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Eosinophil differentiation was induced upon addition of 50 ng/ml SCF, 1 ng/ml each GM-CSF, IL-3 and IL-5 (Peprotech).
14 The shear moduli G of F120 and F140 fibrils (12.7 MPa) are in close proximity to those of other protein assemblies, such as F-actin (9 MPa) 16 and sickle-cell fibrils (SCF, 1 MPa).
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This is suppressed by mutations of the SCF CDC4 (SCF; Skp1/Cul1/F-box protein) ubiquitin ligase complex.
SCF (4 μg/ml) was treated with protease inhibitors PMSF, EDTA, and DTT for 2 h and fibrinogenolytic activity of treated SCF was estimated post incubation.
One of the proposed methods for mitigating this problem is store carry forward (SCF) [1].
Three SCF CO2 conditions at 84, 283, and 476 atm all at 140 °C for 30 min were studied.
Supercritical CO2 fluids (SCF CO2) assisting melting of poly vinylidene fluoride) (PVDF) and the SCF CO2 pressure affecting surface and bulk morphology, melting and crystallization of PVDF were investigated by means of SEM, AFM, FTIR, WAXD, DSC and SAXS.
SCF (Skp1-Cullin-F-box) ubiquitin ligases comprise several dozen modular enzymes that have diverse roles in biological regulation.
Morphological changes, induced by melting of PVDF under SCF CO2 and recrystallization during depressurization of CO2, were found.
The modular SCF (Skp1, cullin, and F box) ubiquitin ligases feature a large family of F box protein substrate receptors that enable recognition of diverse targets.
Experimental data were obtained at constant temperature of 385 °C, pressure of 9.8 MPa, LHSV of 0.25 h and 5000 scf H2/bbl oil.
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