Evidence map›Paper›PMID 31417196›Full record

ReviewNature reviews. Molecular cell biology2019

Advances in protein structure prediction and design.

Brian Kuhlman, Philip Bradley

Abstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 312 papers.

0numbers the graph read from it
0cells of the map it votes in
312citing 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

312 citing papers in PubMed.

  1. MultilevelCurrent research in structural biology · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Backbone double-mutant cycle analysis quantifies hydrogen-bond energies in proteins.Protein science : a publication of the Protein Society · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Cancer-associated TRF1 mutations alter PARP1 interaction dynamics: an in silico study.Mammalian genome : official journal of the International Mammalian Genome Society · 2026
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article

252 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

2 authors.

Brian KuhlmanDepartment of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC, USA. bkuhlman@email.unc.edu.ORCID http://orcid.org/0000-0003-4907-9699
Philip BradleyComputational Biology Program, Fred Hutchinson Cancer Research Center, Seattle, WA, USA. pbradley@fredhutch.org.ORCID http://orcid.org/0000-0002-0224-6464

Funding

GPU workstation for deep learning-based protein design and cryo-EM data processingR35GM131923 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BRIAN A KUHLMAN · 2019 to 2026
$6.1M
High-resolution modeling of protein-RNA interfacesR01GM121487 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI BRADLEY, PHILIP · 2017 to 2020
$1.7M
Rational design and functionalization of circular tandem repeat proteinsR01GM123378 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI BRADLEY, PHILIP · 2017 to 2020
$1.5M
Computational Methods for Requirement-Driven Protein DesignR01GM117968 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KUHLMAN, BRIAN A · 2015 to 2018
$1.3M
NIGMS NIH HHS R01 GM117968NIGMS NIH HHS R01 GM121487NIGMS NIH HHS R01 GM123378NIGMS NIH HHS R35 GM131923
6 · The paper itself

Abstract

The prediction of protein three-dimensional structure from amino acid sequence has been a grand challenge problem in computational biophysics for decades, owing to its intrinsic scientific interest and also to the many potential applications for robust protein structure prediction algorithms, from genome interpretation to protein function prediction. More recently, the inverse problem - designing an amino acid sequence that will fold into a specified three-dimensional structure - has attracted growing attention as a potential route to the rational engineering of proteins with functions useful in biotechnology and medicine. Methods for the prediction and design of protein structures have advanced dramatically in the past decade. Increases in computing power and the rapid growth in protein sequence and structure databases have fuelled the development of new data-intensive and computationally demanding approaches for structure prediction. New algorithms for designing protein folds and protein-protein interfaces have been used to engineer novel high-order assemblies and to design from scratch fluorescent proteins with novel or enhanced properties, as well as signalling proteins with therapeutic potential. In this Review, we describe current approaches for protein structure prediction and design and highlight a selection of the successful applications they have enabled.

Indexed as

AlgorithmsDatabases, ProteinModels, MolecularSequence Analysis, ProteinAnimalsHumansProtein ConformationProteinsProteins

Identifiers

PMID31417196
PMCPMC7032036

What OpenQuestion holds

Textmetadata
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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.