Results 171 to 180 of about 31,607 (207)

Paclitaxel compromises nuclear integrity in interphase through SUN2-mediated cytoskeletal coupling. [PDF]

J Cell Sci
Hale T, Hale VL, Kolata P, Dos Santos Á, Allegretti M.   +4 more
europepmc   +1 more source

The role of eCyPA as an inflammatory biomarker for predicting 28-day mortality in ARDS patients. [PDF]

Respir Res
Chen J, Dai X, Lv J, Liu M, Goligher EC, Deng W.   +5 more
europepmc   +1 more source

Involvement of cyclophilin B in the replication of Japanese encephalitis virus

Involvement of cyclophilin B in the replication of Japanese encephalitis virus
openaire  

Cyclophilin inhibition as potential therapy for liver diseases [PDF]

Journal of Hepatology, 2014
SummaryThe cyclophilins are a group of proteins with peptidyl-prolyl isomerase enzymatic activity, localised in different cellular compartments and involved in a variety of functions related to cell metabolism and energy homeostasis, having enhanced ...
Nikolai V Naoumov
exaly   +3 more sources

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CD147 Is a Signaling Receptor for Cyclophilin B

Biochemical and Biophysical Research Communications, 2001
Cyclophilins A and B (CyPA and CyPB) are cyclosporin A binding proteins that can be secreted in response to inflammatory stimuli. We recently identified CD147 as a cell-surface receptor for CyPA and demonstrated that CD147 is an essential component in the CyPA-initiated signaling cascade that culminates in ERK activation and chemotaxis.
V, Yurchenko, M, O'Connor, W W, Dai, H, Guo, B, Toole, B, Sherry, M, Bukrinsky   +6 more
openaire   +2 more sources

Fluorescence Characterization of the Hydrophobic Pocket of Cyclophilin B

Journal of Fluorescence, 2007
Human cyclophilin B is a monomeric protein that contains two tryptophan residues, Trp104 and 128. Trp128-residue belongs to the binding site of cyclosporin A and is the homologous of Trp 121 in CyPA, while Trp104 residue belongs to the hydrophobic pocket.
J R, Albani, M, Carpentier, C, Lansiaux
openaire   +2 more sources

Molecular Cloning and Characterization of Aspergillus nidulans Cyclophilin B

Fungal Genetics and Biology, 1999
Cyclophilins are an evolutionarily conserved family of proteins which serve as the intracellular receptors for the immunosuppressive drug cyclosporin A. Here we report the characterization of the first cyclophilin cloned from the filamentous fungus Aspergillus nidulans (CYPB).
J D, Joseph, J, Heitman, A R, Means
openaire   +2 more sources

Binding of Active Cyclosporins to Cyclophilin A and B, Complex Formation with Calcineurin A

Biochemical and Biophysical Research Communications, 1993
The binding properties of several active and inactive cyclosporins to the major intracellular receptor proteins, cyclophilin A and B, as well as the interaction with the phosphatase calcineurin were investigated by ELISA and by means of a photoaffinity labeled probe (PL-CS).
Ryffel B, Woerly G, Murray M, Eugster HP, Car B   +4 more
openaire   +3 more sources

Cyclophilin B Deficiency Causes Abnormal Dentin Collagen Matrix

Journal of Proteome Research, 2017
Cyclophilin B (CypB) is an endoplasmic reticulum-resident protein that regulates collagen folding, and also contributes to prolyl 3-hydroxylation (P3H) and lysine (Lys) hydroxylation of collagen. In this study, we characterized dentin type I collagen in CypB null (KO) mice, a model of recessive osteogenesis imperfecta type IX, and compared to those of ...
Masahiko, Terajima, Yuki, Taga, Wayne A, Cabral, Masako, Nagasawa, Noriko, Sumida, Shunji, Hattori, Joan C, Marini, Mitsuo, Yamauchi   +7 more
openaire   +2 more sources