Results 31 to 40 of about 3,959 (198)

Genome-wide characterization of peptidyl-prolyl  cis–trans  isomerases in Penicillium and their regulation by salt stress in a halotolerant P. oxalicum

open access: yesScientific Reports, 2021
Peptidyl-prolyl cis–trans isomerases (PPIases) are the only class of enzymes capable of cis–trans isomerization of the prolyl peptide bond. The PPIases, comprising of different families viz., cyclophilins, FK506-binding proteins (FKBPs), parvulins and ...
Mangaljeet Singh   +9 more
doaj   +1 more source

Molecular and Biochemical Characterization of the Parvulin-Type PPIases in Lotus japonicus         [PDF]

open access: yesPlant Physiology, 2009
Abstract The cis/trans isomerization of the peptide bond preceding proline is an intrinsically slow process, although important in many biological processes in both prokaryotes and eukaryotes. In vivo, this isomerization is catalyzed by peptidyl-prolyl cis/trans-isomerases (PPIases).
Kouri, Evangelia D.   +8 more
openaire   +4 more sources

Data_Sheet_1_Distribution of Peptidyl-Prolyl Isomerase (PPIase) in the Archaea.docx

open access: yes, 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

Characterization of Peptidyl-Prolyl Cis-Trans Isomerase- and Calmodulin-Binding Activity of a Cytosolic Arabidopsis thaliana Cyclophilin AtCyp19-3. [PDF]

open access: yesPLoS ONE, 2015
Cyclophilins, which bind to immunosuppressant cyclosporin A (CsA), are ubiquitous proteins and constitute a multigene family in higher organisms. Several members of this family are reported to catalyze cis-trans isomerisation of the peptidyl-prolyl bond,
Gundeep Kaur   +10 more
doaj   +1 more source

The Activity and Specificity of the Outer Membrane Protein Chaperone SurA Are Modulated by a Proline Isomerase Domain

open access: yesmBio, 2013
SurA is a component of the periplasmic chaperone network that plays a central role in biogenesis of integral outer membrane β-barrel proteins (OMPs) in Escherichia coli.
Dante P. Ricci   +3 more
doaj   +1 more source

Cyclophilin J is a novel peptidyl-prolyl isomerase and target for repressing the growth of hepatocellular carcinoma. [PDF]

open access: yesPLoS ONE, 2015
Cyclophilin J (CYPJ) is a new member of the peptidyl-prolyl cis/trans-isomerase (PPIase) identified with upregulated expression in human glioma. However, the biological function of CYPJ remained unclear.
Jian Chen   +10 more
doaj   +1 more source

Roles of peptidyl prolyl isomerase Pin1 in viral propagation

open access: yesFrontiers in Cell and Developmental Biology, 2022
Peptidyl-prolyl isomerase (PPIase) is a unique enzyme that promotes cis-trans isomerization of a proline residue of a target protein. Peptidyl-prolyl cis-trans isomerase NIMA (never in mitosis A)-interacting 1 (Pin1) is a PPIase that binds to the pSer ...
Machi Kanna   +7 more
doaj   +1 more source

Novel cycloheximide derivatives targeting the moonlighting protein Mip exhibit specific antimicrobial activity against Legionella pneumophila

open access: yesFrontiers in Bioengineering and Biotechnology, 2015
Mip (macrophage infectivity potentiator) and Mip-like proteins are virulence factors in a wide range of pathogens including Legionella pneumophila. These proteins belong to the FK506 binding protein (FKBP) family of peptidyl-prolyl-cis/trans-isomerases ...
Janine eRasch   +11 more
doaj   +1 more source

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

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

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