Evidence map›Paper›PMID 21540645›Full record

ArticlemAbs

Conformational stability and aggregation of therapeutic monoclonal antibodies studied with ANS and Thioflavin T binding.

Veysel Kayser, Naresh Chennamsetty, Vladimir Voynov, Bernhard Helk, Bernhardt L Trout

Abstract 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 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

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  17. Evaluation of fluorescent dyes to measure protein aggregation within mammalian cell culture supernatants.Journal of chemical technology and biotechnology (Oxford, Oxfordshire : 1986) · 2018
    Article
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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

5 authors.

Veysel KayserChemical Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA.
Naresh Chennamsetty
Vladimir Voynov
Bernhard Helk
Bernhardt L Trout

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Characterization of aggregation profiles of monoclonal antibodies (mAb) is gaining importance because an increasing number of mAb-based therapeutics are entering clinical studies and gaining marketing approval. To develop a successful formulation, it is imperative to identify the critical biochemical properties of each potential mAb drug candidate. We investigated the conformational change and aggregation of a human IgG1 using external dye-binding experiments with fluorescence spectroscopy and compared the aggregation profiles obtained to the results of size-exclusion chromatography. We show that using an appropriate dye at selected mAb concentration, unfolding or aggregation can be studied. In addition, dye-binding experiments may be used as conventional assays to study therapeutic mAb stability.

Indexed as

Antibodies, MonoclonalBenzothiazolesChromatography, GelDrug StabilityFluorescent DyesHumansProtein ConformationProtein FoldingProtein StabilitySpectrometry, FluorescenceTemperatureThiazolesAntibodies, MonoclonalBenzothiazolesFluorescent DyesThiazolesthioflavin T

Identifiers

PMID21540645
PMCPMC3218538

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.