Evidence map›Paper›PMID 35167069›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Using Surface Hydrophobicity Together with Empirical Potentials to Identify Protein-Protein Binding Sites: Application to the Interactions of E-cadherins.

Robert L Jernigan, Pranav Khade, Ambuj Kumar, Andrzej Kloczkowski

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Automatic Explanation of Protein-Protein Binding Mechanism: A Preliminary Study.Computational structural bioinformatics : international workshop, CSBW 2024, Boston, MA, USA, November 16, 2024, proceedings. Computational Structural Bioinformatics Workshop (2024 : Boston, Mass.) · 2025
    Article
  7. 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

4 authors.

Robert L JerniganRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, USA. jernigan@iastate.edu.
Pranav KhadeRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, USA.
Ambuj KumarRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, USA.
Andrzej KloczkowskiBattelle Center for Mathematical Medicine, Nationwide Children's Hospital, Columbus, OH, USA.

Funding

Novel Use of Genome Information to Understand MutationsR01HG012117 · NHGRI · IOWA STATE UNIVERSITY · PI JERNIGAN, ROBERT L, KLOCZKOWSKI, ANDRZEJ · 2021 to 2025
$2.3M
Protein Sequence MatchingR01GM127701 · NIGMS · IOWA STATE UNIVERSITY · PI JERNIGAN, ROBERT L, KLOCZKOWSKI, ANDRZEJ · 2018 to 2021
$1.4M
NHGRI NIH HHS R01 HG012117NIGMS NIH HHS R01 GM127701
6 · The paper itself

Abstract

Studying the interactions within protein structures can inform about the details of how proteins of various types interact and aggregate. Empirical contact potentials have proven to be extremely important in the evaluation of individual modeled protein structures, but have found few applications to protein-protein interactions. In part, this is caused by a lack of properly formulated potentials with a proper reference state. Since the comparisons are made between different bound structures, the proper reference state should take into account other contacts. Therefore, a preferred reference state should be defined with respect to a given residue type interacting with an average residue instead of interacting with solvent as typically is used in derivation of statistical contact potentials. Here, a two-stage procedure for generating and evaluating interacting protein pairs is described, and an example of E-cadherin interactions is shown.

Indexed as

CadherinsBinding SitesHydrophobic and Hydrophilic InteractionsProtein BindingSolventsCadherinsSolventsCalcium-dependent adhesionContact potentialsE-cadherinsHydrophobic clusterHydrophobicityProtein aggregationProtein–protein interactionsTransmembrane proteins

Identifiers

PMID35167069
PMCPMC9131873

What OpenQuestion holds

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Registered trials

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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.