Evidence map›Paper›PMID 38916999›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2024

An all-atom protein generative model.

Alexander E Chu, Jinho Kim, Lucy Cheng, Gina El Nesr, Minkai Xu, Richard W Shuai, Po-Ssu Huang

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Zero-shot design of abioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Generative design of intrinsically disordered protein regions with IDiom.bioRxiv : the preprint server for biology · 2026
    Article
  11. Review
  12. Constraint Decoupled Latent Diffusion for Protein Backmapping.Journal of chemical theory and computation · 2026
    Article
  13. Article
  14. AI-Driven De Novo Binder Design: From Structure Prediction to Closed-Loop Optimization.Computational and structural biotechnology journal · 2026
    Review
  15. Review
  16. BoltzGen: Toward Universal Binder Design.bioRxiv : the preprint server for biology · 2025
    Article
  17. GeoEvoBuilder: A deep learning framework for efficient functional and thermostable protein design.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. SLAE: Strictly Local All-atom Environment for Protein Representation.bioRxiv : the preprint server for biology · 2025
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Alexander E ChuBiophysics Program, Stanford University, Stanford, CA 94305.ORCID 0000-0002-6219-7887
Jinho KimDepartment of Bioengineering, Stanford University, Stanford, CA 94305.
Lucy ChengAquarium Learning, San Francisco, CA 94117.
Gina El NesrBiophysics Program, Stanford University, Stanford, CA 94305.ORCID 0000-0003-4857-9464
Minkai XuDepartment of Computer Science, Stanford University, Stanford, CA 94305.ORCID 0009-0007-9735-3767
Richard W ShuaiBiophysics Program, Stanford University, Stanford, CA 94305.ORCID 0000-0001-8375-8180
Po-Ssu HuangBiophysics Program, Stanford University, Stanford, CA 94305.ORCID 0000-0002-7948-2895

Funding

Molecular Biophysics Training Program at StanfordT32GM136568 · NIGMS · STANFORD UNIVERSITY · PI Zev Bryant, KERWYN C. HUANG · 2021 to 2026
$3.7M
Generative neural networks for structure-based antibody designR01GM147893 · NIGMS · STANFORD UNIVERSITY · PI Possu Huang · 2022 to 2026
$1.9M
American Cancer Society (ACS) ACS 134055-IRG-218BASF CARADiscovery Innovation Fund N/AHHS | National Institutes of Health (NIH) R01GM147893National Science Foundation (NSF) N/ANIGMS NIH HHS R01 GM147893NIGMS NIH HHS T32 GM136568Stanford Graduate Fellow N/A
6 · The paper itself

Abstract

Proteins mediate their functions through chemical interactions; modeling these interactions, which are typically through sidechains, is an important need in protein design. However, constructing an all-atom generative model requires an appropriate scheme for managing the jointly continuous and discrete nature of proteins encoded in the structure and sequence. We describe an all-atom diffusion model of protein structure, Protpardelle, which represents all sidechain states at once as a "superposition" state; superpositions defining a protein are collapsed into individual residue types and conformations during sample generation. When combined with sequence design methods, our model is able to codesign all-atom protein structure and sequence. Generated proteins are of good quality under the typical quality, diversity, and novelty metrics, and sidechains reproduce the chemical features and behavior of natural proteins. Finally, we explore the potential of our model to conduct all-atom protein design and scaffold functional motifs in a backbone- and rotamer-free way.

Indexed as

Models, MolecularProtein ConformationProteinsAmino Acid SequenceProteinsfull-atom modelgenerative modelingprotein designprotein structuresidechain generation

Identifiers

PMID38916999
PMCPMC11228509

What OpenQuestion holds

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LicenceCC BY
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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.