Results 171 to 180 of about 3,959 (198)

The β-subunit of pea stem mitochondrial ATP synthase exhibits PPiase activity

Mitochondrion, 2003
A soluble protein with a molecular mass of 55 kDa has been purified from etiolated pea stem mitochondria. The protein exhibits a Mg2+-requiring PPiase activity, with an optimum at pH 9.0, which is not stimulated by monovalent cations, but inhibited by F-, Ca2+, aminomethylenediphosphate and imidodiphosphate.
Marco Zancani, Valentino Casolo, Carlo Peresson   +2 more
exaly   +7 more sources

NMR solution structure and characterization of substrate binding site of the PPIase domain of PrsA protein fromBacillus subtilis

FEBS Letters, 2006
PrsA is a peptidyl-prolyl isomerase (PPIase) from Bacillus subtilis belonging to the parvulin family of PPIases. It is a membrane bound lipoprotein at the membrane–wall interface, involved in folding of exported proteins.
Helena Tossavainen, Perttu Permi, Matti Sarvas   +2 more
exaly   +2 more sources

Archaeal peptidyl prolyl cis-trans isomerases (PPIases)

Frontiers in Bioscience, 2000
PPIases 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
openaire   +2 more sources

PPIase is associated with the diversity of conotoxins from cone snail venom glands

Biochimie, 2015
Cone 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.
Yuanyuan Qiang, Zhenghua Ren, Shangwu Chen   +2 more
exaly   +3 more sources

Identification and characterization of peptides that bind the PPIase domain of Parvulin17

Journal of Peptide Science, 2013
Peptidyl‐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 ...
Elfaki, Imadeldin, Knitsch, Andre, Matena, Anja, Bayer, Peter   +3 more
openaire   +3 more sources

Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90

Acta Crystallographica Section D Biological Crystallography, 2011
Steroid 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
Bracher, A., Kozany, C., Thost, A., Hausch, F.   +3 more
openaire   +6 more sources

The OsCYP19-4 Gene Is Expressed as Multiple Alternatively Spliced Transcripts Encoding Isoforms with Distinct Cellular Localizations and PPIase Activities under Cold Stress

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
Areum Lee, Won Jung, Hyun Park
exaly   +2 more sources

Archaeal peptidyl prolyl cis-trans isomerases (PPIases) update 2004

Frontiers in Bioscience, 2004
PPIases 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, Rintaro, Suzuki, Masahiro, Furutani   +2 more
openaire   +2 more sources

Inhibitors of macrophage infectivity potentiator-like PPIases affect neisserial and chlamydial pathogenicity

International Journal of Antimicrobial Agents, 2016
The pathogenic bacteria Chlamydia trachomatis, Neisseria gonorrhoeae and Neisseria meningitidis express the surface-exposed macrophage infectivity potentiator (MIP)-like protein, which plays a role in their pathogenicity. MIP exhibits a peptidyl-prolyl isomerase (PPIase) activity that is inhibited by rapamycin and FK506.
Anastasija, Reimer, Florian, Seufert, Matthias, Weiwad, Jutta, Ebert, Nicole M, Bzdyl, Charlene M, Kahler, Mitali, Sarkar-Tyson, Ulrike, Holzgrabe, Thomas, Rudel, Vera, Kozjak-Pavlovic   +9 more
openaire   +2 more sources

The binding of FKBP23 to BiP modulates BiP’s ATPase activity with its PPIase activity

Biochemical and Biophysical Research Communications, 2007
Peptidyl-prolyl cis-trans-isomerases (PPIases) are enzymes that can cis-trans-isomerize a Xaa-Pro peptide bond. Three families of PPIases are known: cyclophilins, FKBPs, and parvulins. The physiological functions of the PPIases are only poorly understood.
Ying, Wang, Ruifang, Han, Di, Wu, Jie, Li, Chen, Chen, Hui, Ma, Huaifeng, Mi   +6 more
openaire   +2 more sources