Evidence map›Paper›PMID 33686291›Full record

ArticleNature chemical biology2021

Target protein deglycosylation in living cells by a nanobody-fused split O-GlcNAcase.

Yun Ge, Daniel H Ramirez, Bo Yang, Alexandria K D'Souza, Chanat Aonbangkhen, Stephanie Wong, Christina M Woo

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed, 1 pooled it
6.7field-weighted citation impact, top 2% 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, 1 synthesis or guideline pooled it, 103 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Review
  6. Induced proximity-based therapeutic modalities.Nature reviews. Drug discovery · 2026
    Review
  7. A Scalable Design for Proximity-Inducing Molecules.bioRxiv : the preprint server for biology · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. 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

7 authors at 1 institution in 1 country.

Yun GeDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, USA.ORCID http://orcid.org/0000-0001-6769-5458
Daniel H RamirezDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, USA.ORCID http://orcid.org/0000-0003-3288-9951
Bo YangDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, USA.ORCID http://orcid.org/0000-0003-3534-7517
Alexandria K D'SouzaDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, USA.ORCID http://orcid.org/0000-0003-2429-3218
Chanat AonbangkhenDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, USA.ORCID http://orcid.org/0000-0002-7378-1341
Stephanie WongDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, USA.ORCID http://orcid.org/0000-0001-9144-7841
Christina M WooDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, USA. cwoo@chemistry.harvard.edu.ORCID http://orcid.org/0000-0001-8687-9105
Harvard University · US

Funding

Tools to facilitate manipulation of protein-specific glycosylation stoichiometry in cellsU01CA242098 · NCI · HARVARD UNIVERSITY · PI WOO, CHRISTINA · 2019 to 2021
$1.4M
NCI NIH HHS U01 CA242098
6 · The paper itself

Abstract

O-linked N-acetylglucosamine (O-GlcNAc) is an essential and dynamic post-translational modification that is presented on thousands of nucleocytoplasmic proteins. Interrogating the role of O-GlcNAc on a single target protein is crucial, yet challenging to perform in cells. Herein, we developed a nanobody-fused split O-GlcNAcase (OGA) as an O-GlcNAc eraser for selective deglycosylation of a target protein in cells. After systematic cellular optimization, we identified a split OGA with reduced inherent deglycosidase activity that selectively removed O-GlcNAc from the desired target protein when directed by a nanobody. We demonstrate the generality of the nanobody-fused split OGA using four nanobodies against five target proteins and use the system to study the impact of O-GlcNAc on the transcription factors c-Jun and c-Fos. The nanobody-directed O-GlcNAc eraser provides a new strategy for the functional evaluation and engineering of O-GlcNAc via the selective removal of O-GlcNAc from individual proteins directly in cells.

Indexed as

Antigens, NeoplasmBiological AssayCatalytic DomainDrug Delivery SystemsGene ExpressionGlycosylationHEK293 CellsHistone AcetyltransferasesHumansHyaluronoglucosaminidaseHydrolysisJNK Mitogen-Activated Protein KinasesMembrane GlycoproteinsNuclear Pore Complex ProteinsPlasmidsProtein BindingAntigens, NeoplasmHistone AcetyltransferasesHyaluronoglucosaminidaseJNK Mitogen-Activated Protein KinasesJunB protein, humanMembrane GlycoproteinsNuclear Pore Complex Proteinsnuclear pore protein p62OGA protein, humanRecombinant Fusion ProteinsSingle-Domain AntibodiesSP1 protein, humanSp1 Transcription FactorTranscription Factors

Identifiers

PMID33686291
PMCPMC8085020
OpenAlexW3135254146

What OpenQuestion holds

Textmetadata
LicenceTDM
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.