Cell Survival Enabled by Leakage of a Labile Metabolic Intermediate.

Autor: Medina-Carmona, Encarnación, Gutierrez-Rus, Luis I, Manssour-Triedo, Fadia, Newton, Matilda S, Gamiz-Arco, Gloria, Mota, Antonio J, Reiné, Pablo, Cuerva, Juan Manuel, Ortega-Muñoz, Mariano, Andrés-León, Eduardo, Ortega-Roldan, Jose Luis, Seelig, Burckhard, Ibarra-Molero, Beatriz, Sanchez-Ruiz, Jose M

Publikováno v: Molecular Biology & Evolution; Mar2023, Vol. 40 Issue 3, p1-22, 22p

Characterizing Protein-Protein Interactions Using Solution NMR Spectroscopy

Autor: Ortega-Roldan , Jose Luis, Blackledge , Martin, Jensen , Malene Ringkjøbing

Publikováno v: Methods in Molecular Biology
Methods in Molecular Biology, Humana Press/Springer Imprint, 2018, 1764, pp.73-85. ⟨10.1007/978-1-4939-7759-8_5⟩
Methods in Molecular Biology, 2018, 1764, pp.73-85. ⟨10.1007/978-1-4939-7759-8_5⟩
Methods in molecular biology (Clifton, N.J.)
Methods in molecular biology (Clifton, N.J.), 2018, 1764, pp.73-85. 〈10.1007/978-1-4939-7759-8_5〉

International audience; In this chapter, we describe how NMR chemical shift titrations can be used to study the interaction between two proteins with emphasis on mapping the interface of the complex and determining the binding affinity from a quantit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::3b3a7812d7b8e5792e9523ea24a8b908
https://hal.archives-ouvertes.fr/hal-01807808

Solution NMR studies reveal the location of the second transmembrane domain of the human sigma-1 receptor

Autor: Ortega-Roldan, Jose Luis, Ossa, Felipe, Amin, Nader T., Schnell, Jason R.

Publikováno v: In FEBS Letters 27 February 2015 589(5):659-665

Characterizing weak protein-protein complexes by NMR residual dipolar couplings

Autor: Ringkjøbing Jensen, Malene, Ortega Roldan, Jose Luis, Salmon, Loic, Van Nuland, Nico, Blackledge, Martin

Protein-protein interactions occur with a wide range of affinities from tight complexes characterized by femtomolar dissociation constants to weak, and more transient, complexes of millimolar affinity. Many of the weak and transiently formed protein-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3848::e3d345334a277ce14427126f96159f7d
https://biblio.vub.ac.be/vubir/characterizing-weak-proteinprotein-complexes-by-nmr-residual-dipolar-couplings(799c2086-cb35-4544-9383-db4b66a4ab18).html

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