Statistical analysis of sequential motifs at biologically relevant protein-protein interfaces.

Yair Frank, Ron Unger, Hanoch Senderowitz

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Article in Computational and structural biotechnology journal, 2024. 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

0.5field-weighted citation impact, top 38% 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

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 2 citations in OpenAlex.

Integrative Computational Chemistry Approaches in Modern Drug Discovery: Advances in Docking, Pharmacophore Modeling, Molecular Dynamics, and Virtual Screening.Pharmaceutics · 2026
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4 · The record

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5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Yair FrankDepartment of Chemistry, Bar-Ilan University, Ramat-Gan 5290002, Israel.

Ron UngerFaculty of Life Sciences, Bar-Ilan University, Ramat-Gan 5290002, Israel.

Hanoch SenderowitzDepartment of Chemistry, Bar-Ilan University, Ramat-Gan 5290002, Israel.

Bar-Ilan University · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Understanding protein-protein interactions (PPIs) at the molecular level may lead to innovations in medicine and biochemistry. The assumption that there are certain "hot spots" on protein surfaces that mediate their interactions with other proteins has led to a search for specific sequences involved in protein-protein contacts. In this work, we analyze sequential amino acid motifs, both at the single motif and at the motif-motif level, across a large and diverse dataset of biologically relevant protein-protein interfaces retrieved from the PDB, comparing their presence at interfaces and surfaces in a statistically rigorous manner. At the single motif level, our results indicate statistically significant over-presence of hydrophobic and in particular aromatic residues and under-presence of charged residues at protein-protein interfaces. Certain PPI-mediating motifs reported in the literature (

Indexed as

Energetic quantificationProtein-protein interactionsProtein sequencesSequential motifsStatistical analysis

Identifiers

PMID38550974

DOI10.1016/j.csbj.2024.03.004

PMCPMC10973581

OpenAlexW4392551060

What OpenQuestion holds

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LicenceCC BY-NC-ND

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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.