Evidence map›Paper›PMID 29351988›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Confirmation of intersubunit connectivity and topology of designed protein complexes by native MS.

Aniruddha Sahasrabuddhe, Yang Hsia, Florian Busch, William Sheffler, Neil P King, David Baker, Vicki H Wysocki

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Native Proteomics by Capillary Zone Electrophoresis-Mass Spectrometry.Angewandte Chemie (International ed. in English) · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Improving the secretion of designed protein assemblies through negative design of cryptic transmembrane domains.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Recent technological developments for native mass spectrometry.Biochimica et biophysica acta. Proteins and proteomics · 2022
    Review
  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

7 authors.

Aniruddha SahasrabuddheDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
Yang HsiaDepartment of Biochemistry, University of Washington, Seattle, WA 98195.
Florian BuschDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
William ShefflerDepartment of Biochemistry, University of Washington, Seattle, WA 98195.
Neil P KingDepartment of Biochemistry, University of Washington, Seattle, WA 98195.
David BakerDepartment of Biochemistry, University of Washington, Seattle, WA 98195; dabaker@uw.edu wysocki.11@osu.edu.ORCID 0000-0001-7896-6217
Vicki H WysockiDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210; dabaker@uw.edu wysocki.11@osu.edu.

Funding

Development of Surface-Induced Dissociation Ion Mobility MS, a Structrl Biol ToolR01GM113658 · NIGMS · OHIO STATE UNIVERSITY · PI WYSOCKI, VICKI H. · 2015 to 2018
$1.1M
NIGMS NIH HHS R01 GM113658
6 · The paper itself

Abstract

Computational protein design provides the tools to expand the diversity of protein complexes beyond those found in nature. Understanding the rules that drive proteins to interact with each other enables the design of protein-protein interactions to generate specific protein assemblies. In this work, we designed protein-protein interfaces between dimers and trimers to generate dodecameric protein assemblies with dihedral point group symmetry. We subsequently analyzed the designed protein complexes by native MS. We show that the use of ion mobility MS in combination with surface-induced dissociation (SID) allows for the rapid determination of the stoichiometry and topology of designed complexes. The information collected along with the speed of data acquisition and processing make SID ion mobility MS well-suited to determine key structural features of designed protein complexes, thereby circumventing the requirement for more time- and sample-consuming structural biology approaches.

Indexed as

AvidinLactoglobulinsMass SpectrometryModels, MolecularMultiprotein ComplexesPrealbuminProtein EngineeringProtein Interaction Domains and MotifsRecombinant ProteinsAvidinLactoglobulinsMultiprotein ComplexesPrealbuminRecombinant Proteinscomputational designheterododecamersion mobilitynative mass spectrometrysurface-induced dissociation

Identifiers

PMID29351988
PMCPMC5819399

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.