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pro vyhledávání: '"NGF interactions"'
Autor:
Francesca Paoletti, Franci Merzel, Alberto Cassetta, Iza Ogris, Sonia Covaceuszach, Jože Grdadolnik, Doriano Lamba, Simona Golič Grdadolnik
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss , Pp 2938-2949 (2021)
The Nerve Growth Factor (NGF) neurotrophin acts in the maintenance and growth of neuronal populations. Despite the detailed knowledge of NGF’s role in neuron physiology, the structural and mechanistic determinants of NGF bioactivity modulated by es
Externí odkaz:
https://doaj.org/article/0e69f71ab9aa45d18dd7e75feb7b36e5
Autor:
Doriano Lamba, Sonia Covaceuszach, Franci Merzel, Alberto Cassetta, Francesca Paoletti, Simona Golic Grdadolnik, Iza Ogris, Jože Grdadolnik
Publikováno v:
Computational and Structural Biotechnology Journal 19 (2021): 2938–2949. doi:10.1016/j.csbj.2021.05.009
info:cnr-pdr/source/autori:Paoletti F.; Merzel F.; Cassetta A.; Ogris I.; Covaceuszach S.; Grdadolnik J.; Lamba D.; Golic Grdadolnik S./titolo:Endogenous modulators of neurotrophin signaling: Landscape of the transient ATP-NGF interactions/doi:10.1016%2Fj.csbj.2021.05.009/rivista:Computational and Structural Biotechnology Journal/anno:2021/pagina_da:2938/pagina_a:2949/intervallo_pagine:2938–2949/volume:19
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 2938-2949 (2021)
Computational and Structural Biotechnology Journal
info:cnr-pdr/source/autori:Paoletti F.; Merzel F.; Cassetta A.; Ogris I.; Covaceuszach S.; Grdadolnik J.; Lamba D.; Golic Grdadolnik S./titolo:Endogenous modulators of neurotrophin signaling: Landscape of the transient ATP-NGF interactions/doi:10.1016%2Fj.csbj.2021.05.009/rivista:Computational and Structural Biotechnology Journal/anno:2021/pagina_da:2938/pagina_a:2949/intervallo_pagine:2938–2949/volume:19
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 2938-2949 (2021)
Computational and Structural Biotechnology Journal
Graphical abstract
Highlights • High-resolution solution NMR structure of rhNGF has been determined. • Quinary interactions characterize ATP binding to rhNGF. • SPR, ITC and STD-NMR reveal ATP binding to rhNGF with mM affinity. • NMR and
Highlights • High-resolution solution NMR structure of rhNGF has been determined. • Quinary interactions characterize ATP binding to rhNGF. • SPR, ITC and STD-NMR reveal ATP binding to rhNGF with mM affinity. • NMR and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dad8b1ec3a685ab9524b7c239670f5be
https://doi.org/10.1016/j.csbj.2021.05.009
https://doi.org/10.1016/j.csbj.2021.05.009
Akademický článek
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