Evidence map›Paper›PMID 33398026›Full record

ArticleNature communications2021

Site-specific incorporation of citrulline into proteins in mammalian cells.

Santanu Mondal, Shu Wang, Yunan Zheng, Sudeshna Sen, Abhishek Chatterjee, Paul R Thompson

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.8field-weighted citation impact, top 4% 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

39 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. [Determination of the derivatization reactivity betweenSe pu = Chinese journal of chromatography · 2024
    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

6 authors at 3 institutions in 1 country.

Santanu MondalDepartment of Biochemistry and Molecular Pharmacology, UMass Medical School, 364 Plantation Street, Worcester, MA, 01605, USA.
Shu WangDepartment of Chemistry, Boston College, Chestnut Hill, MA, 02467, USA.
Yunan ZhengDepartment of Chemistry, Boston College, Chestnut Hill, MA, 02467, USA.
Sudeshna SenDepartment of Biochemistry and Molecular Pharmacology, UMass Medical School, 364 Plantation Street, Worcester, MA, 01605, USA.
Abhishek ChatterjeeDepartment of Chemistry, Boston College, Chestnut Hill, MA, 02467, USA. abhishek.chatterjee@bc.edu.ORCID 0000-0002-6231-5302
Paul R ThompsonDepartment of Biochemistry and Molecular Pharmacology, UMass Medical School, 364 Plantation Street, Worcester, MA, 01605, USA. paul.thompson@umassmed.edu.ORCID 0000-0002-1621-3372
Boston College · USUniversity of Massachusetts Chan Medical School · USUMass Memorial Health Care · US

Funding

Chemical probes to decipher PAD biologyR35GM118112 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI Paul R Thompson · 2016 to 2026
$9.5M
A genetically encoded toolset to decipher the biology of post-translational modifications in the mammalian proteomeR35GM136437 · NIGMS · BOSTON COLLEGE · PI Abhishek Chatterjee · 2020 to 2026
$4.0M
NIGMS NIH HHS R35 GM118112NIGMS NIH HHS R35 GM136437
6 · The paper itself

Abstract

Citrullination is a post-translational modification (PTM) of arginine that is crucial for several physiological processes, including gene regulation and neutrophil extracellular trap formation. Despite recent advances, studies of protein citrullination remain challenging due to the difficulty of accessing proteins homogeneously citrullinated at a specific site. Herein, we report a technology that enables the site-specific incorporation of citrulline (Cit) into proteins in mammalian cells. This approach exploits an engineered E. coli-derived leucyl tRNA synthetase-tRNA pair that incorporates a photocaged-citrulline (SM60) into proteins in response to a nonsense codon. Subsequently, SM60 is readily converted to Cit with light in vitro and in living cells. To demonstrate the utility of the method, we biochemically characterize the effect of incorporating Cit at two known autocitrullination sites in Protein Arginine Deiminase 4 (PAD4, R372 and R374) and show that the R372Cit and R374Cit mutants are 181- and 9-fold less active than the wild-type enzyme. This technology possesses the potential to decipher the biology of citrullination.

Indexed as

AnimalsCitrullineGreen Fluorescent ProteinsHEK293 CellsHumansMammalsProtein-Arginine Deiminase Type 4ProteomicsUltraviolet RaysCitrullineenhanced green fluorescent proteinGreen Fluorescent ProteinsProtein-Arginine Deiminase Type 4

Identifiers

PMID33398026
PMCPMC7782748
OpenAlexW3120145114

What OpenQuestion holds

Textmetadata
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.