Evidence map›Paper›PMID 29787234›Full record

ReviewACS chemical biology2018

Unfolding the Mysteries of Protein Metamorphosis.

Acacia F Dishman, Brian F Volkman

Abstract readReview
In one paragraph

Review in ACS chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing 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

57 citing papers in PubMed.

  1. Shining light on the dark proteome with unstructural biology.Current research in structural biology · 2026
    Article
  2. Fold-Switching Proteins.Annual review of biophysics · 2026
    Review
  3. Article
  4. Article
  5. Mapping the energy landscape of a fold-switching protein MAD2.Protein science : a publication of the Protein Society · 2025
    Article
  6. Article
  7. Residue Interactions Guide Translational Diffusion of Proteins.The journal of physical chemistry. B · 2025
    Article
  8. Seesaw protein: Design of a protein that adopts interconvertible alternative functional conformations and its dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Review
  11. Article
  12. Skyrmion engineering with origami.Scientific reports · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Fluid protein fold space and its implications.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  18. Article
  19. Metamorphic protein folding as evolutionary adaptation.Trends in biochemical sciences · 2023
    Review
  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.

Acacia F DishmanDepartment of Biochemistry , Medical College of Wisconsin , Milwaukee , Wisconsin 53226 , United States.
Brian F VolkmanDepartment of Biochemistry , Medical College of Wisconsin , Milwaukee , Wisconsin 53226 , United States.ORCID 0000-0002-6681-5179

Funding

Medical Scientist Training ProgramT32GM080202 · NIGMS · MEDICAL COLLEGE OF WISCONSIN · PI BARBIERI, JOSEPH T, SALZMAN, NITA H · 2010 to 2024
$5.7M
Structural Basis for Chemokine FunctionR01AI058072 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI VOLKMAN, BRIAN F · 2004 to 2019
$4.1M
Structural Basis for Chemokine FunctionR37AI058072 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI Brian F Volkman · 2020 to 2026
$2.8M
Structural and energetic origins of metamorphic protein foldingR56AI103225 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI VOLKMAN, BRIAN F · 2013 to 2013
$353k
Structure-Function Investigation of Chemokine-GPCR Signaling in Tumor Progression and MetastasisF30CA236182 · NCI · MEDICAL COLLEGE OF WISCONSIN · PI DISHMAN, ACACIA F · 2019 to 2023
$242k
NCI NIH HHS F30 CA236182NIAID NIH HHS R01 AI058072NIAID NIH HHS R37 AI058072NIAID NIH HHS R56 AI103225NIGMS NIH HHS T32 GM080202
6 · The paper itself

Abstract

Since the proposal of Anfinsen's thermodynamic hypothesis in 1963, our understanding of protein folding and dynamics has gained significant appreciation of its nuance and complexity. Intrinsically disordered proteins, chameleonic sequences, morpheeins, and metamorphic proteins have broadened the protein folding paradigm. Here, we discuss noncanonical protein folding patterns, with an emphasis on metamorphic proteins, and we review known metamorphic proteins that occur naturally and that have been engineered in the laboratory. Finally, we discuss research areas surrounding metamorphic proteins that are primed for future exploration, including evolution, drug discovery, and the quest for previously unrecognized metamorphs. As we enter an age where we are capable of complex bioinformatic searches and de novo protein design, we are primed to search for previously unrecognized metamorphic proteins and to design our own metamorphs to act as targeted, switchable drugs; biosensors; and more.

Indexed as

Protein FoldingAnimalsBacteriaHumansIntrinsically Disordered ProteinsProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein EngineeringProtein UnfoldingIntrinsically Disordered Proteins

Identifiers

PMID29787234
PMCPMC6007232

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.