The peculiar role of the A2V mutation in amyloid-β (Aβ) 1-42 molecular assembly

Journal of Biological Chemistry

Volumn 289, Issue 35, 2014, Pages 4143-24152

  Messa, Massimo ^a   Colombo, Laura ^a   Del Favero, Elena ^b   Cantù, Laura ^b   Stoilova, Tatiana ^a   Cagnotto, Alfredo ^a   Rossi, Alessandro ^a   Morbin, Michela ^c   Di Fede, Giuseppe ^c   Tagliavini, Fabrizio ^c   Salmona, Mario ^a  

^a MARIO NEGRI INSTITUTE FOR PHARMACOLOGICAL RESEARCH   (Italy)

^b UNIVERSITY OF MILAN   (Italy)

^c DEPARTMENT OF NEUROSURGERY   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC FORCE MICROSCOPY; KINETICS; OLIGOMERS; X RAY DIFFRACTION;

EQUI-MOLAR SOLUTION; FLUORESCENCE EMISSION; HYDROPHOBIC RESIDUES; INTERMOLECULAR INTERACTIONS; LASER LIGHT SCATTERING; MOLECULAR ASSEMBLY; OLIGOMER FORMATIONS; STRUCTURAL CHARACTERIZATION;

PEPTIDES;

AMYLOID BETA PROTEIN[1-42]; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT;

AMINO ACID SEQUENCE; ARTICLE; ATOMIC FORCE MICROSCOPY; CIRCULAR DICHROISM; CONFORMATION; CONTROLLED STUDY; ELECTRON MICROSCOPY; HYDROPHOBICITY; LIGHT SCATTERING; MOLECULAR INTERACTION; MUTATION; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FOLDING; PROTEIN UNFOLDING; WILD TYPE; X RAY DIFFRACTION; CHEMISTRY; GENETICS; HUMAN; KINETICS; POLYMERIZATION; SMALL ANGLE SCATTERING; SPECTROFLUOROMETRY;

AMYLOID BETA-PEPTIDES; CIRCULAR DICHROISM; HUMANS; KINETICS; MICROSCOPY, ATOMIC FORCE; MUTATION; PEPTIDE FRAGMENTS; POLYMERIZATION; PROTEIN FOLDING; SCATTERING, SMALL ANGLE; SPECTROMETRY, FLUORESCENCE; X-RAY DIFFRACTION;

EID: 84906871317     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.576256     Document Type: Article

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