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1.
Nat Chem Biol ; 15(11): 1129, 2019 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-31439938

RESUMO

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

2.
Nat Chem Biol ; 15(8): 764-775, 2019 08.
Artigo em Inglês | MEDLINE | ID: mdl-31320759

RESUMO

Accumulation of unfolded proteins at the endoplasmic reticulum (ER) is a salient attribute of many human diseases including obesity, liver disorders, cancer, diabetes and neurodegeneration. To restore ER proteostasis, cells activate the unfolded protein response (UPR), a signaling pathway that imposes adaptive programs or triggers apoptosis of damaged cells. The UPR is critical to sustain the normal function of specialized secretory cells (i.e., pancreatic ß cells and B lymphocytes) and to control the production of lipids and cholesterol in the liver. In the context of disease, adaptive UPR responses have been linked to the growth of solid tumors, whereas chronic ER stress contributes to cell dysfunction in brain diseases, metabolic syndromes, among other conditions. Here we discuss recent developments in the design and optimization of novel compounds to manipulate UPR signaling and their efficacy in various disease models.


Assuntos
Sistemas de Liberação de Medicamentos , Transdução de Sinais , Resposta a Proteínas não Dobradas , Animais , Estresse do Retículo Endoplasmático/efeitos dos fármacos , Estresse do Retículo Endoplasmático/fisiologia , Humanos , Neoplasias/tratamento farmacológico , Neoplasias/metabolismo
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