Evidence map›Paper›PMID 34876561›Full record

ArticleNature communications2021

Discovery of indole-modified aptamers for highly specific recognition of protein glycoforms.

Alex M Yoshikawa, Alexandra Rangel, Trevor Feagin, Elizabeth M Chun, Leighton Wan, Anping Li, Leonhard Moeckl, Diana Wu, Michael Eisenstein, Sharon Pitteri and 1 more

Erratum issuedOpen access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

20 citing papers in PubMed, 49 citations in OpenAlex.

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  13. Diverse applications and development of aptamer detection technology.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2023
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 1 country.

Alex M YoshikawaDepartment of Chemical Engineering, Stanford University, Stanford, CA, 94305, USA.
Alexandra RangelDepartment of Radiology, Stanford University, Stanford, CA, 94305, USA.
Trevor FeaginDepartment of Radiology, Stanford University, Stanford, CA, 94305, USA.
Elizabeth M ChunDepartment of Radiology, Stanford University, Stanford, CA, 94305, USA.
Leighton WanDepartment of Bioengineering, Stanford University, Stanford, CA, 94305, USA.
Anping LiDepartment of Radiology, Stanford University, Stanford, CA, 94305, USA.
Leonhard MoecklDepartment of Chemistry, Stanford University, Stanford, CA, 94305, USA.
Diana WuDepartment of Bioengineering, Stanford University, Stanford, CA, 94305, USA.
Michael EisensteinDepartment of Radiology, Stanford University, Stanford, CA, 94305, USA.
Sharon PitteriDepartment of Radiology, Stanford University, Stanford, CA, 94305, USA.ORCID http://orcid.org/0000-0002-3119-873X
H Tom SohDepartment of Radiology, Stanford University, Stanford, CA, 94305, USA. tsoh@stanford.edu.ORCID http://orcid.org/0000-0001-9443-857X
Stanford University · USChan Zuckerberg Initiative (United States) · US

Funding

Real-time biosensor for mapping the function of the pancreasOT2OD025342 · OD · STANFORD UNIVERSITY · PI SOH, HYONGSOK TOM · 2018 to 2021
$4.6M
NIH HHS OT2 OD025342
6 · The paper itself

Abstract

Glycosylation is one of the most abundant forms of post-translational modification, and can have a profound impact on a wide range of biological processes and diseases. Unfortunately, efforts to characterize the biological function of such modifications have been greatly hampered by the lack of affinity reagents that can differentiate protein glycoforms with robust affinity and specificity. In this work, we use a fluorescence-activated cell sorting (FACS)-based approach to generate and screen aptamers with indole-modified bases, which are capable of recognizing and differentiating between specific protein glycoforms. Using this approach, we were able to select base-modified aptamers that exhibit strong selectivity for specific glycoforms of two different proteins. These aptamers can discriminate between molecules that differ only in their glycan modifications, and can also be used to label glycoproteins on the surface of cultured cells. We believe our strategy should offer a generally-applicable approach for developing useful reagents for glycobiology research.

Indexed as

Binding SitesCrystallography, X-RayDictyosteliumFetuinsFlow CytometryGlycoproteinsHigh-Throughput Screening AssaysHumansIndolesPolysaccharidesProteinsFetuinsGlycoproteinsindoleIndolesPolysaccharidesProteins

Identifiers

PMID34876561
PMCPMC8651674
OpenAlexW4225610192

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.