All Outputs (3)

The mammalian unfolded protein response (2005)
Journal Article
Schröder, M., & Kaufman, R. (2005). The mammalian unfolded protein response. Annual Review of Biochemistry, 74, 739-789

In the endoplasmic reticulum (ER) secretory and transmembrane proteins fold into their native conformation and undergo posttranslational modifications important for their activity and structure. When protein folding in the ER is inhibited, signal tra... Read More about The mammalian unfolded protein response.

ER stress signalling by regulated splicing: IRE1/HAC1/XBP1 (2005)
Journal Article
Back, S., Schröder, M., Lee, K., Zhang, K., & Kaufman, R. (2005). ER stress signalling by regulated splicing: IRE1/HAC1/XBP1. Methods, 35(4), 395-416. https://doi.org/10.1016/j.ymeth.2005.03.001

The endoplasmic reticulum (ER) serves many specialized functions in the cell including calcium storage and gated release, biosynthesis of membrane and secretory proteins, and production of lipids and sterols. Therefore, the ER integrates many interna... Read More about ER stress signalling by regulated splicing: IRE1/HAC1/XBP1.

ER stress and the unfolded protein response (2005)
Journal Article
Schröder, M., & Kaufman, R. (2005). ER stress and the unfolded protein response. Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis, 569(1-2), 29-63. https://doi.org/10.1016/j.mrfmmm.2004.06.056

Conformational diseases are caused by mutations altering the folding pathway or final conformation of a protein. Many conformational diseases are caused by mutations in secretory proteins and reach from metabolic diseases, e.g. diabetes, to developme... Read More about ER stress and the unfolded protein response.