ReviewChemistry (Weinheim an der Bergstrasse, Germany)2012
Protein conformational switches: from nature to design.
Review in Chemistry (Weinheim an der Bergstrasse, Germany), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers, 1 of them a synthesis that pooled 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.
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.
Who cites it
56 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Identifying and profiling structural similarities between Spike of SARS-CoV-2 and other viral or host proteins with Machaon.Communications biology · 2023Pooled it
- Zeolites and Zeolite-Based Materials at the Biointerface: From Haemostasis and Biomolecule Separation to Theranostic Applications.Molecules (Basel, Switzerland) · 2026Review
- Affinity-Activated Protein Switches for Modular and Signal-ON Detection of Small Molecules.Analytical chemistry · 2026Article
- ConforFold recovers alternative protein conformations beyond MSA subsampling.Protein science : a publication of the Protein Society · 2026Article
- Disentangling coevolutionary constraints for modeling protein conformational heterogeneity.Communications chemistry · 2026Article
- A comprehensive benchmarking of the AlphaFold3 for predicting biomacromolecules and their interactions.Briefings in bioinformatics · 2025Article
- Elastic analysis bridges structure and dynamics of an AAA+ molecular motor.PLoS computational biology · 2025Article
- Programmable Host-Guest Recognition for Shape-Shifting Supramolecular Nanostructure States.ACS nano · 2025Article
- Molecular Modelling in Bioactive Peptide Discovery and Characterisation.Biomolecules · 2025Review
- Aromatic-aromatic interactions drive fold switch of GA95 and GB95 with three residue difference.Chemical science · 2025Article
- In Silico Investigation of Phytochemicals From Clinically Tested Herbal Extracts as Potential Dihydrofolate Reductase Inhibitors for Buruli Ulcer.BioMed research international · 2025Article
- Neutron spin echo shows pHLIP is capable of retarding membrane thickness fluctuations.Biochimica et biophysica acta. Biomembranes · 2024Article
- Structure prediction of alternative protein conformations.Nature communications · 2024Article
- Conformation-Dependent Hydrogen-Bonding Interactions in a Switchable Artificial Metalloprotein.Biochemistry · 2024Article
- Designed allosteric protein logic.Cell discovery · 2024Article
- The interaction networks of small rubber particle proteins in the latex ofFrontiers in plant science · 2024Article
- Non-Covalent Interactions Enforce Conformation in Switchable and Water-Soluble Diketopiperazine-Pyridine Foldamers.Angewandte Chemie (International ed. in English) · 2023Article
- Design of stimulus-responsive two-state hinge proteins.Science (New York, N.Y.) · 2023Article
- Strategies for Conditional Regulation of Proteins.JACS Au · 2023Review
- Design and characterization of a protein fold switching network.Nature communications · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Protein conformational switches alter their shape upon receiving an input signal, such as ligand binding, chemical modification, or change in environment. The apparent simplicity of this transformation--which can be carried out by a molecule as small as a thousand atoms or so--belies its critical importance to the life of the cell as well as its capacity for engineering by humans. In the realm of molecular switches, proteins are unique because they are capable of performing a variety of biological functions. Switchable proteins are therefore of high interest to the fields of biology, biotechnology, and medicine. These molecules are beginning to be exploited as the core machinery behind a new generation of biosensors, functionally regulated enzymes, and "smart" biomaterials that react to their surroundings. As inspirations for these designs, researchers continue to analyze existing examples of allosteric proteins. Recent years have also witnessed the development of new methodologies for introducing conformational change into proteins that previously had none. Herein we review examples of both natural and engineered protein switches in the context of four basic modes of conformational change: rigid-body domain movement, limited structural rearrangement, global fold switching, and folding-unfolding. Our purpose is to highlight examples that can potentially serve as platforms for the design of custom switches. Accordingly, we focus on inducible conformational changes that are substantial enough to produce a functional response (e.g., in a second protein to which it is fused), yet are relatively simple, structurally well-characterized, and amenable to protein engineering efforts.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.