The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins.

The lumen of the endoplasmic reticulum contains a number of distinct molecular chaperones and folding factors, which modulate the folding and assembly of newly synthesized proteins and protein complexes. A subset of these luminal components are specific for glycoproteins, and, like calnexin and calreticulin, the thiol-dependent reductase ERp57 has been shown to interact specifically with soluble secretory proteins bearing N-linked carbohydrate. Calnexin and calreticulin also interact with glycosylated integral membrane proteins, and in this study we have examined the interaction of ERp57 with these substrates. As with soluble proteins, the binding of ERp57 to an integral membrane protein is dependent upon the protein bearing an N-glycan that has undergone glucose trimming. Furthermore, ERp57 binds to newly synthesized glycoproteins in combination with either calnexin or calreticulin. We propose that ERp57 acts in concert with calnexin and calreticulin to modulate glycoprotein folding and enforce the glycoprotein specific quality control mechanism operating in the endoplasmic reticulum.[1]


WikiGenes - Universities