Results 51 to 60 of about 3,959 (198)
PthA2 inhibits the PPIase activity of CsCyp.
, 2013 (A) The PPIase activity of recombinant CsCyp protein was evaluated by the α-chymotrypsin-coupled assay. Enzyme activity was measured immediately after the addition of α-chymotrypsin and the substrate into the reaction mixture.
Bruna Medeia de Campos (315139) +4 more
core +1 more source
Table_1_Update on the Neisseria Macrophage Infectivity Potentiator-Like PPIase Protein.xlsx
, 2022 Neisseria pathogens express a Macrophage Infectivity Potentiator Protein (MIP), which belongs to the FK506 binding protein (FKBP) family of proteins that exhibit peptidyl-prolyl cis/trans isomerase (PPIase) activity.
Myron Christodoulides (142926)
core +1 more source
PpiD is a player in the network of periplasmic chaperones in
BMC Microbiology, 2010 Background The inner membrane-anchored periplasmic folding factor PpiD is described as a parvulin-like peptidyl prolyl isomerase (PPIase) that assists in the maturation of the major beta-barrel outer membrane proteins (OMPs) of Escherichia coli.
Behrens-Kneip Susanne +2 more
doaj +1 more source
Table_2_Update on the Neisseria Macrophage Infectivity Potentiator-Like PPIase Protein.docx
, 2022 Neisseria pathogens express a Macrophage Infectivity Potentiator Protein (MIP), which belongs to the FK506 binding protein (FKBP) family of proteins that exhibit peptidyl-prolyl cis/trans isomerase (PPIase) activity.
Myron Christodoulides (142926)
core +1 more source
Image_2_Update on the Neisseria Macrophage Infectivity Potentiator-Like PPIase Protein.tif
, 2022 Neisseria pathogens express a Macrophage Infectivity Potentiator Protein (MIP), which belongs to the FK506 binding protein (FKBP) family of proteins that exhibit peptidyl-prolyl cis/trans isomerase (PPIase) activity.
Myron Christodoulides (142926)
core +1 more source
Molecular docking analysis of juglone with parvulin-type PPiase PrsA from Staphylococcus aureus
Bioinformation, 2023 Staphylococcus aureus is an opportunistic pathogen that causes variety of infections range from mild skin diseases to life-threatening sepsis. It is also notorious for acquiring resistance to numerous antibiotics. Parvulin-type peptidyl-prolyl cis-trans isomerase (PPiase) domain containing PrsA protein is considered as an essential folding factor for ...
Dipten, Laskar +2 more
openaire +2 more sources
Abnormal type I collagen post-translational modification and crosslinking in a cyclophilin B KO mouse model of recessive osteogenesis imperfecta. [PDF]
PLoS Genetics, 2014 Cyclophilin B (CyPB), encoded by PPIB, is an ER-resident peptidyl-prolyl cis-trans isomerase (PPIase) that functions independently and as a component of the collagen prolyl 3-hydroxylation complex.
Wayne A Cabral +14 more
doaj +1 more source
Components of SurA required for outer membrane biogenesis in uropathogenic Escherichia coli.
PLoS ONE, 2008 BackgroundSurA is a periplasmic peptidyl-prolyl isomerase (PPIase) and chaperone of Escherichia coli and other Gram-negative bacteria. In contrast to other PPIases, SurA appears to have a distinct role in chaperoning newly synthesized porins destined for
Kristin M Watts, David A Hunstad
doaj +1 more source
Frontiers in Microbiology, 2022 Brucella spp. are the etiological agent of animal and human brucellosis. We have reported previously that cyclophilins of Brucella (CypA and CypB) are upregulated within the intraphagosomal replicative niche and required for stress adaptation and host ...
Emanuel J. Muruaga +5 more
doaj +1 more source