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170 (0,06s)

Project

Investigation of the mechanism of membrane translocation of the adenylate cyclase toxin (IAA5020907)

The adenylate cyclase toxin (ACT) paralyses a variety of cells by uncontrolled synthesis of cAMP. Penetration of ACT into cells is a rather iniwue example by fluorescence spectroscopy and immunodetection, using our set of a...

CE - Biochemie

  • 1999 - 2003
  • 7 321 tis. Kč
  • 4 975 tis. Kč
  • AV ČR
Project

Nature and role(s) of the posttranslational modification(s) required for activities of an RTX toxin the adenylate cyclase toxin of bordetella pertussis (GA310/95/1048)

EE - Mikrobiologie, virologie

  • 1995 - 1997
  • 1 030 tis. Kč
  • 1 030 tis. Kč
  • GA ČR
Project

Role of the pore-forming activity in adenylate cyclase toxin action and Bordetella virulence (GAP302/12/0460)

The adenylate cyclase toxin-hemolysin (CyaA) is a multifunctional RTX protein playing a key role in virulence of pathogenic Bordetella. It translocates an adenylate cyclase enzyme into cytosol of host phag...

CE - Biochemie

  • 2012 - 2016
  • 15 307 tis. Kč
  • 15 307 tis. Kč
  • GA ČR
Project

Molecular mechanisms of membrane interaction and translocation of adenylate cyclase toxin from Bordetella pertussis (GA15-09157S)

The multifunctional adenylate cyclase toxin (CyaA) is a key virulence factor of Bordetella pertussis that causes a highly contagious respiratory disease called pertussis or whooping cough. CyaA is a fusion of an N-terminal ...

CE - Biochemie

  • 2015 - 2017
  • 5 994 tis. Kč
  • 5 994 tis. Kč
  • GA ČR
Project

Molecular mechanism of adenylate cyclase toxin penetration into phagocytes (IAA500200914)

We propose to investigate the mechanistic details of adenylate cyclase toxin (CyaA) penetration across cellular membrane of myeloid phagocytes. Structural of CyaA in phagocyte membrane and the kinetics and role in toxin...

EB - Genetika a molekulární biologie

  • 2009 - 2013
  • 7 666 tis. Kč
  • 7 666 tis. Kč
  • AV ČR
Project

Deciphering the role of acylated domain in the membrane penetration of Bordetella pertussis adenylate cyclase toxin (GA19-04607S)

The adenylate cyclase toxin-hemolysin (CyaA) plays a key role in virulence of the whooping cough agent Bordetella pertussis. CyaA translocates an AC enzyme into cytosol of CD11b+ phagocytes and subverts their bactericidal f...

Microbiology

  • 2019 - 2021
  • 9 821 tis. Kč
  • 9 821 tis. Kč
  • GA ČR
Project

Targeted drug design for bioterrorism prevention. Development of effective inhibitors of the adenylate cyclase toxin of Bordetella pertusis and Bacillus anthracis. (VG20102015046)

inhibitorsof the adenylate cyclase toxin of Bordetella pertusis and Bacillus anthracis...

CC - Organická chemie

  • 2010 - 2015
  • 41 350 tis. Kč
  • 41 345 tis. Kč
  • MV
Project

Interaction of adenylate cyclase toxin with complement receptor 3 (GAP302/11/0580)

The adenylate cyclase toxin (CyaA) is a key virulence factor of the whooping cough agent Bordetella pertussis that binds host myeloid phagocytic cells through the beta-2 integrin CD11b/CD18 (complement receptor 3). The mech...

EB - Genetika a molekulární biologie

  • 2011 - 2015
  • 12 958 tis. Kč
  • 12 958 tis. Kč
  • GA ČR
Project

Study of the interaction of adenylate cyclase toxin with the integrin receptor CD11b/CD18 (GP204/07/P105)

Adenylate cyclase toxin (ACT) is a key virulence factor of the whooping cough agent Bordetella pertussis. Due to its unique ability to penetrate into target cells by both direct translocation and receptor-mediated endocytos...

EB - Genetika a molekulární biologie

  • 2007 - 2009
  • 1 389 tis. Kč
  • 1 389 tis. Kč
  • GA ČR
Project

Investigation of mechanism of membrane translocation of the adenylate cyclase toxin (IAA5020611)

The adenylate cyclase toxin (ACT) is a key virulence factor of the whooping cough pathogen Bordetella pertussis. ACT exhibits several unique features dedicated translocation machinery other than the toxin itself. U...

EB - Genetika a molekulární biologie

  • 1996 - 1998
  • 1 826 tis. Kč
  • 1 571 tis. Kč
  • AV ČR
  • 1 - 10 out of 170