Extracellular environment modulates the formation and propagation of particular amyloid structures

Molecular Microbiology

Volumn 92, Issue 4, 2014, Pages 698-715

  Westergard, Laura ^a   True, Heather L ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PROTEIN; POLYPEPTIDE; PRION PROTEIN; PROTEIN VARIANT; SUP35 PROTEIN; UNCLASSIFIED DRUG; AMYLOID; PRION; RNQ1 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; SUP35 PROTEIN, S CEREVISIAE; TRANSLATION TERMINATION FACTOR;

ARTICLE; BIOCHEMISTRY; CELL GROWTH; CELL METABOLISM; CELL STRESS; CONTROLLED STUDY; DISEASE TRANSMISSION; EXTRACELLULAR MATRIX; MOLECULAR MODEL; NONHUMAN; PHENOTYPE; PHENOTYPIC VARIATION; PHYSIOLOGY; PRION DISEASE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; METABOLISM; PHYSIOLOGICAL STRESS; PRION; SACCHAROMYCES CEREVISIAE;

SACCHAROMYCES CEREVISIAE;

AMYLOID; PEPTIDE TERMINATION FACTORS; PRIONS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; STRESS, PHYSIOLOGICAL;

EID: 84899910555     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12579     Document Type: Article

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