Evidence map›Paper›PMID 42750698›Full record

ReviewiScience2026

Shape-shifting proteins and the subtlety in their form and function.

Prakash Kulkarni, Supriyo Bhattacharya, Atish Mohanty, Sravani Ramisetty, Evan Pisick, John Orban, Vladimir Uversky, Keith Weninger, Sui Huang, Tsui-Fen Chou and 2 more

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in iScience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

12 authors.

Prakash KulkarniDepartment of Medical Oncology, City of Hope Medical Center, Duarte, CA, USA.
Supriyo BhattacharyaDepartment of Computational and Quantitative Medicine, Beckman Research Institute, City of Hope National Medical Center, Duarte, CA 91010-3000, USA.
Atish MohantyDepartment of Medical Oncology, City of Hope Medical Center, Duarte, CA, USA.
Sravani RamisettyDepartment of Medical Oncology, City of Hope Medical Center, Duarte, CA, USA.
Evan PisickCity of Hope Chicago, 2520 Elisha Avenue, Zion, IL 60099, USA.
John OrbanW. M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, MD, USA.
Vladimir UverskyDepartment of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL, USA.
Keith WeningerDepartment of Physics, North Carolina State University, Raleigh, NC 27695, USA.
Sui HuangInstitute for Systems Biology, Seattle, WA, USA.
Tsui-Fen ChouDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA, USA.
Paul W SternbergDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA, USA.
Ravi SalgiaDepartment of Medical Oncology, City of Hope Medical Center, Duarte, CA, USA.

Funding

Transgenic Mouse FacilityP30CA033572 · NCI · CITY OF HOPE/BECKMAN RESEARCH INSTITUTE · PI John Charles Williams · 1985 to 2026
$86.3M
NCI NIH HHS P30 CA033572
6 · The paper itself

Abstract

Shape-shifting proteins include intrinsically disordered proteins (IDPs) and fold-switching, or metamorphic proteins. They make up a significant fraction of the "dark proteome" in the protein universe. In this essay, we highlight some often misconceived or underappreciated features of shape-shifting proteins: First, the subtlety of the structure of IDPs; second, the relationship between intrinsic disorder and allostery, third, the possibility of discerning IDP conformational preferences based on energy landscape theory, and fourth, the contributions of disordered regions to fold switching in metamorphic proteins. Lastly, we highlight emerging evidence that fold-switching/metamorphic proteins may contribute to phenotypic plasticity and adaptive evolution by acting as evolutionary capacitors.

Indexed as

allosteryconformational dynamicsdark proteomeenergy landscapeintrinsically disordered Proteinsshapeshifting proteins

Identifiers

PMID42750698
PMCPMC13577884

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.