Genome sequence of a diabetes-prone rodent reveals a mutation hotspot around the ParaHox gene cluster

Autor: Kyle Serikawa, Peter W. H. Holland, John F Mulley, Adam D Hargreaves, Guojie Zhang, Peter Gildsig Jansen, Ferdinand Marlétaz, Brian A. Fox, Signe Vendelbo Horn Pedersen, R. Scott Heller, Matilde Thye Hansen, Enrico Spiga, Shiping Liu, William R. Taylor, Long Zhou, Fang Li, Josef Christensen, Shameek Biswas

Publikováno v: Hargreaves, A D, Zhou, L, Christensen, J, Marlétaz, F, Liu, S, Li, F, Jansen, P G, Spiga, E, Hansen, M T, Pedersen, S V H, Biswas, S, Serikawa, K, Fox, B A, Taylor, W R, Mulley, J F, Zhang, G, Heller, R S & Holland, P W H 2017, ' Genome sequence of a diabetes-prone rodent reveals a mutation hotspot around the ParaHox gene cluster ', Proceedings of the National Academy of Sciences of the United States of America, vol. 114, no. 29, pp. 7677-7682 . https://doi.org/10.1073/pnas.1702930114

Significance A core question in evolutionary biology is how mutation and selection adapt and constrain species to specialized habitats. We sequenced the genome of the sand rat, a desert rodent susceptible to nutritionally induced diabetes, and discov

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::841ca8d9c38b5c1b7001062aa9c8fd81
https://curis.ku.dk/portal/da/publications/genome-sequence-of-a-diabetesprone-rodent-reveals-a-mutation-hotspot-around-the-parahox-gene-cluster(d7dbe76b-ad99-45e5-b233-0a905ab723ea).html

Electrostatic-Consistent Coarse-Grained Potentials for Molecular Simulations of Proteins

Autor: Davide Alemani, Matteo T. Degiacomi, Enrico Spiga, Michele Cascella, Matteo Dal Peraro

Publikováno v: JOURNAL OF CHEMICAL THEORY AND COMPUTATION

We present a new generation of coarse-grained (CG) potentials that account for a simplified electrostatic description of soluble proteins. The treatment of permanent electrostatic dipoles of the backbone and polar side-chains allows to simulate prote

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::419dd119ae6406afc0eddbbda9d6c767
https://doi.org/10.1021/ct400137q

Facilitated Permeation of Antibiotics across Membrane Channels − Interaction of the Quinolone Moxifloxacin with the OmpF Channel

Autor: Patrícia Neves, Tivadar Mach, Matteo Ceccarelli, Helge Weingart, Mathias Winterhalter, Enrico Spiga, Paula Gameiro, Paolo Ruggerone

Publikováno v: Journal of the American Chemical Society
130 (2008): 13301–13309. doi:10.1021/ja803188c
info:cnr-pdr/source/autori:Mach, T; Neves, P; Spiga, E; Weingart, H; Winterhalter, M; Ruggerone, P; Ceccarelli, M; Gameiro, P/titolo:Facilitated permeation of antibiotics across membrane channels-Interaction of the quinolone moxifloxacin with the OmpF channel/doi:10.1021%2Fja803188c/rivista:Journal of the American Chemical Society (Print)/anno:2008/pagina_da:13301/pagina_a:13309/intervallo_pagine:13301–13309/volume:130

The facilitated influx of moxifloxacin through the most abundant channel in the outer cell wall of gram-negative bacteria was investigated. Molecular modeling provided atomic details of the interaction with the channel surface, revealed the preferred

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82e305951c2384d570226bdf27a8d43e
https://doi.org/10.1021/ja803188c

Dissecting the effects of concentrated carbohydrate solutions on protein diffusion, hydration, and internal dynamics

Autor: Enrico Spiga, Luciano A. Abriata, Matteo Dal Peraro, Francesco Piazza

Publikováno v: Journal of Physical Chemistry B
Journal of Physical Chemistry B, American Chemical Society, 2014, 118 (20), pp.5310-5321
JOURNAL OF PHYSICAL CHEMISTRY B

International audience; We present herein a thorough description of the effects of high glucose concentrations on the diffusion, hydration and internal dynamics of ubiquitin, as predicted from extensive molecular dynamics simulations on several syste

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3525329c9bba18bbbea7bb8bdc727ea
https://pubmed.ncbi.nlm.nih.gov/24773474

Structure-Function Paradigm in Human Myoglobin: How a Single-Residue Substitution Affects NO Reactivity at Low pO(2)

Autor: Matteo Ceccarelli, Alessandra Vezzoli, Bruno Fink, Simona Mrakic-Sposta, Maristella Gussoni, Enrico Spiga, Mariano Casu, Rosaria Russo, Mariano Andrea Scorciapino

Publikováno v: Journal of the American Chemical Society
135 (2013): 7534–7544. doi:10.1021/ja400213t
info:cnr-pdr/source/autori:Scorciapino, M.A.; Spiga, E.; Vezzoli, A.; Mrakic-Sposta, S.;Russo, R.; Fink, B.; Casu, M.; Gussoni, M.; Ceccarelli, M./titolo:Structure-Function Paradigm in Human Myoglobin: How a Single-Residue Substitution Affects NO Reactivity at Low pO(2)/doi:10.1021%2Fja400213t/rivista:Journal of the American Chemical Society (Print)/anno:2013/pagina_da:7534/pagina_a:7544/intervallo_pagine:7534–7544/volume:135
Journal of the American Chemical Society (Online) 135 (2013): 7534–7544. doi:10.1021/ja400213t
info:cnr-pdr/source/autori:Mariano Andrea Scorciapino; Enrico Spiga*; Alessandra Vezzoli; Simona Mrakic-Sposta; Rosaria Russo; Bruno Fink; Mariano Casu; Maristella Gussoni; Matteo Ceccarelli./titolo:Structure-function paradigm in Human Myoglobin: how a single-residue substitution affects NO reactivity at low pO2./doi:10.1021%2Fja400213t/rivista:Journal of the American Chemical Society (Online)/anno:2013/pagina_da:7534/pagina_a:7544/intervallo_pagine:7534–7544/volume:135

This work is focused on the two more expressed human myoglobin isoforms. In the literature, their different overexpression in high-altitude natives was proposed to be related to alternative/complementary functions in hypoxia. Interestingly, they diff

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52d1809006452b04546b579dd938c3b2