Cyclophilin D reduces Ca2+ sequestration by complement 1q binding protein. [PDF]
Adegbite O +4 more
europepmc +1 more source
Pin1 WW Domain Ligand Library Synthesized with an Easy Solid-Phase Phosphorylating Reagent. [PDF]
Chen XR +5 more
europepmc +1 more source
A novel bivalent interaction mode underlies a non-catalytic mechanism for Pin1-mediated protein kinase C regulation. [PDF]
Chen XR +6 more
europepmc +1 more source
The role of the FKBP51-Hsp90 complex in Alzheimer's disease: An emerging new drug target. [PDF]
Jeanne X +3 more
europepmc +1 more source
IN SILICO ANALYSIS OF PIN4, PARVULIN TYPE PPIASE FROM SOIL AMOEBA (DICTYOSTELIUM DISCOIDEUM)
openaire +3 more sources
The Role of SurA PPIase Domains in Preventing Aggregation of the Outer-Membrane Proteins tOmpA and OmpT [PDF]
SurA is a conserved ATP-independent periplasmic chaperone involved in the biogenesis of outer-membrane proteins (OMPs). Escherichia coli SurA has a core domain and two peptidylprolyl isomerase (PPIase) domains, the role(s) of which remain unresolved.
Julia R Humes +2 more
exaly +7 more sources
The peptidyl-prolyl- cis/trans -isomerase (PPIase) macrophage infectivity potentiator (Mip) contributes to the pathogenicity and fitness of L. pneumophila , the causative agent of Legionnaires’ disease.
Mustafa Safa Karagöz +2 more
exaly +6 more sources
Human CyP33 binds specifically to mRNA and binding stimulates PPIase activity of hCyP33 [PDF]
Human nuclear cyclophilin 33 (hCyP33) was the first protein which was found to contain an RNA‐binding motif and a PPIase domain. It was not known what cellular and physiological roles are played by the RNA‐binding activity as well as the PPIase activity of hCyP33.
Wang, Ying +6 more
exaly +4 more sources
Crystal Structure of the PP2A Phosphatase Activator: Implications for Its PP2A-Specific PPIase Activity [PDF]
PTPA, an essential and specific activator of protein phosphatase 2A (PP2A), functions as a peptidyl prolyl isomerase (PPIase). We present here the crystal structures of human PTPA and of the two yeast orthologs (Ypa1 and Ypa2), revealing an all alpha-helical protein fold that is radically different from other PPIases.
Nicolas Leulliot +2 more
exaly +5 more sources

