Results 201 to 210 of about 7,127 (231)
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FEBS Letters, 2020
Arabidopsis thaliana CYP71 (AtCYP71) is a chromatin‐remodeling protein that promotes shoot apical meristem (SAM) differentiation. The N terminus of AtCYP71 contains a noncanonical WD domain, and the C terminus contains an enzymatic peptidyl‐prolyl ...
S. Lakhanpal +3 more
semanticscholar +1 more source
Arabidopsis thaliana CYP71 (AtCYP71) is a chromatin‐remodeling protein that promotes shoot apical meristem (SAM) differentiation. The N terminus of AtCYP71 contains a noncanonical WD domain, and the C terminus contains an enzymatic peptidyl‐prolyl ...
S. Lakhanpal +3 more
semanticscholar +1 more source
Archaeal peptidyl prolyl cis-trans isomerases (PPIases)
Frontiers in Bioscience, 2000PPIases 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
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The β-subunit of pea stem mitochondrial ATP synthase exhibits PPiase activity
Mitochondrion, 2003A 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.
ZANCANI, Marco +6 more
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EMBO Journal, 2001 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
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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
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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
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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
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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