Evidence map›Paper›PMID 25451037›Full record

ArticleJournal of molecular biology2015

A general computational approach for repeat protein design.

Fabio Parmeggiani, Po-Ssu Huang, Sergey Vorobiev, Rong Xiao, Keunwan Park, Silvia Caprari, Min Su, Jayaraman Seetharaman, Lei Mao, Haleema Janjua and 3 more

Abstract read
In one paragraph

Article in Journal of molecular biology, 2015. 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. Article
  2. Article
  3. Design, synthesis, and characterization of protein origami based on self-assembly of a brick and staple artificial protein pair.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Modular repeat protein sculpting using rigid helical junctions.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Development and applications of artificial symmetrical proteins.Computational and structural biotechnology journal · 2020
    Review
  12. Article
  13. Ambidextrous helical nanotubes from self-assembly of designed helical hairpin motifs.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Article
  15. Article
  16. The variable lymphocyte receptor as an antibody alternative.Current opinion in biotechnology · 2018
    Review
  17. Frustration, function and folding.Current opinion in structural biology · 2018
    Review
  18. Article
  19. Article
  20. 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

13 authors.

Fabio ParmeggianiDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
Po-Ssu HuangDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
Sergey VorobievDepartment of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, NY 10027, USA.
Rong XiaoCenter for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry and Department of Biochemistry, Robert Wood Johnson Medical School, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA; Northeast Structural Genomics Consortium, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA.
Keunwan ParkDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
Silvia CaprariDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA.
Min SuDepartment of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, NY 10027, USA.
Jayaraman SeetharamanDepartment of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, NY 10027, USA.
Lei MaoCenter for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry and Department of Biochemistry, Robert Wood Johnson Medical School, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA; Northeast Structural Genomics Consortium, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA.
Haleema JanjuaCenter for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry and Department of Biochemistry, Robert Wood Johnson Medical School, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA; Northeast Structural Genomics Consortium, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA.
Gaetano T MontelioneCenter for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry and Department of Biochemistry, Robert Wood Johnson Medical School, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA; Northeast Structural Genomics Consortium, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA.
John HuntDepartment of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, NY 10027, USA.
David BakerDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA; Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA.

Funding

University of Georgia ProjectU54GM094597 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI ROST, BURKHARD · 2010 to 2014
$36.9M
Howard Hughes Medical InstituteNIGMS NIH HHS U54 GM094597NIGMS NIH HHS U54-GM094597
6 · The paper itself

Abstract

Repeat proteins have considerable potential for use as modular binding reagents or biomaterials in biomedical and nanotechnology applications. Here we describe a general computational method for building idealized repeats that integrates available family sequences and structural information with Rosetta de novo protein design calculations. Idealized designs from six different repeat families were generated and experimentally characterized; 80% of the proteins were expressed and soluble and more than 40% were folded and monomeric with high thermal stability. Crystal structures determined for members of three families are within 1Å root-mean-square deviation to the design models. The method provides a general approach for fast and reliable generation of stable modular repeat protein scaffolds.

Indexed as

Computer SimulationAmino Acid SequenceAnkyrinsArmadillo Domain ProteinsBiocompatible MaterialsCrystallography, X-RayLeucine-Rich Repeat ProteinsMicrofilament ProteinsModels, MolecularMolecular Sequence DataMolecular StructureProtein ConformationProtein EngineeringProteinsSequence AlignmentSequence Analysis, ProteinAnkyrinsArmadillo Domain ProteinsBiocompatible MaterialsLeucine-Rich Repeat ProteinsMicrofilament ProteinsProteinscomputational designde novo designidealized proteinsrepeat proteinsthermodynamic stability

Identifiers

PMID25451037
PMCPMC4303030

What OpenQuestion holds

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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.