Evidence map›Paper›PMID 28472066›Full record

ArticlePloS one2017

Connecting high-temperature and low-temperature protein stability and aggregation.

Mónica Rosa, Christopher J Roberts, Miguel A Rodrigues

Abstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Immobilization of Phospholipase D on FeMolecules (Basel, Switzerland) · 2025
    Article
  7. Article
  8. International journal of molecular sciences · 2024
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. ATR-FTIR Biosensors for Antibody Detection and Analysis.International journal of molecular sciences · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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.

Mónica RosaCentro de Química Estrutural, Department of Chemical Engineering, Instituto Superior Técnico, Universidade de Lisboa, Lisboa, Portugal.
Christopher J RobertsDepartment of Chemical & Biomolecular Engineering, University of Delaware, Newark, Delaware, United States of America.
Miguel A RodriguesCentro de Química Estrutural, Department of Chemical Engineering, Instituto Superior Técnico, Universidade de Lisboa, Lisboa, Portugal.ORCID http://orcid.org/0000-0001-9841-441X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein aggregation is a long-standing problem for preservation of proteins in both laboratory settings and for commercial biotechnology products. It is well established that heating (cooling) can accelerate (slow) aggregation by populating (depopulating) unfolded or partially unfolded monomer states that are key intermediates in aggregation processes. However, there is a long-standing question of whether the same mechanism(s) that lead to aggregation under high-temperature stress are relevant for low-temperature stress such as in refrigerated or supercooled liquids. This report shows the first direct comparison of "hot" and "cold" aggregation kinetics and folding/unfolding thermodynamics, using bovine hemoglobin as a model system. The results suggest that the same mechanism for non-native aggregation holds from "hot" to "cold" temperatures, with an aggregation temperature-of-maximum-stability slightly below 0°C. This highlights that sub-zero temperatures can induce cold-mediated aggregation, even in the absence of freezing stresses. From a practical perspective, the results suggests the possibility that cold-stress may be a useful alternative to heat-stress for extrapolating predictions of protein shelf life at refrigerated conditions, as well as providing a foundation for more mechanistic studies of cold-stress conditions in future work. A comparison between isochoric and isobaric methods is also briefly discussed.

Indexed as

Cold TemperatureHot TemperatureProtein StabilityAnimalsCattleChromatography, GelThermodynamics

Identifiers

PMID28472066
PMCPMC5417562

What OpenQuestion holds

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Registered trials

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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.