Evidence map›Paper›PMID 36748325›Full record

ReviewEssays in biochemistry2023

Surface-sampling mass spectrometry to study proteins and protein complexes.

Kei F Carver Wong, Rebecca E Greatorex, Charlotte E Gidman, Sidrah Rahman, Rian L Griffiths

Open access · hybridAbstract readReview
In one paragraph

Review in Essays in biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.5field-weighted citation impact, top 21% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. MALDI spatial proteomics: a mini review of approaches and techniques.Analytical methods : advancing methods and applications · 2026
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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 at 1 institution in 1 country.

Kei F Carver WongSchool of Pharmacy, University of Nottingham, Nottingham NG7 2RD, U.K.ORCID 0000-0001-9279-1433
Rebecca E GreatorexSchool of Pharmacy, University of Nottingham, Nottingham NG7 2RD, U.K.
Charlotte E GidmanSchool of Pharmacy, University of Nottingham, Nottingham NG7 2RD, U.K.
Sidrah RahmanSchool of Pharmacy, University of Nottingham, Nottingham NG7 2RD, U.K.
Rian L GriffithsSchool of Pharmacy, University of Nottingham, Nottingham NG7 2RD, U.K.ORCID 0000-0002-1601-4664
University of Nottingham · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This review aims to summarise the current capabilities of surface mass spectrometry (MS) approaches that offer intact protein analysis, and that of non-covalent complexes. Protein analysis is largely achieved via matrix-assisted laser desorption/ionisation (MALDI), which is in itself a surface analysis approach or solvent-based electrospray ionisation (ESI). Several surface sampling approaches have been developed based on ESI, and those that have been used for intact protein analysis will be discussed below. The extent of protein coverage, top-down elucidation, and probing of protein structure for native proteins and non-covalent complexes will be discussed for each approach. Strategies for improving protein analysis, ranging from sample preparation, and sampling methods to instrument modifications and the inclusion of ion mobility separation in the workflow will also be discussed. The relative benefits and drawbacks of each approach will be summarised, providing an overview of current capabilities.

Indexed as

ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationProteinsimaging techniquesmass spectrometryproteomicssurface analysis

Identifiers

PMID36748325
PMCPMC10070487
OpenAlexW4319334450

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.