Evidence map›Paper›PMID 26237170›Full record

ArticleJournal of the American Chemical Society2015

Supramolecular Glycosylation Accelerates Proteolytic Degradation of Peptide Nanofibrils.

Dan Yuan, Junfeng Shi, Xuewen Du, Ning Zhou, Bing Xu

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

14 citing papers in PubMed, 40 citations in OpenAlex.

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  11. Heterotypic Supramolecular Hydrogels.Journal of materials chemistry. B · 2016
    Article
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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.

Dan YuanDepartment of Chemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02454, United States.
Junfeng ShiDepartment of Chemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02454, United States.
Xuewen DuDepartment of Chemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02454, United States.
Ning ZhouDepartment of Chemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02454, United States.
Bing XuDepartment of Chemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02454, United States.
Brandeis University · US

Funding

Subcellular Enzyme-instructed self-assembly for molecular anticancer nanomedicinesR01CA142746 · NCI · BRANDEIS UNIVERSITY · PI Bing Xu · 2010 to 2026
$6.4M
NCI NIH HHS R01 CA142746NCI NIH HHS R01CA142746
6 · The paper itself

Abstract

Despite the recent consensus that the oligomers of amyloid peptides or aberrant proteins are cytotoxic species, there is still a need for an effective way to eliminate the oligomers. Based on the fact that normal proteins are more glycosylated than pathogenic proteins, we show that a conjugate of nucleobase, peptide, and saccharide binds to peptides from molecular nanofibrils and accelerates the proteolytic degradation of the molecular nanofibrils. As the first example of the use of supramolecular glycosylation to dissociate molecular nanofibrils and to accelerate the degradation of peptide aggregates, this work illustrates a new method that ultimately may lead to an effective approach for degrading cytotoxic oligomers of peptides or aberrant proteins.

Indexed as

Amino Acid MotifsCalorimetryEpitopesGlycoconjugatesGlycosylationHydrogelsMicroscopy, Electron, TransmissionPeptidesProteolysisSolid-Phase Synthesis TechniquesEpitopesGlycoconjugatesHydrogelsPeptides

Identifiers

PMID26237170
PMCPMC4941208
OpenAlexW1433445337

What OpenQuestion holds

Textmetadata
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.