Evidence map›Paper›PMID 41659604›Full record

ArticlebioRxiv : the preprint server for biology2026

Topological reprogramming transforms an integral membrane oligosaccharyltransferase into a water-soluble glycosylation catalyst.

Yong Hyun Kwon, Ljubica Mihaljević, Keehun Kim, David E Kim, Thomas C Donahue, Erik J Bidstrup, Chandra K Bandi, Belen Sotomayor, Sophia W Hulbert, Kathryn A Myers and 8 more

Abstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2026. 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
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.

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

18 authors.

Yong Hyun KwonRobert F. Smith School of Chemical and Biomolecular Engineering, Cornell University, 120 Olin Hall, Ithaca, NY 14853, USA.ORCID 0000-0002-0070-2382
Ljubica MihaljevićDepartment of Biochemistry, Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
Keehun KimRobert F. Smith School of Chemical and Biomolecular Engineering, Cornell University, 120 Olin Hall, Ithaca, NY 14853, USA.
David E KimDepartment of Biochemistry, Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.ORCID 0000-0002-0023-956X
Thomas C DonahueRobert F. Smith School of Chemical and Biomolecular Engineering, Cornell University, 120 Olin Hall, Ithaca, NY 14853, USA.
Erik J BidstrupRobert F. Smith School of Chemical and Biomolecular Engineering, Cornell University, 120 Olin Hall, Ithaca, NY 14853, USA.
Chandra K BandiRobert F. Smith School of Chemical and Biomolecular Engineering, Cornell University, 120 Olin Hall, Ithaca, NY 14853, USA.
Belen SotomayorRobert F. Smith School of Chemical and Biomolecular Engineering, Cornell University, 120 Olin Hall, Ithaca, NY 14853, USA.
Sophia W HulbertBiochemistry, Molecular and Cell Biology (BMCB), Cornell University, Ithaca, NY 14853, USA.
Kathryn A MyersDepartment of Bioengineering, Stanford University, Stanford, CA 94305 USA.
Anru TianDepartment of Bioengineering, Stanford University, Stanford, CA 94305 USA.
Mariah CulpepperDepartment of Biochemistry, Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
Dario MizrachiDepartment of Physiology & Developmental Biology, Brigham Young University, Provo, UT 84602, USA.
Thapakorn JaroentomeechaiDepartment of Biotechnology, Faculty of Science, Mahidol University, Bangkok 10400, Thailand.
Henrik ClausenDepartment of Cellular and Molecular Medicine, Faculty of Health Sciences, Copenhagen Center for Glycomics, University of Copenhagen, Copenhagen, Denmark.
Michael C JewettDepartment of Bioengineering, Stanford University, Stanford, CA 94305 USA.
David BakerDepartment of Biochemistry, Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
Matthew P DeLisaRobert F. Smith School of Chemical and Biomolecular Engineering, Cornell University, 120 Olin Hall, Ithaca, NY 14853, USA.ORCID 0000-0003-3226-1566

Funding

Training future leaders at the chemistry-biology interfaceT32GM138826 · NIGMS · CORNELL UNIVERSITY · PI Jeremy Baskin · 2021 to 2026
$2.6M
Technologies to predict and probe glycosyl transferR01GM127578 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GRAY, JEFFREY J · 2018 to 2020
$1.6M
Immuno-Engineering: Integrated Engineering and Immunology TrainingT32EB023860 · NIBIB · CORNELL UNIVERSITY · PI AUGUST, AVERY, PUTNAM, DAVID A · 2018 to 2022
$933k
NIBIB NIH HHS T32 EB023860NIGMS NIH HHS R01 GM127578NIGMS NIH HHS T32 GM138826
6 · The paper itself

Abstract

Glycosyltransferases (GTs) catalyze the formation of new glycosidic bonds and thus are vital for synthesizing nature's vast repertoire of glycans and glycoconjugates and for engineering glycan-related medicines and materials. However, obtaining detailed structural and functional insights for the >750,000 known GTs is limited by difficulties associated with their efficient recombinant expression. Members of the GT-C fold, in particular, pose the most significant expression challenges due to the integration and folding requirements of their multiple membrane-spanning regions. Here, we address this challenge by engineering water-soluble variants of an archetypal GT-C fold enzyme, namely the oligosaccharyltransferase PglB from

Identifiers

PMID41659604
PMCPMC12879670

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.