Results 131 to 140 of about 3,214 (169)

The role of the FKBP51-Hsp90 complex in Alzheimer's disease: An emerging new drug target. [PDF]

Cell Stress Chaperones
Jeanne X, Török Z, Vigh L, Prodromou C.   +3 more
europepmc   +1 more source

The mechanisms of Pin1 as targets for cancer therapy. [PDF]

Front Immunol
Liu C, Dan L, Li Q, Bajinka O, Yuan X.
europepmc   +1 more source

Effects of a Protease Inhibitor Camostat Mesilate on Gut Microbial Function in Patients with Irritable Bowel Syndrome: A Pilot Randomized Placebo-Controlled Study.

Digestion
Kanazawa M, Miyamoto K, Kano M, Inooka K, Oka K, Takahashi M, Mano N, Fukudo S.   +7 more
europepmc   +1 more source

IN SILICO ANALYSIS OF PIN4, PARVULIN TYPE PPIASE FROM SOIL AMOEBA (DICTYOSTELIUM DISCOIDEUM)

openaire   +3 more sources

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The β-subunit of pea stem mitochondrial ATP synthase exhibits PPiase activity

Mitochondrion, 2003
A soluble protein with a molecular mass of 55 kDa has been purified from etiolated pea stem mitochondria. The protein exhibits a Mg2+-requiring PPiase activity, with an optimum at pH 9.0, which is not stimulated by monovalent cations, but inhibited by F-, Ca2+, aminomethylenediphosphate and imidodiphosphate.
Andrea Urbani, Angelo Vianello, Marco Zancani   +2 more
exaly   +7 more sources

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

Journal 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.
David Westhead, David Brockwell, Julia Humes   +2 more
exaly   +5 more sources

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

Infection 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.
Michael Steinert, Mathias Müsken, JOSÉ Manuel Borrero De Acuna   +2 more
exaly   +5 more sources

Archaeal peptidyl prolyl cis-trans isomerases (PPIases)

Frontiers in Bioscience, 2000
PPIases are ubiquitous in living organisms. While 3 families of PPIases, cyclophilin (CyP), FK506 binding protein (FKBP) and parvulin (Pvn), have been studied in detail in Eukarya and Bacteria (eubacteria), little is known about archaeal PPIases. Among 2 cyclophilins found in Archaea, only Halobacterium cyclophilin (HcCyP19) has been characterized.
T, Maruyama, M, Furutani
openaire   +2 more sources

PPIase is associated with the diversity of conotoxins from cone snail venom glands

Biochimie, 2015
Cone snails are incredibly rich sources of bioactive conopeptides with potential for use in neuroscience research and novel drug development. In order to investigate the synthesis of diversified conopeptides in venom glands, the proteome and peptidome profiles of conus venom were analyzed using HPLC and mass spectrometry.
Anlong Xu, Yuanyuan Qiang, Shangwu Chen   +2 more
exaly   +3 more sources

Identification and characterization of peptides that bind the PPIase domain of Parvulin17

Journal of Peptide Science, 2013
Peptidyl‐prolyl cis‐trans isomerases (PPIases) are the enzymes that increase the rate of isomerization of the peptide bond N‐terminal to the proline substrate. Par14 and its isoform Par17 belong to the Parvulin family of PPIases. Par14 can bind AT‐rich double‐stranded DNA and was shown to be part of the pre‐ribosomal ribonucleoprotein (pre‐rRNP ...
Elfaki, Imadeldin, Knitsch, Andre, Matena, Anja, Bayer, Peter   +3 more
openaire   +3 more sources