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| | [No title] |
 | | Proper folding, post-translational modifications, and oligomerization of the secretory proteins in the endoplasmic reticulum (ER)1 are essential prerequisites for their recruitment into the transport vesicles heading toward the cell exterior (1). |
 | | Quality control of potential cargo proteins is accomplished by the molecular chaperones that monitor fidelity of the protein folding and prevent premature export of incorrectly folded or incompletely assembled secretory proteins from the ER (2). |
 | | Circumstantial evidence, such as inducibility in certain cell types under the ER stress conditions (3), high expression in the secretory tissues (4, 5), and co-localization with the ER chaperones (3), suggests that a recently discovered, ubiquitously expressed endoplasmic reticulum lumenal protein, ERp29, may complement this group of ER chaperones. |
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