Evidence map›Paper›PMID 24174400›Full record

ReviewThe AAPS journal2014

High-throughput biophysical analysis of protein therapeutics to examine interrelationships between aggregate formation and conformational stability.

Rajoshi Chaudhuri, Yuan Cheng, C Russell Middaugh, David B Volkin

Abstract readReview
In one paragraph

Review in The AAPS journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

38 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Article
  3. Assessment of Recombinant β-Propeller Phytase of theJournal of fungi (Basel, Switzerland) · 2025
    Article
  4. Article
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  6. Protein Stability: Enhancement and Measurement.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
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  8. Review
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  13. Toward Drug-Like Multispecific Antibodies by Design.International journal of molecular sciences · 2020
    Review
  14. Article
  15. 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

4 authors at 1 institution in 1 country.

Rajoshi ChaudhuriDepartment of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, Lawrence, Kansas, 66047, USA.
Yuan Cheng
C Russell Middaugh
David B Volkin
University of Kansas · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Stabilization and formulation of therapeutic proteins against physical instability, both structural alterations and aggregation, is particularly challenging not only due to each protein's unique physicochemical characteristics but also their susceptibility to the surrounding milieu (pH, ionic strength, excipients, etc.) as well as various environmental stresses (temperature, agitation, lyophilization, etc.). The use of high-throughput techniques can significantly aid in the evaluation of stabilizing solution conditions by permitting a more rapid evaluation of a large matrix of possible combinations. In this mini-review, we discuss both key physical degradation pathways observed for protein-based drugs and the utility of various high-throughput biophysical techniques to aid in protein formulation development to minimize their occurrence. We then focus on four illustrative case studies with therapeutic protein candidates of varying sizes, shapes and physicochemical properties to explore different analytical challenges in monitoring protein physical instability. These include an IgG2 monoclonal antibody, an albumin-fusion protein, a recombinant pentameric plasma glycoprotein, and an antibody fragment (Fab). Future challenges and opportunities to improve and apply high-throughput approaches to protein formulation development are also discussed.

Indexed as

Chemistry Techniques, AnalyticalDrug StabilityProtein StabilityProtein ConformationProteinsProteins

Identifiers

PMID24174400
PMCPMC3889527
OpenAlexW2032556503

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.