Evidence map›Paper›PMID 42907623›Full record

ReviewAdvances in experimental medicine and biology2026

Applications of Matrix-Assisted Laser Desorption Ionization In-Source Decay Mass Spectrometry.

Yue Ju

Abstract readReview
PubMed Publisher
In one paragraph

Review in Advances in experimental medicine and biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

1 author.

Yue JuBruker Daltonics Inc., San Jose, CA, USA. yue.ju@bruker.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Matrix-Assisted Laser Desorption Ionization In-Source Decay (MALDI-ISD) Mass Spectro-metry is a very powerful tool for providing terminal sequence information of biomolecules with minimal sample preparations. Fragmentation is induced at the position where hydrogen radical transfers from the matrix to analyte in the MALDI-ISD process by proposed mechanism. Uniform fragmentation in MALDI-ISD generates relative simple ion spectra of readable sequence ladders with labile modifications retained, which is advantageous over other fragmentation methods such as collision-induced dissociation (CID) for characterizing modifications. MALDI-ISD has been applied to de novo sequencing of a 13.6 kDa protein and fully validates sequences of therapeutic antibodies, showing its promising potential in examining reference sequences of biotherapeutics unambiguously. It has also been successfully applied to the analysis of modifications such as posttranslational modifications (PTMs) and PEGylation. Here, we discuss the application of MALDI-ISD in protein sequencing and modification analysis by featuring representative studies in details.

Indexed as

ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationAmino Acid SequenceAnimalsHumansProtein Processing, Post-TranslationalSequence Analysis, ProteinProteins

Identifiers

PMID42907623

What OpenQuestion holds

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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.