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Membrane protein chaperone and sodium chloride modulate the kinetics and morphology of amyloid beta aggregation.
Sun, Christopher; Slade, Leah; Mbonu, Prisca; Ordner, Hunter; Mitchell, Connor; Mitchell, Matthew; Liang, Fu-Cheng.
Affiliation
  • Sun C; Department of Biology, Midwestern State University, Wichita Falls, TX, USA.
  • Slade L; Department of Chemistry, Midwestern State University, Wichita Falls, TX, USA.
  • Mbonu P; Department of Biology, Midwestern State University, Wichita Falls, TX, USA.
  • Ordner H; Department of Chemistry, Midwestern State University, Wichita Falls, TX, USA.
  • Mitchell C; Department of Chemistry, Midwestern State University, Wichita Falls, TX, USA.
  • Mitchell M; Department of Chemistry, Midwestern State University, Wichita Falls, TX, USA.
  • Liang FC; Department of Chemistry, Midwestern State University, Wichita Falls, TX, USA.
FEBS J ; 291(1): 158-176, 2024 01.
Article in En | MEDLINE | ID: mdl-37786925
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Amyloid beta-Peptides / Signal Recognition Particle / Molecular Chaperones / Chloroplast Proteins / Protein Aggregates / Membrane Proteins Limits: Humans Language: En Journal: FEBS J Journal subject: BIOQUIMICA Year: 2024 Document type: Article Affiliation country: United States Country of publication: United kingdom
Fulltext
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Amyloid beta-Peptides / Signal Recognition Particle / Molecular Chaperones / Chloroplast Proteins / Protein Aggregates / Membrane Proteins Limits: Humans Language: En Journal: FEBS J Journal subject: BIOQUIMICA Year: 2024 Document type: Article Affiliation country: United States Country of publication: United kingdom