Lista de obras - Miguel Mompeán - Dominio Público Uruguay

"Structural characterization of the minimal segment of TDP-43 competent for aggregation".

artículo científico

An Amyloid-Like Pathological Conformation of TDP-43 Is Stabilized by Hypercooperative Hydrogen Bonds

artículo científico publicado en 2016

Combining Classical MD and QM calculations to elucidate complex system nucleation: a twisted, three-stranded, parallel β-sheet seeds amyloid fibril conception.

artículo científico publicado en 2014

Complex System Assembly Underlies a Two-Tiered Model of Highly Delocalized Electrons.

artículo científico publicado en 2016

Dysregulation of TDP-43 intracellular localization and early onset ALS are associated with a TARDBP S375G variant

artículo científico publicado en 2018

Electrostatic Repulsion Governs TDP-43 C-terminal Domain Aggregation

artículo científico publicado en 2016

Insights into protein-carbohydrate recognition: A novel binding mechanism for CBM family 43.

artículo científico publicado en 2017

Intrinsically Disordered Domains, Amyloids and Protein Liquid Phases: Evolving Concepts and Open Questions.

artículo científico publicado en 2017

Mimicry by a viral RHIM

scientific article published on 21 January 2019

NMR assignments for the C-terminal domain of human TDP-43

artículo científico publicado en 2021

Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions.

artículo científico publicado en 2017

Pushing nuclear magnetic resonance sensitivity limits with microfluidics and photo-chemically induced dynamic nuclear polarization

artículo científico publicado en 2018

SUMOylation Regulates TDP-43 Splicing Activity and Nucleocytoplasmic Distribution

artículo científico publicado en 2021

Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43.

artículo científico publicado en 2015

Structural insight into the XTACC3/XMAP215 interaction from CD and NMR studies on model peptides.

artículo científico publicado en 2017

The Singular NMR Fingerprint of a Polyproline II Helical Bundle

scientific article published on 29 November 2018

The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex.

artículo científico publicado en 2018

The TDP-43 N-terminal domain structure at high resolution

artículo científico publicado en 2016

Lista de obras de Miguel Mompeán

"Structural characterization of the minimal segment of TDP-43 competent for aggregation".

An Amyloid-Like Pathological Conformation of TDP-43 Is Stabilized by Hypercooperative Hydrogen Bonds

Combining Classical MD and QM calculations to elucidate complex system nucleation: a twisted, three-stranded, parallel β-sheet seeds amyloid fibril conception.

Complex System Assembly Underlies a Two-Tiered Model of Highly Delocalized Electrons.

Dysregulation of TDP-43 intracellular localization and early onset ALS are associated with a TARDBP S375G variant

Electrostatic Repulsion Governs TDP-43 C-terminal Domain Aggregation

Insights into protein-carbohydrate recognition: A novel binding mechanism for CBM family 43.

Intrinsically Disordered Domains, Amyloids and Protein Liquid Phases: Evolving Concepts and Open Questions.

Mimicry by a viral RHIM

NMR assignments for the C-terminal domain of human TDP-43

Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions.

Pushing nuclear magnetic resonance sensitivity limits with microfluidics and photo-chemically induced dynamic nuclear polarization

SUMOylation Regulates TDP-43 Splicing Activity and Nucleocytoplasmic Distribution

Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43.

Structural insight into the XTACC3/XMAP215 interaction from CD and NMR studies on model peptides.

The Singular NMR Fingerprint of a Polyproline II Helical Bundle

The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex.

The TDP-43 N-terminal domain structure at high resolution