Evidence map›Paper›PMID 35651816›Full record

ArticleFrontiers in molecular biosciences2022

Measuring Protein Aggregation and Stability Using High-Throughput Biophysical Approaches.

Tristan O C Kwan, Stefan A Kolek, Amy E Danson, Rosana I Reis, Ines S Camacho, Patrick D Shaw Stewart, Isabel Moraes

Abstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Fluorescence-Based Protein Stability Monitoring-A Review.International journal of molecular sciences · 2024
    Review
  6. Article
  7. 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

7 authors.

Tristan O C KwanNational Physical Laboratory, Teddington, United Kingdom.
Stefan A KolekDouglas Instruments Ltd., Hungerford, United Kingdom.
Amy E DansonNational Physical Laboratory, Teddington, United Kingdom.
Rosana I ReisNational Physical Laboratory, Teddington, United Kingdom.
Ines S CamachoNational Physical Laboratory, Teddington, United Kingdom.
Patrick D Shaw StewartDouglas Instruments Ltd., Hungerford, United Kingdom.
Isabel MoraesNational Physical Laboratory, Teddington, United Kingdom.

Funding

Wellcome Trust
6 · The paper itself

Abstract

Structure-function relationships of biological macromolecules, in particular proteins, provide crucial insights for fundamental biochemistry, medical research and early drug discovery. However, production of recombinant proteins, either for structure determination, functional studies, or to be used as biopharmaceutical products, is often hampered by their instability and propensity to aggregate in solution

Indexed as

CDcryo-EMcrystallographyDLSdrug discoveryDSFhigh-throughputprotein aggregation

Identifiers

PMID35651816
PMCPMC9149252

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.