Evidence map›Paper›PMID 22274989›Full record

ReviewProtein science : a publication of the Protein Society2012

Fluorine: a new element in protein design.

Benjamin C Buer, E Neil G Marsh

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Perfluorocarbons in Chemical Biology.Chembiochem : a European journal of chemical biology · 2020
    Review
  11. Article
  12. Article
  13. Synthesis and Diels-Alder Reactivity of 4-Fluoro-4-Methyl-4International journal of molecular sciences · 2020
    Article
  14. 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

2 authors.

Benjamin C BuerDepartment of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA.
E Neil G Marsh

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluorocarbons are quintessentially man-made molecules, fluorine being all but absent from biology. Perfluorinated molecules exhibit novel physicochemical properties that include extreme chemical inertness, thermal stability, and an unusual propensity for phase segregation. The question we and others have sought to answer is to what extent can these properties be engineered into proteins? Here, we review recent studies in which proteins have been designed that incorporate highly fluorinated analogs of hydrophobic amino acids with the aim of creating proteins with novel chemical and biological properties. Fluorination seems to be a general and effective strategy to enhance the stability of proteins, both soluble and membrane bound, against chemical and thermal denaturation, although retaining structure and biological activity. Most studies have focused on small proteins that can be produced by peptide synthesis as synthesis of large proteins containing specifically fluorinated residues remains challenging. However, the development of various biosynthetic methods for introducing noncanonical amino acids into proteins promises to expand the utility of fluorinated amino acids in protein design.

Indexed as

HalogenationAmino AcidsChemical PhenomenaChemistry Techniques, SyntheticFluorineFluorocarbonsHydrophobic and Hydrophilic InteractionsModels, MolecularProtein EngineeringProtein FoldingProtein Interaction MappingProteinsProtein StabilitySolubilityThermodynamicsAmino AcidsFluorineFluorocarbonsProteins

Identifiers

PMID22274989
PMCPMC3375745

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.