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21 in total

1. Stochastic simulation of structural properties of natively unfolded and denatured proteins.

Authors: David Curcó; Catherine Michaux; Guillaume Roussel; Emmanuel Tinti; Eric A Perpète; Carlos Alemán
Journal: J Mol Model Date: 2012-05-29 Impact factor: 1.810

2. Allostery in a disordered protein: oxidative modifications to α-synuclein act distally to regulate membrane binding.

Authors: Eva Sevcsik; Adam J Trexler; Joanna M Dunn; Elizabeth Rhoades
Journal: J Am Chem Soc Date: 2011-04-14 Impact factor: 15.419

Review 3. 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.

Authors: Orkid Coskuner-Weber; Vladimir N Uversky
Journal: Int J Mol Sci Date: 2018-01-24 Impact factor: 5.923

Review 4. Amyloidogenesis of Tau protein.

Authors: Bartosz Nizynski; Wojciech Dzwolak; Krzysztof Nieznanski
Journal: Protein Sci Date: 2017-09-13 Impact factor: 6.725

5. p15PAF is an intrinsically disordered protein with nonrandom structural preferences at sites of interaction with other proteins.

Authors: Alfredo De Biasio; Alain Ibáñez de Opakua; Tiago N Cordeiro; Maider Villate; Nekane Merino; Nathalie Sibille; Moreno Lelli; Tammo Diercks; Pau Bernadó; Francisco J Blanco
Journal: Biophys J Date: 2014-02-18 Impact factor: 4.033

Amino acid bulkiness defines the local conformations and dynamics of natively unfolded alpha-synuclein and tau.

1. Stochastic simulation of structural properties of natively unfolded and denatured proteins.

2. Allostery in a disordered protein: oxidative modifications to α-synuclein act distally to regulate membrane binding.

Review 3. 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.

Review 4. Amyloidogenesis of Tau protein.

5. p15PAF is an intrinsically disordered protein with nonrandom structural preferences at sites of interaction with other proteins.

Review 6. Exploring the accessible conformations of N-terminal acetylated α-synuclein.

7. Sequence feature-based prediction of protein stability changes upon amino acid substitutions.

8. The loss of inhibitory C-terminal conformations in disease associated P123H β-synuclein.

9. Residual structure, backbone dynamics, and interactions within the synuclein family.

10. Probing the urea dependence of residual structure in denatured human alpha-lactalbumin.