The glaucoma-associated olfactomedin domain of myocilin forms polymorphic fibrils that are constrained by partial unfolding and peptide sequence

Journal of Molecular Biology

Volumn 426, Issue 4, 2014, Pages 921-935

  Hill, Shannon E ^a   Donegan, Rebecca K ^a   Lieberman, Raquel L ^a  

^a GEORGIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

amyloid; atomic force microscopy; circular dichroism; protein misfolding; protein structure

Indexed keywords

AMYLOID; MONOMER; MYOCILIN; OLIGOMER; SODIUM CHLORIDE; AMYLOID PROTEIN; OLFACTOMEDIN DOMAIN OF MYOCILIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; CONTROLLED STUDY; GLAUCOMA; INFRARED SPECTROSCOPY; MORPHOLOGY; PARTICLE SIZE; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTEIN UNFOLDING; SCREENING; TEMPERATURE; WILD TYPE; ATOMIC FORCE MICROSCOPY; CIRCULAR DICHROISM; HYDROPHOBICITY; INTRAOCULAR HYPERTENSION; PATHOGENESIS; PEPTIDE SYNTHESIS; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SINGLE NUCLEOTIDE POLYMORPHISM; THERMOSTABILITY; TRABECULAR MESHWORK;

AFM; AMYLOID; ANILINONAPHTHALENE-1-SULFONATE; ANS; ATOMIC FORCE MICROSCOPY; CIRCULAR DICHROISM; ENDOPLASMIC RETICULUM; ER; FOURIER TRANSFORM INFRARED SPECTROSCOPY; FTIR; PROTEIN MISFOLDING; PROTEIN STRUCTURE; TEV; THIOFLAVIN T; THT; TM; TOBACCO ETCH VIRUS; TRABECULAR MESHWORK;

AMINO ACID SEQUENCE; AMYLOID; CIRCULAR DICHROISM; CYTOSKELETAL PROTEINS; EXTRACELLULAR MATRIX PROTEINS; EYE PROTEINS; GLAUCOMA; GLYCOPROTEINS; HUMANS; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SODIUM CHLORIDE;

EID: 84893655063     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.12.002     Document Type: Article

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