Temperature dependence of chaperone-like activity and oligomeric state of αB-crystallin
about
The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: a light and X-ray scattering investigation.Acid-denatured Green Fluorescent Protein (GFP) as model substrate to study the chaperone activity of protein disulfide isomeraseSmall heat-shock proteins: important players in regulating cellular proteostasis.Effect of disulfide crosslinking on thermal transitions and chaperone-like activity of human small heat shock protein HspB1.Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils.Structural properties of silkworm small heat-shock proteins: sHSP19.9 and sHSP20.8.
P2860
Temperature dependence of chaperone-like activity and oligomeric state of αB-crystallin
description
im April 2006 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована у квітні 2006
@uk
name
Temperature dependence of chaperone-like activity and oligomeric state of αB-crystallin
@en
Temperature dependence of chaperone-like activity and oligomeric state of αB-crystallin
@nl
type
label
Temperature dependence of chaperone-like activity and oligomeric state of αB-crystallin
@en
Temperature dependence of chaperone-like activity and oligomeric state of αB-crystallin
@nl
prefLabel
Temperature dependence of chaperone-like activity and oligomeric state of αB-crystallin
@en
Temperature dependence of chaperone-like activity and oligomeric state of αB-crystallin
@nl
P2093
P50
P1476
Temperature dependence of chaperone-like activity and oligomeric state of αB-crystallin
@en
P2093
Federico Bennardini
Francesco Spinozzi
Franco Rustichelli
Giovanni Maria Mura
Maria Luisa Ganadu
P304
P356
10.1016/J.BBAPAP.2006.02.003
P577
2006-04-01T00:00:00Z