Identification of essential acidic residues of outer membrane protease OmpT supports a novel active site-Reference-Cited by-同舟云学术

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Identification of essential acidic residues of outer membrane protease OmpT supports a novel active site

Published:2001-09-21 Issue:3 Volume:505 Page:426-430
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Kramer R.Arjen,Vandeputte-Rutten Lucy,de Roon Gerard Jan,Gros Piet,Dekker Niek,Egmond Maarten R.

Publisher

Wiley

Subject

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

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(01)02863-0/fullpdf

Reference33 articles.

1. Purification, characterization, and primary structure of Escherichia coli protease VII with specificity for paired basic residues: identity of protease VII and OmpT

2. Complete nucleotide sequence and deduced amino acid sequence of theompT gene ofEscherichia coliK-12

3. [27] Omptin: An Escherichia coli outer membrane proteinase that activates plasminogen

4. In vitro folding, purification and characterization of Escherichia coli outer membrane protease OmpT

5. Substrate Specificity of the Integral Membrane Protease OmpT Determined by Spatially Addressed Peptide Libraries

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1. Protamine cleavage specificity of the avian pathogen Escherichia coli OmpT reveals two substrate-binding sites related to virulence;Frontiers in Veterinary Science;2024-09-05

2. Dynamic topology-mediated maturation of β-barrel proteins in BAM-catalyzed folding;2023-11-07

3. E. coli outer membrane protein T (OmpT) nanopore for peptide sensing;Biochemical and Biophysical Research Communications;2023-10

4. Molecular Insights into Substrate Binding of the Outer Membrane Enzyme OmpT;Catalysts;2023-01-17

5. Physiology and structure of pathogenic Escherichia coli pOmpT reveal two substrate-binding sites;2022-06-17

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