Investigating the effects of mutations on protein aggregation in the cell.
about
Sequence determinants of protein aggregation: tools to increase protein solubility.Dissecting the role of critical residues and substrate preference of a Fatty Acyl-CoA Synthetase (FadD13) of Mycobacterium tuberculosisComparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formationSDM--a server for predicting effects of mutations on protein stability and malfunction.A computational-experimental approach identifies mutations that enhance surface expression of an oseltamivir-resistant influenza neuraminidase.A structural systems biology approach for quantifying the systemic consequences of missense mutations in proteins.RNA mutagenesis yields highly diverse mRNA libraries for in vitro protein evolution.Directed evolution to re-adapt a co-evolved network within an enzyme.On the effect of protein conformation diversity in discriminating among neutral and disease related single amino acid substitutions.Missense meanderings in sequence space: a biophysical view of protein evolution.Ishemia-reperfusion enhances GAPDH nitration in aging skeletal muscle.Enhancing the stability and solubility of TEV protease using in silico design.Development of a dehalogenase-based protein fusion tag capable of rapid, selective and covalent attachment to customizable ligands.Studies on bacterial inclusion bodies.Exploring critical determinants of protein amyloidogenesis: a review.Amyloidogenic sequences in native protein structures.Aberrantly increased hydrophobicity shared by mutants of Cu,Zn-superoxide dismutase in familial amyotrophic lateral sclerosis.Structural Insights into l-Tryptophan Dehydrogenase from a Photoautotrophic Cyanobacterium, Nostoc punctiformeConformational Stability and Pathogenic Misfolding of the Integral Membrane Protein PMP22.Association between foldability and aggregation propensity in small disulfide-rich proteinsThe fast-folding HP35 double mutant has a substantially reduced primary folding free energy barrier.Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state.Charge substitution shows that repulsive electrostatic interactions impede the oligomerization of Alzheimer amyloid peptides.Type III secretion as a generalizable strategy for the production of full-length biopolymer-forming proteins.The Relation between α-Helical Conformation and Amyloidogenicity.Accurate prediction of functional, structural, and stability changes in PITX2 mutations using in silico bioinformatics algorithms.Thioflavin-S staining coupled to flow cytometry. A screening tool to detect in vivo protein aggregation
P2860
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P2860
Investigating the effects of mutations on protein aggregation in the cell.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年學術文章
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name
Investigating the effects of mutations on protein aggregation in the cell.
@en
Investigating the effects of mutations on protein aggregation in the cell.
@nl
type
label
Investigating the effects of mutations on protein aggregation in the cell.
@en
Investigating the effects of mutations on protein aggregation in the cell.
@nl
prefLabel
Investigating the effects of mutations on protein aggregation in the cell.
@en
Investigating the effects of mutations on protein aggregation in the cell.
@nl
P2093
P2860
P356
P1476
Investigating the effects of mutations on protein aggregation in the cell
@en
P2093
Christopher M Dobson
Fabrizio Chiti
Sara Zoffoli
P2860
P304
10607-10613
P356
10.1074/JBC.M412951200
P407
P577
2004-12-16T00:00:00Z