Dimos Kapetis

Correction to: Non-extensitivity and criticality of atomic hydropathicity around a voltage-gated sodium channel’s pore: a modeling study

Markos N. Xenakis, Dimos Kapetis, Yang Yang, Jordi Heijman et autres

nl, it, us (code pays fourni par la source)

Hydropathicity-based prediction of pain-causing NaV1.7 variants

Markos N. Xenakis, Dimos Kapetis, Yang Yang, Monique M. Gerrits et autres

BACKGROUND: Mutation-induced variations in the functional architecture of the NaV1.7 channel protein are causally related to a broad spectrum of human pain disorders. Predicting in silico the phenotype of NaV1.7 variant is of major clinical importance; it can aid in reducing costs …

nl, it, us (code pays fourni par la source)

Non-extensitivity and criticality of atomic hydropathicity around a voltage-gated sodium channel’s pore: a modeling study

Markos N. Xenakis, Dimos Kapetis, Yang Yang, Jordi Heijman et autres

Voltage-gated sodium channels (NavChs) are pore-forming membrane proteins that regulate the transport of sodium ions through the cell membrane. Understanding the structure and function of NavChs is of major biophysical, as well as clinical, importance given their key role in cellular pathophysiology. …

nl, it, us (code pays fourni par la source)

Hydropathicity-Based Prediction of Pain-Causing NaV1.7 Variants

Markos N. Xenakis, Dimos Kapetis, Yang Yang, Monique M. Gerrits et autres

Abstract Background: Mutation-induced variations in the functional architecture of the NaV1.7 channel protein are causally related to a broad spectrum of human pain disorders. Predicting in silico the phenotype of NaV1.7 variant is of major clinical importance; it can aid in reducing …

nl, it, us (code pays fourni par la source)

Cumulative hydropathic topology of a voltage‐gated sodium channel at atomic resolution

Markos N. Xenakis, Dimos Kapetis, Yang Yang, Jordi Heijman et autres

Voltage-gated sodium channels (NavChs) are biological pores that control the flow of sodium ions through the cell membrane. In humans, mutations in genes encoding NavChs can disrupt physiological cellular activity thus leading to a wide spectrum of diseases. Here, we present a …

nl, it, us (code pays fourni par la source)

The transcriptome of cell cultures derived from muscle biopsies of controls and spastic patients is affected by botulinum toxin type A

Marina Mora, Simona Zanotti, Dimos Kapetis, Sara Gibertini et autres

it (code pays fourni par la source)

Botulinum toxin type A affects the transcriptome of cell cultures derived from muscle biopsies of controls and spastic patients

Simona Zanotti, Dimos Kapetis, Sara Gibertini, Franco Salerno et autres

it (code pays fourni par la source)

Network topology of NaV1.7 mutations in sodium channel-related painful disorders

Dimos Kapetis, Jenny Sassone, Yang Yang, Barbara Galbardi et autres

Gain-of-function mutations in SCN9A gene that encodes the voltage-gated sodium channel NaV1.7 have been associated with a wide spectrum of painful syndromes in humans including inherited erythromelalgia, paroxysmal extreme pain disorder and small fibre neuropathy. These mutations change the biophysical properties of …

it, us, nl, fr (code pays fourni par la source)

Additional file 15: S5. of Network topology of NaV1.7 mutations in sodium channel-related painful disorders

Dimos Kapetis, Jenny Sassone, Yang Yang, Barbara Galbardi et autres

YASARA. Structural modelling of V1267 NaV1.7 variant and their interatomic bonds. (SCE 706Â kb)

Additional file 13: S4. of Network topology of NaV1.7 mutations in sodium channel-related painful disorders

Dimos Kapetis, Jenny Sassone, Yang Yang, Barbara Galbardi et autres

YASARA. Structural modelling of H858 NaV1.7 variant and their interatomic bonds. (SCE 775Â kb)

Additional file 12: S3. of Network topology of NaV1.7 mutations in sodium channel-related painful disorders

Dimos Kapetis, Jenny Sassone, Yang Yang, Barbara Galbardi et autres

YASARA. Structural modelling of L858 NaV1.7 variant and their interatomic bonds. (SCE 707Â kb)

Additional file 10: S1. of Network topology of NaV1.7 mutations in sodium channel-related painful disorders

Dimos Kapetis, Jenny Sassone, Yang Yang, Barbara Galbardi et autres

YASARA. Structural modelling of F216 NaV1.7 variant and their interatomic bonds. (SCE 709Â kb)