Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein - Wikidata - awgldk - TriplyDB

Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein

Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein

http://www.wikidata.org/entity/Q27665069

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Structural and physico-chemical effects of disease and non-disease nsSNPs on proteins Progress on low susceptibility mechanisms of transmissible spongiform encephalopathies Redistribution of flexibility in stabilizing antibody fragment mutants follows Le Châtelier's principle Mutations in Antibody Fragments Modulate Allosteric Response Via Hydrogen-Bond Network Fluctuations.Changes in Lysozyme Flexibility upon Mutation Are Frequent, Large and Long-Ranged.Unique Properties of the Rabbit Prion Protein Oligomer Prion protein oligomer and its neurotoxicity.Molecular dynamics studies on the buffalo prion protein.In Vitro Approach To Identify Key Amino Acids in Low Susceptibility of Rabbit Prion Protein to Misfolding.Molecular dynamics studies on the NMR structures of rabbit prion protein wild type and mutants: surface electrostatic charge distributions.The structural stability of wild-type horse prion protein.Distinct effects of Cu2+-binding on oligomerization of human and rabbit prion proteins.Protein misfolding cyclic amplification induces the conversion of recombinant prion protein to PrP oligomers causing neuronal apoptosis.Molecular dynamics studies on the structural stability of wild-type dog prion protein.Distinct effects of mutations on biophysical properties of human prion protein monomers and oligomers.Detailed computational analysis revealed mutation V210I on PrP induced conformational conversion on β2-α2 loop and α2-α3.A review on the salt bridge ASP177-ARG163 (O-N) of wild-type rabbit prion protein.

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Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein

http://www.wikidata.org/entity/Q27665069

description

2010 nî lūn-bûn

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2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2010 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年学术文章

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2010年学术文章

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2010年学术文章

@zh-hans

2010年学术文章

@zh-my

2010年学术文章

@zh-sg

2010年學術文章

@yue

name

Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein

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Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein

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Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein

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Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein

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Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein

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Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein

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prefLabel

Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein

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Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein

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Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein

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JOURNAL.PONE.0013273

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Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein

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Donghai Lin

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Jing Hong

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Jun Li

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Minqian Xiong

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Wenming Yao

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Yi Wen

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P2860

Generating a prion with bacterially expressed recombinant prion protein.

NMR solution structure of the human prion protein

NMR structure of the bovine prion protein

NMR structures of three single-residue variants of the human prion protein

Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases

NMR structure of the bank vole prion protein at 20 degrees C contains a structured loop of residues 165-171

Prion protein NMR structure from tammar wallaby (Macropus eugenii) shows that the beta2-alpha2 loop is modulated by long-range sequence effects

Unique Structural Characteristics of the Rabbit Prion Protein

NMR structure of the mouse prion protein domain PrP(121-231)

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Prion protein family

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