Literature DB >> 24136711

Triggered sorting and co-assembly of genetically engineered protein microdomains in the cytoplasm.

Pu Shi1, Yi-An Lin, Martha Pastuszka, Honggang Cui, J Andrew Mackay.   

Abstract

Elastin-like polypeptides (ELPs) are genetically encoded protein polymers that reversibly phase separate in response to stimuli. They respond sharply to small shifts in temperature and form dense microdomains in the living eukaryotic cytosol. For the first time, this communication illustrates how to tune the ELP sequence and architecture for either co-assembly or sorting of distinct proteins into microdomains within a living cell.
© 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Entities:  

Keywords:  confocal microscopy; elastin-like polypeptides; intracellular sorting; macromolecular assembly; protein polymer

Mesh：

Substances：

Year:  2013        PMID： 24136711      PMCID： PMC3947098          DOI： 10.1002/adma.201303356

Source DB:  PubMed          Journal:  Adv Mater        ISSN： 0935-9648            Impact factor:   30.849


  17 in total

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6.  Design and cellular internalization of genetically engineered polypeptide nanoparticles displaying adenovirus knob domain.

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Review 7.  Intracellular sorting and transport of proteins.

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Authors:  Martha K Pastuszka; Siti M Janib; Isaac Weitzhandler; Curtis T Okamoto; Sarah Hamm-Alvarez; J Andrew Mackay
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10.  Kinetic quantification of protein polymer nanoparticles using non-invasive imaging.

Authors:  S M Janib; S Liu; R Park; M K Pastuszka; P Shi; A S Moses; M M Orosco; Y-A Lin; H Cui; P S Conti; Z Li; J A MacKay
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4.  Single-Cell Quantification of the Transition Temperature of Intracellular Elastin-like Polypeptides.

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