Structural Determinants of Amyloid B-Protein Oligomerization
نویسندگان
چکیده
منابع مشابه
In silico study of amyloid -protein folding and oligomerization
Experimental findings suggest that oligomeric forms of the amyloid protein (A ) play a critical role in Alzheimer’s disease. Thus, elucidating their structure and the mechanisms of their formation is critical for developing therapeutic agents. We use discrete molecular dynamics simulations and a four-bead protein model to study oligomerization of two predominant alloforms, A 40 and A 42, at the...
متن کاملFamilial Alzheimer's disease mutations differentially alter amyloid β-protein oligomerization.
Although most cases of Alzheimer's disease (AD) are sporadic, ∼5% of cases are genetic in origin. These cases, known as familial Alzheimer's disease (FAD), are caused by mutations that alter the rate of production or the primary structure of the amyloid β-protein (Aβ). Changes in the primary structure of Aβ alter the peptide's assembly and toxic activity. Recently, a primary working hypothesis ...
متن کاملAmino Acid Position-specific Contributions to Amyloid Β- Protein Oligomerization
Understanding the structural and assembly dynamics of the amyloid β-protein (Aβ) has direct relevance to the development of therapeutic agents for Alzheimer's disease. To elucidate these dynamics, we combined scanning amino acid substitution with a method for quantitative determination of the Aβ oligomer frequency distribution, PhotoInduced Cross-linking of Unmodified Proteins (PICUP), to perfo...
متن کامل3D domain swapping, protein oligomerization, and amyloid formation.
In 3D domain swapping, first described by Eisenberg, a structural element of a monomeric protein is replaced by the same element from another subunit. This process requires partial unfolding of the closed monomers that is then followed by adhesion and reconstruction of the original fold but from elements contributed by different subunits. If the interactions are reciprocal, a closed-ended dimer...
متن کاملA molecular switch in amyloid assembly: Met35 and amyloid beta-protein oligomerization.
Aberrant protein oligomerization is an important pathogenetic process in vivo. In Alzheimer's disease (AD), the amyloid beta-protein (Abeta) forms neurotoxic oligomers. The predominant in vivo Abeta alloforms, Abeta40 and Abeta42, have distinct oligomerization pathways. Abeta42 monomers oligomerize into pentamer/hexamer units (paranuclei) which self-associate to form larger oligomers. Abeta40 d...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2010
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2009.12.2485