Results 41 to 50 of about 3,959 (198)
Table_1_Distribution of Peptidyl-Prolyl Isomerase (PPIase) in the Archaea.XLSX
, 2021 Cis-trans isomerization of the peptide bond prior to proline is an intrinsically slow process but plays an essential role in protein folding. In vivo cis-trans isomerization reaction is catalyzed by Peptidyl-prolyl isomerase (PPIases), a category of ...
Anchal (11534377) +2 more
core +1 more source
Mutational effects of Cys113 on structural dynamics of Pin1
Biophysics and Physicobiology, 2019 Pin1 is a peptidyl-prolyl isomerase (PPIase) which catalyzes cis/trans isomerization of pS/pT-P bond. Its activity is related to various cellular functions including suppression of Alzheimer’s disease. A cysteine residue C113 is known to be important for
Teikichi Ikura +2 more
doaj +1 more source
Table_8_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
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
Table_6_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
BMC Plant Biology, 2019 Background Cyclophilins (CYPs), belonging to the peptidyl prolyl cis/trans isomerase (PPIase) superfamily, play important roles during plant responses to biotic and abiotic stresses.
Jun Yang +8 more
doaj +1 more source
Image_3_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
Pin1 modulates the type 1 immune response. [PDF]
PLoS ONE, 2007 BACKGROUND/ABSTRACT: Immune responses initiated by T cell receptor (TCR) and costimulatory molecule mediated signaling culminate in maximal cytokine mRNA production and stability.
Stephane Esnault +7 more
doaj +1 more source
Table_5_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
Table_7_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