Selective Immobilization of Fusion Proteins on Poly(hydroxyalkanoate) Microbeads

2005 ◽  
Vol 77 (17) ◽  
pp. 5755-5759 ◽  
Author(s):  
Seok Jae Lee ◽  
Jong Pil Park ◽  
Tae Jung Park ◽  
Sang Yup Lee ◽  
Seongnam Lee ◽  
...  
Keyword(s):  
Fusion Proteins ◽  
Selective Immobilization

Covalent and Selective Immobilization of Fusion Proteins

2003 ◽  
Vol 125 (26) ◽  
pp. 7810-7811 ◽  
Author(s):  
Maik Kindermann ◽  
Nathalie George ◽  
Nils Johnsson ◽  
Kai Johnsson
Keyword(s):  
Fusion Proteins ◽  
Selective Immobilization

Covalent and selective immobilization of GST fusion proteins with fluorophosphonate-based probes

2018 ◽  
Vol 54 (37) ◽  
pp. 4661-4664 ◽  
Author(s):  
Xiafeng Wang ◽  
Tianlin Guo ◽  
Jiahui Chen ◽  
Xiaofeng Li ◽  
Yiqing Zhou ◽  
...  
Keyword(s):  
Fusion Proteins ◽  
Solid Support ◽  
Selective Immobilization ◽  
Gst Fusion Proteins

Fluorophosphonate probes covalently immobilize proteins onto solid support by reacting with tyrosine 111 in the GST tag.

Identification of common and distinct epigenetic re-programming properties of Core-Binding Factor (CBF) Fusion Proteins

2016 ◽  
Vol 228 (03) ◽  
Author(s):  
J Loke ◽  
A Ptasinska ◽  
MR Imperato ◽  
SA Assi ◽  
P Cauchy ◽  
...  
Keyword(s):  
Fusion Proteins ◽  
Core Binding Factor ◽  
Binding Factor

Fusion proteins CDGM and 4CDGM enhance B cell proliferation

2017 ◽  
Vol 2 (2) ◽  
Author(s):  
Shiqiang Lu ◽  
Xiaoyi Lu ◽  
Zehua Sun
Keyword(s):  
Cell Proliferation ◽  
B Cell ◽  
Fusion Proteins

Self-Assembling Micelles Based on an Intrinsically Disordered Protein Domain

2018 ◽  
Author(s):  
Sarah Klass ◽  
Matthew J. Smith ◽  
Tahoe Fiala ◽  
Jessica Lee ◽  
Anthony Omole ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Fusion Proteins ◽  
Organic Molecules ◽  
Intrinsically Disordered Protein ◽  
Protein Domain ◽  
Enzymatic Cleavage ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Self Assembling ◽  
Protein Tag

Herein, we describe a new series of fusion proteins that have been developed to self-assemble spontaneously into stable micelles that are 27 nm in diameter after enzymatic cleavage of a solubilizing protein tag. The sequences of the proteins are based on a human intrinsically disordered protein, which has been appended with a hydrophobic segment. The micelles were found to form across a broad range of pH, ionic strength, and temperature conditions, with critical micelle concentration (CMC) values below 1 µM being observed in some cases. The reported micelles were found to solubilize hydrophobic metal complexes and organic molecules, suggesting their potential suitability for catalysis and drug delivery applications.

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