Evidence map›Paper›PMID 32916312›Full record

ArticleEuropean journal of medicinal chemistry2020

Some thermodynamic effects of varying nonpolar surfaces in protein-ligand interactions.

David L Cramer, Bo Cheng, Jianhua Tian, John H Clements, Rachel M Wypych, Stephen F Martin

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

Article in European journal of medicinal chemistry, 2020. 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
0.7field-weighted citation impact, top 32% 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, 10 citations in OpenAlex.

  1. Article
  2. Article
  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

6 authors at 1 institution in 1 country.

David L CramerDepartment of Chemistry and the Institute of Cellular and Molecular Biology, The University of Texas, Austin, TX 78712, USA.
Bo ChengDepartment of Chemistry and the Institute of Cellular and Molecular Biology, The University of Texas, Austin, TX 78712, USA.
Jianhua TianDepartment of Chemistry and the Institute of Cellular and Molecular Biology, The University of Texas, Austin, TX 78712, USA.
John H ClementsDepartment of Chemistry and the Institute of Cellular and Molecular Biology, The University of Texas, Austin, TX 78712, USA.
Rachel M WypychDepartment of Chemistry and the Institute of Cellular and Molecular Biology, The University of Texas, Austin, TX 78712, USA.
Stephen F MartinDepartment of Chemistry and the Institute of Cellular and Molecular Biology, The University of Texas, Austin, TX 78712, USA. Electronic address: sfmartin@mail.utexas.edu.
The University of Texas at Austin · US

Funding

Studies of Molecular Recognition in Biological SystemsR01GM084965 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI MARTIN, STEPHEN · 2008 to 2010
$880k
NIGMS NIH HHS R01 GM084965
6 · The paper itself

Abstract

Understanding how making structural changes in small molecules affects their binding affinities for targeted proteins is central to improving strategies for rational drug design. To assess the effects of varying the nature of nonpolar groups upon binding entropies and enthalpies, we designed and prepared a set of Grb2-SH2 domain ligands, Ac-pTyr-Ac

Indexed as

CalorimetryCrystallography, X-RayGRB2 Adaptor ProteinHumansHydrophobic and Hydrophilic InteractionsLigandsOligopeptidesProtein Bindingsrc Homology DomainsThermodynamicsGRB2 Adaptor ProteinGRB2 protein, humanLigandsOligopeptidesGrb2 SH2 domainHydrophobic effectsisothermal titration calorimetryProtein-ligand interactionsThermodynamics

Identifiers

PMID32916312
PMCPMC7680455
OpenAlexW3080859858

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.