High hydrostatic pressure as a tool to study protein aggregation and amyloidosis.
about
Classification and characterization of therapeutic antibody aggregates.Refolding of proteins from inclusion bodies is favored by a diminished hydrophobic effect at elevated pressures.Ultra-high-pressure inactivation of prion infectivity in processed meat: a practical method to prevent human infection.The role of the 132-160 region in prion protein conformational transitions.Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils.Molecular dynamics of thermoenzymes at high temperature and pressure: a review.Pressure-accelerated dissociation of amyloid fibrils in wild-type hen lysozyme.Unexpected high pressure effects on the structural properties of condensed whey protein systems.Effects of solutes on solubilization and refolding of proteins from inclusion bodies with high hydrostatic pressure.Folding intermediates of the prion protein stabilized by hydrostatic pressure and low temperature.Maximizing recovery of native protein from aggregates by optimizing pressure treatment.Enhanced preparation of adeno-associated viral vectors by using high hydrostatic pressure to selectively inactivate helper adenovirus.Specific volume and adiabatic compressibility measurements of native and aggregated recombinant human interleukin-1 receptor antagonist: density differences enable pressure-modulated refolding.Biocatalytic reaction and recycling by using CO2-induced organic-aqueous tunable solvents.Some physico-chemical parameters that influence proteinase K resistance and the infectivity of PrPSc after high pressure treatment.Properties of hydration shells of protein molecules at their pressure- and temperature-induced native-denatured transition.High-pressure refolding of human vascular endothelial growth factor (VEGF) recombinantly expressed in bacterial inclusion bodies: refolding optimization, and feasibility assessment.Leptospira interrogans thermolysin refolded at high pressure and alkaline pH displays proteolytic activity against complement C3.
P2860
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P2860
High hydrostatic pressure as a tool to study protein aggregation and amyloidosis.
description
2002 nî lūn-bûn
@nan
2002 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մարտին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
High hydrostatic pressure as a tool to study protein aggregation and amyloidosis.
@ast
High hydrostatic pressure as a tool to study protein aggregation and amyloidosis.
@en
High hydrostatic pressure as a tool to study protein aggregation and amyloidosis.
@nl
type
label
High hydrostatic pressure as a tool to study protein aggregation and amyloidosis.
@ast
High hydrostatic pressure as a tool to study protein aggregation and amyloidosis.
@en
High hydrostatic pressure as a tool to study protein aggregation and amyloidosis.
@nl
prefLabel
High hydrostatic pressure as a tool to study protein aggregation and amyloidosis.
@ast
High hydrostatic pressure as a tool to study protein aggregation and amyloidosis.
@en
High hydrostatic pressure as a tool to study protein aggregation and amyloidosis.
@nl
P2093
P1476
High hydrostatic pressure as a tool to study protein aggregation and amyloidosis.
@en
P2093
John F Carpenter
Matthew Seefeldt
Theodore W Randolph
P304
P356
10.1016/S0167-4838(01)00346-6
P407
P577
2002-03-01T00:00:00Z