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Archaeal peptidyl prolyl cis-trans isomerases (PPIases)
Frontiers in Bioscience, 2000PPIases 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
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Multidomain Peptidyl Prolyl cis/trans Isomerases
Biochimica et Biophysica Acta (BBA) - General Subjects, 2015Peptidyl prolyl cis/trans isomerases (PPIases) assist the folding and restructuring of client proteins by catalysis of the slow rotational motion of peptide bonds preceding a proline residue. Catalysis is performed by relatively small, distinct protein domains of 10 to 18kDa for all PPIase families.
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Prolyl cis/trans isomerase signalling pathways in cancer
Current Opinion in Pharmacology, 2011It is an emerging view that in many cases cell signalling relies on slow conformational interconversions of the backbone of key proteins as exemplified by the prolyl cis/trans isomerization, and that prolyl cis/trans isomerases (PPIases), such as cyclophilins, FK506-binding proteins and the parvulin-like Pin1, serve to integrate temporally and ...
Martin, Theuerkorn +2 more
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Food polyphenols targeting peptidyl prolyl cis/trans isomerase Pin1
Biochemical and Biophysical Research Communications, 2018We searched for inhibitors against prolyl isomerase Pin1 in order to develop functional foods to prevent and cure various Pin1 related diseases such as cancer, diabetes, cardiovascular disease, Alzheimers's disease, and so on. We created a polyphenol library consisting of ingredients in healthy foods and beverages, since polyphenols like ...
Masafumi Hidaka +8 more
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Archaeal peptidyl prolyl cis-trans isomerases (PPIases) update 2004
Frontiers in Bioscience, 2004PPIases are ubiquitous in living organisms. While three 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.
Tadashi, Maruyama +2 more
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A PEPTIDYL PROLYL CIS-TRANS ISOMERASE FROM AN EXTREME THERMOPHILIC ARCHAEON
Protein & Peptide Letters, 1994A peptidyl prolyl cis-trans isomerase has been detected in the cmde extract of the extreme thermophilic archaeon Sulfolobus solfataricus on the basis of its ability to catalyze the isomerization of the peptide bond in the peptide N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide.
GUAGLIARDI, ANNAMARIA +5 more
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Peptidylprolyl Cis / Trans Isomerases (Immunophilins): Biological Diversity - Targets - Functions
Current Topics in Medicinal Chemistry, 2003Information recovered from genome sequencing projects, multiple sequence alignments, structural analyses of PPIase and published records were used in deciphering the biological diversity, functions and targets of four groups of proteins encoded by dissimilar sets of sequences whose spatial representations exhibit peptidylprolyl cis/trans isomerase ...
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Maleate cis-trans isomerase from Arthrobacter sp. TPU 5446
Journal of Fermentation and Bioengineering, 1995A gram-positive aerobic bacterium, Arthrobacter sp. strain TPU 5446 with a high maleate cis-trans isomerase (MAI) activity, was isolated from soil. Enzyme activity was induced when the strain was cultivated in the presence of maleic acid and yeast extract as the carbon and nitrogen sources, respectively.
Yasuo Kato +2 more
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A Continuous Spectrophotometric Direct Assay for Peptidyl Prolyl cis-trans Isomerases
Biochemical and Biophysical Research Communications, 1993m-Nitrotyrosine incorporated into proline peptides of the general sequence -Xxx-Pro-Tyr(m-NO2)- responds to cis-trans Xxx-Pro conformational transition by changes in the pKa of its side-chain hydroxyl (Garel and Siffert, 1979). We exploited this effect to develop a continuous direct (uncoupled) assay for peptidyl prolyl cis-trans isomerases.
C, García-Echeverría +3 more
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Peptidyl-prolyl cis-trans isomerases: structure and functions.
Biochemistry. Biokhimiia, 1999Peptidyl-prolyl cis-trans isomerases (PPI) catalyze cis-trans isomerization of imide bonds in peptides and proteins. This review summarizes the literature on the structure and functions of PPIs, their involvement in protein folding, and organization of PPI-containing receptors and membrane channels.
B K, Pliyev, B Y, Gurvits
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