Results 141 to 150 of about 7,181 (160)
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Gene, 2016
Peptidylprolyl isomerase A (PPIA) is a peptidyl-prolyl cis-trans isomerase that is known to play a critical role in the development of many human cancers. However, the precise biological function of PPIA in hepatocellular carcinoma (HCC) remains largely unclear.
Lin Zhou, Chuanhui Peng, Jian Wu
exaly +3 more sources
Peptidylprolyl isomerase A (PPIA) is a peptidyl-prolyl cis-trans isomerase that is known to play a critical role in the development of many human cancers. However, the precise biological function of PPIA in hepatocellular carcinoma (HCC) remains largely unclear.
Lin Zhou, Chuanhui Peng, Jian Wu
exaly +3 more sources
Journal of Medicinal Chemistry, 1995
Four analogs of cyclosporin A (CsA) were synthesized to determine if the biological activities of CsA analogs generated by multiple amino acid replacements are predictable from the effects on biological activity of analogs with single residue changes. CsA analogs [Phe7]CsA (8a), [D-MeAla3,Phe7]CsA (8b), [D-Ser8,Phe7]CsA (8c), and [D-MeAla3,Phe7,D-Ser8 ...
Ming-Kuan Hu, Daniel H Rich
exaly +3 more sources
Four analogs of cyclosporin A (CsA) were synthesized to determine if the biological activities of CsA analogs generated by multiple amino acid replacements are predictable from the effects on biological activity of analogs with single residue changes. CsA analogs [Phe7]CsA (8a), [D-MeAla3,Phe7]CsA (8b), [D-Ser8,Phe7]CsA (8c), and [D-MeAla3,Phe7,D-Ser8 ...
Ming-Kuan Hu, Daniel H Rich
exaly +3 more sources
Possible involvement of peptidylprolyl isomerase Pin1 in rheumatoid arthritis
Pathology International, 2010The peptidylprolyl isomerase Pin1 is over‐expressed in some human diseases including malignancies and chronic inflammatory diseases, this suggests that it contributes to the constitutive activation of certain intracellular signaling pathways that promote cell proliferation and cell invasion.
Akiko, Nagaoka +7 more
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Journal of Medicinal Chemistry, 2011
Phage panning led to the discovery of a disulfide-cyclized peptide CRYPEVEIC that inhibits Pin1 activity with a K(I) of 0.5 μM. NMR chemical shift perturbation experiments show that cyclic CRYPEVEIC binds to the active site of Pin1. Pin1 residues K63 and R68, which bind the phosphate of substrate peptides, do not show a significant chemical shift ...
Kelly E, Duncan +9 more
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Phage panning led to the discovery of a disulfide-cyclized peptide CRYPEVEIC that inhibits Pin1 activity with a K(I) of 0.5 μM. NMR chemical shift perturbation experiments show that cyclic CRYPEVEIC binds to the active site of Pin1. Pin1 residues K63 and R68, which bind the phosphate of substrate peptides, do not show a significant chemical shift ...
Kelly E, Duncan +9 more
openaire +2 more sources
Biochemical and Biophysical Research Communications, 1999
We report here the existence of a subfamily of eukaryotic parvulin proteins that have strong sequence homology with E. coli parvulin, but lack the WW domain found in previously described eukarytoic parvulins. We hence term members of this subfamily EPVH (eukaryotic parvulin homologue).
S, Rulten, J, Thorpe, J, Kay
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We report here the existence of a subfamily of eukaryotic parvulin proteins that have strong sequence homology with E. coli parvulin, but lack the WW domain found in previously described eukarytoic parvulins. We hence term members of this subfamily EPVH (eukaryotic parvulin homologue).
S, Rulten, J, Thorpe, J, Kay
openaire +2 more sources
Peptidylprolyl Cis / Trans Isomerases (Immunophilins): Biological Diversity - Targets - Functions
Current Topics in Medicinal Chemistry, 2003Information recovered from genome sequencing projects, multiple sequence alignments, structural analyses of PPIase and published records were used in deciphering the biological diversity, functions and targets of four groups of proteins encoded by dissimilar sets of sequences whose spatial representations exhibit peptidylprolyl cis/trans isomerase ...
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Cloning and characterization of peptidylprolyl isomerase B in the silkworm, Bombyx mori
2011Peptidylprolyl isomerases (PPIases) play essential roles in protein folding and are implicated in immune response and cell cycle control. Our previous proteomic analysis indicated that Bombyx mori PPIases may be involved in anti- Bombyx mori nucleopolyhedrovirus (BmNPV) response. To help investigate this mechanism, we cloned a B.
Xia, H +7 more
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Peptidylprolyl cis/trans isomerase activity and molecular evolution of vertebrate Cyclophilin A.
Yi chuan = Hereditas, 2017Peptidylprolyl isomerases (PPIase) cyclophilin A (CypA, encoded by PPIA) is a typical member of the Cyclophilin family and is involved in protein folding/translocation, signal transduction, inflammation, immune system regulation, apoptosis and virus replication.
Li-qian, Ren +4 more
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Small Molecule Inhibitors of Peptidylprolyl cis/trans Isomerase
Current Enzyme Inhibition, 2010Tadashi Mori, Takafumi Uchida
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