Glycopolymers stabilize protein folding and protein-protein interactions via enthalpic interactions.

Sabrina M Richter, Neal Brook, Alex J Guseman

Abstract read

In one paragraph

Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing 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

1 citing paper in PubMed.

Glycopolymers stabilize protein folding and protein-protein interactions via enthalpic interactions.Protein science : a publication of the Protein Society · 2026
Article

4 · The record

Corrections and comments

Update of
Glycopolymers stabilize protein folding and protein-protein interactions via enthalpic interactions.2025

5 · Who and what money

Authors and funding

3 authors.

Sabrina M RichterDepartment of Chemistry and Biochemistry, University of California, San Diego, California, USA.

Neal BrookDepartment of Chemistry and Biochemistry, University of California, San Diego, California, USA.

Alex J GusemanDepartment of Chemistry and Biochemistry, University of California, San Diego, California, USA.ORCID https://orcid.org/0000-0002-9796-5719

Funding

UC San Diego FIRST ProgramU54CA272220 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Deborah L Wingard · 2022 to 2026

$21.2M

Developing Lectins as Inhibitors of Coronavirus Spike ProteinsR00GM145970 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Alex Joseph Guseman · 2024 to 2026

$747k

NCI NIH HHS U54 CA272220NCI NIH HHS U54CA272220NIGMS NIH HHS R00 GM145970NIGMS NIH HHS R00GM145970

6 · The paper itself

Abstract

Macromolecular crowding is ubiquitous in physiological environments, perturbing the thermodynamics and kinetics of proteins via excluded volume and nonspecific chemical interactions. While crowding has been well studied in vitro and in cells, the inert sugar polymers used to simulate crowding lack the chemical characteristics of biomolecules. Emerging studies guide the development of more relevant models of crowding in the cell, but little work has been done to discern crowding effects on proteins at the cell surface. Using

Indexed as

HeparinHyaluronic AcidMucinsProtein FoldingProtein BindingProtein StabilityThermodynamicsHeparinHyaluronic AcidMucins19F NMRglycocalyxmacromolecular crowdingprotein folding

Identifiers

PMID41427734

DOI10.1002/pro.70403

PMCPMC12720779

What OpenQuestion holds

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Registered trials

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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.