of Quantitative Health Sciences, Cleveland Clinic Foundation, OH, USA.
Anthony J BerdisDepartment of Chemistry, Cleveland State University, OH, USA.
Md Faiz AhmadDepartment of Pharmacology, Case Western Reserve University, Cleveland, OH, USA.
Michael E HarrisDepartment of Biochemistry, Case Western Reserve University, Cleveland, OH, USA.
Chris G DealwisDepartment of Pharmacology, Case Western Reserve University, Cleveland, OH, USA.
Case Western Reserve University · USCleveland Clinic · USCleveland State University · US

Funding

Structure-Function and Inhibition of Rnr1R01CA100827 · NCI · UNIVERSITY OF TENNESSEE KNOXVILLE · PI DEALWIS, CHRIS G · 2003 to 2011
$2.5M
Training Programs in Cancer PharmacologyR25CA148052 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI NOY, NOA · 2010 to 2014
$2.1M
Investigating the structural assembly of RNR multimersR01GM100887 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI DEALWIS, CHRIS G · 2012 to 2015
$1.2M
NCI NIH HHS R01 CA100827NCI NIH HHS R25 CA148052NIGMS NIH HHS R01 GM100887
6 · The paper itself

Abstract

Sml1 is an intrinsically disordered protein inhibitor of Saccharomyces cerevisiae ribonucleotide reductase (ScRR1), but its inhibition mechanism is poorly understood. RR reduces ribonucleoside diphosphates to their deoxy forms, and balances the nucleotide pool. Multiple turnover kinetics show that Sml1 inhibition of dGTP/ADP- and ATP/CDP-bound ScRR follows a mixed inhibition mechanism. However, Sml1 cooperatively binds to the ES complex in the dGTP/ADP form, whereas with ATP/CDP, Sml1 binds weakly and noncooperatively. Gel filtration and mutagenesis studies indicate that Sml1 does not alter the oligomerization equilibrium and the CXXC motif is not involved in the inhibition. The data suggest that Sml1 is an allosteric inhibitor.

Indexed as

Allosteric RegulationAmino Acid MotifsProtein BindingProtein MultimerizationRibonucleotide ReductasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsRibonucleotide ReductasesRnr1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSML1 protein, S cerevisiaeenzyme kineticsintrinsically disordered proteinmixed inhibitionnucleotidesoligomerization

Identifiers

PMID27155231
PMCPMC4925217
OpenAlexW2346262925

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.