Serum albumin prevents protein aggregation and amyloid formation and retains chaperone-like activity in the presence of physiological ligands.
about
Conditional disorder in chaperone action.Macromolecular crowding as a suppressor of human IAPP fibril formation and cytotoxicity.Development and evaluation of multiplexed immunoassay for detection of antibodies to HPV vaccine typesAdsorbing/dissolving Lyoprotectant Matrix Technology for Non-cryogenic Storage of Archival Human SeraThe role of crowded physiological environments in prion and prion-like protein aggregationInvestigation of the Biological Impact of Charge Distribution on a NTR1-Targeted Peptide.Is Autophagy Dysfunction a Key to Exfoliation Glaucoma?Purification of the subcellular compartment in which exogenous antigens undergo endoplasmic reticulum-associated degradation from dendritic cells.Sensitivity of human pluripotent stem cells to insulin precipitation induced by peristaltic pump-based medium circulation: considerations on process development.New Evidence for the Mechanism of Action of a Type-2 Diabetes Drug Using a Magnetic Bead-Based Automated Biosensing Platform.Function, structure, and stability of enzymes confined in agarose gels.Regulating extracellular proteostasis capacity through the unfolded protein response.Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7210.Navigating the structure-function-evolutionary relationship of CsaA chaperone in archaea.SdhE-dependent formation of a functional Acetobacter pasteurianus succinate dehydrogenase in Gluconobacter oxydans--a first step toward a complete tricarboxylic acid cycle.Multifactorial Analysis of a Biomarker Pool for Alzheimer Disease Risk in a North Indian Population.Silver and ultrasmall iron oxides nanoparticles in hydrocolloids: effect of magnetic field and temperature on self-organization.Detection of the anticoagulant drug warfarin by palladium complexes.The proteome of neurofilament-containing protein aggregates in blood.
P2860
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P2860
Serum albumin prevents protein aggregation and amyloid formation and retains chaperone-like activity in the presence of physiological ligands.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Serum albumin prevents protein ...... ence of physiological ligands.
@en
type
label
Serum albumin prevents protein ...... ence of physiological ligands.
@en
prefLabel
Serum albumin prevents protein ...... ence of physiological ligands.
@en
P2860
P356
P1476
Serum albumin prevents protein ...... sence of physiological ligands
@en
P2093
Andrea C Nunez
Simon B Easterbrook-Smith
P2860
P304
21530-21540
P356
10.1074/JBC.M112.372961
P407
P577
2012-05-01T00:00:00Z