Evidence map›Paper›PMID 34207845›Full record

ReviewMolecules (Basel, Switzerland)2021

Exploiting Protein N-Terminus for Site-Specific Bioconjugation.

Lucia De Rosa, Rossella Di Stasi, Alessandra Romanelli, Luca Domenico D'Andrea

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

14 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Peptide Tags for Site-Selective Nonenzymatic Covalent Modification of Proteins.Journal of peptide science : an official publication of the European Peptide Society · 2025
    Review
  3. Novel Peptide-Drug Conjugates with Dual Anticancer Activity.International journal of molecular sciences · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Recent Advances in Bioorthogonal Ligation and Bioconjugation.Topics in current chemistry (Cham) · 2023
    Review
  9. Article
  10. Article
  11. Review
  12. Fast Cysteine Bioconjugation Chemistry.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  13. Review
  14. 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

4 authors at 3 institutions in 1 country.

Lucia De RosaIstituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134 Napoli, Italy.ORCID 0000-0003-2386-4402
Rossella Di StasiIstituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134 Napoli, Italy.
Alessandra RomanelliDipartimento di Scienze Farmaceutiche, Università Degli Studi di Milano, Via Venezian 21, 20133 Milano, Italy.ORCID 0000-0002-7609-4061
Luca Domenico D'AndreaIstituto di Scienze e Tecnologie Chimiche "Giulio Natta", CNR Via M. Bianco 9, 20131 Milano, Italy.ORCID 0000-0002-2589-216X
Institute of Biostructure and Bioimaging · ITIstituto di Chimica Biomolecolare · ITUniversity of Milan · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although a plethora of chemistries have been developed to selectively decorate protein molecules, novel strategies continue to be reported with the final aim of improving selectivity and mildness of the reaction conditions, preserve protein integrity, and fulfill all the increasing requirements of the modern applications of protein conjugates. The targeting of the protein N-terminal alpha-amine group appears a convenient solution to the issue, emerging as a useful and unique reactive site universally present in each protein molecule. Herein, we provide an updated overview of the methodologies developed until today to afford the selective modification of proteins through the targeting of the N-terminal alpha-amine. Chemical and enzymatic strategies enabling the selective labeling of the protein N-terminal alpha-amine group are described.

Indexed as

AminesAzidesBinding SitesClick ChemistryMolecular Probe TechniquesProtein DomainsProteinsAminesAzidesProteinsaldehyde proteinazide proteinchemical ligationchemo-selective reactionclick-chemistrymolecular probeprotein labeling

Identifiers

PMID34207845
PMCPMC8228110
OpenAlexW3167073055

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.