Results 191 to 200 of about 7,127 (231)
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Identification and characterization of peptides that bind the PPIase domain of Parvulin17
Journal of Peptide Science, 2013Peptidyl‐prolyl cis‐trans isomerases (PPIases) are the enzymes that increase the rate of isomerization of the peptide bond N‐terminal to the proline substrate. Par14 and its isoform Par17 belong to the Parvulin family of PPIases. Par14 can bind AT‐rich double‐stranded DNA and was shown to be part of the pre‐ribosomal ribonucleoprotein (pre‐rRNP ...
Imadeldin Elfaki +3 more
semanticscholar +4 more sources
PPIase is associated with the diversity of conotoxins from cone snail venom glands.
Biochimie, 2015Cone snails are incredibly rich sources of bioactive conopeptides with potential for use in neuroscience research and novel drug development. In order to investigate the synthesis of diversified conopeptides in venom glands, the proteome and peptidome profiles of conus venom were analyzed using HPLC and mass spectrometry.
Lei Wang +9 more
semanticscholar +3 more sources
Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90.
Acta Crystallographica Section D Biological Crystallography, 2011Steroid hormone receptors are key components of mammalian stress and sex hormone systems. Many of them rely on the Hsp90 chaperone system for full function and are further fine-tuned by Hsp90-associated peptidyl-prolyl isomerases such as FK506-binding proteins 51 and 52. FK506-binding protein 51 (FKBP51) has been shown to reduce glucocorticoid receptor
A. Bracher +3 more
semanticscholar +7 more sources
Human CyP33 binds specifically to mRNA and binding stimulates PPIase activity of hCyP33 [PDF]
FEBS Letters, 2008 Human nuclear cyclophilin 33 (hCyP33) was the first protein which was found to contain an RNA‐binding motif and a PPIase domain. It was not known what cellular and physiological roles are played by the RNA‐binding activity as well as the PPIase activity of hCyP33.
Ying Wang +6 more
exaly +4 more sources
PPIase activities and interaction partners of FK506‐binding proteins in the wheat thylakoid
Physiologia Plantarum, 2011FK506‐binding proteins (FKBPs) and cyclophilins, collectively called immunophilins, conserve peptidyl‐prolyl cis/trans isomerase (PPIase) active sites, although many lack PPIase activity. The chloroplast thylakoid contains a large proportion of the plant immunophilin family, but their functions within this compartment are unclear.
Peter J Gollan
exaly +5 more sources
Crystal Structure of the PP2A Phosphatase Activator: Implications for Its PP2A-Specific PPIase Activity [PDF]
Molecular Cell, 2006 PTPA, an essential and specific activator of protein phosphatase 2A (PP2A), functions as a peptidyl prolyl isomerase (PPIase). We present here the crystal structures of human PTPA and of the two yeast orthologs (Ypa1 and Ypa2), revealing an all alpha-helical protein fold that is radically different from other PPIases.
Nicolas Leulliot
exaly +4 more sources
PPIase independent chaperone‐like function of recombinant human Cyclophilin A during arginine kinase refolding [PDF]
FEBS Letters, 2013 Whether Cyclophilin A (CyPA) functions as a foldase or a chaperone when assisting protein folding has long been argued. In this study, we engineered four variants of recombinant human Cyclophilin A (rhCyPA), all of which were inactive to tetrapeptide ...
Xin-Chao Zhang +3 more
exaly +4 more sources
Molecular Plant, 2018
Phytophthora pathogens secrete a large arsenal of effectors that manipulate host processes to create an environment conducive to pathogen colonization. However, the underlying mechanisms by which Phytophthora effectors manipulate host plant cells still ...
Tingting Li, Wenqin Lu, Yu Du
exaly +2 more sources
Phytophthora pathogens secrete a large arsenal of effectors that manipulate host processes to create an environment conducive to pathogen colonization. However, the underlying mechanisms by which Phytophthora effectors manipulate host plant cells still ...
Tingting Li, Wenqin Lu, Yu Du
exaly +2 more sources
International Journal of Molecular Sciences, 2016 Alternative splicing (AS) is an important molecular mechanism by which single genes can generate multiple mRNA isoforms. We reported previously that, in Oryza sativa, the cyclophilin 19-4 (OsCYP19-4.1) transcript was significantly upregulated in response
Hyun-Soon Kim +2 more
exaly +2 more sources