Evidence map›Paper›PMID 37918563›Full record

ArticleJournal of molecular biology2023

What Strengthens Protein-Protein Interactions: Analysis and Applications of Residue Correlation Networks.

Ta I Hung, Yun-Jung Hsieh, Wei-Lin Lu, Kuen-Phon Wu, Chia-En A Chang

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. AI-Guided Binding Mechanisms and Molecular Dynamics for MERS-CoV.International journal of molecular sciences · 2026
    Article
  3. Article
  4. Article
  5. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

Ta I HungDepartment of Chemistry, University of California, Riverside, United States; Department of Bioengineering, University of California, Riverside, United States.
Yun-Jung HsiehInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan; Institute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan.
Wei-Lin LuInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
Kuen-Phon WuInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan; Institute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan. Electronic address: kpwu@gate.sinica.edu.tw.
Chia-En A ChangDepartment of Chemistry, University of California, Riverside, United States. Electronic address: chiaenc@ucr.edu.
National Taiwan University · TWUniversity of California, Riverside · USInstitute of Biological Chemistry, Academia Sinica · TW

Funding

Next-Generation GPU Computing Resource for Simulating Ligand-Protein Binding Kinetics/MechanismR01GM109045 · NIGMS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI CHANG, CHIA-EN · 2014 to 2023
$2.8M
NIGMS NIH HHS R01 GM109045
6 · The paper itself

Abstract

Identifying residues critical to protein-protein binding and efficient design of stable and specific protein binders are challenging tasks. Extending beyond the direct contacts in a protein-protein binding interface, our study employs computational modeling to reveal the essential network of residue interactions and dihedral angle correlations critical in protein-protein recognition. We hypothesized that mutating residues exhibiting highly correlated dynamic motion within the interaction network could efficiently optimize protein-protein interactions to create tight and selective protein binders. We tested this hypothesis using the ubiquitin (Ub) and MERS coronaviral papain-like protease (PLpro) complex, since Ub is a central player in multiple cellular functions and PLpro is an antiviral drug target. Our designed ubiquitin variant (UbV) hosting three mutated residues displayed a ∼3,500-fold increase in functional inhibition relative to wild-type Ub. Further optimization of two C-terminal residues within the Ub network resulted in a K

Indexed as

Coronavirus Papain-Like ProteasesMiddle East Respiratory Syndrome CoronavirusUbiquitinProtein BindingCoronavirus Papain-Like ProteasesUbiquitindihedral angle correlation networknanomolar binderpapain-like proteaseprotein-based inhibitorsubiquitin variant

Identifiers

PMID37918563
PMCPMC11637584
OpenAlexW4388073407

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.