ArticleBiomacromolecules2012
A tunable and reversible platform for the intracellular formation of genetically engineered protein microdomains.
Article in Biomacromolecules, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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Who cites it
23 citing papers in PubMed, 35 citations in OpenAlex.
- Optogenetic Translocation to Subcellular Compartments through Regulation of Protein Avidity.ACS synthetic biology · 2026Article
- A Thermogenetic Tool Employing Elastin-like Polypeptides for Controlling Programmed Cell Death.ACS nano · 2025Article
- Article
- Programmability and biomedical utility of intrinsically-disordered protein polymers.Advanced drug delivery reviews · 2024Review
- Extremely Sensitive Genetically Encoded Temperature Indicator Enabling Measurement at the Organelle Level.ACS sensors · 2024Article
- Multiplexed dynamic control of temperature to probe and observe mammalian cells.bioRxiv : the preprint server for biology · 2024Article
- A highly-sensitive genetically encoded temperature indicator exploiting a temperature-responsive elastin-like polypeptide.Scientific reports · 2021Article
- De novo engineering of intracellular condensates using artificial disordered proteins.Nature chemistry · 2020Article
- Human Granulocyte-Macrophage Colony-Stimulating Factor Fused to Elastin-Like Polypeptides Assembles Biologically-Active Nanoparticles.Bioconjugate chemistry · 2020Article
- Caveolin elastin-like polypeptide fusions mediate temperature-dependent assembly of caveolar microdomains.ACS biomaterials science & engineering · 2020Article
- A new temperature-dependent strategy to modulate the epidermal growth factor receptor.Biomaterials · 2018Article
- Tunable assembly of protein-microdomains in living vertebrate embryos.Advanced biosystems · 2018Article
- Convergence of Artificial Protein Polymers and Intrinsically Disordered Proteins.Biochemistry · 2018Article
- Elastin-like polypeptide switches: A design strategy to detect multimeric proteins.Protein science : a publication of the Protein Society · 2017Article
- Elastin-like polypeptides: Therapeutic applications for an emerging class of nanomedicines.Journal of controlled release : official journal of the Controlled Release Society · 2016Review
- An amphipathic alpha-helical peptide from apolipoprotein A1 stabilizes protein polymer vesicles.Journal of controlled release : official journal of the Controlled Release Society · 2014Article
- Controlled release from recombinant polymers.Journal of controlled release : official journal of the Controlled Release Society · 2014Review
- Flipping the Switch on Clathrin-Mediated Endocytosis using Thermally Responsive Protein Microdomains.Advanced functional materials · 2014Article
- Triggered sorting and co-assembly of genetically engineered protein microdomains in the cytoplasm.Advanced materials (Deerfield Beach, Fla.) · 2014Article
- Genetically engineered nanocarriers for drug delivery.International journal of nanomedicine · 2014Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
From mitochondria to the nuclear envelope, the controlled assembly of micro- and nanostructures is essential for life; however, the level at which we can deliberately engineer the assembly of microstructures within intracellular environments remains primitive. To overcome this obstacle, we present a platform to reversibly assemble genetically engineered protein microdomains (GEPMs) on the time scale of minutes within living cells. Biologically inspired from the human protein tropoelastin, these protein polymers form a secondary aqueous phase above a tunable transition temperature. This assembly process is easily manipulated to occur at or near physiological temperature by adjusting molecular weight and hydrophobicity. We fused protein polymers to green fluorescent protein (GFP) to visualize their behavior within the cytoplasm. While soluble, these polymers have a similar intracellular diffusion constant as cytosolic proteins at 7.4 μm(2)/s; however, above their phase transition temperature, the proteins form distinct microdomains (0.1-2 μm) with a reduced diffusion coefficient of 1.1 μm(2)/s. Microdomain assembly and disassembly are both rapid processes with half-lives of 3.8 and 1.0 min, respectively. Via selection of the protein polymer, the assembly temperature is tunable between 20 and 40 °C. This approach may be useful to control intracellular formation of genetically engineered proteins and protein complexes into concentrated microdomains.
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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.