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Causative factors for formation of toxic islet amyloid polypeptide oligomer in type 2 diabetes mellitusEdge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphataseThe PTEN Long N-tail is intrinsically disordered: increased viability for PTEN therapyAmyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases.Evidence for the adaptation of protein pH-dependence to subcellular pH.Protein aggregation profile of the bacterial cytosol.An evolutionary trade-off between protein turnover rate and protein aggregation favors a higher aggregation propensity in fast degrading proteins.Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins.Cellular strategies for regulating functional and nonfunctional protein aggregation.A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides.Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins.X chromosome reactivation perturbs intracellular self/not-self discrimination.Computational approaches to understanding protein aggregation in neurodegeneration.Prediction of the aggregation propensity of proteins from the primary sequence: aggregation properties of proteomes.Prediction of amyloid aggregation in vivo.Motif mining: an assessment and perspective for amyloid fibril prediction tool.Evolutionary selection for protein aggregation.Predicting aggregation-prone sequences in proteins.Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein.Understanding and predicting protein misfolding and aggregation: Insights from proteomics.Protein aggregation profile of the human kinomeAntifragility and Tinkering in Biology (and in Business) Flexibility Provides an Efficient Epigenetic Way to Manage Risk.Sequence-based analysis of protein energy landscapes reveals nonuniform thermal adaptation within the proteome.The generation of antimicrobial peptide activity: a trade-off between charge and aggregation?The aggregation properties of Escherichia coli proteins associated with their cellular abundance
P2860
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P2860
description
2008 nî lūn-bûn
@nan
2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Aggregation propensity of the human proteome
@ast
Aggregation propensity of the human proteome
@en
Aggregation propensity of the human proteome
@nl
type
label
Aggregation propensity of the human proteome
@ast
Aggregation propensity of the human proteome
@en
Aggregation propensity of the human proteome
@nl
prefLabel
Aggregation propensity of the human proteome
@ast
Aggregation propensity of the human proteome
@en
Aggregation propensity of the human proteome
@nl
P2093
P2860
P1476
Aggregation propensity of the human proteome
@en
P2093
Elodie Monsellier
Fabrizio Chiti
Niccolò Taddei
P2860
P304
P356
10.1371/JOURNAL.PCBI.1000199
P407
P577
2008-10-01T00:00:00Z