Evidence map›Paper›PMID 31062957›Full record

ArticleAnalytical chemistry2019

Direct Mass Spectrometry Analysis of Protein Complexes and Intact Proteins up to >70 kDa from Tissue.

Rian L Griffiths, Albert Konijnenberg, Rosa Viner, Helen J Cooper

Erratum issuedAbstract read
In one paragraph

Article in Analytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Rian L GriffithsSchool of Biosciences , University of Birmingham , Edgbaston , Birmingham B15 2TT , U.K.
Albert KonijnenbergThermo Fisher Scientific , Achtseweg Noord 5 , 5651 GG Eindhoven , The Netherlands.
Rosa VinerThermo Fisher Scientific , 355 River Oaks Parkway , San Jose , California 95134 , United States.
Helen J CooperSchool of Biosciences , University of Birmingham , Edgbaston , Birmingham B15 2TT , U.K.ORCID 0000-0003-4590-9384

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Native liquid extraction surface analysis (LESA) mass spectrometry allows direct analysis of folded proteins and protein complexes from biological substrates, such as dried blood spots and thin tissue sections, by use of native-like extraction/ionization solvents. Previously, we have demonstrated native LESA mass spectrometry of folded proteins up to 16 kDa as well as the 64 kDa hemoglobin tetramer, from mouse tissues. With denaturing LESA solvents, the highest mass protein detected in tissue to date is ∼37 kDa. Here, we demonstrate native LESA mass spectrometry by use of a Q Exactive UHMR Hybrid Quadrupole-Orbitrap (QE-UHMR) mass spectrometer, pushing the upper mass limit of proteins detected in tissue to >70 kDa. Moreover, a protein trimer of 42 kDa was detected and its stoichiometry confirmed by higher energy collision dissociation (HCD). The benefits of inclusion of detergents in the LESA sampling solvent are also demonstrated.

Indexed as

Protein MultimerizationAnimalsBrain ChemistryDetergentsKidneyMaleMass SpectrometryMultiprotein ComplexesProtein DenaturationProteinsRats, WistarDetergentsMultiprotein ComplexesProteins

Identifiers

PMID31062957
PMCPMC7006965

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.