N
Nelson P. Barrera
Researcher at Pontifical Catholic University of Chile
Publications - 57
Citations - 2462
Nelson P. Barrera is an academic researcher from Pontifical Catholic University of Chile. The author has contributed to research in topics: Receptor & Protein subunit. The author has an hindex of 23, co-authored 52 publications receiving 2217 citations. Previous affiliations of Nelson P. Barrera include University of Cambridge.
Papers
More filters
Journal ArticleDOI
Micelles Protect Membrane Complexes from Solution to Vacuum
TL;DR: By protecting a membrane protein complex within a n-dodecyl-β-d-maltoside micelle, a powerful strategy is demonstrated that will enable the subunit stoichiometry and ligand-binding properties of membrane complexes to be determined directly, by precise determination of the masses of intact complexes and dissociated subunits.
Journal ArticleDOI
Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding.
Min Zhou,Nina Morgner,Nelson P. Barrera,Nelson P. Barrera,Argyris Politis,Shoshanna C Isaacson,Dijana Matak-Vinkovic,Takeshi Murata,Ricardo A. Bernal,Daniela Stock,Daniela Stock,Carol V. Robinson +11 more
TL;DR: It is shown that rotary adenosine triphosphatases (ATPases)/synthases from Thermus thermophilus and Enterococcus hirae can be maintained intact with membrane and soluble subunit interactions preserved in vacuum and can link specific lipid and nucleotide binding with distinct regulatory roles.
Journal ArticleDOI
Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize.
Nelson P. Barrera,Susan J. Ormond,Robert M. Henderson,Ruth D. Murrell-Lagnado,J. Michael Edwardson +4 more
TL;DR: In this article, chemical cross-linking and direct imaging of individual P2X(2) receptors by atomic force microscopy (AFM) was conducted to confirm the presence of trimers, and the mean molecular volume of the receptor determined by AFM (409 nm(3) points to a trimeric structure.
Journal ArticleDOI
Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions
Nelson P. Barrera,Shoshanna C Isaacson,Min Zhou,Vassiliy N. Bavro,Alex Welch,Theresia A. Schaedler,Markus A. Seeger,Ricardo Núñez Miguel,Vladimir M. Korkhov,Hendrik W. van Veen,Henrietta Venter,Adrian R. Walmsley,Christopher G. Tate,Carol V. Robinson +13 more
TL;DR: A general mass spectrometry approach is described to determine subunit stoichiometry and lipid binding in intact membrane protein complexes by subjecting the complex to multiple collisions and releasing the intact complex largely devoid of detergent.
Journal ArticleDOI
Advances in the mass spectrometry of membrane proteins: from individual proteins to intact complexes.
TL;DR: Exciting possibilities now exist to go beyond primary and secondary structure to reveal the tertiary and quaternary interactions of soluble and membrane subunits within intact assemblies of more than 700 kDa.