Evidence map›Paper›PMID 35022400›Full record

ArticleNature communications2022

Mammalian brain glycoproteins exhibit diminished glycan complexity compared to other tissues.

Sarah E Williams, Maxence Noel, Sylvain Lehoux, Murat Cetinbas, Ramnik J Xavier, Ruslan I Sadreyev, Edward M Scolnick, Jordan W Smoller, Richard D Cummings, Robert G Mealer

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
8.5field-weighted citation impact, top 1% 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

66 citing papers in PubMed, 102 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Parkinson's Disease-Associated Remodeling of SynapticJournal of proteome research · 2026
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  5. GalNAc-T13 maintains neurite architecture and memory retention via O-GalNAc glycosylation of seizure protein 6.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Disrupted O-GalNAc glycosylation as a mechanism and biomarker ofbioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Article
  9. Review
  10. International journal of molecular sciences · 2025
    Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Neuromuscular Defects in aBiomolecules · 2025
    Article
  18. Review
  19. Article
  20. Article

6 more citing papers are in PubMed but not listed here.

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

10 authors at 3 institutions in 1 country.

Sarah E WilliamsPsychiatric and Neurodevelopmental Genetics Unit, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.
Maxence NoelDepartment of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0003-2621-7374
Sylvain LehouxDepartment of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.
Murat CetinbasDepartment of Molecular Biology, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.
Ramnik J XavierDepartment of Molecular Biology, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0002-5630-5167
Ruslan I SadreyevDepartment of Molecular Biology, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.
Edward M ScolnickPsychiatric and Neurodevelopmental Genetics Unit, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.
Jordan W SmollerPsychiatric and Neurodevelopmental Genetics Unit, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0002-0381-6334
Richard D CummingsDepartment of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0002-8918-5034
Robert G MealerPsychiatric and Neurodevelopmental Genetics Unit, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA. rmealer@partners.org.ORCID http://orcid.org/0000-0001-5963-2836
Beth Israel Deaconess Medical Center · USBroad Institute · USHarvard University · US

Funding

Pilot & Feasibility ProgramP30DK043351 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI RAYMOND T CHUNG · 1991 to 2026
$35.3M
ROLE OF DIETARY CONSTITUENTS ON GENE EXPRESSION IN INTESTINAL EPITHELIUMP30DK040561 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI Elizabeth Austen Lawson, Takara Leah Stanley · 1994 to 2026
$31.6M
Overall Priority Score P41GM103694 · NIGMS · EMORY UNIVERSITY · PI CUMMINGS, RICHARD D · 2013 to 2018
$6.9M
Glycoproteomics and the Glycosylation Code of the Brain in Asymptomatic and Symptomatic Alzheimer’s DiseaseRF1AG062181 · NIA · BETH ISRAEL DEACONESS MEDICAL CENTER · PI CUMMINGS, RICHARD D, SEYFRIED, NICHOLAS THOMAS · 2018 to 2018
$4.1M
Translational Neuroscience Training for CliniciansT32MH112485 · NIMH · MASSACHUSETTS GENERAL HOSPITAL · PI BUCKNER, RANDY L, ROFFMAN, JOSHUA LAWRENCE · 2018 to 2022
$1.7M
NIA NIH HHS RF1 AG062181NIDDK NIH HHS P30 DK040561NIDDK NIH HHS P30 DK043351NIGMS NIH HHS P41 GM103694NIMH NIH HHS T32 MH112485
6 · The paper itself

Abstract

Glycosylation is essential to brain development and function, but prior studies have often been limited to a single analytical technique and excluded region- and sex-specific analyses. Here, using several methodologies, we analyze Asn-linked and Ser/Thr/Tyr-linked protein glycosylation between brain regions and sexes in mice. Brain N-glycans are less complex in sequence and variety compared to other tissues, consisting predominantly of high-mannose and fucosylated/bisected structures. Most brain O-glycans are unbranched, sialylated O-GalNAc and O-mannose structures. A consistent pattern is observed between regions, and sex differences are minimal compared to those in plasma. Brain glycans correlate with RNA expression of their synthetic enzymes, and analysis of glycosylation genes in humans show a global downregulation in the brain compared to other tissues. We hypothesize that this restricted repertoire of protein glycans arises from their tight regulation in the brain. These results provide a roadmap for future studies of glycosylation in neurodevelopment and disease.

Indexed as

AnimalsBrainExtracellular Matrix ProteinsFemaleGlycoproteinsGlycosylationMaleMammalsMannoseMiceMice, Inbred C57BLPolysaccharidesProteoglycan Link ProteinProteoglycansExtracellular Matrix ProteinsGlycoproteinsMannosePolysaccharidesProteoglycan Link ProteinProteoglycans

Identifiers

PMID35022400
PMCPMC8755730
OpenAlexW4205504028

What OpenQuestion holds

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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.