Evidence map›Paper›PMID 32088185›Full record

ReviewJournal of molecular biology2020

Protein Footprinting: Auxiliary Engine to Power the Structural Biology Revolution.

Mark R Chance, Erik R Farquhar, Sichun Yang, David T Lodowski, Janna Kiselar

Abstract readReview
In one paragraph

Review in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

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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.

Mark R ChanceCase Center for Proteomics and Bioinformatics, USA; Case Center for Synchrotron Biosciences, USA; Department of Nutrition, Case Western Reserve University, School of Medicine, 10900 Euclid Ave., Cleveland, OH, 44106, USA. Electronic address: mark.chance@case.edu.
Erik R FarquharCase Center for Synchrotron Biosciences, USA.
Sichun YangCase Center for Proteomics and Bioinformatics, USA; Department of Nutrition, Case Western Reserve University, School of Medicine, 10900 Euclid Ave., Cleveland, OH, 44106, USA.
David T LodowskiCase Center for Proteomics and Bioinformatics, USA; Department of Nutrition, Case Western Reserve University, School of Medicine, 10900 Euclid Ave., Cleveland, OH, 44106, USA.
Janna KiselarCase Center for Proteomics and Bioinformatics, USA; Department of Nutrition, Case Western Reserve University, School of Medicine, 10900 Euclid Ave., Cleveland, OH, 44106, USA.

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Multifaceted Modeling of Estrogen ReceptorR01GM114056 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI YANG, SICHUN · 2015 to 2024
$3.3M
NIBIB NIH HHS P30 EB009998NIGMS NIH HHS R01 GM114056
6 · The paper itself

Abstract

Structural biology is entering an exciting time where many new high-resolution structures of large complexes and membrane proteins are determined regularly. These advances have been driven by over fifteen years of technology advancements, first in macromolecular crystallography, and recently in Cryo-electron microscopy. These structures are allowing detailed questions about functional mechanisms of the structures, and the biology enabled by these structures, to be addressed for the first time. At the same time, mass spectrometry technologies for protein structure analysis, "footprinting" studies, have improved their sensitivity and resolution dramatically and can provide detailed sub-peptide and residue level information for validating structures and interactions or understanding the dynamics of structures in the context of ligand binding or assembly. In this perspective, we review the use of protein footprinting to extend our understanding of macromolecular systems, particularly for systems challenging for analysis by other techniques, such as intrinsically disordered proteins, amyloidogenic proteins, and other proteins/complexes so far recalcitrant to existing methods. We also illustrate how the availability of high-resolution structural information can be a foundation for a suite of hybrid approaches to divine structure-function relationships beyond what individual techniques can deliver.

Indexed as

Amyloidogenic ProteinsCryoelectron MicroscopyCrystallography, X-RayHumansIntrinsically Disordered ProteinsModels, MolecularMultiprotein ComplexesProtein ConformationProtein FootprintingProteinsAmyloidogenic ProteinsIntrinsically Disordered ProteinsMultiprotein ComplexesProteinsfootprintinghybrid methodsmass spectrometryproteinsstructural biology

Identifiers

PMID32088185
PMCPMC7245549

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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.