scholarly journals Factor Xa subsite mapping by proteome-derived peptide libraries improved using WebPICS, a resource for proteomic identification of cleavage sites

2011 ◽  
Vol 392 (11) ◽  
Author(s):  
Oliver Schilling ◽  
Ulrich auf dem Keller ◽  
Christopher M. Overall
Keyword(s):  
Factor Xa ◽  
Site Specificity ◽  
Cleavage Sites ◽  
Web Based ◽  
Protease Cleavage ◽  
Proteomic Approach ◽  
Site Selectivity ◽  
User Access ◽  
Proteomic Identification ◽  
Subsite Mapping

Abstract Proteomic identification of protease cleavage site specificity (PICS) is a recent proteomic approach for the easy mapping of protease subsite preferences that determines both the prime- and non-prime side specificity concurrently. Here we greatly facilitate user access by providing an automated and simple web-based data-analysis resource termed WebPics (http://clipserve.clip.ubc.ca/pics/). We demonstrate the utility of WebPics analysis of PICS data by determining the substrate specificity of factor Xa from P6-P6’, an important blood coagulation protease that proteolytically generates thrombin from prothrombin. PICS confirms existing data on non-prime site specificity and refines our knowledge of factor Xa prime-site selectivity.

Family-wide characterization of matrix metalloproteinases from Arabidopsis thaliana reveals their distinct proteolytic activity and cleavage site specificity

2013 ◽  
Vol 457 (2) ◽  
pp. 335-346 ◽  
Author(s):  
Giada Marino ◽  
Pitter F. Huesgen ◽  
Ulrich Eckhard ◽  
Christopher M. Overall ◽  
Wolfgang P. Schröder ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Cleavage Site ◽  
Biochemical Properties ◽  
Site Specificity ◽  
Sequence Specificity ◽  
Cleavage Sites ◽  
Protease Cleavage ◽  
Protease Cleavage Sites ◽  
Proteomic Identification

The five recombinant MMP-like proteins of Arabidopsis thaliana have specific biochemical properties. Detailed analysis of their sequence specificity using proteomic identification of protease cleavage sites revealed cleavage profiles similar to human MMPs.

Proteomic Identification of Protease Cleavage Sites Characterizes Prime and Non-prime Specificity of Cysteine Cathepsins B, L, and S

2011 ◽  
Vol 10 (12) ◽  
pp. 5363-5373 ◽  
Author(s):  
Martin L. Biniossek ◽  
Dorit K. Nägler ◽  
Christoph Becker-Pauly ◽  
Oliver Schilling
Keyword(s):  
Cleavage Sites ◽  
Protease Cleavage ◽  
Cysteine Cathepsins ◽  
Protease Cleavage Sites ◽  
Proteomic Identification

scholarly journals A novel HIV vaccine targeting the protease cleavage sites

2017 ◽  
Vol 14 (1) ◽  
Author(s):  
Hongzhao Li ◽  
Robert W. Omange ◽  
Francis A. Plummer ◽  
Ma Luo
Keyword(s):  
Hiv Vaccine ◽  
Cleavage Sites ◽  
Protease Cleavage ◽  
Protease Cleavage Sites

scholarly journals Evaluating the Performance of Novel JWT Revocation Strategy

2021 ◽  
Author(s):  
László Viktor Jánoky ◽  
Péter Ekler ◽  
János Levendovszky
Keyword(s):  
Access Control ◽  
Real World ◽  
Mathematical Framework ◽  
Web Based ◽  
Novel Approach ◽  
User Access ◽  
Digital Signing

JSON Web Tokens (JWT) provide a scalable, distributed way of user access control for modern web-based systems. The main advantage of the scheme is that the tokens are valid by themselves – through the use of digital signing – also imply its greatest weakness. Once issued, there is no trivial way to revoke a JWT token. In our work, we present a novel approach for this revocation problem, overcoming some of the problems of currently used solutions. To compare our solution to the established solutions, we also introduce the mathematical framework of comparison, which we ultimately test using real-world measurements.

Sign in / Sign up

Export Citation Format

Share Document