Evidence map›Paper›PMID 31182711›Full record

ArticleNature communications2019

Single-site glycine-specific labeling of proteins.

Landa Purushottam, Srinivasa Rao Adusumalli, Usha Singh, V B Unnikrishnan, Dattatraya Gautam Rawale, Mansi Gujrati, Ram Kumar Mishra, Vishal Rai

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.2field-weighted citation impact, top 3% 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

32 citing papers in PubMed, 82 citations in OpenAlex.

  1. Review
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  9. Review
  10. Article
  11. Recent Advances in Bioorthogonal Ligation and Bioconjugation.Topics in current chemistry (Cham) · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. ACS central science · 2023
    Review
  16. Review
  17. Article
  18. Article
  19. Chemical Conjugation to Less Targeted Proteinogenic Amino Acids.Chembiochem : a European journal of chemical biology · 2022
    Review
  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

8 authors at 1 institution in 1 country.

Landa PurushottamDepartment of Chemistry, Indian Institute of Science Education and Research (IISER) Bhopal, Bhopal, 462066, India.
Srinivasa Rao AdusumalliDepartment of Chemistry, Indian Institute of Science Education and Research (IISER) Bhopal, Bhopal, 462066, India.
Usha SinghDepartment of Biological Sciences, Indian Institute of Science Education and Research (IISER) Bhopal, Bhopal, 462066, India.
V B UnnikrishnanDepartment of Chemistry, Indian Institute of Science Education and Research (IISER) Bhopal, Bhopal, 462066, India.
Dattatraya Gautam RawaleDepartment of Chemistry, Indian Institute of Science Education and Research (IISER) Bhopal, Bhopal, 462066, India.
Mansi GujratiDepartment of Biological Sciences, Indian Institute of Science Education and Research (IISER) Bhopal, Bhopal, 462066, India.
Ram Kumar MishraDepartment of Biological Sciences, Indian Institute of Science Education and Research (IISER) Bhopal, Bhopal, 462066, India.
Vishal RaiDepartment of Chemistry, Indian Institute of Science Education and Research (IISER) Bhopal, Bhopal, 462066, India. vrai@iiserb.ac.in.ORCID http://orcid.org/0000-0002-6078-3516
Indian Institute of Science Education and Research, Bhopal · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Labeling of native proteins invites interest from diverse segments of science. However, there remains the significant unmet challenge in precise labeling at a single site of a protein. Here, we report the site-specific labeling of natural or easy-to-engineer N-terminus Gly in proteins with remarkable efficiency and selectivity. The method generates a latent nucleophile from N-terminus imine that reacts with an aldehyde to deliver an aminoalcohol under physiological conditions. It differentiates N-Gly as a unique target amongst other proteinogenic amino acids. The method allows single-site labeling of proteins in isolated form and extends to lysed cells. It administers an orthogonal aldehyde group primed for late-stage tagging with an affinity tag,

Indexed as

AldehydesEscherichia coliFluorescent DyesFluorineGlycineHEK293 CellsHumansInsulinProteinsReceptor, InsulinStaining and LabelingAldehydesFluorescent DyesFluorineGlycineInsulinProteinsReceptor, Insulin

Identifiers

PMID31182711
PMCPMC6557831
OpenAlexW2951747643

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.