Evidence map›Paper›PMID 31920645›Full record

ReviewFrontiers in pharmacology2019

From Synthesis to Characterization of Site-Selective PEGylated Proteins.

Lisandra Herrera Belén, Carlota de Oliveira Rangel-Yagui, Jorge F Beltrán Lissabet, Brian Effer, Manuel Lee-Estevez, Adalberto Pessoa, Rodrigo L Castillo, Jorge G Farías

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in pharmacology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 50 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. PEGylated therapeutics in the clinic.Bioengineering & translational medicine · 2024
    Review
  11. Article
  12. Semi-Telechelic Polymers from Mechanochemical C─C Bond Activation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  13. Review
  14. Article
  15. Review
  16. OrganometallicBioconjugate chemistry · 2022
    Article
  17. Review
  18. Review
  19. Article
  20. Review
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 4 institutions in 2 countries.

Lisandra Herrera BelénDepartment of Chemical Engineering, Faculty of Engineering and Science, Universidad de La Frontera, Temuco, Chile.
Carlota de Oliveira Rangel-YaguiDepartment of Biochemical and Pharmaceutical Technology, School of Pharmaceutical Sciences, University of Sao Paulo, Sao Paulo, Brazil.
Jorge F Beltrán LissabetDepartment of Chemical Engineering, Faculty of Engineering and Science, Universidad de La Frontera, Temuco, Chile.
Brian EfferDepartment of Chemical Engineering, Faculty of Engineering and Science, Universidad de La Frontera, Temuco, Chile.
Manuel Lee-EstevezFaculty of Health Sciences, Universidad Autónoma de Chile, Temuco, Chile.
Adalberto PessoaDepartment of Biochemical and Pharmaceutical Technology, School of Pharmaceutical Sciences, University of Sao Paulo, Sao Paulo, Brazil.
Rodrigo L CastilloDepartment of Internal Medicine East, Faculty of Medicine, University of Chile, Santiago de Chile, Chile.
Jorge G FaríasDepartment of Chemical Engineering, Faculty of Engineering and Science, Universidad de La Frontera, Temuco, Chile.
Universidad de La Frontera · CLUniversidade de São Paulo · BRUniversidad Autónoma de Chile · CLUniversity of Chile · CL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Covalent attachment of therapeutic proteins to polyethylene glycol (PEG) is widely used for the improvement of its pharmacokinetic and pharmacological properties, as well as the reduction in reactogenicity and related side effects. This technique named PEGylation has been successfully employed in several approved drugs to treat various diseases, even cancer. Some methods have been developed to obtain PEGylated proteins, both in multiple protein sites or in a selected amino acid residue. This review focuses mainly on traditional and novel examples of chemical and enzymatic methods for site-selective PEGylation, emphasizing in N-terminal PEGylation, that make it possible to obtain products with a high degree of homogeneity and preserve bioactivity. In addition, the main assay methods that can be applied for the characterization of PEGylated molecules in complex biological samples are also summarized in this paper.

Indexed as

characterizationenzymatic ligationN-terminal PEGylationprotein PEGylationsite-selective conjugation

Identifiers

PMID31920645
PMCPMC6930235
OpenAlexW2994975398

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.