Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism
The formation of well‐ordered fibrillar protein deposits is common to a large group of
amyloid‐associated disorders. This group consists of several major human diseases such …
amyloid‐associated disorders. This group consists of several major human diseases such …
[PDF][PDF] Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism
Y Porat, A Abramowitz, E Gazit - Chem Biol Drug Des, 2005 - academia.edu
The formation of well-ordered fibrillar protein deposits is common to a large group of
amyloidassociated disorders. This group consists of several major human diseases such as …
amyloidassociated disorders. This group consists of several major human diseases such as …
Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism.
Y Porat, A Abramowitz, E Gazit - Chemical Biology & Drug Design, 2006 - europepmc.org
The formation of well-ordered fibrillar protein deposits is common to a large group of amyloid-
associated disorders. This group consists of several major human diseases such as …
associated disorders. This group consists of several major human diseases such as …
[引用][C] Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism
Y Porat, A Abramowitz, E Gazit - Chemical Biology Drug Design, 2006 - cir.nii.ac.jp
Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic
Interactions as a Common Inhibition Mechanism | CiNii Research CiNii 国立情報学研究所 学術 …
Interactions as a Common Inhibition Mechanism | CiNii Research CiNii 国立情報学研究所 学術 …
Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism
Y Porat, A Abramowitz, E Gazit - Chemical biology & …, 2006 - pubmed.ncbi.nlm.nih.gov
The formation of well-ordered fibrillar protein deposits is common to a large group of amyloid-
associated disorders. This group consists of several major human diseases such as …
associated disorders. This group consists of several major human diseases such as …
[PDF][PDF] Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism
E Gazit - 2005 - Citeseer
The formation of well-ordered fibrillar protein deposits is common to a large group of
amyloidassociated disorders. This group consists of several major human diseases such as …
amyloidassociated disorders. This group consists of several major human diseases such as …
[PDF][PDF] Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism
Y Porat, A Abramowitz, E Gazit - Chem Biol Drug Des, 2005 - tau.ac.il
The formation of well-ordered fibrillar protein deposits is common to a large group of
amyloidassociated disorders. This group consists of several major human diseases such as …
amyloidassociated disorders. This group consists of several major human diseases such as …
[PDF][PDF] Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism
Y Porat, A Abramowitz, E Gazit - Chem Biol Drug Des, 2005 - tau.ac.il
The formation of well-ordered fibrillar protein deposits is common to a large group of
amyloidassociated disorders. This group consists of several major human diseases such as …
amyloidassociated disorders. This group consists of several major human diseases such as …