Evidence map›Paper›PMID 34611867›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Cell Free Remodeling of Glycosylation of Antibodies.

Letícia Martins Mota, Venkata S Tayi, Michael Butler

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

3 authors.

Letícia Martins MotaCell Technology Group, National Institute for Bioprocessing, Research and Training (NIBRT), Dublin, Ireland.
Venkata S TayiDepartment of Microbiology, University of Manitoba, Winnipeg, Canada.
Michael ButlerNational Institute for Bioprocessing, Research and Training (NIBRT), Dublin, Ireland. Michael.butler@nibrt.ie.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The N-glycosylation profile of a monoclonal antibody (mAb) is a critical quality attribute in relation to its therapeutic application. The control of this profile during biomanufacture is difficult because of the multiple parameters that affect the glycosylation metabolism within the cell and the environment in which the cell is grown. One of the approaches that can be used to produce a preferred glycan profile or a single glycoform is through chemoenzymatic remodeling during the isolation of a mAb. Here we describe protocols that can be utilized to produce preferred glycoforms that include galactosylated, agalactosylated, or sialylated glycoforms following isolation of a mAb. Methods for analysis and assignment of structures of the samples following glycoengineering are also described. Chemoenzymatic modeling of mAb glycans has the potential for scale-up and to be introduced into biomanufacturing of mAbs with higher specific therapeutic activities.

Indexed as

Antibodies, MonoclonalGlycosylationPolysaccharidesAntibodies, MonoclonalPolysaccharides2-Aminobenzamide (2-AB)CHO cellGalactosylationGlycanGlycoengineeringGlycosylationHILIC-HPLCMonoclonal antibody (mAb)N-glycansPNGase FProtein-ASialylation

Identifiers

PMID34611867

What OpenQuestion holds

Textmetadata
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.