Aqueous Solutions of Peptides and Trialkylamines Lead to Unexpected Peptide Modification.

Yiran Ma, Puja J Gandhi, James P Reilly

Open access · goldAbstract read

In one paragraph

Article in Molecules (Basel, Switzerland), 2021. 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 89% 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, 1 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

3 authors at 1 institution in 1 country.

Yiran MaDepartment of Chemistry, Indiana University, Bloomington, IN 47405, USA.

Puja J GandhiDepartment of Chemistry, Indiana University, Bloomington, IN 47405, USA.

James P ReillyDepartment of Chemistry, Indiana University, Bloomington, IN 47405, USA.ORCID 0000-0002-9784-1804

Indiana University Bloomington · US

Funding

Characterizing proteasome-substrate interactions by mass spectrometry proteomicsR01GM135264 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI CLEMMER, DAVID E., MATOUSCHEK, ANDREAS · 2020 to 2024

$1.4M

National Science Foundation CHE-1904749NIGMS NIH HHS R01 GM135264NIH HHS R01 GM135264-01

6 · The paper itself

Abstract

When trialkylamines are added to buffered solutions of peptides, unexpected adducts can be formed. These adducts correspond to Schiff base products. The source of the reaction is the unexpected presence of aldehydes in amines. The aldehydes can be detected in a few ways. Most importantly, they can lead to unanticipated results in proteomics experiments. Their undesirable effects can be minimized through the addition of other amines.

Indexed as

AldehydesAminesAmino Acid SequenceHemoglobinsPeptidesPolyaminesProteinsProteolysisSchiff BasesSolutionsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationAldehydesAminesHemoglobinsPeptidesPolyaminesProteinsSchiff BasesSolutionsprotein modificationSchiff basetriethylamine

Identifiers

PMID34770892

DOI10.3390/molecules26216481

PMCPMC8587169

OpenAlexW3209904018

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.