Endogenous modulators of neurotrophin signaling: Landscape of the transient ATP-NGF interactions

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

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dad8b1ec3a685ab9524b7c239670f5be
https://doi.org/10.1016/j.csbj.2021.05.009

Conformational triggers associated with influenza matrix protein 1 polymerization

Autor: Jolyon K. Claridge, Jason R. Schnell, Faiz Mohd-Kipli, Alex Jiang, Jelena Habjanič

Publikováno v: The Journal of Biological Chemistry

A central role for the influenza matrix protein 1 (M1) is to form a polymeric coat on the inner leaflet of the host membrane that ultimately provides shape and stability to the virion. M1 polymerizes upon binding membranes, but triggers for conversio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f2511df3f85af9fd3f946220a7f2382
https://doi.org/10.1016/j.jbc.2021.100316

The muscle-relaxing C-terminal peptide from troponin I populates a nascent helix, facilitating binding to tropomyosin with a potent therapeutic effect

Autor: Han-Zhong Feng, Felipe Hornos, Jian Ping Jin, Martina Palomino-Schätzlein, Bruno Rizzuti, José L. Neira, David F. Wieczorek

Publikováno v: Zaguán. Repositorio Digital de la Universidad de Zaragoza
instname
Zaguán: Repositorio Digital de la Universidad de Zaragoza
Universidad de Zaragoza
JOURNAL OF BIOLOGICAL CHEMISTRY
r-CIPF. Repositorio Institucional Producción Científica del Centro de Investigación Principe Felipe (CIPF)
Universitat Rovira i virgili (URV)
The Journal of Biological Chemistry

The conserved C-terminal end segment of troponin I (TnI) plays a critical role in regulating muscle relaxation. This function is retained in the isolated C-terminal 27 amino acid peptide (residues 184-210) of human cardiac TnI (HcTnI-C27): When added

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::009fc79036334ac9d5af5ed53edbd703
http://zaguan.unizar.es/record/101648

Peptidoglycan binding by a pocket on the accessory NTF2-domain of Pgp2 directs helical cell shape of Campylobacter jejuni

Autor: Martin E. Tanner, Jacob A. Brockerman, Chang Sheng-Huei Lin, Jean-Pierre Simorre, Erin C. Gaynor, Jenny Vermeulen, Lawrence P. McIntosh, Anson C. K. Chan, Arvind Soni, Michael E. P. Murphy

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, 2021, 296, pp.100528. ⟨10.1016/j.jbc.2021.100528⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2021, 296, pp.100528. ⟨10.1016/j.jbc.2021.100528⟩
The Journal of Biological Chemistry

International audience; The helical morphology of Campylobacter jejuni, a bacterium involved in host gut colonization and pathogenesis in humans, is determined by the structure of the peptidoglycan (PG) layer. This structure is dictated by trimming o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d0e0e23388d36bc0f74269c64db3c73
https://hal.science/hal-03328690

Biophysical characterization of the ETV6 PNT domain polymerization interfaces

Autor: Mark Okon, Michael E. P. Murphy, Lawrence P. McIntosh, Michel Roberge, Chloe A. N. Gerak, Sophia Y. Cho, Maxim Kolesnikov, Richard B. Sessions

Publikováno v: The Journal of Biological Chemistry
et al. 2021, ' Biophysical characterization of the ETV6 PNT domain polymerization interfaces ', Journal of Biological Chemistry, vol. 296, 100284 . https://doi.org/10.1016/j.jbc.2021.100284

ETV6 is an E26 transformation specific family transcriptional repressor that self-associates by its PNT domain to facilitate cooperative DNA binding. Chromosomal translocations frequently generate constitutively active oncoproteins with the ETV6 PNT

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::417827eebb9108a5ecca46d54baa0d8e
https://doi.org/10.1101/2020.08.21.262121