Multidimensional Structure-Activity Relationship of a Protein in Its Aggregated States

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Shear-stress-mediated refolding of proteins from aggregates and inclusion bodies Amyloid Aggregates Arise from Amino Acid Condensations under Prebiotic Conditions.

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Q21559300-8309564C-66CF-4A3D-9058-4F4004A9E72F Q41942780-A8D40AD1-8072-4F92-9CAB-7EB4570E7818

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Multidimensional Structure-Activity Relationship of a Protein in Its Aggregated States

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http://www.wikidata.org/entity/Q57909663

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im April 2010 veröffentlichter wissenschaftlicher Artikel

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wetenschappelijk artikel

@nl

наукова стаття, опублікована у квітні 2010

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Multidimensional Structure-Activity Relationship of a Protein in Its Aggregated States

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Multidimensional Structure-Activity Relationship of a Protein in Its Aggregated States

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Multidimensional Structure-Activity Relationship of a Protein in Its Aggregated States

@en

Multidimensional Structure-Activity Relationship of a Protein in Its Aggregated States

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Multidimensional Structure-Activity Relationship of a Protein in Its Aggregated States

@en

Multidimensional Structure-Activity Relationship of a Protein in Its Aggregated States

@nl

P1476

Multidimensional Structure-Activity Relationship of a Protein in Its Aggregated States

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P2093

David Eisenberg

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

David Schubert

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

Lei Wang

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

Michael R. Sawaya

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

Roland Riek

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

P2860

Functional amyloid formation within mammalian tissue.

Structure of the cross-beta spine of amyloid-like fibrils

Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain

Atomic structures of amyloid cross-beta spines reveal varied steric zippers

Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core

A yeast prion provides a mechanism for genetic variation and phenotypic diversity

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

Aggresomes, inclusion bodies and protein aggregation

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3996-4000

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

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scholarly article

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10.1002/ANGE.201000068

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

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

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122

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

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2010-04-15T00:00:00Z

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protein structure

Multidimensional Structure-Activity Relationship of a Protein in Its Aggregated States

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P2860

P2860

Multidimensional Structure-Activity Relationship of a Protein in Its Aggregated States

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P1433

P1476

P2093

P2860

P304

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P356

P433

P478

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P921

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P1433

P1476

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P2860

P304

P31

P356

P433

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P577

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