Unfolded annealing molecular dynamics conformers for wild-type and disease-associated variants of alpha-synuclein show no propensity for beta-sheetformation

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Journal of Biophysical Chemistry

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"Unfolded annealing molecular dynamics conformers for wild-type and disease-associated variants of alpha-synuclein show no propensity for beta-sheetformation"
written by D. Balesh, Z. Ramjan, W.B. Floriano,
published by Journal of Biophysical Chemistry, Vol.2 No.2, 2011

has been cited by the following article(s):

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[6]	Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and …
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[9]	Phase transitions and structure analysis in wild-type, A30P, E46K, and A53T mutants of α-synuclein
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[10]	Early oligomerization stages for the non-amyloid component of α-synuclein amyloid
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[11]	études des premières étapes d'oligomérisation de la région Non-Aβ Component de l'a-synucléine et de Aβ1-40
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[12]	Structures and free energy landscapes of the wild-type and A30P mutant-type α-synuclein proteins with dynamics
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[14]	Structures and free energy landscapes of the A53T mutant-type α-synuclein protein and impact of A53T mutation on the structures of the wild-type α-synuclein protein …
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[15]	Characterization of the molecular interaction between α-synuclein and prion protein

[1]	In silico analysis of alpha‐synuclein protein variants and posttranslational modifications related to Parkinson's disease Journal of Cellular Biochemistry, 2024 DOI:10.1002/jcb.30523

[2]	Impact of Phosphorylation on the Physiological Form of Human alpha-Synuclein in Aqueous Solution Journal of Chemical Information and Modeling, 2024 DOI:10.1021/acs.jcim.4c01172

[3]	α-Synuclein: An All-Inclusive Trip Around its Structure, Influencing Factors and Applied Techniques Frontiers in Chemistry, 2021 DOI:10.3389/fchem.2021.666585

[4]	Insights into the Molecular Mechanisms of Alzheimer’s and Parkinson’s Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology International Journal of Molecular Sciences, 2018 DOI:10.3390/ijms19020336

[5]	Insights into the Molecular Mechanisms of Alzheimer’s and Parkinson’s Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology International Journal of Molecular Sciences, 2018 DOI:10.3390/ijms19020336

[6]	Phase transitions and structure analysis in wild-type, A30P, E46K, and A53T mutants of α-synuclein European Biophysics Journal, 2016 DOI:10.1007/s00249-015-1103-0

[7]	Early oligomerization stages for the non-amyloid component of α-synuclein amyloid The Journal of Chemical Physics, 2014 DOI:10.1063/1.4896381

[8]	Early oligomerization stages for the non-amyloid component of α-synuclein amyloid The Journal of Chemical Physics, 2014 DOI:10.1063/1.4896381

[9]	Structures and Free Energy Landscapes of the A53T Mutant-Type α-Synuclein Protein and Impact of A53T Mutation on the Structures of the Wild-Type α-Synuclein Protein with Dynamics ACS Chemical Neuroscience, 2013 DOI:10.1021/cn400041j

[10]	Structures and Free Energy Landscapes of the Wild-Type and A30P Mutant-Type α-Synuclein Proteins with Dynamics ACS Chemical Neuroscience, 2013 DOI:10.1021/cn300198q

[11]	Structures and Free Energy Landscapes of the A53T Mutant-Type α-Synuclein Protein and Impact of A53T Mutation on the Structures of the Wild-Type α-Synuclein Protein with Dynamics ACS Chemical Neuroscience, 2013 DOI:10.1021/cn400041j

[12]	Structures and Free Energy Landscapes of the Wild-Type and A30P Mutant-Type α-Synuclein Proteins with Dynamics ACS Chemical Neuroscience, 2013 DOI:10.1021/cn300198q

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