[HTML][HTML] Amyloidogenic mutation promotes fibril formation of the N-terminal apolipoprotein AI on lipid membranes
C Mizuguchi, F Ogata, S Mikawa, K Tsuji, T Baba… - Journal of Biological …, 2015 - ASBMB
The N-terminal amino acid 1–83 fragment of apolipoprotein AI (apoA-I) has a strong
propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability …
propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability …
Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein AI on Lipid Membranes
C Mizuguchi, F Ogata, S Mikawa… - The Journal of …, 2015 - pubmed.ncbi.nlm.nih.gov
The N-terminal amino acid 1-83 fragment of apolipoprotein AI (apoA-I) has a strong
propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability …
propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability …
[引用][C] Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein AI on Lipid Membranes
C Mizuguchi, F Ogata, S Mikawa, K Tsuji… - Journal of Biological …, 2015 - cir.nii.ac.jp
Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein AI on Lipid
Membranes | CiNii Research CiNii 国立情報学研究所 学術情報ナビゲータ[サイニィ] 詳細へ移動 …
Membranes | CiNii Research CiNii 国立情報学研究所 学術情報ナビゲータ[サイニィ] 詳細へ移動 …
Amyloidogenic mutation promotes fibril formation of the N-terminal apolipoprotein AI on lipid membranes
C Mizuguchi, F Ogata, S Mikawa… - Journal of …, 2015 - okayama.elsevierpure.com
The N-terminal amino acid 1-83 fragment of apolipoprotein AI (apoA-I) has a strong
propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability …
propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability …
[HTML][HTML] Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein AI on Lipid Membranes
C Mizuguchi, F Ogata, S Mikawa, K Tsuji… - The Journal of …, 2015 - ncbi.nlm.nih.gov
Background: The N-terminal fragment of amyloidogenic apoA-I mutants deposits as fibrils by
unknown mechanisms. Results: The G26R mutation partially prevents helix formation of the …
unknown mechanisms. Results: The G26R mutation partially prevents helix formation of the …
[HTML][HTML] Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein AI on Lipid Membranes
C Mizuguchi, F Ogata, S Mikawa, K Tsuji, T Baba… - Journal of Biological …, 2015 - Elsevier
The N-terminal amino acid 1–83 fragment of apolipoprotein AI (apoA-I) has a strong
propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability …
propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability …
Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein AI on Lipid Membranes.
C Mizuguchi, F Ogata, S Mikawa, K Tsuji… - The Journal of …, 2015 - europepmc.org
The N-terminal amino acid 1–83 fragment of apolipoprotein AI (apoA-I) has a strong
propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability …
propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability …
Amyloidogenic mutation promotes fibril formation of the N-terminal apolipoprotein AI on lipid membranes
C Mizuguchi, F Ogata, S Mikawa… - Journal of …, 2015 - okayama.elsevierpure.com
抄録 The N-terminal amino acid 1-83 fragment of apolipoprotein AI (apoA-I) has a strong
propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability …
propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability …
Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein AI on Lipid Membranes.
C Mizuguchi, F Ogata, S Mikawa, K Tsuji… - The Journal of …, 2015 - europepmc.org
The N-terminal amino acid 1–83 fragment of apolipoprotein AI (apoA-I) has a strong
propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability …
propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability …