In silico derived small molecules targeting the finger-finger interaction between the histone lysine methyltransferase NSD1 and Nizp1 repressor

Autor: Andrea Berardi, Michela Ghitti, Giovanna Musco, Giacomo Quilici

Publikováno v: Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal, Vol 18, Iss, Pp 4082-4092 (2020)

Graphical abstract
PHD fingers are small chromatin binding domains, that alone or in tandem work as versatile interaction platforms for diversified activities, ranging from the decoding of the modification status of histone tails to the specific

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8156c5f89e960b8b8b4491de62254aa5
http://europepmc.org/articles/PMC7736721

The lipopolysaccharide-transporter complex LptB2FG also displays adenylate kinase activity in vitro dependent on the binding partners LptC/LptA

Autor: Cédric Laguri, Isabel Ayala, Karine Giandoreggio-Barranco, Jean-Pierre Simorre, Tiago Baeta, Paola Sperandeo, Elisabete C.C. M. Moura, Alessandra Polissi

Publikováno v: The Journal of Biological Chemistry
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2021, pp.101313. ⟨10.1016/j.jbc.2021.101313⟩
Journal of Biological Chemistry, 2021, pp.101313. ⟨10.1016/j.jbc.2021.101313⟩

Lipopolysaccharide (LPS) is an essential glycolipid that covers the surface of gram-negative bacteria. The transport of LPS involves a dedicated seven-protein transporter system called the lipopolysaccharide transport system (Lpt) machinery that phys

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::018f1cad516d0bb6de3e883a7812f6f8
http://europepmc.org/articles/PMC8633020

Self-acetylation at the active site of phosphoenolpyruvate carboxykinase (PCK1) controls enzyme activity

Autor: Thomas Hicks, Adrián Velázquez-Campoy, Jesús Angulo, Alexis J. Lawton, Pedro Latorre-Muro, John M. Denu, Cristina Hernández-Ruiz, Josue Baeza, Ignacio Delso, José Alberto Carrodeguas, Ramon Hurtado-Guerrero

Publikováno v: Latorre-Muro, P, Baeza, J, Hurtado-Guerrero, R, Hicks, T, Delso, I, Hernández-Ruiz, C, Velázquez-Campoy, A, Lawton, A J, Angulo, J, Denu, J M & Carrodeguas, J A 2021, ' Self-acetylation at the active site of phosphoenolpyruvate carboxykinase (PCK1) controls enzyme activity ', Journal of Biological Chemistry, vol. 296, 100205 . https://doi.org/10.1074/jbc.RA120.015103
Digital.CSIC. Repositorio Institucional del CSIC
instname
idUS: Depósito de Investigación de la Universidad de Sevilla
Universidad de Sevilla (US)
idUS. Depósito de Investigación de la Universidad de Sevilla
The Journal of Biological Chemistry

Acetylation is known to regulate the activity of cytosolic phosphoenolpyruvate carboxykinase (PCK1), a key enzyme in gluconeogenesis, by promoting the reverse reaction of the enzyme (converting phosphoenolpyruvate to oxaloacetate). It is also known t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e83e207f9e31506752cd94b38dcddcdf
http://hdl.handle.net/10261/261527

Insights into the regulation of eukaryotic elongation factor 2 kinase and the interplay between its domains

Autor: Christopher G. Proud, Stephen J. Finn, Claire E. Moore, Craig R. Pigott, Halina Mikolajek, Curtis W. Phippen, Jörn M. Werner

Publikováno v: Biochemical Journal

eEF2K (eukaryotic elongation factor 2 kinase) is a Ca2+/CaM (calmodulin)-dependent protein kinase which regulates the translation elongation machinery. eEF2K belongs to the small group of so-called ‘α-kinases’ which are distinct from the main eu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b83b3c623a49b85e69e1d150671e99ab
https://pubmed.ncbi.nlm.nih.gov/22115317

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

Autor: Paoletti F; Laboratory for Molecular Structural Dynamics, Theory Department, National Institute of Chemistry, Hajdrihova 19, SI-1001 Ljubljana, Slovenia., Merzel F; Laboratory for Molecular Structural Dynamics, Theory Department, National Institute of Chemistry, Hajdrihova 19, SI-1001 Ljubljana, Slovenia., Cassetta A; Institute of Crystallography - C.N.R.- Trieste Outstation. Area Science Park - Basovizza, S.S.14 - Km. 163.5, I-34149 Trieste, Italy., Ogris I; Laboratory for Molecular Structural Dynamics, Theory Department, National Institute of Chemistry, Hajdrihova 19, SI-1001 Ljubljana, Slovenia., Covaceuszach S; Institute of Crystallography - C.N.R.- Trieste Outstation. Area Science Park - Basovizza, S.S.14 - Km. 163.5, I-34149 Trieste, Italy., Grdadolnik J; Laboratory for Molecular Structural Dynamics, Theory Department, National Institute of Chemistry, Hajdrihova 19, SI-1001 Ljubljana, Slovenia., Lamba D; Institute of Crystallography - C.N.R.- Trieste Outstation. Area Science Park - Basovizza, S.S.14 - Km. 163.5, I-34149 Trieste, Italy.; Interuniversity Consortium 'Biostructures and Biosystems National Institute', Viale delle Medaglie d'Oro 305, I-00136 Roma, Italy., Golič Grdadolnik S; Laboratory for Molecular Structural Dynamics, Theory Department, National Institute of Chemistry, Hajdrihova 19, SI-1001 Ljubljana, Slovenia.

Publikováno v: Computational and structural biotechnology journal [Comput Struct Biotechnol J] 2021 May 07; Vol. 19, pp. 2938-2949. Date of Electronic Publication: 2021 May 07 (Print Publication: 2021).