Requirement of Peptidyl-Prolyl Cis/Trans isomerases and chaperones for cellular uptake of bacterial AB-type toxins [PDF]
Frontiers in Cellular and Infection Microbiology, 2022 Bacterial AB-type toxins are proteins released by the producing bacteria and are the causative agents for several severe diseases including cholera, whooping cough, diphtheria or enteric diseases.
Katharina Ernst
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Genome-wide characterization of peptidyl-prolyl cis–trans isomerases in Penicillium and their regulation by salt stress in a halotolerant P. oxalicum [PDF]
Scientific 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
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Insights into Peptidyl-Prolyl cis-trans Isomerases from Clinically Important Protozoans: From Structure to Potential Biotechnological Applications [PDF]
PathogensPeptidyl-prolyl cis/trans isomerases (PPIases) are present in a wide variety of microorganisms, including protozoan parasites such as Trypanosoma cruzi, Trypanosoma brucei, Trichomonas vaginalis, Leishmania major, Leishmania donovani, Plasmodium ...
Verónica Aranda-Chan +7 more
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Compression of Large Sets of Sequence Data Reveals Fine Diversification of Functional Profiles in Multigene Families of Proteins: A Study for Peptidyl-Prolyl cis/trans Isomerases (PPIase) [PDF]
Biomolecules, 2019 In this technical note, we describe analyses of more than 15,000 sequences of FK506-binding proteins (FKBP) and cyclophilins, also known as peptidyl-prolyl cis/trans isomerases (PPIases).
Andrzej Galat
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Editorial: Peptidyl-prolyl cis/trans isomerases (PPIases) in host-pathogen interactions [PDF]
Frontiers in Cellular and Infection Microbiology, 2022 Michael Steinert
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Proline Isomerization: From the Chemistry and Biology to Therapeutic Opportunities
Biology, 2023 Proline isomerization, the process of interconversion between the cis- and trans-forms of proline, is an important and unique post-translational modification that can affect protein folding and conformations, and ultimately regulate protein functions and
Deepti Gurung +5 more
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Cyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradation. [PDF]
PLoS ONE, 2010 Peptidyl-prolyl cis/trans isomerases (PPIs) catalyze cis/trans isomerization of peptide bonds preceding proline residues. The involvement of PPI family members in protein refolding has been established in test tube experiments.
Riccardo Bernasconi +5 more
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A Redox-Sensitive Cysteine Is Required for PIN1At Function
Frontiers in Plant Science, 2021 Parvulins are ubiquitous peptidyl-prolyl isomerases (PPIases) required for protein folding and regulation. Among parvulin members, Arabidopsis PIN1At, human PIN1, and yeast ESS1 share a conserved cysteine residue but differ by the presence of an N ...
Benjamin Selles +5 more
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Calcineurin Undergoes a Conformational Switch Evoked via Peptidyl-Prolyl Isomerization. [PDF]
PLoS ONE, 2015 A limited repertoire of PPP family of serine/threonine phosphatases with a highly conserved catalytic domain acts on thousands of protein targets to orchestrate myriad central biological roles.
Alicia Guasch +8 more
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Frontiers in Plant Science, 2022 Peptidyl-prolyl cis-trans isomerases (PPIases) are ubiquitous proteins which are essential for cis-trans isomerisation of peptide bonds preceding the proline residue.
Anantika Suri +4 more
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