Investigating the effects of mutations on protein aggregation in the cell. - Wikidata - awgldk - TriplyDB

Investigating the effects of mutations on protein aggregation in the cell.

Investigating the effects of mutations on protein aggregation in the cell.

http://www.wikidata.org/entity/Q45195856

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 tuberculosis Comparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formation SDM--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 punctiforme Conformational Stability and Pathogenic Misfolding of the Integral Membrane Protein PMP22.Association between foldability and aggregation propensity in small disulfide-rich proteins The 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.

http://www.wikidata.org/entity/Q45195856

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

@wuu

2004年学术文章

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2004年学术文章

@zh-cn

2004年学术文章

@zh-hans

2004年学术文章

@zh-my

2004年学术文章

@zh-sg

2004年學術文章

@yue

2004年學術文章

@zh-hant

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

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P1433

Journal of Biological Chemistry

P1476

Investigating the effects of mutations on protein aggregation in the cell

@en

P2093

Christopher M Dobson

http://www.w3.org/2001/XMLSchema#string

Fabrizio Chiti

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Sara Zoffoli

http://www.w3.org/2001/XMLSchema#string

P2860

A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro

Rational design of potent human transthyretin amyloid disease inhibitors

Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly

Synthesis and characterization of potent bivalent amyloidosis inhibitors that bind prior to transthyretin tetramerization

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

Molecular chaperones in the cytosol: from nascent chain to folded protein

Protein folding and misfolding

Folding proteins in fatal ways

Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain

Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations

P304

10607-10613

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scholarly article

P356

10.1074/JBC.M412951200

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11

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280

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Massimo Stefani

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2004-12-16T00:00:00Z

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15611128

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