Results 171 to 180 of about 7,517 (194)

Programmable enhancement of endogenous mRNA translation through CRISPR-guided epitranscriptomic regulation. [PDF]

Cell Discov
Cheng Y, Zhu G, Zhou X, Liu Y, Pan Y, Guo X, Li D, Liao G, Liu C, Hu X, Shao G, Gu Z, Liu L, Jiang W, Li G.   +14 more
europepmc   +1 more source

The proteome study of germinated Puccinia triticina urediniospores reveals a novel effector protein required for virulence. [PDF]

Sci Rep
Ozketen AC, Cetinturk M, Rampitsch C, Tatlises EA, Tatlises MB, Bakkeren G, Hasancebi S, Gunel A.   +7 more
europepmc   +1 more source

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Downregulation of Peptidylprolyl isomerase A promotes cell death and enhances doxorubicin-induced apoptosis in hepatocellular carcinoma

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.
Chuanhui Peng, Heng Xiao, Haiyang Xie
exaly   +3 more sources

Cyclosporin Analogs Modified in the 3,7,8-Positions: Substituent Effects on Peptidylprolyl Isomerase Inhibition and Immunosuppressive Activity Are Nonadditive

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 ...
Daniel H Rich
exaly   +3 more sources

A peptidylprolyl cis/trans isomerase from Xenopus laevis skin: cloning, biochemical characterization and putative role in the secretion

Peptides, 2003
In amphibian skin secretions, a peptidylprolyl cis/trans isomerase activity was detected. A Xenopus laevis skin cDNA coding for this protein was cloned, sequenced and over-expressed in Escherichia coli.
Rossella Mièle, Marina Borro, Maria Luisa Mangoni   +2 more
exaly   +2 more sources

Structural Insights into Substrate Binding by Pv FKBP35, a Peptidylprolyl cis-trans Isomerase from the Human Malarial Parasite Plasmodium vivax

Eukaryotic Cell, 2013
The immunosuppressive drug FK506 binding proteins (FKBPs), an immunophilin family with the immunosuppressive drug FK506 binding property, exhibit peptidylprolyl cis-trans isomerase (PPIase) activity.
Asha Manikkoth Balakrishna, Insaf Ahmed Qureshi, Julien Lescar   +2 more
exaly   +2 more sources

Possible involvement of peptidylprolyl isomerase Pin1 in rheumatoid arthritis

Pathology International, 2010
The 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, Naohiro, Takizawa, Ryohei, Takeuchi, Yutaka, Inaba, Izumi, Saito, Yoji, Nagashima, Tomoyuki, Saito, Ichiro, Aoki   +7 more
openaire   +2 more sources

Discovery and Characterization of a Nonphosphorylated Cyclic Peptide Inhibitor of the Peptidylprolyl Isomerase, Pin1

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, Brian R, Dempsey, Lauren E, Killip, Jarrett, Adams, Melanie L, Bailey, Gilles A, Lajoie, David W, Litchfield, Christopher J, Brandl, Gary S, Shaw, Brian H, Shilton   +9 more
openaire   +2 more sources

Identification of Eukaryotic Parvulin Homologues: A New Subfamily of Peptidylprolyl cis–trans Isomerases

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
openaire   +2 more sources