Nanoprobing of misfolding and interactions of amyloid β 42 protein

Nanomedicine: Nanotechnology, Biology, and Medicine

Volumn 10, Issue 4, 2014, Pages 871-878

  Kim, Bo Hyun ^a,b   Lyubchenko, Yuri L ^a  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^b Korea Advanced Institute of Science and Technology (KAIST)   (South Korea)

Author keywords

Amyloid beta; Contour length; Dimerization pathways; Misfolding; Single molecule force spectroscopy

Indexed keywords

ASSEMBLY; DIMERS; GLYCOPROTEINS; MOLECULES; NANOSTRUCTURES; NEURODEGENERATIVE DISEASES; PEPTIDES;

ALZHEIMER'S DISEASE; AMYLOID BETAS; ATOMIC FORCE SPECTROSCOPY; C-TERMINAL SEGMENTS; CONTOUR LENGTHS; MISFOLDING; SELF ASSEMBLY PROCESS; SINGLE MOLECULE FORCE SPECTROSCOPY;

SELF ASSEMBLY;

AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; CYSTEINE; MALEIMIDE; NANOMATERIAL; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT;

ARTICLE; CONTROLLED STUDY; DIMERIZATION; DISSOCIATION; HYDRODYNAMICS; IMMOBILIZATION; NANOPROBING; NANOTECHNOLOGY; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN MISFOLDING; PROTEIN STRUCTURE; SINGLE MOLECULE FORCE SPECTROSCOPY; SPECTROSCOPY; ALZHEIMER DISEASE; CHEMISTRY; HUMAN; METABOLISM; PH; PROTEIN MULTIMERIZATION;

ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; HUMANS; HYDROGEN-ION CONCENTRATION; PEPTIDE FRAGMENTS; PROTEIN FOLDING; PROTEIN MULTIMERIZATION;

EID: 84900309223     PISSN: 15499634     EISSN: 15499642     Source Type: Journal    
DOI: 10.1016/j.nano.2013.11.016     Document Type: Article

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