Results 31 to 40 of about 7,127 (231)
Scientific Reports, 2023 Penicillium species are an industrially important group of fungi. Cyclophilins are ubiquitous proteins and several members of this family exhibit peptidyl-prolyl cis–trans isomerase (PPIase) activity.
Mangaljeet Singh +6 more
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Scientific Reports, 2021 Peptidyl-prolyl cis–trans isomerases (PPIases) are the only class of enzymes capable of cis–trans isomerization of the prolyl peptide bond. The PPIases, comprising of different families viz., cyclophilins, FK506-binding proteins (FKBPs), parvulins and ...
Mangaljeet Singh +9 more
doaj +1 more source
The PPIase Activity of CypB Is Essential for the Activation of Both AKT/mTOR and XBP1s Signaling Pathways during the Differentiation of 3T3-L1 Preadipocytes [PDF]
NutrientsWonchae Choe, Insug Kang, kyung-sik
exaly +2 more sources
Characterization of Peptidyl-Prolyl Cis-Trans Isomerase- and Calmodulin-Binding Activity of a Cytosolic Arabidopsis thaliana Cyclophilin AtCyp19-3. [PDF]
PLoS ONE, 2015 Cyclophilins, which bind to immunosuppressant cyclosporin A (CsA), are ubiquitous proteins and constitute a multigene family in higher organisms. Several members of this family are reported to catalyze cis-trans isomerisation of the peptidyl-prolyl bond,
Gundeep Kaur +10 more
doaj +1 more source
Cyclophilin-A is bound to through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex [PDF]
, 2004 Although cyclophilin A (CyP-A) is a relatively abundant small immunophilin present in the cytoplasm of all mammalian cells, its general function(s) in the absence of the immunosuppressant drug cyclosporin A is not known.
Galigniana, Mario Daniel +3 more
core +2 more sources
International Journal of Molecular Sciences, 2020 Consistent with a role in catalyzing rate-limiting step of protein folding, removal of genes encoding cytoplasmic protein folding catalysts belonging to the family of peptidyl-prolyl cis/trans isomerases (PPIs) in Escherichia coli confers conditional ...
P. Wojtkiewicz +5 more
semanticscholar +1 more source
Peptidyl-Proline Isomerases (PPIases): Targets for Natural Products and Natural Product-Inspired Compounds. [PDF]
Journal of medicinal chemistry, 2016 Peptidyl-proline isomerases (PPIases) are a chaperone superfamily comprising the FK506-binding proteins (FKBPs), cyclophilins, and parvulins. PPIases catalyze the cis/trans isomerization of proline, acting as a regulatory switch during folding, activation, and/or degradation of many proteins.
Dunyak, Bryan M, Gestwicki, Jason E
openaire +4 more sources
Hsp90-binding immunophilins link p53 to dynein during p53 transport to the nucleus [PDF]
, 2004 The tumor suppressor protein p53 is known to be transported to the nucleus along microtubular tracks by cytoplasmic dynein. However, the connection between p53 and the dynein motor protein complex has not been established.
Galigniana, Mario Daniel +4 more
core +1 more source
PPIases Par14/Par17 Affect HBV Replication in Multiple Ways
Viruses, 2023 Human parvulin 14 (Par14) and parvulin 17 (Par17) are peptidyl-prolyl cis/trans isomerases that upregulate hepatitis B virus (HBV) replication by binding to the conserved 133Arg-Pro134 (RP) motif of HBc and core particles, and 19RP20-28RP29 motifs of HBx. In the absence of HBx, Par14/Par17 have no effect on HBV replication. Interaction with Par14/Par17
openaire +3 more sources
mBio, 2013 SurA is a component of the periplasmic chaperone network that plays a central role in biogenesis of integral outer membrane β-barrel proteins (OMPs) in Escherichia coli.
Dante P. Ricci +3 more
doaj +1 more source