Results 141 to 150 of about 3,214 (169)
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.
Wang, Ying +6 more
exaly +3 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
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
Bracher, A. +3 more
openaire +6 more sources
High‐resolution insights into binding of unfolded polypeptides by the PPIase chaperone SlpA
The FASEB Journal, 2012SlpA is a 2‐domain protein consisting of an FK506‐binding protein (FKBP) domain that harbors the peptidyl‐prolyl cis / trans ‐isomerase (PPIase) active site and a small insert‐in‐flap (IF) domain that endows the protein with chaperone activity.
Quistgaard EM, Nordlund P, Löw C
openaire +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.
Gollan, Peter J. +2 more
openaire +3 more sources
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
openaire +2 more sources
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 +9 more
openaire +2 more sources
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 +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, 2007Peptidyl-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 +6 more
openaire +2 more sources
Chaperone-Like Proteins in Inflammation and Immunomodulation: Examples of Resistin and PPIases
2019Hsp and other small proteins that function as an accessory chaperones interact with the cellular signaling network. They come up as an immediate response to stress when cells face the challenge of its own programmed death response. Chaperokines, with their inflammation and immune modulatory potential, try to strike the balance between recovery to ...
Saurabh Pandey +2 more
openaire +1 more source
Journal of Biochemistry, 1999
The Schizosaccharomyces pombe gene, fkp39(+), encoding a homolog of FKBP(FK506 binding protein)-type peptidyl prolyl cis-trans isomerase (PPIase), was isolated and the primary structure was determined. This gene product (SpFkbp39p) showed PPIase enzymatic activity in a chymotrypsin-dependent enzyme assay involving recombinant SpFkbp39p.
R, Himukai, T, Kuzuhara, M, Horikoshi
openaire +2 more sources
The Schizosaccharomyces pombe gene, fkp39(+), encoding a homolog of FKBP(FK506 binding protein)-type peptidyl prolyl cis-trans isomerase (PPIase), was isolated and the primary structure was determined. This gene product (SpFkbp39p) showed PPIase enzymatic activity in a chymotrypsin-dependent enzyme assay involving recombinant SpFkbp39p.
R, Himukai, T, Kuzuhara, M, Horikoshi
openaire +2 more sources
Biochimica et Biophysica Acta (BBA) - General Subjects, 2015
Protein folding is crucial for proteins' specific functions and is facilitated by various types of enzymes and molecular chaperones. The peptidyl prolyl cis/trans isomerases (PPIase) are one of these families of enzymes. They ubiquitously exist inside the cell and there are eight PPIases in the rough endoplasmic reticulum (rER), a compartment where the
Yoshihiro, Ishikawa +2 more
openaire +2 more sources
Protein folding is crucial for proteins' specific functions and is facilitated by various types of enzymes and molecular chaperones. The peptidyl prolyl cis/trans isomerases (PPIase) are one of these families of enzymes. They ubiquitously exist inside the cell and there are eight PPIases in the rough endoplasmic reticulum (rER), a compartment where the
Yoshihiro, Ishikawa +2 more
openaire +2 more sources