Evidence map›Paper›PMID 38297184›Full record

ArticleNature methods2024

Direct prediction of intrinsically disordered protein conformational properties from sequence.

Jeffrey M Lotthammer, Garrett M Ginell, Daniel Griffith, Ryan J Emenecker, Alex S Holehouse

Abstract read
In one paragraph

Article in Nature methods, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers.

0numbers the graph read from it
0cells of the map it votes in
140citing 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

140 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Structural Features of a Tiny Viral Protein, ORF7b of SARS-CoV-2.International journal of molecular sciences · 2026
    Article
  12. Article
  13. Article
  14. Article
  15. Distinguishing near- versus off-critical phase behaviors of intrinsically disordered proteins.Reports on progress in physics. Physical Society (Great Britain) · 2026
    Article
  16. Physics-guided design of intrinsically disordered proteins.bioRxiv : the preprint server for biology · 2026
    Article
  17. Article
  18. Article
  19. The Polymers of Life: Exploring Cellular Function Through Polymer Concepts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  20. Article

80 more citing papers are in PubMed but not listed here.

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.

Jeffrey M Lotthammer *Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA.ORCID http://orcid.org/0000-0002-5022-7006
Garrett M Ginell *Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA.ORCID http://orcid.org/0000-0001-6511-5480
Daniel Griffith *Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA.ORCID http://orcid.org/0000-0002-9633-9601
Ryan J EmeneckerDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA.
Alex S HolehouseDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA. alex.holehouse@wustl.edu.ORCID http://orcid.org/0000-0002-4155-5729

Funding

Human Frontier Science Program (HFSP) RGP0015/2022NSF | BIO | Division of Biological Infrastructure (DBI) 2213983NSF | BIO | Division of Molecular and Cellular Biosciences (MCB) 2128068NSF | BIO | Division of Molecular and Cellular Biosciences (MCB) 2139839
6 · The paper itself

Abstract

Intrinsically disordered regions (IDRs) are ubiquitous across all domains of life and play a range of functional roles. While folded domains are generally well described by a stable three-dimensional structure, IDRs exist in a collection of interconverting states known as an ensemble. This structural heterogeneity means that IDRs are largely absent from the Protein Data Bank, contributing to a lack of computational approaches to predict ensemble conformational properties from sequence. Here we combine rational sequence design, large-scale molecular simulations and deep learning to develop ALBATROSS, a deep-learning model for predicting ensemble dimensions of IDRs, including the radius of gyration, end-to-end distance, polymer-scaling exponent and ensemble asphericity, directly from sequences at a proteome-wide scale. ALBATROSS is lightweight, easy to use and accessible as both a locally installable software package and a point-and-click-style interface via Google Colab notebooks. We first demonstrate the applicability of our predictors by examining the generalizability of sequence-ensemble relationships in IDRs. Then, we leverage the high-throughput nature of ALBATROSS to characterize the sequence-specific biophysical behavior of IDRs within and between proteomes.

Indexed as

Intrinsically Disordered ProteinsPolymersProtein ConformationIntrinsically Disordered ProteinsPolymers

Identifiers

PMID38297184
PMCPMC10927563

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.