Characterizing intermolecular interactions that initiate native-like protein aggregation. - Wikidata - awgldk - TriplyDB

Characterizing intermolecular interactions that initiate native-like protein aggregation.

Characterizing intermolecular interactions that initiate native-like protein aggregation.

http://www.wikidata.org/entity/Q41807230

about

Mechanism of Protein Kinetic Stabilization by Engineered Disulfide Crosslinks Edge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphatase Understanding protein aggregation from the view of monomer dynamics Amyloid β-protein oligomers and Alzheimer's disease.Information flow and protein dynamics: the interplay between nuclear magnetic resonance spectroscopy and molecular dynamics simulations.Equilibrium Ensembles for Insulin Folding from Bias-Exchange Metadynamics.Delicate balance between functionally required flexibility and aggregation risk in a β-rich protein.Effect of the surface charge distribution on the fluid phase behavior of charged colloids and proteins.Impact of deglycosylation and thermal stress on conformational stability of a full length murine IgG2a monoclonal antibody: observations from molecular dynamics simulations.Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies.

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P2860

Characterizing intermolecular interactions that initiate native-like protein aggregation.

http://www.wikidata.org/entity/Q41807230

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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2012年论文

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2012年论文

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name

Characterizing intermolecular interactions that initiate native-like protein aggregation.

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type

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Characterizing intermolecular interactions that initiate native-like protein aggregation.

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Characterizing intermolecular interactions that initiate native-like protein aggregation.

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J.BPJ.2012.03.057

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Biophysical Journal

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Characterizing intermolecular interactions that initiate native-like protein aggregation.

@en

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Alfonso De Simone

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Fabrizio Chiti

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P2860

Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS

Protein misfolding, functional amyloid, and human disease

Primary structure effects on peptide group hydrogen exchange

Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility

Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution.

The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid.

Identification of the core structure of lysozyme amyloid fibrils by proteolysis.

Amyloid formation by globular proteins under native conditions.

Sequence and structural determinants of amyloid fibril formation.

"Native-like aggregation" of the acylphosphatase from Sulfolobus solfataricus and its biological implications.

P304

2595-2604

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scholarly article

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10.1016/J.BPJ.2012.03.057

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11

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102

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Francesco Bemporad

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2012-06-05T00:00:00Z

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227396378

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22713575

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Acylphosphatase

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3368139

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