Evidence for a large dispensable segment in the subtilisin-like catalytic domain of the Lactococcus lactis cell-envelope proteinas-Reference-Cited by-同舟云学术

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Evidence for a large dispensable segment in the subtilisin-like catalytic domain of the Lactococcus lactis cell-envelope proteinas

Published:1994 Issue:8 Volume:7 Page:991-996
ISSN:1741-0126
Container-title:"Protein Engineering, Design and Selection"
language:en
Short-container-title:Protein Eng Des Sel

Author:

Bruinenberg Paul G.,Doesburg Paul,Alting Arno C.,Exterkate Fred A.,Vos Willem M.de,Siezen Roland J.

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/7/8/991/4391590/7-8-991.pdf

Cited by 28 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

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2. Comparative Structure Analysis of the Multi-Domain, Cell Envelope Proteases of Lactic Acid Bacteria;Microorganisms;2023-09-08

3. Auto- and Hetero-Catalytic Processing of the N-Terminal Propeptide Promotes the C-Terminal Fibronectin Type III Domain-Mediated Dimerization of a Thermostable Vpr-like Protease;Applied and Environmental Microbiology;2022-11-08

4. Exosite binding modulates the specificity of the immunomodulatory enzyme ScpA, a C5a inactivating bacterial protease;Computational and Structural Biotechnology Journal;2022

5. Enzyme kinetic and binding studies identify determinants of specificity for the immunomodulatory enzyme ScpA, a C5a inactivating bacterial protease;Computational and Structural Biotechnology Journal;2021

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