Evidence map›Paper›PMID 25436502›Full record

ArticlePloS one2014

Coupled protein diffusion and folding in the cell.

Minghao Guo, Hannah Gelman, Martin Gruebele

Abstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Enzymes in a human cytoplasm model organize into submetabolon complexes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Review
  5. Threading single proteins through pores to compare their energy landscapes.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Review
  7. Review
  8. Proteins: "Boil 'Em, Mash 'Em, Stick 'Em in a Stew".The journal of physical chemistry. B · 2019
    Review
  9. Review
  10. Inhibitory Receptor Diffusion Dynamics.Frontiers in molecular neuroscience · 2019
    Article
  11. Article
  12. Article
  13. Article
  14. Weak protein-protein interactions in live cells are quantified by cell-volume modulation.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Article
  16. Fast-folding proteins under stress.Cellular and molecular life sciences : CMLS · 2015
    Review
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.

Minghao GuoDepartment of Physics, University of Illinois, Urbana, IL, United States of America.
Hannah GelmanDepartment of Physics, University of Illinois, Urbana, IL, United States of America.
Martin GruebeleDepartment of Physics, University of Illinois, Urbana, IL, United States of America; Department of Chemistry and Center for Biophysics and Computational Biology, University of Illinois, Urbana, IL, United States of America.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

When a protein unfolds in the cell, its diffusion coefficient is affected by its increased hydrodynamic radius and by interactions of exposed hydrophobic residues with the cytoplasmic matrix, including chaperones. We characterize protein diffusion by photobleaching whole cells at a single point, and imaging the concentration change of fluorescent-labeled protein throughout the cell as a function of time. As a folded reference protein we use green fluorescent protein. The resulting region-dependent anomalous diffusion is well characterized by 2-D or 3-D diffusion equations coupled to a clustering algorithm that accounts for position-dependent diffusion. Then we study diffusion of a destabilized mutant of the enzyme phosphoglycerate kinase (PGK) and of its stable control inside the cell. Unlike the green fluorescent protein control's diffusion coefficient, PGK's diffusion coefficient is a non-monotonic function of temperature, signaling 'sticking' of the protein in the cytosol as it begins to unfold. The temperature-dependent increase and subsequent decrease of the PGK diffusion coefficient in the cytosol is greater than a simple size-scaling model suggests. Chaperone binding of the unfolding protein inside the cell is one plausible candidate for even slower diffusion of PGK, and we test the plausibility of this hypothesis experimentally, although we do not rule out other candidates.

Indexed as

Models, MolecularProtein FoldingCell Line, TumorCytosolDiffusionEnzyme StabilityHSP70 Heat-Shock ProteinsHumansMutationPhosphoglycerate KinaseProtein ConformationHSP70 Heat-Shock ProteinsPhosphoglycerate Kinase

Identifiers

PMID25436502
PMCPMC4249841

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.