Evidence map›Paper›PMID 23837885›Full record

ReviewBioconjugate chemistry2013

Enzymatic labeling of proteins: techniques and approaches.

Mohammad Rashidian, Jonathan K Dozier, Mark D Distefano

Abstract readReview
In one paragraph

Review in Bioconjugate chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
–field-weighted citation impact
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

83 citing papers in PubMed.

  1. Article
  2. Review
  3. Flavin transferase ApbE: From discovery to applications.The Journal of biological chemistry · 2025
    Review
  4. Click Chemistry-Based Bioconjugation of Iron Oxide Nanoparticles.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  5. Site-specific bioconjugation and nuclear imaging.Current opinion in chemical biology · 2024
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Chemical Approaches to Synthetic Drug Delivery Systems for Systemic Applications.Angewandte Chemie (International ed. in English) · 2022
    Review
  16. Article
  17. Article
  18. Article
  19. Molecular photoswitches in aqueous environments.Chemical Society reviews · 2021
    Review
  20. Article

23 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

3 authors.

Mohammad Rashidian
Jonathan K Dozier
Mark D Distefano

Funding

Chemistry-Biology Interface Training GrantT32GM008700 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI DISTEFANO, MARK D · 1999 to 2018
$4.0M
MECHANISM AND FUNCTION OF PROTEIN PRENYLATIONR01GM058842 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI DISTEFANO, MARK D · 1998 to 2010
$2.6M
Enzymatic Protein LabelingR01GM084152 · NIGMS · UNIVERSITY OF MINNESOTA · PI DISTEFANO, MARK D · 2010 to 2019
$2.6M
NIGMS NIH HHS GM058842NIGMS NIH HHS GM084152NIGMS NIH HHS R01 GM058842NIGMS NIH HHS R01 GM084152NIGMS NIH HHS T32 GM008700
6 · The paper itself

Abstract

Site-specific modification of proteins is a major challenge in modern chemical biology due to the large number of reactive functional groups typically present in polypeptides. Because of its importance in biology and medicine, the development of methods for site-specific modification of proteins is an area of intense research. Selective protein modification procedures have been useful for oriented protein immobilization, for studies of naturally occurring post-translational modifications, for creating antibody–drug conjugates, for the introduction of fluorophores and other small molecules on to proteins, for examining protein structure, folding, dynamics, and protein–protein interactions, and for the preparation of protein–polymer conjugates. One of the most important approaches for protein labeling is to incorporate bioorthogonal functionalities into proteins at specific sites via enzymatic reactions. The incorporated tags then enable reactions that are chemoselective, whose functional groups not only are inert in biological media, but also do not occur natively in proteins or other macromolecules. This review article summarizes the enzymatic strategies, which enable site-specific functionalization of proteins with a variety of different functional groups. The enzymes covered in this review include formylglycine generating enzyme, sialyltransferases, phosphopantetheinyltransferases, O-GlcNAc post-translational modification, sortagging, transglutaminase, farnesyltransferase, biotin ligase, lipoic acid ligase, and N-myristoyltransferase.

Indexed as

Amino Acid SequenceAnimalsEnzymesHumansMolecular Sequence DataProtein Processing, Post-TranslationalProteinsStaining and LabelingEnzymesProteins

Identifiers

PMID23837885
PMCPMC3864113

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.