Protein aggregation from inclusion bodies to amyloid and biomaterials.
about
Mechanisms of islet amyloidosis toxicity in type 2 diabetesStreamlined protein expression and purification using cleavable self-aggregating tagsMeasurement of amyloid formation by turbidity assay-seeing through the cloudA consensus method for the prediction of 'aggregation-prone' peptides in globular proteins.Active protein aggregates induced by terminally attached self-assembling peptide ELK16 in Escherichia coliStructural analysis of peptide-analogues of human Zona Pellucida ZP1 protein with amyloidogenic properties: insights into mammalian Zona Pellucida formationSingle-molecule fluorescence reveals sequence-specific misfolding in multidomain proteinsSmall surfactant-like peptides can drive soluble proteins into active aggregates.Selective inhibition of aggregation/fibrillation of bovine serum albumin by osmolytes: Mechanistic and energetics insights.Spontaneous structural transition and crystal formation in minimal supramolecular polymer modelPrediction of the aggregation propensity of proteins from the primary sequence: aggregation properties of proteomes.Autophagy coupling interplay: can improve cellular repair and aging?Integrating mechanical and biological control of cell proliferation through bioinspired multieffector materials.Functional protein aggregates: just the tip of the iceberg.Eukaryotic aggresomes: from a model of conformational diseases to an emerging type of immobilized biocatalyzers.Mining databases for protein aggregation: a review.A nanostructured bacterial bioscaffold for the sustained bottom-up delivery of protein drugs.Functional inclusion bodies produced in bacteria as naturally occurring nanopills for advanced cell therapies.Bacterial mimetics of endocrine secretory granules as immobilized in vivo depots for functional protein drugs.Amylin receptor: a common pathophysiological target in Alzheimer's disease and diabetes mellitusPackaging protein drugs as bacterial inclusion bodies for therapeutic applicationsRole of aromatic interactions in amyloid formation by islet amyloid polypeptide.Structural studies of "aggregation-prone" peptide-analogues of teleostean egg chorion ZPB proteins.Selective Knockdowns in Maize by Sequence-Specific Protein Aggregation.Sequence-Specific Protein Aggregation Generates Defined Protein Knockdowns in Plants.
P2860
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P2860
Protein aggregation from inclusion bodies to amyloid and biomaterials.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Protein aggregation from inclusion bodies to amyloid and biomaterials.
@ast
Protein aggregation from inclusion bodies to amyloid and biomaterials.
@en
type
label
Protein aggregation from inclusion bodies to amyloid and biomaterials.
@ast
Protein aggregation from inclusion bodies to amyloid and biomaterials.
@en
prefLabel
Protein aggregation from inclusion bodies to amyloid and biomaterials.
@ast
Protein aggregation from inclusion bodies to amyloid and biomaterials.
@en
P1476
Protein aggregation from inclusion bodies to amyloid and biomaterials.
@en
P2093
Anna Mitraki
P304
P356
10.1016/S1876-1623(10)79003-9
P577
2010-01-01T00:00:00Z