Results 181 to 190 of about 3,959 (198)
Some of the next articles are maybe not open access.
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
Biochimica et Biophysica Acta (BBA) - General Subjects
Peptidyl prolyl cis/trans isomerases (PPIases), a ubiquitously distributed superfamily of enzymes, associated with signal transduction, trafficking, assembly, biofilm formation, stress tolerance, cell cycle regulation, gene expression and tissue regeneration, is a key regulator of metabolic disorders and microbial virulence.
Roopshali, Rakshit +4 more
openaire +2 more sources
Peptidyl prolyl cis/trans isomerases (PPIases), a ubiquitously distributed superfamily of enzymes, associated with signal transduction, trafficking, assembly, biofilm formation, stress tolerance, cell cycle regulation, gene expression and tissue regeneration, is a key regulator of metabolic disorders and microbial virulence.
Roopshali, Rakshit +4 more
openaire +2 more sources
Biological Chemistry, 2003
We analysed eight monoclonal antibodies (mAbs) directed against the Mip (macrophage infectivity potentiator) protein, a virulence factor of the intracellular pathogen Legionella pneumophila. Mip belongs to the FK506-binding proteins (FKBPs) and exhibits peptidyl prolyl cis/trans isomerase (PPIase) activity. Five of the mAbs recognised epitopes in the C-
Jürgen H, Helbig +10 more
openaire +2 more sources
We analysed eight monoclonal antibodies (mAbs) directed against the Mip (macrophage infectivity potentiator) protein, a virulence factor of the intracellular pathogen Legionella pneumophila. Mip belongs to the FK506-binding proteins (FKBPs) and exhibits peptidyl prolyl cis/trans isomerase (PPIase) activity. Five of the mAbs recognised epitopes in the C-
Jürgen H, Helbig +10 more
openaire +2 more sources