Results 241 to 250 of about 431,479 (299)
Secreted Nonstructural Protein 3 is a Pathogenic Determinant of Orbivirus
This study uncovers a conserved PIP2‐dependent secretory pathway of orbivirus NS3 that induces vascular leakage. Pharmacological disruption of PIP2‐NS3 interaction significantly reduces viral pathogenicity and provides protective efficacy in murine models, establishing PIP2‐mediated NS3 secretion as both a key virulence determinant and a promising ...
Junyong Guan +11 more
wiley +1 more source
Adhesion‐Driven Removal of Microplastics From Aquatic Systems by Using Microgel Glues
Soft polymeric microgels function as “glues” that aggregate diverse microplastics through multivalent adhesion, promoting their interfacial deposition and co‐precipitation for efficient removal from water. Remarkably, this approach remains effective even for nanoscale plastic particles as small as 50 nm.
Jinmeng Zhang +5 more
wiley +1 more source
Dynamic decellularized hydrogels are prepared using bovine decellularized small intestine submucosa (SIS) norbornene (dSIS‐NB). Bovine dSIS contained significant amounts of disulfide‐rich fibrillin‐I, enabling ‘self‐clickable’ thiol‐norbornene gelation and spatiotemporal tuning of hydrogel physicochemical properties.
Van Thuy Duong +4 more
wiley +1 more source
The study elucidates that paternal preconception stress can drive offspring hyperresponsivity of the stress system via hypomethylation of a specific DNA region in sperm. This key link is confirmed in a cohort of prospective fathers: the epigenetic alteration is associated with elevated stress hormone levels.
Mengxi Lu +10 more
wiley +1 more source
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Interaction between casein and sodium dodecyl sulfate
Journal of Colloid and Interface Science, 2007The interaction of the anionic surfactant sodium dodecyl sulfate (SDS) with 2.0 mg/ml casein was first investigated using isothermal titration calorimetry (ITC), dynamic light scattering (DLS), and fluorescence spectra. ITC results show that individual SDS molecules first bind to casein micelles by the hydrophobic interaction.
Yan, Liu, Rong, Guo
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Removal of sodium dodecyl sulfate from proteins
Analytical Biochemistry, 1975Abstract A convenient and relatively simple electrodialysis method for the removal of sodium dodecyl sulfate (SDS) from proteins is described. Six samples can be processed simultaneously. The kinetics of removal of SDS from proteins by equilibrium dialysis and electrodialysis have been studied.
G P, Tuszynski, L, Warren
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Molecular Mobility in Solid Sodium Dodecyl Sulfate
The Journal of Physical Chemistry B, 2011Here we report on the molecular mobility in solid sodium dodecyl sulfate (SDS), a commonly used surfactant, as measured by high-resolution neutron scattering in the temperature range 175-400 K. While the quasielastic data showed the presence of dynamical motion at and above 210 K, the fixed energy window (FEW) data indicated that the dynamics is ...
S, Mitra +4 more
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Acid-Catalyzed Hydrolysis of Sodium Dodecyl Sulfate
Journal of Pharmaceutical Sciences, 1985The acid-catalyzed hydrolysis of sodium dodecyl sulfate (1) and the effect of 1-dodecanol (2) on this hydrolysis were investigated. The rate of hydrolysis was followed by measuring the rate of production of HSO-4 using a pH-stat. The rate constant (kH+) below the critical micelle concentration (CMC) increased with increasing concentrations of 2, up to ...
M, Nakagaki, S, Yokoyama
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Hair protein removal by sodium dodecyl sulfate
Colloids and Surfaces B: Biointerfaces, 2005The effect of sodium dodecyl sulfate (SDS) on protein loss was studied. Three kinds of human hair were tested by rubbing or immersion in water or immersion in SDS solution, at 25, 40 and 70 degrees C. Under friction, hair treated with SDS solution loses seven times more protein than in water, while by immersion, protein loss is roughly two times higher
Rita, de Cássia Comis Wagner +1 more
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Removal of sodium dodecyl sulfate from proteins
Analytical Biochemistry, 1978Effective removal of sodium dodecyl sulfate from proteins in water or sodium phosphate buffer was achieved by column chromatography using the ion-retardation resin AG11A8. An average recovery of 83% protein was obtained, while 0.1 to 1.4 moles of sodium dodecyl sulfate remained on each mole of protein.
O H, Kapp, S N, Vinogradov
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