Evidence map›Paper›PMID 33345277›Full record

ArticleThe Biochemical journal2021

Spontaneous protein-protein crosslinking at glutamine and glutamic acid residues in long-lived proteins.

Michael G Friedrich, Zhen Wang, Kevin L Schey, Roger J W Truscott

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2021. 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
0.4field-weighted citation impact, top 45% 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, 9 citations in OpenAlex.

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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

4 authors at 2 institutions in 2 countries.

Michael G FriedrichIllawarra Health and Medical Research Institute, and Molecular Horizons, University of Wollongong, Wollongong, NSW 2522, Australia.
Zhen WangDepartment of Biochemistry and Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN, U.S.A.
Kevin L ScheyDepartment of Biochemistry and Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN, U.S.A.
Roger J W TruscottIllawarra Health and Medical Research Institute, and Molecular Horizons, University of Wollongong, Wollongong, NSW 2522, Australia.
University of Wollongong · AUVanderbilt University · US

Funding

Shop Module CoreP30EY008126 · NEI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI David J. Calkins · 1989 to 2026
$19.6M
Mechanisms of Protein Aging in Normal and Cataractous LensesR01EY024258 · NEI · VANDERBILT UNIVERSITY · PI SCHEY, KEVIN L · 2014 to 2022
$2.6M
NEI NIH HHS P30 EY008126NEI NIH HHS R01 EY024258
6 · The paper itself

Abstract

Long-lived proteins (LLPs) are susceptible to the accumulation of both enzymatic and spontaneous post-translational modifications (PTMs). A prominent PTM observed in LLPs is covalent protein-protein crosslinking. In this study, we examined aged human lenses and found several proteins to be crosslinked at Glu and Gln residues. This new covalent bond involves the amino group of Lys or an α-amino group. A number of these crosslinks were found in intermediate filament proteins. Such crosslinks could be reproduced experimentally by incubation of Glu- or Gln-containing peptides and their formation was consistent with an amino group attacking a glutarimide intermediate. These findings show that both Gln and Glu residues can act as sites for spontaneous covalent crosslinking in LLPs and they provide a mechanistic explanation for an otherwise puzzling observation, that a major fraction of Aβ in the human brain is crosslinked via Glu 22 and the N-terminal amino group.

Indexed as

CataractEye ProteinsGlutamic AcidGlutamineHumansLens, CrystallineLysineMiddle AgedPiperidonesProtein Interaction Domains and MotifsProtein Processing, Post-TranslationalYoung AdultEye ProteinsGlutamic AcidGlutamineglutarimideLysinePiperidonesageAlzheimer's diseasehuman lenslong-lived proteinsprotein crosslinks

Identifiers

PMID33345277
PMCPMC9188286
OpenAlexW3116391240

What OpenQuestion holds

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LicenceTDM
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.