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Search Results to Xiaohu Mei

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One or more keywords matched the following properties of Mei, Xiaohu

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Research Expertise & Professional Interests Cardiovascular disease remains the leading cause of death in United States. Apolipoprotein A-I (apoA-I) is the major protein in high-density lipoprotein (HDL) and plays a vital role during the process of reverse cholesterol transport (RCT). Knowledge of the high-resolution structure of full-length apoA-I is essential for a molecular understanding of the function of HDL at various steps during the RCT pathway. Due to the flexible nature of apoA-I and inherent aggregation properties, the structure of full-length apoA-I has evaded description for over three decades. We use the techniques of modern molecular biophysics and structural biology to study the structure and function of apoA-I. We primarily rely on protein crystallography and molecular modeling coupled with SAXS to study the structure of apoA-I. In addition, circular dichroism, fluorescence microscope, electron microscopy, NMR and cellular assay are used to understand the function of apoA-I.

One or more keywords matched the following items that are connected to Mei, Xiaohu

Item TypeName
Concept Amyloid
Concept Protein Binding
Concept Protein Conformation
Concept Protein Processing, Post-Translational
Concept Protein Structure, Secondary
Concept Protein Structure, Tertiary
Concept Protein Folding
Concept Protein Structure, Quaternary
Concept Mutant Proteins
Concept Protein Multimerization
Concept Protein Stability
Concept Protein Unfolding
Concept Protein Aggregation, Pathological
Academic Article Crystal structure of C-terminal truncated apolipoprotein A-I reveals the assembly of high density lipoprotein (HDL) by dimerization.
Academic Article The crystal structure of the C-terminal truncated apolipoprotein A-I sheds new light on amyloid formation by the N-terminal fragment.
Academic Article Structural basis for distinct functions of the naturally occurring Cys mutants of human apolipoprotein A-I.
Academic Article Binding of human apoA-I[K107del] variant to TG-rich particles: implications for mechanisms underlying hypertriglyceridemia.
Academic Article Surface behavior of apolipoprotein A-I and its deletion mutants at model lipoprotein interfaces.
Academic Article Amyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing - a common mechanism of apolipoprotein A-I misfolding in familial amyloidosis and atherosclerosis.
Academic Article Lipid-free Apolipoprotein A-I Structure: Insights into HDL Formation and Atherosclerosis Development.
Academic Article Structural Stability and Local Dynamics in Disease-Causing Mutants of Human Apolipoprotein A-I: What Makes the Protein Amyloidogenic?
Academic Article Probing the C-terminal domain of lipid-free apoA-I demonstrates the vital role of the H10B sequence repeat in HDL formation.
Academic Article Structural stability and local dynamics in disease-causing mutants of human apolipoprotein a-I: what makes the protein amyloidogenic?
Academic Article A consensus model of human apolipoprotein A-I in its monomeric and lipid-free state.
Academic Article N-terminal mutation of apoA-I and interaction with ABCA1 reveal mechanisms of nascent HDL biogenesis.

Highlights
Search Criteria
  • Protein
  • misfolding
  • amyloid
  • diseases