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Ubiquitin chains: a new way of screening for regulatory differences in pulmonary hypertension

Protein ubiquitination serves many regulatory functions; in addition to degradation, ubiquitination has roles in intracellular trafficking, cell cycle, innate immunity, and more. Using mass spectrometry, it is possible to assess the ubiquitination state of every protein simultaneously. In this issue...

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Detalles Bibliográficos
Autores principales: Rathinasabapathy, Anandharajan, West, James D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: SAGE Publications 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6109854/
https://www.ncbi.nlm.nih.gov/pubmed/30124137
http://dx.doi.org/10.1177/2045894018796782
Descripción
Sumario:Protein ubiquitination serves many regulatory functions; in addition to degradation, ubiquitination has roles in intracellular trafficking, cell cycle, innate immunity, and more. Using mass spectrometry, it is possible to assess the ubiquitination state of every protein simultaneously. In this issue, Wade et al. have for the first time done just that in a hypoxic mouse model of pulmonary hypertension (PH). New techniques drive new discoveries; their work is important not just because they have found new ways to intervene in known PH-related pathways but have found regulation of proteins not previously associated with disease.