2026-08-29T14:07:54Zhttps://repisalud.isciii.es/rest/oai/request

oai:repisalud.isciii.es:20.500.12105/258692025-12-18T12:56:49Zcom_20.500.12105_19586com_20.500.12105_2202col_20.500.12105_19587

00925njm 22002777a 4500 dc Lozano-Prieto, Marta author Camafeita, Emilio author Jorge, Inmaculada author Laguillo-Gómez, Andrea author Barrero-Rodríguez, Rafael author Devesa, Cristina A author Pertusa, Clara author Calvo, Enrique author Sánchez-Madrid, Francisco author Vázquez, Jesús author Martin-Cofreces, Noa B author 2024-07-30 Mass-tolerant open search methods allow the high-throughput analysis of modified peptides by mass spectrometry. These techniques have paved the way to unbiased analysis of post-translational modifications in biological contexts, as well as of chemical modifications produced during the manipulation of protein samples. In this work, we have analyzed in-depth a wide variety of samples of different biological origin, including cells, extracellular vesicles, secretomes, centrosomes and tissue preparations, using Comet-ReCom, a recently improved version of the open search engine Comet-PTM. Our results demonstrate that glutamic acid residues undergo intensive methyl esterification when protein digestion is performed using in-gel techniques, but not using gel-free approaches. This effect was highly specific to Glu and was not found for other methylable residues such as Asp. J Proteomics. 2024 Jul 30:304:105229. Journal of Proteomics 38880355 https://hdl.handle.net/20.500.12105/25869 Closed search Open search Post-translational modification Proteomics Systems biology In-gel protein digestion using acidic methanol produces a highly selective methylation of glutamic acid residues.