Evidence map›Paper›PMID 39109193›Full record

ArticlemicroPublication biology2024

Potassium cations expand the conformation ensemble of

Abigail Sholes, Roland Asongakap, Sophia Jaconski, Jonathan Monroe, Christopher E Berndsen

Abstract read
In one paragraph

Article in microPublication biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. 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.

Abigail SholesChemistry and Biochemistry, James Madison University.
Roland AsongakapChemistry and Biochemistry, University of Illinois-Chicago.
Sophia JaconskiChemistry and Biochemistry, James Madison University.
Jonathan MonroeChemistry and Biochemistry, James Madison University.
Christopher E BerndsenChemistry and Biochemistry, James Madison University.

Funding

User Training and OutreachP30GM124169 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI PAUL David ADAMS, Gregory L Hura · 2017 to 2026
$28.6M
A Pixel Array Detector System for Small Angle X-ray ScatteringS10OD018483 · OD · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI CLASSEN, SCOTT · 2014 to 2014
$998k
NIGMS NIH HHS P30 GM124169NIH HHS S10 OD018483
6 · The paper itself

Abstract

The process for and regulatory mechanism controlling the synthesis and degradation of the polysaccharide starch are only superficially understood. β-amylases (BAMs) are enzymes that hydrolyze starch into maltose which is further used to drive metabolism and other cellular processes. Most BAMs in plants can function as monomeric enzymes and have hyperbolic kinetics. BAM2 from

Identifiers

PMID39109193
PMCPMC11301517

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.