Update on the Neisseria Macrophage Infectivity Potentiator-Like PPIase Protein
Frontiers in Cellular and Infection Microbiology, 2022 Neisseria pathogens express a Macrophage Infectivity Potentiator Protein (MIP), which belongs to the FK506 binding protein (FKBP) family of proteins that exhibit peptidyl-prolyl cis/trans isomerase (PPIase) activity.
Myron Christodoulides
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HSP-90/kinase complexes are stabilized by the large PPIase FKB-6 [PDF]
Scientific Reports, 2021 Protein kinases are important regulators in cellular signal transduction. As one major type of Hsp90 client, protein kinases rely on the ATP-dependent molecular chaperone Hsp90, which maintains their structure and supports their activation.
Siyuan Sima +7 more
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Introduction to Peptidyl-Prolyl cis/trans Isomerase (PPIase) Series [PDF]
Biomolecules, 2019 About 30 years after the discovery of peptidyl-prolyl cis/trans isomerases (PPIases), research on this group of proteins has become somewhat calmer than it used to be, but it still generates lots of interest [...]
Andrzej Galat
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Cyclophilin J PPIase Inhibitors Derived from 2,3-Quinoxaline-6 Amine Exhibit Antitumor Activity [PDF]
Frontiers in Pharmacology, 2018 Cyclophilin J (CyPJ), also called peptidylprolyl isomerase like 3, has been identified as a novel member of the cyclophilin family. Our previous research has resolved the three-dimensional structure of CyPJ and demonstrated the peptidylprolyl cis–trans ...
Xuemei Zhao +7 more
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PpiA, a surface PPIase of the cyclophilin family in Lactococcus lactis.
PLoS ONE, 2012 BackgroundProtein 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 ...
Nicolas Trémillon +10 more
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AtFKBP53: a chimeric histone chaperone with functional nucleoplasmin and PPIase domains [PDF]
Nucleic Acids Research, 2019 FKBP53 is one of the seven multi-domain FK506-binding proteins present in Arabidopsis thaliana, and it is known to get targeted to the nucleus. It has a conserved PPIase domain at the C-terminus and a highly charged N-terminal stretch, which has been ...
A. Singh +4 more
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Peptidyl-prolyl isomerase (PPIase): an emerging area in tumor biology
Cancer Research Frontiers, 2017 Peptidyl-prolyl isomerase (PPIase) catalyzes the interconversion of a specific Pro-imide bond between the cis and trans conformations. Such conformational interconversion by PPIases at the backbone of key signaling proteins is an emerging area of active ...
P. Nath
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Frontiers in Microbiology, 2018 Clostridioides difficile is the main cause for nosocomial antibiotic associated diarrhea and has become a major burden for the health care systems of industrial countries.
Can Murat Ünal +11 more
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NMR assignments of the FKBP-type PPIase domain of FKBP42 from Arabidopsis thaliana [PDF]
Biomolecular NMR Assignments, 2012 The Atfkbp42 gene is associated with reduced and disoriented growth of Arabidopsis thaliana. Resonance assignments are reported for the FKBP-type PPIase domain of AtFKBP42. Signal intensities reveal an additional structure element that is atypical for such FKBP domains.
N. Burgardt +4 more
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Identification of RNA targets for the nuclear multidomain cyclophilin atCyp59 and their effect on PPIase activity [PDF]
Nucleic Acids Research, 2012 AtCyp59 is a multidomain cyclophilin containing a peptidyl-prolyl cis/trans isomerase (PPIase) domain and an evolutionarily highly conserved RRM domain.
O. Bannikova +5 more
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