Evidence map›Paper›PMID 32286308›Full record

ArticleNature communications2020

Quantifying the heterogeneity of macromolecular machines by mass photometry.

Adar Sonn-Segev, Katarina Belacic, Tatyana Bodrug, Gavin Young, Ryan T VanderLinden, Brenda A Schulman, Johannes Schimpf, Thorsten Friedrich, Phat Vinh Dip, Thomas U Schwartz and 7 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 papers.

0numbers the graph read from it
0cells of the map it votes in
129citing papers in PubMed
20.4field-weighted citation impact, top 1% of its field
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

129 citing papers in PubMed, 224 citations in OpenAlex.

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69 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

17 authors at 6 institutions in 4 countries.

Adar Sonn-Segev *Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK.
Katarina Belacic *Research Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Campus-Vienna-Biocenter 1, 1030, Vienna, Austria.ORCID http://orcid.org/0000-0002-4024-5497
Tatyana Bodrug *Department of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA.
Gavin YoungPhysical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK.
Ryan T VanderLindenDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, 38105, USA.
Brenda A SchulmanDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, 38105, USA.ORCID http://orcid.org/0000-0002-3083-1126
Johannes SchimpfAlbert-Ludwigs-Universität, Institut für Biochemie, Albertstr. 21, Chemie-Hochhaus, 79104, Freiburg i. Br., Germany.
Thorsten FriedrichAlbert-Ludwigs-Universität, Institut für Biochemie, Albertstr. 21, Chemie-Hochhaus, 79104, Freiburg i. Br., Germany.ORCID http://orcid.org/0000-0002-0813-7883
Phat Vinh DipDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA.ORCID http://orcid.org/0000-0002-1535-9644
Thomas U SchwartzDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA.ORCID http://orcid.org/0000-0001-8012-1512
Benedikt BauerResearch Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Campus-Vienna-Biocenter 1, 1030, Vienna, Austria.
Jan-Michael PetersResearch Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Campus-Vienna-Biocenter 1, 1030, Vienna, Austria.
Weston B StruwePhysical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK.
Justin L P BeneschPhysical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK.ORCID http://orcid.org/0000-0002-1507-3742
Nicholas G BrownDepartment of Pharmacology and Lineberger Comprehensive Cancer Center, University of North Carolina School of Medicine, Chapel Hill, NC, 27599, USA. nbrown1@med.unc.edu.ORCID http://orcid.org/0000-0002-6141-0164
David HaselbachResearch Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Campus-Vienna-Biocenter 1, 1030, Vienna, Austria. david.haselbach@imp.ac.at.ORCID http://orcid.org/0000-0002-5276-5633
Philipp KukuraPhysical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK. philipp.kukura@chem.ox.ac.uk.ORCID http://orcid.org/0000-0003-0136-7704
University of Oxford · GBResearch Institute of Molecular Pathology · ATMassachusetts Institute of Technology · USSt. Jude Children's Research Hospital · USUniversity of Freiburg · DEUniversity of North Carolina at Chapel Hill · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
Virology, Immunology, and Microbiology CoreP30AI050410 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DAVID M. MARGOLIS · 2001 to 2026
$76.9M
MOLECULAR AND CELLULAR BIOPHYSICS TRAINING PROGRAMT32GM008570 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KUHLMAN, BRIAN A, SLEP, KEVIN C · 1995 to 2022
$5.1M
High Resolution Assembly Structure of The Nuclear Pore ComplexR01GM077537 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SCHWARTZ, THOMAS · 2007 to 2019
$4.3M
Spindle Assembly Checkpoint SilencingR35GM128855 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Nicholas Gene Brown · 2018 to 2026
$4.1M
E3-mediated Ubiquitin-like Protein LigationR37GM069530 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI SCHULMAN, BRENDA A · 2014 to 2018
$2.0M
Howard Hughes Medical InstituteNCI NIH HHS P30 CA021765NIAID NIH HHS P30 AI050410NIGMS NIH HHS R01 GM077537NIGMS NIH HHS R35 GM128855NIGMS NIH HHS R37 GM069530NIGMS NIH HHS T32 GM008570
6 · The paper itself

Abstract

Sample purity is central to in vitro studies of protein function and regulation, and to the efficiency and success of structural studies using techniques such as x-ray crystallography and cryo-electron microscopy (cryo-EM). Here, we show that mass photometry (MP) can accurately characterize the heterogeneity of a sample using minimal material with high resolution within a matter of minutes. To benchmark our approach, we use negative stain electron microscopy (nsEM), a popular method for EM sample screening. We include typical workflows developed for structure determination that involve multi-step purification of a multi-subunit ubiquitin ligase and chemical cross-linking steps. When assessing the integrity and stability of large molecular complexes such as the proteasome, we detect and quantify assemblies invisible to nsEM. Our results illustrate the unique advantages of MP over current methods for rapid sample characterization, prioritization and workflow optimization.

Indexed as

Anaphase-Promoting Complex-CyclosomeAnimalsCattleCryoelectron MicroscopyElectrophoresis, Polyacrylamide GelEscherichia coliMass SpectrometryProteasome Endopeptidase ComplexProtein BindingAnaphase-Promoting Complex-CyclosomeProteasome Endopeptidase Complex

Identifiers

PMID32286308
PMCPMC7156492
OpenAlexW3015312131

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.