Evidence map›Paper›PMID 34280436›Full record

ArticleThe Journal of biological chemistry2021

Letting go: Deep computational modeling insights into pH-dependent calcium affinity.

Matthias Buck

Abstract readComment
In one paragraph

Article in The Journal of biological chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author.

Matthias BuckDepartment of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio, USA. Electronic address: Matthias.Buck@case.edu.

Funding

Structure and function of plexin - co-receptor interactionsR01EY029169 · NEI · CASE WESTERN RESERVE UNIVERSITY · PI BUCK, MATTHIAS · 2018 to 2021
$2.1M
NEI NIH HHS R01 EY029169
6 · The paper itself

Abstract

Calcium and other cofactors can feature as key additions to a molecular interface, to the extent that the cofactor is completely buried in the bound state. How can such an interaction be regulated then? The answer: By facilitating a switch through an allosteric network. Although a number of unbinding mechanisms are being characterized, an extensive computational study by Joswig et al. reveals a detailed model for the pattern recognition receptor langerin.

Indexed as

Lectins, C-TypeMannose-Binding LectinsAntigens, CDCalciumHydrogen-Ion ConcentrationAntigens, CDCalciumLectins, C-TypeMannose-Binding Lectinsallosteryendosomelangerinlectin receptormolecular dynamics simulationprotein–calcium interactionprotein–carbohydrate bindingprotein–ligand dissociationstructure–function relationshipunbinding process

Identifiers

PMID34280436
PMCPMC8350533

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.