Evidence map›Paper›PMID 22143762›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Computational design of a symmetric homodimer using β-strand assembly.

P Benjamin Stranges, Mischa Machius, Michael J Miley, Ashutosh Tripathy, Brian Kuhlman

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

  1. Article
  2. Design of amyloidogenic peptide traps.Nature chemical biology · 2024
    Article
  3. Review
  4. Article
  5. Antibody interfaces revealed through structural mining.Computational and structural biotechnology journal · 2022
    Article
  6. Protein Assembly by Design.Chemical reviews · 2021
    Review
  7. Transferrin receptor targeting by de novo sheet extension.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. A threonine zipper that mediates protein-protein interactions: Structure and prediction.Protein science : a publication of the Protein Society · 2018
    Article
  13. Review
  14. Cyclic oligomer design with de novo αβ-proteins.Protein science : a publication of the Protein Society · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Computational design and experimental verification of a symmetric protein homodimer.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
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.

P Benjamin StrangesDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Mischa Machius
Michael J Miley
Ashutosh Tripathy
Brian Kuhlman

Funding

Virology Research Program (Program 4)P30CA016086 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Deborah F. Tate · 1985 to 2026
$201.5M
Designing Affinity and Specificity at Protein InterfacesR01GM073960 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KUHLMAN, BRIAN A · 2005 to 2018
$3.1M
NCI NIH HHS P30 CA016086NIGMS NIH HHS R01 GM073960NIGMS NIH HHS R01-GM073960
6 · The paper itself

Abstract

Computational design of novel protein-protein interfaces is a test of our understanding of protein interactions and has the potential to allow modification of cellular physiology. Methods for designing high-affinity interactions that adopt a predetermined binding mode have proved elusive, suggesting the need for new strategies that simplify the design process. A solvent-exposed backbone on a β-strand is thought of as "sticky" and β-strand pairing stabilizes many naturally occurring protein complexes. Here, we computationally redesign a monomeric protein to form a symmetric homodimer by pairing exposed β-strands to form an intermolecular β-sheet. A crystal structure of the designed complex closely matches the computational model (rmsd = 1.0 Å). This work demonstrates that β-strand pairing can be used to computationally design new interactions with high accuracy.

Indexed as

Crystallography, X-RayDimerizationDNAEscherichia coliLightMolecular ConformationProtein ConformationProtein EngineeringProteinsProtein Structure, SecondaryScattering, RadiationSoftwareSolventsSurface PropertiesThermodynamicsUltracentrifugationDNAProteinsSolvents

Identifiers

PMID22143762
PMCPMC3251150

What OpenQuestion holds

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Registered trials

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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.