Pathogenic serum amyloid A 1.1 shows a long oligomer-rich fibrillation lag phase contrary to the highly amyloidogenic non-pathogenic SAA2.2

Journal of Biological Chemistry

Volumn 288, Issue 4, 2013, Pages 2744-2755

  Srinivasan, Saipraveen ^a,b   Patke, Sanket ^b,c   Wang, Yun ^a,b   Ye, Zhuqiu ^a,b   Litt, Jeffrey ^b,c   Srivastava, Sunit K ^b   Lopez, Maria M ^b   Kurouski, Dmitry ^d   Lednev, Igor K ^d   Kane, Ravi S ^b,c   Colón, Wilfredo ^a,b  

^a Research Rensselaer Polytechnic Institute   (United States)

^b RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^c RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^d STATE UNIVERSITY OF NEW YORK   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBRIL; AMYLOIDOGENICITY; BILAYER MEMBRANES; BIOPHYSICAL PROPERTIES; DEEP UV; FIBRIL MORPHOLOGY; IN-VITRO; ISOFORMS; LAG PHASE; MOUSE STRAIN; QUATERNARY STRUCTURE; SEQUENCE IDENTITY; SERUM AMYLOID A;

ATOMIC FORCE MICROSCOPY; BODY FLUIDS; GLYCOPROTEINS; MAMMALS; MORPHOLOGY; OLIGOMERIZATION; OLIGOMERS; PATHOLOGY;

PROTEINS;

OLIGOMER; SERUM AMYLOID A; SERUM AMYLOID A 1.1; SERUM AMYLOID A 2.2; UNCLASSIFIED DRUG;

ARTICLE; ATOMIC FORCE MICROSCOPY; BILAYER MEMBRANE; CIRCULAR DICHROISM; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; CYTOTOXICITY TEST; EMBRYO; HUMAN; HUMAN CELL; IN VITRO STUDY; MEMBRANE PERMEABILITY; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN FUNCTION; PROTEIN QUATERNARY STRUCTURE; PROTEIN REFOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; PROTEIN TRANSPORT; RAMAN SPECTROMETRY; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; ULTRAVIOLET SPECTROPHOTOMETRY;

AMYLOIDOSIS; ANIMALS; BIOPHYSICS; CIRCULAR DICHROISM; HEK293 CELLS; HUMANS; INFLAMMATION; KINETICS; MICE; MICROSCOPY, ATOMIC FORCE; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN ISOFORMS; RECOMBINANT PROTEINS; SERUM AMYLOID A PROTEIN; SPECTROPHOTOMETRY, ULTRAVIOLET;

EID: 84873878454     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.394155     Document Type: Article

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