Phosphorylation of Thr9 Affects the Folding Landscape of the N-Terminal Segment of Human AGT Enhancing Protein Aggregation of Disease-Causing Mutants

Autor: Jose L. Neira, Athi N. Naganathan, Noel Mesa-Torres, Eduardo Salido, Angel L. Pey

Publikováno v: Molecules, Vol 27, Iss 24, p 8762 (2022)

The mutations G170R and I244T are the most common disease cause in primary hyperoxaluria type I (PH1). These mutations cause the misfolding of the AGT protein in the minor allele AGT-LM that contains the P11L polymorphism, which may affect the foldin

Externí odkaz: https://doaj.org/article/70acc055b13a40a58a70307115ca250f

Molecular Recognition of PTS-1 Cargo Proteins by Pex5p: Implications for Protein Mistargeting in Primary Hyperoxaluria

Autor: Noel Mesa-Torres, Nenad Tomic, Armando Albert, Eduardo Salido, Angel L. Pey

Publikováno v: Biomolecules, Vol 5, Iss 1, Pp 121-141 (2015)

Peroxisomal biogenesis and function critically depends on the import of cytosolic proteins carrying a PTS1 sequence into this organelle upon interaction with the peroxin Pex5p. Recent structural studies have provided important insights into the molec

Externí odkaz: https://doaj.org/article/1bcf810147104784bfadbf1289225d25

Determination of Ligand Profiles for Pseudomonas aeruginosa Solute Binding Proteins

Autor: Matilde Fernández, Miriam Rico-Jiménez, Álvaro Ortega, Abdelali Daddaoua, Ana Isabel García García, David Martín-Mora, Noel Mesa Torres, Ana Tajuelo, Miguel A. Matilla, Tino Krell

Publikováno v: International Journal of Molecular Sciences, Vol 20, Iss 20, p 5156 (2019)

Solute binding proteins (SBPs) form a heterogeneous protein family that is found in all kingdoms of life. In bacteria, the ligand-loaded forms bind to transmembrane transporters providing the substrate. We present here the SBP repertoire of Pseudomon

Externí odkaz: https://doaj.org/article/d837f68735fa4488a7f5c7f0fa5f8ccc

Phosphorylation compromises FAD binding and intracellular stability of wild-type and cancer-associated NQO1: Insights into flavo-proteome stability

Autor: Noel Mesa-Torres, Rubén Martín-Escolano, Angel L. Pey, José L. Neira, Encarnación Medina-Carmona, Rita Guzzi, Juan Luis Pacheco-Garcia, Bruno Rizzuti

Publikováno v: International Journal of Biological Macromolecules. 125:1275-1288

Over a quarter million of protein phosphorylation sites have been identified so far, although the effects of site-specific phosphorylation on protein function and stability, as well as their possible impact in the phenotypic manifestation in genetic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25280a761415d41841ec2a8fd4976561
https://doi.org/10.1016/j.ijbiomac.2018.09.108

Insight into the specificity and severity of pathogenic mechanisms associated with missense mutations through experimental and structural perturbation analyses

Autor: Noel Mesa-Torres, Salvador Ventura, Cristina Batlle, Encarnación Medina-Carmona, Elisa Oppici, Barbara Cellini, Athi N. Naganathan, Isabel Betancor-Fernández, Silvia Grottelli, Eduardo Salido, Angel L. Pey, Jaime Santos

Publikováno v: HUMAN MOLECULAR GENETICS
r-FSJD. Repositorio Institucional de Producción Científica de la Fundació Sant Joan de Déu
instname
r-FSJD: Repositorio Institucional de Producción Científica de la Fundació Sant Joan de Déu
Fundació Sant Joan de Déu

Most pathogenic missense mutations cause specific molecular phenotypes through protein destabilization. However, how protein destabilization is manifested as a given molecular phenotype is not well understood. We develop here a structural and energet

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a18408fdb2abd5f22b38d4ee636bfda
https://doi.org/10.1093/hmg/ddy323