Results 161 to 170 of about 3,959 (198)

Cyclophilin D reduces Ca2+ sequestration by complement 1q binding protein. [PDF]

open access: yesBiochem J
Adegbite O   +4 more
europepmc   +1 more source

Pin1 WW Domain Ligand Library Synthesized with an Easy Solid-Phase Phosphorylating Reagent. [PDF]

open access: yesBiochemistry
Chen XR   +5 more
europepmc   +1 more source

The Role of SurA PPIase Domains in Preventing Aggregation of the Outer-Membrane Proteins tOmpA and OmpT [PDF]

open access: yesJournal of Molecular Biology, 2019
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

Legionella pneumophila PPIase Mip Interacts with the Bacterial Proteins SspB, Lpc2061, and FlaA and Promotes Flagellation

open access: yesInfection and Immunity, 2022
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]

open access: yesFEBS Letters, 2008
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]

open access: yesMolecular Cell, 2006
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

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