Evidence map›Paper›PMID 33075302›Full record

ArticleArchives of biochemistry and biophysics2020

The phosphate moiety of phosphoenolpyruvate does NOT contribute to allosteric regulation of liver pyruvate kinase by fructose-1,6-bisphosphate

Benjamin M Chappell, Aron W Fenton

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

Article in Archives of biochemistry and biophysics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 54% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

2 authors at 1 institution in 1 country.

Benjamin M ChappellDepartment of Biochemistry and Molecular Biology, The University of Kansas Medical Center, Kansas City, KS, United States.
Aron W FentonDepartment of Biochemistry and Molecular Biology, The University of Kansas Medical Center, Kansas City, KS, United States. Electronic address: afenton@kumc.edu.
University of Kansas Medical Center · US

Funding

Dissecting Allostery in Pyruvate KinaseR01GM115340 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI FENTON, ARON W · 2016 to 2019
$1.4M
NIGMS NIH HHS R01 GM115340
6 · The paper itself

Abstract

A linked-function theory for allostery allows for a differentiation between those protein-ligand interactions that contribute the most to ligand binding and those protein-ligand interactions that contribute to the allosteric mechanism. This potential distinction is the basis for analogue studies used to determine which chemical moieties on the allosteric effector contribute to allostery. Although less recognized, the same separation of functions is possible for substrate-enzyme interactions. When evaluating allosteric regulation in human liver pyruvate kinase, the use of a range of monovalent cations (K

Indexed as

Allosteric RegulationFructosediphosphatesHumansLiverPhosphoenolpyruvatePyruvate Kinasefructose-1,6-diphosphateFructosediphosphatesPhosphoenolpyruvatePyruvate KinaseAllosteric regulationAllosteryPyruvate kinaseSubstrate analogue

Identifiers

PMID33075302
PMCPMC8201620
OpenAlexW3092837904

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.