Evidence map›Paper›PMID 17325008›Full record

ArticleBiophysical journal2007

Fluorescence microscopy evidence for quasi-permanent attachment of antifreeze proteins to ice surfaces.

Natalya Pertaya, Christopher B Marshall, Carlos L DiPrinzio, Larry Wilen, Erik S Thomson, J S Wettlaufer, Peter L Davies, Ido Braslavsky

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2007. 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
7.3field-weighted citation impact, top 3% 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

28 citing papers in PubMed, 119 citations in OpenAlex.

  1. On the engulfment of antifreeze proteins by ice.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Extended Temperature Range of the Ice-Binding Protein Activity.Langmuir : the ACS journal of surfaces and colloids · 2024
    Article
  3. Divergent Mechanisms of Ice Growth Inhibition by Antifreeze Proteins.Methods in molecular biology (Clifton, N.J.) · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Peptidic Antifreeze Materials: Prospects and Challenges.International journal of molecular sciences · 2019
    Review
  10. Review
  11. Article
  12. Article
  13. Putting life on ice: bacteria that bind to frozen water.Journal of the Royal Society, Interface · 2016
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Microfluidic experiments reveal that antifreeze proteins bound to ice crystals suffice to prevent their growth.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

8 authors at 3 institutions in 2 countries.

Natalya PertayaDepartment of Physics and Astronomy, Ohio University, Athens, Ohio, USA.
Christopher B Marshall
Carlos L DiPrinzio
Larry Wilen
Erik S Thomson
J S Wettlaufer
Peter L Davies
Ido Braslavsky
Ohio University · USQueen's University · CAYale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many organisms are protected from freezing by the presence of extracellular antifreeze proteins (AFPs), which bind to ice, modify its morphology, and prevent its further growth. These proteins have a wide range of applications including cryopreservation, frost protection, and as models in biomineralization research. However, understanding their mechanism of action remains an outstanding challenge. While the prevailing adsorption-inhibition hypothesis argues that AFPs must bind irreversibly to ice to arrest its growth, other theories suggest that there is exchange between the bound surface proteins and the free proteins in solution. By conjugating green fluorescence protein (GFP) to a fish AFP (Type III), we observed the binding of the AFP to ice. This was accomplished by monitoring the presence of GFP-AFP on the surface of ice crystals several microns in diameter using fluorescence microscopy. The lack of recovery of fluorescence after photobleaching of the GFP component of the surface-bound GFP-AFP shows that there is no equilibrium surface-solution exchange of GFP-AFP and thus supports the adsorption-inhibition mechanism for this type of AFP. Moreover, our study establishes the utility of fluorescently labeled AFPs as a research tool for investigating the mechanisms underlying the activity of this diverse group of proteins.

Indexed as

IceModels, ChemicalModels, MolecularAdsorptionAntifreeze ProteinsBinding SitesComputer SimulationMicroscopy, FluorescenceProtein BindingSurface PropertiesAntifreeze ProteinsIce

Identifiers

PMID17325008
PMCPMC1853139
OpenAlexW2100218311

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.