Evidence map›Paper›PMID 39324697›Full record

ReviewProtein science : a publication of the Protein Society2024

Aggrescan4D: A comprehensive tool for pH-dependent analysis and engineering of protein aggregation propensity.

Mateusz Zalewski, Valentin Iglesias, Oriol Bárcenas, Salvador Ventura, Sebastian Kmiecik

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. STAGE: A compact and versatile TnpB-based genome editing toolkit forProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Improving the solubility of single domain antibodies using VH-like hallmark residues.Protein science : a publication of the Protein Society · 2025
    Article
  7. Three scenarios for amyloid transformation in the context of the funnel model.Computational and structural biotechnology journal · 2025
    Article
  8. Review
  9. Review
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

5 authors.

Mateusz ZalewskiFaculty of Chemistry, Biological and Chemical Research Center, University of Warsaw, Warsaw, Poland.ORCID 0000-0002-3436-8829
Valentin IglesiasDepartament de Bioquímica i Biologia Molecular, Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Barcelona, Spain.
Oriol BárcenasDepartament de Bioquímica i Biologia Molecular, Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Barcelona, Spain.
Salvador VenturaDepartament de Bioquímica i Biologia Molecular, Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Barcelona, Spain.ORCID 0000-0002-9652-6351
Sebastian KmiecikFaculty of Chemistry, Biological and Chemical Research Center, University of Warsaw, Warsaw, Poland.ORCID 0000-0001-7623-0935

Funding

Generalitat de Catalunya 2021-SGR-00635 AGAICREA, ICREA-Academia 2020National Science Center Sheng2021/40/Q/NZ2/00078Polish National Agency for Academic Exchange under the ULAM NAWA Programme BPN/ULM/2023/1/00189/U/00001Spanish Ministry of Science and Innovation PID2022-137963OB-I00
6 · The paper itself

Abstract

Aggrescan4D (A4D) is an advanced computational tool designed for predicting protein aggregation, leveraging structural information and the influence of pH. Building upon its predecessor, Aggrescan3D (A3D), A4D has undergone numerous enhancements aimed at assisting the improvement of protein solubility. This manuscript reviews A4D's updated functionalities and explains the fundamental principles behind its pH-dependent calculations. Additionally, it presents an antibody case study to evaluate its performance in comparison with other structure-based predictors. Notably, A4D integrates advanced protein engineering protocols with pH-dependent calculations, enhancing its utility in advising solubility-enhancing mutations. A4D considers the impact of structural flexibility on aggregation propensities, and includes a large set of precalculated predictions. These capabilities should help to open new avenues for both understanding and managing protein aggregation. A4D is accessible through a dedicated web server at https://biocomp.chem.uw.edu.pl/a4d/.

Indexed as

Protein AggregatesProtein EngineeringHydrogen-Ion ConcentrationProteinsSoftwareSolubilityProtein AggregatesProteinscomputational biologymonoclonal antibodiespH‐dependent aggregationprotein aggregationprotein engineeringprotein solubilityprotein stabilitystructural bioinformatics

Identifiers

PMID39324697
PMCPMC11425640

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.