Results 31 to 40 of about 3,214 (169)

Cyclohexyl ketone inhibitors of Pin1 dock in a trans-diaxial cyclohexane conformation. [PDF]

open access: yesPLoS ONE, 2012
Cyclohexyl ketone substrate analogue inhibitors (Ac-pSer-Ψ[C = OCH]-Pip-tryptamine) of Pin1, the cell cycle regulatory peptidyl-prolyl isomerase (PPIase), were designed and synthesized as potential electrophilic acceptors for the Pin1 active site Cys113 ...
Guoyan G Xu   +2 more
doaj   +1 more source

Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex [PDF]

open access: yesNature Communications, 2018
AbstractThe molecular chaperone Hsp90 is critical for the maintenance of cellular homeostasis and represents a promising drug target. Despite increasing knowledge on the structure of Hsp90, the molecular basis of substrate recognition and pro-folding by Hsp90/co-chaperone complexes remains unknown.
Javier Oroz   +13 more
openaire   +9 more sources

Flanking N- and C-terminal domains of PrsA in Streptococcus suis type 2 are crucial for inducing cell death independent of TLR2 recognition

open access: yesVirulence, 2023
Streptococcus suis type 2 (SS2), a major emerging/re-emerging zoonotic pathogen found in humans and pigs, can cause severe clinical infections, and pose public health issues.
Xiaowu Jiang   +6 more
doaj   +1 more source

Mutational effects of Cys113 on structural dynamics of Pin1

open access: yesBiophysics 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

PpiA, a Surface PPIase of the Cyclophilin Family in Lactococcus lactis

open access: yesPLoS ONE, 2012
Protein folding in the envelope is a crucial limiting step of protein export and secretion. In order to better understand this process in Lactococcus lactis, a lactic acid bacterium, genes encoding putative exported folding factors like Peptidyl Prolyl Isomerases (PPIases) were searched for in lactococcal genomes.In L.
Trémillon, Nicolas   +10 more
openaire   +7 more sources

PPIases Par14/Par17 Affect HBV Replication in Multiple Ways

open access: yesViruses, 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

Genome-wide identification of cyclophilin genes in Gossypium hirsutum and functional characterization of a CYP with antifungal activity against Verticillium dahliae

open access: yesBMC 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

Pin1 modulates the type 1 immune response. [PDF]

open access: yesPLoS 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

Identification of RNA targets for the nuclear multidomain cyclophilin atCyp59 and their effect on PPIase activity [PDF]

open access: yesNucleic Acids Research, 2012
AtCyp59 is a multidomain cyclophilin containing a peptidyl-prolyl cis/trans isomerase (PPIase) domain and an evolutionarily highly conserved RRM domain. Deregulation of this class of cyclophilins has been shown to affect transcription and to influence phosphorylation of the C-terminal repeat domain of the largest subunit of the RNA polymerase II.
Bannikova, Olga   +5 more
openaire   +2 more sources

PpiD is a player in the network of periplasmic chaperones in Escherichia coli

open access: yesBMC Microbiology, 2010
Background The inner membrane-anchored periplasmic folding factor PpiD is described as a parvulin-like peptidyl prolyl isomerase (PPIase) that assists in the maturation of the major beta-barrel outer membrane proteins (OMPs) of Escherichia coli.
Behrens-Kneip Susanne   +2 more
doaj   +1 more source

Home - About - Disclaimer - Privacy