Additional file 2: of The association between Parkinson’s disease and melanoma: a systematic review and meta-analysis

Quality assessment of studies included in the Meta-analysis. Criterion include five parts: 1) definition of PD diagnosis; 2) validation of PD diagnosis; 3) adjustment for confounding factors; 4) source and definition of cancer diagnoses; 5) representativeness of cases. Potential total scores ranged from 0 to 9. (PDF 127 kb

N‑Heterocyclic Carbene–Palladium(II)–4,5-Dihydrooxazole Complexes: Synthesis and Catalytic Activity toward Amination of Aryl Chlorides

A series of novel N-heterocyclic carbene–palladium­(II)–4,5-dihydrooxazole (NHC-Pd^II-Ox) complexes <b>3</b> were successfully synthesized from commercially available imidazolium salts <b>1</b>, PdCl₂, and 4,5-dihydrooxazoles <b>2</b> in a one-step process, and these complexes showed efficient catalytic activity toward the amination of aryl chlorides. Both secondary and primary amines were tolerated under the same reaction conditions. Under the optimal reaction conditions, the expected coupling products were obtained in moderate to high yields

Artesunate reverses cytarabine resistance in acute myeloid leukemia by blocking the JAK/STAT3 signaling

Although cytarabine (AraC) has greatly contributed to improving the prognosis of patients with acute myeloid leukemia (AML), many patients developed drug resistance and eventually succumbed to AML. Thus, resistance to AraC is a major obstacle to improve the efficacy of chemotherapy in AML. Hence, this study aimed to demonstrate that artesunate (ART) can reliably induce cell death in vitro and block AraC resistance. AML cell lines resistant to AraC were first constructed by repeated dosing for 5 months. Further, we analyzed whether ART intervention affected the sensitivity of AraC-resistant cells to AraC by cell function experiments, mainly including CCK-8 to assess cell viability, flow cytometry to examine apoptosis, and Western blotting to measure the Janus kinase (JAK)/signal transducers and activators of transcription 3 (STAT3) pathway protein expression. Furthermore, whether JAK/STAT3 pathway knockdown has a blocking effect on the efficacy of ART was also assessed. Co-treatment of ART and AraC increased the sensitivity of AML cells to AraC. Also, it effectively reversed the resistance of AML cells to AraC that is shown by the significantly reduced proliferation and increased apoptosis rates. ART intervention suppressed the activation of the JAK/STAT3 signaling pathway in AraC-resistant AML cells, suggesting that the function of ART in reversing AraC resistance is indeed dependent on the JAK/STAT3 signaling pathway. In summary, ART enhanced the sensitivity of AML/AraC-resistant cells to AraC by modulating the JAK/STAT3 pathway.</p

Apparent thermodynamic parameters associated with urea-induced unfolding transitions of recHuPrP^C and recRaPrP^C at 25°C.

<p>The buffer contained 20 mM NaOAc, pH 5.5. ΔG^H2O_N→U is designated as the apparent free energy of unfolding extrapolated to zero concentration of denaturant, m_N→U is the cooperativity of the unfolding transition, and C_m is the concentration of urea required to denature 50% of the protein. The CD spectrum was an average of three consecutive scans. Each experiment was repeated in triplicate for each sample.</p

Urea-induced unfolding transitions of recRaPrP^C and recHuPrP^C proteins analyzed at 25°C by Far-UV CD spectroscopy.

<p>The buffer contained 20 mM NaOAc, pH 5.5. The unfolded fraction calculated from Δε at 222 nm is plotted as a function of the urea concentration. Insert: ΔG (kJ/mol) versus the urea concentration.</p

NaCl concentration-dependent oligomerization of recHuPrP^C and recRaPrP^C monitored by gel filtration chromatography.

<p>The oligomerization experiments of prion proteins were conducted in the buffer (20 mM NaOAc, 50–200 mM NaCl, pH 4.0) at 57°C (n = 3; Error bars, S.D.).</p

Apparent thermodynamic parameters associated with thermal-induced unfolding transitions of recHuPrP^C and recRaPrP^C.

<p>The buffer contained 20 mM NaOAc, 0–200 mM NaCl, pH 5.5. ΔG^0°C_N→U is designated as the apparent free energy of unfolding extrapolated to 0°C, m_N→U is the cooperativity of the unfolding transition, and T_m is the temperature at the midpoint of unfolding. The CD spectrum was an average of three consecutive scans. One experiment was conducted for each sample.</p

Comparison of recHuPrP^O-induced and recRaPrP^O-induced toxicities on human glioblastoma cell lines U87.

<p>Cells were incubated with oligomeric PrP^O proteins at different concentrations for 48 h (37°C). Cytotoxicity was quanitified as a function of cell viability by the MTS assay (n = 3, mean±SD; *, <i>p</i><0.01; ***, <i>p</i><0.001; by Multiple Comparison Test).</p

Characterization of monomer and oligomer properties for human and rabbit prion proteins.

<p>Oligomerization of human prion protein (A) and rabbit prion protein (B) in the buffer (20 mM NaOAc, 150 mM NaCl, pH 4.0) was monitored by gel filtration chromatography. The prion protein oligomers were prepared with a buffer (20 mM NaOAc, 150 mM NaCl, pH 4.0) at 47°C. Particle sizes of both human prion protein (C) and rabbit prion protein (D) were analyzed by DLS spectroscopy. Secondary structures of human prion protein (E) and rabbit prion protein (F) were detected by Far-UV CD spectroscopy. Both DLS and CD experiments were performed at 25°C. The buffer used for prion monomers contained 20 mM NaOAc, pH 5.5.</p

Incubation temperature-dependent oligomerization of recHuPrP^C and recRaPrP^C monitored by gel filtration chromatography.

<p>The oligomerization experiments of prion proteins were conducted in a buffer (20 mM NaOAc, 150 mM NaCl, pH 4.0) at 37–67°C (n = 3; Error bars, S.D.).</p