Evidence map›Paper›PMID 42527600›Full record

ArticleNature2026

Rational design of disordered proteins for sequence-function investigation.

Kara Hunter, Trevor Brandt, Karina Guadalupe, Kavindu C Kolamunna, Jeffrey M Lotthammer, Nora M Shamoon, Jessica K Niblo, Brooke Nicholson, Lea M Day, Alec Martinez and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Physics-guided design of intrinsically disordered proteins.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors.

Kara Hunter *Department of Chemistry, Syracuse University, Syracuse, NY, USA.
Trevor Brandt *Department of Chemistry, Syracuse University, Syracuse, NY, USA.ORCID http://orcid.org/0009-0005-2702-1738
Karina Guadalupe *Department of Chemistry and Biochemistry, University of California, Merced, Merced, CA, USA.
Kavindu C KolamunnaDepartment of Chemistry, Syracuse University, Syracuse, NY, USA.ORCID http://orcid.org/0009-0009-0910-9268
Jeffrey M LotthammerDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St Louis, MO, USA.
Nora M ShamoonDepartment of Chemistry and Biochemistry, University of California, Merced, Merced, CA, USA.ORCID http://orcid.org/0000-0002-1466-1286
Jessica K NibloDepartment of Chemistry, Syracuse University, Syracuse, NY, USA.ORCID http://orcid.org/0000-0001-9378-6097
Brooke NicholsonDepartment of Chemistry, Syracuse University, Syracuse, NY, USA.
Lea M DayDepartment of Chemistry, Syracuse University, Syracuse, NY, USA.ORCID http://orcid.org/0009-0001-0026-153X
Alec MartinezDepartment of Chemistry and Biochemistry, University of California, Merced, Merced, CA, 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
Shahar SukenikDepartment of Chemistry, Syracuse University, Syracuse, NY, USA. ssukenik@syr.edu.ORCID http://orcid.org/0000-0003-3855-9574
Ryan J EmeneckerDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St Louis, MO, USA. remenecker@wustl.edu.ORCID http://orcid.org/0000-0001-7055-2773

Funding

G-RISE at UC MercedT32GM141862 · NIGMS · UNIVERSITY OF CALIFORNIA, MERCED · PI GOPINATHAN, AJAY, LIWANG, ANDY · 2021 to 2025
$2.7M
Uncovering the structural underpinnings of function in disordered transcription factor regionsR35GM137926 · NIGMS · UNIVERSITY OF CALIFORNIA, MERCED · PI Shahar Sukenik · 2020 to 2026
$2.5M
Uncovering the regulatory logic of gene expression encoded by disordered regionsDP2CA290639 · NCI · WASHINGTON UNIVERSITY · PI Alex S Holehouse · 2023 to 2026
$2.3M
NCI NIH HHS DP2 CA290639NIGMS NIH HHS R35 GM137926NIGMS NIH HHS T32 GM141862
6 · The paper itself

Abstract

Despite lacking a stable three-dimensional structure, intrinsically disordered protein regions (IDRs) are ubiquitous across all kingdoms of life and have essential cellular roles

Indexed as

Computational BiologyIntrinsically Disordered ProteinsProtein EngineeringAmino Acid SequenceAnimalsHumansModels, MolecularProtein FoldingStructure-Activity RelationshipIntrinsically Disordered Proteins

Identifiers

PMID42527600
PMCPMC13575894

What OpenQuestion holds

Textmetadata
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.