Aβ (1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease
Increasing evidence has suggested that formation and propagation of misfolded aggregates
of 42-residue human amyloid β (Aβ (1–42)), rather than of the more abundant Aβ (1–40) …
of 42-residue human amyloid β (Aβ (1–42)), rather than of the more abundant Aβ (1–40) …
[PDF][PDF] Aβ (1–42) Fibril Structure Illuminates Self-recognition and Replication of Amyloid in Alzheimer's
Y Xiao, B Ma, D McElheny, S Parthasarathy, F Long… - Nat Struct Mol Biol, 2015 - Citeseer
Increasing evidence suggests that formation and propagation of misfolded aggregates of 42-
residue human amyloid β (Aβ (1–42)), rather than the more abundant Aβ (1–40), provokes …
residue human amyloid β (Aβ (1–42)), rather than the more abundant Aβ (1–40), provokes …
Aβ (1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease.
Y Xiao, B Ma, D McElheny… - Nature Structural & …, 2015 - search.ebscohost.com
Increasing evidence has suggested that formation and propagation of misfolded aggregates
of 42-residue human amyloid β (Aβ (1-42)), rather than of the more abundant Aβ (1-40) …
of 42-residue human amyloid β (Aβ (1-42)), rather than of the more abundant Aβ (1-40) …
[引用][C] Aβ (1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease
Y Xiao - Nat Struct Mol Biol, 2015 - cir.nii.ac.jp
Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's
disease | 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 検索 …
disease | 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 検索 …
[HTML][HTML] Aβ (1–42) Fibril Structure Illuminates Self-recognition and Replication of Amyloid in Alzheimer's
Y Xiao, B Ma, D McElheny… - Nature structural & …, 2015 - ncbi.nlm.nih.gov
Increasing evidence suggests that formation and propagation of misfolded aggregates of 42-
residue human amyloid β (Aβ (1–42)), rather than the more abundant Aβ (1–40), provokes …
residue human amyloid β (Aβ (1–42)), rather than the more abundant Aβ (1–40), provokes …
A [beta](1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease
Y Xiao, B Ma, D McElheny, S Parthasarathy… - Nature Structural and …, 2015 - go.gale.com
Increasing evidence has suggested that formation and propagation of misfolded aggregates
of 42-residue human amyloid [beta](A [beta](1-42)), rather than of the more abundant A …
of 42-residue human amyloid [beta](A [beta](1-42)), rather than of the more abundant A …
Aβ (1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease.
Y Xiao, B Ma, D McElheny, S Parthasarathy… - Nature Structural & …, 2015 - europepmc.org
Increasing evidence suggests that formation and propagation of misfolded aggregates of 42-
residue human amyloid β (Aβ (1–42)), rather than the more abundant Aβ (1–40), provokes …
residue human amyloid β (Aβ (1–42)), rather than the more abundant Aβ (1–40), provokes …
Aβ (1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease
Y Xiao, B Ma, D McElheny, S Parthasarathy… - Nature Structural & …, 2015 - hero.epa.gov
Increasing evidence has suggested that formation and propagation of misfolded aggregates
of 42-residue human amyloid β (Aβ (1-42)), rather than of the more abundant Aβ (1-40) …
of 42-residue human amyloid β (Aβ (1-42)), rather than of the more abundant Aβ (1-40) …
Aβ (1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease
Y Xiao, B Ma, D McElheny… - Nature structural & …, 2015 - pubmed.ncbi.nlm.nih.gov
Increasing evidence has suggested that formation and propagation of misfolded aggregates
of 42-residue human amyloid β (Aβ (1-42)), rather than of the more abundant Aβ (1-40) …
of 42-residue human amyloid β (Aβ (1-42)), rather than of the more abundant Aβ (1-40) …
Aβ (1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease.
Y Xiao, B Ma, D McElheny, S Parthasarathy… - Nature Structural & …, 2015 - europepmc.org
Increasing evidence suggests that formation and propagation of misfolded aggregates of 42-
residue human amyloid β (Aβ (1–42)), rather than the more abundant Aβ (1–40), provokes …
residue human amyloid β (Aβ (1–42)), rather than the more abundant Aβ (1–40), provokes …