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Beyond protein folding: The pleiotropic functions of PPIases in cellular processes and microbial virulence

Biochimica et Biophysica Acta (BBA) - General Subjects
Peptidyl prolyl cis/trans isomerases (PPIases), a ubiquitously distributed superfamily of enzymes, associated with signal transduction, trafficking, assembly, biofilm formation, stress tolerance, cell cycle regulation, gene expression and tissue regeneration, is a key regulator of metabolic disorders and microbial virulence.
Roopshali, Rakshit   +4 more
openaire   +2 more sources

The PPIase Active Site of Legionella pneumophila Mip Protein Is Involved in the Infection of Eukaryotic Host Cells

Biological Chemistry, 2003
We analysed eight monoclonal antibodies (mAbs) directed against the Mip (macrophage infectivity potentiator) protein, a virulence factor of the intracellular pathogen Legionella pneumophila. Mip belongs to the FK506-binding proteins (FKBPs) and exhibits peptidyl prolyl cis/trans isomerase (PPIase) activity. Five of the mAbs recognised epitopes in the C-
Jürgen H, Helbig   +10 more
openaire   +2 more sources

PPIase

2018
openaire   +1 more source

PPIase Pin1

2018
openaire   +1 more source

Gene cloning and characterization of thermostable peptidyl prolyl cis-trans isomerase (PPIase) from Bacillus stearothermophilus SIC1

Journal of Bioscience and Bioengineering, 1995
Masahiro Takagi   +2 more
exaly  

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