Literature DB >> 22934808

Yersinia pestis and approaches to targeting its outer protein H protein-tyrosine phosphatase (YopH).

M Bahta1, T R Burke.   

Abstract

Plague is an infectious disease with a high mortality rate that has repeatedly impacted human society. It remains a threat in many parts of the world today. Plague is caused by the bacterium, Yersinia pestis (Y. pestis), which has as one of its required virulence factors, the protein-tyrosine phosphatase, YopH. Therefore, YopH represents a potential target for the treatment of Y. pestis infection. Recent recognition of Y. pestis as a possible bioterrorism agent and the fact that it is still the cause of endemic disease around the world make it an important object of study and heighten the need for new anti-plague agents. The current review covers aspects of plague and its historical occurrence and summarizes approaches to developing YopH inhibitors.

Entities:  

Mesh:

Substances:

Year:  2012        PMID: 22934808     DOI: 10.2174/092986712803988866

Source DB:  PubMed          Journal:  Curr Med Chem        ISSN: 0929-8673            Impact factor:   4.530


  5 in total

1.  High-resolution crystal structures of the D1 and D2 domains of protein tyrosine phosphatase epsilon for structure-based drug design.

Authors:  George T Lountos; Sreejith Raran-Kurussi; Bryan M Zhao; Beverly K Dyas; Terrence R Burke; Robert G Ulrich; David S Waugh
Journal:  Acta Crystallogr D Struct Biol       Date:  2018-10-02       Impact factor: 7.652

Review 2.  Yersinia pestis: mechanisms of entry into and resistance to the host cell.

Authors:  Yuehua Ke; Zeliang Chen; Ruifu Yang
Journal:  Front Cell Infect Microbiol       Date:  2013-12-24       Impact factor: 5.293

3.  Redox process is crucial for inhibitory properties of aurintricarboxylic acid against activity of YopH: virulence factor of Yersinia pestis.

Authors:  Alicja Kuban-Jankowska; Kamlesh K Sahu; Pawel Niedzialkowski; Magdalena Gorska; Jack A Tuszynski; Tadeusz Ossowski; Michal Wozniak
Journal:  Oncotarget       Date:  2015-07-30

4.  Aurintricarboxylic acid structure modifications lead to reduction of inhibitory properties against virulence factor YopH and higher cytotoxicity.

Authors:  Alicja Kuban-Jankowska; Kamlesh K Sahu; Magdalena Gorska; Pawel Niedzialkowski; Jack A Tuszynski; Tadeusz Ossowski; Michal Wozniak
Journal:  World J Microbiol Biotechnol       Date:  2016-08-25       Impact factor: 3.312

5.  Chicoric acid binds to two sites and decreases the activity of the YopH bacterial virulence factor.

Authors:  Alicja Kuban-Jankowska; Kamlesh K Sahu; Magdalena Gorska; Jack A Tuszynski; Michal Wozniak
Journal:  Oncotarget       Date:  2016-01-19
  5 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.