Insight into the aggregation of lipase from Pseudomonas sp. using mutagenesis: protection of aggregation prone region by adoption of α-helix structure-Reference-Cited by-同舟云学术

Insight into the aggregation of lipase from Pseudomonas sp. using mutagenesis: protection of aggregation prone region by adoption of α-helix structure

Published:2018-11-01 Issue:11 Volume:31 Page:419-426
ISSN:1741-0126
Container-title:Protein Engineering, Design and Selection
language:en
Short-container-title:

Author:

Rashno Fatemeh¹,Khajeh Khosro¹,Dabirmanesh Bahareh¹,Sajedi Reza H¹,Chiti Fabrizio²

Affiliation:

1. Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran

2. Department of Biomedical, Experimental and Clinical Sciences, Section of Biochemistry, University of Florence, Viale Morgagni 50, Florence, Italy

Funder

Tarbiat Modares University

Iran’s National Elites Foundation

University of Florence

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/31/11/419/28667359/gzz003.pdf

Reference41 articles.

1. Breaking the amyloidogenicity code: Methods to predict amyloids from amino acid sequence

2. Efficient refolding of recombinant lipase from Escherichia coli inclusion bodies by response surface methodology

3. High-level expression of lipase in Escherichia coli and recovery of active recombinant enzyme through in vitro refolding

4. Prediction of amyloid aggregation in vivo

5. Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase

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