Evidence map›Paper›PMID 36447399›Full record

ArticlemAbs

A glyco-engineering approach for site-specific conjugation to Fab glycans.

Maria L Jaramillo, Traian Sulea, Yves Durocher, Mauro Acchione, Melissa J Schur, Anna Robotham, John F Kelly, Marie-France Goneau, Alma Robert, Yuneivy Cepero-Donates and 1 more

Open access · goldAbstract read
In one paragraph

Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

6 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Article
  3. Advancements in antibody-drug conjugates as cancer therapeutics.Journal of the National Cancer Center · 2025
    Review
  4. Article
  5. Review
  6. 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

11 authors at 1 institution in 1 country.

Maria L JaramilloHuman Health Therapeutics Research Centre, National Research Council Canada, 6100 Royalmount Avenue, H4P 2R2, Montreal, Qc, Canada.
Traian SuleaHuman Health Therapeutics Research Centre, National Research Council Canada, 6100 Royalmount Avenue, H4P 2R2, Montreal, Qc, Canada.
Yves DurocherHuman Health Therapeutics Research Centre, National Research Council Canada, 6100 Royalmount Avenue, H4P 2R2, Montreal, Qc, Canada.
Mauro AcchioneHuman Health Therapeutics Research Centre, National Research Council Canada, 6100 Royalmount Avenue, H4P 2R2, Montreal, Qc, Canada.
Melissa J SchurHuman Health Therapeutics Research Centre, National Research Council Canada, 100 Sussex Drive, K1A 0R6, Ottawa, ON, Canada.
Anna RobothamHuman Health Therapeutics Research Centre, National Research Council Canada, 100 Sussex Drive, K1A 0R6, Ottawa, ON, Canada.
John F KellyHuman Health Therapeutics Research Centre, National Research Council Canada, 100 Sussex Drive, K1A 0R6, Ottawa, ON, Canada.
Marie-France GoneauHuman Health Therapeutics Research Centre, National Research Council Canada, 100 Sussex Drive, K1A 0R6, Ottawa, ON, Canada.
Alma RobertHuman Health Therapeutics Research Centre, National Research Council Canada, 6100 Royalmount Avenue, H4P 2R2, Montreal, Qc, Canada.
Yuneivy Cepero-DonatesHuman Health Therapeutics Research Centre, National Research Council Canada, 6100 Royalmount Avenue, H4P 2R2, Montreal, Qc, Canada.
Michel GilbertHuman Health Therapeutics Research Centre, National Research Council Canada, 100 Sussex Drive, K1A 0R6, Ottawa, ON, Canada.ORCID 0000-0002-0204-4408
National Research Council Canada · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Effective processes for synthesizing antibody-drug conjugates (ADCs) require: 1) site-specific incorporation of the payload to avoid interference with binding to the target epitope, 2) optimal drug/antibody ratio to achieve sufficient potency while avoiding aggregation or solubility problems, and 3) a homogeneous product to facilitate approval by regulatory agencies. In conventional ADCs, the drug molecules are chemically attached randomly to antibody surface residues (typically Lys or Cys), which can interfere with epitope binding and targeting, and lead to overall product heterogeneity, long-term colloidal instability and unfavorable pharmacokinetics. Here, we present a more controlled process for generating ADCs where drug is specifically conjugated to only Fab

Indexed as

ImmunoconjugatesPolysaccharidesAntibodies, MonoclonalCetuximabEpitopesHumansTrastuzumabAntibodies, MonoclonalCetuximabEpitopesImmunoconjugatesPolysaccharidesTrastuzumabActinobacillusantibodycetuximabdrug conjugateFab glycansialyltransferasetrastuzumab

Identifiers

PMID36447399
PMCPMC9715014
OpenAlexW4310573307

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.