再び折り畳む、リフォールディングする
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English Journal
- Efficient production of a correctly folded mouse α-defensin, cryptdin-4, by refolding during inclusion body solubilization.
- Tomisawa S1, Sato Y1, Kamiya M1, Kumaki Y1, Kikukawa T1, Kawano K1, Demura M1, Nakamura K2, Ayabe T2, Aizawa T3.
- Protein expression and purification.Protein Expr Purif.2015 Aug;112:21-8. doi: 10.1016/j.pep.2015.04.007. Epub 2015 Apr 23.
- Mammalian α-defensins contribute to innate immunity by exerting antimicrobial activity against various pathogens. To perform structural and functional analysis of α-defensins, large amounts of α-defensins are essential. Although many expression systems for the production of recombinant α-defensi
- PMID 25913370
- Atomistic mechanism of polyphenol amyloid aggregation inhibitors: molecular dynamics study of Curcumin, Exifone, and Myricetin interaction with the segment of tau peptide oligomer.
- Berhanu WM1, Masunov AE.
- Journal of biomolecular structure & dynamics.J Biomol Struct Dyn.2015 Jul;33(7):1399-411. doi: 10.1080/07391102.2014.951689. Epub 2014 Sep 9.
- Amyloid fibrils are highly ordered protein aggregates associated with many diseases affecting millions of people worldwide. Polyphenols such as Curcumin, Exifone, and Myricetin exhibit modest inhibition toward fibril formation of tau peptide which is associated with Alzheimer's disease. However, the
- PMID 25093402
- Coronavirus and influenza virus proteolytic priming takes place in tetraspanin-enriched membrane microdomains.
- Earnest JT1, Hantak MP1, Park JE1, Gallagher T2.
- Journal of virology.J Virol.2015 Jun 1;89(11):6093-104. doi: 10.1128/JVI.00543-15. Epub 2015 Apr 1.
- Coronaviruses (CoVs) and low-pathogenicity influenza A viruses (LP IAVs) depend on target cell proteases to cleave their viral glycoproteins and prime them for virus-cell membrane fusion. Several proteases cluster into tetraspanin-enriched microdomains (TEMs), suggesting that TEMs are preferred viru
- PMID 25833045
Japanese Journal
- A New Method to Evaluate the Unfolding Activity of Chaperone Unit ClpA Based on Fe–S Cluster Disruption
- Ohgita Takashi,Okuno Takashi,Hama Susumu,Tsuchiya Hiroyuki,Kogure Kentaro
- CHEMICAL & PHARMACEUTICAL BULLETIN 59(5), 657-661, 2011
- … ATP-dependent proteases unfold their substrates and then refold (via chaperone activity) or degrade (via protease activity) them. …
- NAID 130000648883
- Bacterial Expression, Refolding, Functional Characterization, and Mass Spectrometric Identification of Full-Length Human PPAR-γ
- LI Wei,YUAN Yonghua,LUO Zongwei,ZHENG Xiaohong,ZHAO Ling,DUAN Wen,YU Yu
- Bioscience, biotechnology, and biochemistry 74(6), 1173-1180, 2010-06-23
- … A simplified refolding setup, capable of gradual buffer exchange and continuous protein feeding, was used to refold the denatured PPAR-γ with approximately 66% yield. …
- NAID 10027556025
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再折りたたみ、リフォールディング
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