Functional analysis of the propeptides of subtilisin E and aqualysin I as intramolecular chaperones-Reference-Cited by-同舟云学术

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Functional analysis of the propeptides of subtilisin E and aqualysin I as intramolecular chaperones

Published:2001-11-14 Issue:2 Volume:508 Page:210-214
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Takagi Hiroshi,Koga Mihoko,Katsurada Saori,Yabuta Yukihiro,Shinde Ujwal,Inouye Masayori,Nakamori Shigeru

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(01)03053-8/fullpdf

Reference37 articles.

1. Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process

2. Protein memory through altered folding mediated by intramolecular chaperones

3. The αlytic protease pro-region does not require a physical linkage to activate the protease domain in vivo

4. A protein-folding reaction under kinetic control

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1. Microbial proteases and their applications;Frontiers in Microbiology;2023-09-14

2. Maturation of subtilisin-like protease NbSLP1 from microsporidia Nosema bombycis;Frontiers in Cellular and Infection Microbiology;2022-08-15

3. Enhanced activity of Rhizomucor miehei lipase by directed saturation mutation of the propeptide;Enzyme and Microbial Technology;2021-10

4. Progress in Microbial Degradation of Feather Waste;Frontiers in Microbiology;2019-12-05

5. Combining Pro-peptide Engineering and Multisite Saturation Mutagenesis To Improve the Catalytic Potential of Keratinase;ACS Synthetic Biology;2019-01-22

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