Evidence map›Paper›PMID 35551261›Full record

ArticleNature chemical biology2022

Chemical editing of proteoglycan architecture.

Timothy R O'Leary, Meg Critcher, Tesia N Stephenson, Xueyi Yang, Abdullah A Hassan, Noah M Bartfield, Richard Hawkins, Mia L Huang

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2022. 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
2.3field-weighted citation impact, top 11% 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, 28 citations in OpenAlex.

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  10. Imaging ofScience advances · 2023
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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

8 authors at 1 institution in 1 country.

Timothy R O'Leary *Department of Molecular Medicine, Scripps Research, Jupiter, FL, USA.
Meg Critcher *Department of Molecular Medicine, Scripps Research, Jupiter, FL, USA.ORCID http://orcid.org/0000-0002-3048-4072
Tesia N StephensonDepartment of Molecular Medicine, Scripps Research, Jupiter, FL, USA.
Xueyi YangDepartment of Molecular Medicine, Scripps Research, Jupiter, FL, USA.
Abdullah A HassanDepartment of Molecular Medicine, Scripps Research, Jupiter, FL, USA.ORCID http://orcid.org/0000-0002-7143-6122
Noah M BartfieldDepartment of Molecular Medicine, Scripps Research, Jupiter, FL, USA.
Richard HawkinsDepartment of Molecular Medicine, Scripps Research, Jupiter, FL, USA.ORCID http://orcid.org/0000-0002-7481-5419
Mia L HuangDepartment of Molecular Medicine, Scripps Research, Jupiter, FL, USA. miahuang@scripps.edu.ORCID http://orcid.org/0000-0001-9909-9554
Scripps Research Institute · US

Funding

Bridging the Glycome and Proteome with Chemical BiologyR35GM142462 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI Mia L Huang · 2021 to 2026
$2.9M
Chemical editing of nanoscale proteoglycan architecture and organization to control cellularR00HD090292 · NICHD · SCRIPPS FLORIDA · PI HUANG, MIA L · 2018 to 2020
$900k
Bruker Avance III HD 600 MHz NMR spectrometerS10OD021550 · OD · SCRIPPS FLORIDA · PI KOJETIN, DOUGLAS · 2017 to 2017
$600k
Chemical editing of nanoscale proteoglycan architecture and organization to control cellular differentiationK99HD090292 · NICHD · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HUANG, MIA L · 2017 to 2017
$130k
NICHD NIH HHS K99 HD090292NICHD NIH HHS R00 HD090292NIGMS NIH HHS R35 GM142462NIH HHS S10 OD021550
6 · The paper itself

Abstract

Proteoglycans are heterogeneous macromolecular glycoconjugates that orchestrate many important cellular processes. While much attention has focused on the poly-sulfated glycosaminoglycan chains that decorate proteoglycans, other important elements of their architecture, such as core proteins and membrane localization, have garnered less emphasis. Hence, comprehensive structure-function relationships that consider the replete proteoglycan architecture as glycoconjugates are limited. Here we present an extensive approach to study proteoglycan structure and biology by fabricating defined semisynthetic modular proteoglycans that can be tailored for cell surface display. The expression of proteoglycan core proteins with unnatural amino acids permits bioorthogonal click chemistry with functionalized glycosaminoglycans for methodical dissection of the parameters required for optimal binding and function of various proteoglycan-binding proteins. We demonstrate that these sophisticated materials can recapitulate the functions of native proteoglycan ectodomains in mouse embryonic stem cell differentiation and cancer cell spreading while permitting the analysis of the contributing architectural elements toward function.

Indexed as

ProteoglycansAnimalsCell MembraneMiceProteoglycans

Identifiers

PMID35551261
PMCPMC9205196
OpenAlexW4280533999

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.