Evidence map›Paper›PMID 36413329›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Improved Identification of Protease Cleavage Sites by In-gel Reductive Dimethylation.

Stefanie Royek, Stefanie Brück, Jens Pfannstiel, Annick Stintzi, Andreas Schaller

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Article in Methods in molecular biology (Clifton, N.J.), 2023. 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, top 67% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

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

5 authors at 1 institution in 1 country.

Stefanie RoyekDepartment of Plant Physiology and Biochemistry, University of Hohenheim, Stuttgart, Germany.
Stefanie BrückDepartment of Plant Physiology and Biochemistry, University of Hohenheim, Stuttgart, Germany.
Jens PfannstielCore Facility Hohenheim, Mass Spectrometry Unit, University of Hohenheim, Stuttgart, Germany.
Annick StintziDepartment of Plant Physiology and Biochemistry, University of Hohenheim, Stuttgart, Germany.
Andreas SchallerDepartment of Plant Physiology and Biochemistry, University of Hohenheim, Stuttgart, Germany. andreas.schaller@uni-hohenheim.de.
University of Hohenheim · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A critical step in the functional characterization of proteases is the identification of physiologically relevant substrates, which often starts with a collection of candidate proteins. To test these candidates and identify specific processing sites, in vitro cleavage assays are typically used, followed by polyacrylamide gel electrophoresis (SDS-PAGE) to separate and visualize the cleavage products. For the identification of cleavage sites, the sequences at the N- or C-terminal ends of the cleavage products need to be identified, which is the most challenging step in this procedure. Here, we describe a method for the reliable identification of the N-termini of polypeptides after separation by SDS-PAGE. The procedure relies on in-gel labeling of the N-terminal-free amino group by reductive dimethylation, followed by tryptic digestion and analysis of resulting peptides by mass spectrometry. N-terminal peptides are readily identified by the 28 Da mass dimethyl tag linked to their first amino acid.

Indexed as

EndopeptidasesPeptide HydrolasesAmino AcidsElectrophoresis, Polyacrylamide GelMass SpectrometryAmino AcidsEndopeptidasesPeptide HydrolasesCleavage specificityMass spectrometryN-terminusPrecursor processingProteolysisReductive dimethylationSDS-PAGE

Identifiers

PMID36413329
OpenAlexW4309660147

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.