Evidence map›Paper›PMID 26420872›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Chemically tunable mucin chimeras assembled on living cells.

Jessica R Kramer, Bibiana Onoa, Carlos Bustamante, Carolyn R Bertozzi

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
3.2field-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

53 citing papers in PubMed, 115 citations in OpenAlex.

  1. Site-specific O-glycans influence lacritin structure and multimerization in tears.Protein science : a publication of the Protein Society · 2026
    Article
  2. Article
  3. The protease cathepsin K can debulk the cancer glycocalyx.The Journal of biological chemistry · 2026
    Article
  4. Review
  5. An Ultrapotent, Ultraeconomical, Antifreeze Polypeptide.Advanced materials (Deerfield Beach, Fla.) · 2026
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Synthetic Lipid Biology.Chemical reviews · 2025
    Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Synthetic Antifreeze Glycoproteins with Potent Ice-Binding Activity.Chemistry of materials : a publication of the American Chemical Society · 2024
    Article
  18. Article
  19. Mirror Image Mucins and Thio Mucins with Tunable Biodegradation.Journal of the American Chemical Society · 2023
    Article
  20. Article
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

4 authors at 3 institutions in 1 country.

Jessica R KramerDepartment of Chemistry, Stanford University, Stanford, CA 94305;
Bibiana OnoaInstitute for Quantitative Biosciences, University of California, Berkeley, CA 94720;
Carlos BustamanteInstitute for Quantitative Biosciences, University of California, Berkeley, CA 94720; Department of Chemistry, University of California, Berkeley, CA 94720; Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720; Department of Physics, University of California, Berkeley, CA 94720; Kavli Energy Nanosciences Institute at Berkeley, University of California, Berkeley, CA 94720; Howard Hughes Medical Institute, University of California, Berkeley, CA 94720;
Carolyn R BertozziDepartment of Chemistry, Stanford University, Stanford, CA 94305; Howard Hughes Medical Institute, Stanford University, Stanford, CA 94305 bertozzi@stanford.edu.
University of California, Berkeley · USHoward Hughes Medical Institute · USStanford University · US

Funding

Investigations of Golgi EnzymesR01GM059907 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERTOZZI, CAROLYN · 1999 to 2016
$5.9M
"A molecular approach toward elucidating the role of the mucin glycocalyx in cancF32GM109600 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KRAMER, JESSICA · 2014 to 2016
$163k
NIGMS NIH HHS F32 GM109600NIGMS NIH HHS R01 GM059907
6 · The paper itself

Abstract

Mucins are a family of secreted and transmembrane glycoproteins characterized by a massive domain of dense O-glycosylation on serine and threonine residues. Mucins are intimately involved in immunity and cancer, yet elucidation of the biological roles of their glycodomains has been complicated by their massive size, domain polymorphisms, and variable glycosylation patterns. Here we developed a synthetic route to a library of compositionally defined, high-molecular weight, dual end-functionalized mucin glycodomain constructs via N-carboxyanhydride polymerization. These glycopolypeptides are the first synthetic analogs to our knowledge to feature the native α-GalNAc linkage to serine with molecular weights similar to native mucins, solving a nearly 50-year synthetic challenge. Physical characterization of the mimics revealed insights into the structure and properties of mucins. The synthetic glycodomains were end-functionalized with an optical probe and a tetrazine moiety, which allowed site-specific bioorthogonal conjugation to an engineered membrane protein on live mammalian cells. This strategy in protein engineering will open avenues to explore the biological roles of cell surface mucins.

Indexed as

GlycosylationHEK293 CellsHumansMucinsProtein Structure, TertiaryRecombinant Fusion ProteinsMucinsRecombinant Fusion ProteinsglycoproteinmucinN-carboxyanhydridepolypeptideprotein engineering

Identifiers

PMID26420872
PMCPMC4611660
OpenAlexW2121074337

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.