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Titlebook: Stress-Inducible Cellular Responses; U. Feige,I. Yahara,B. S. Polla Book 1996 Birkhäuser Verlag 1996 Chaperone.Molekularbiologie.biology.c

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Protein folding and assembly in the endoplasmic reticulumes an oxidizing environment, has high levels of calcium, and contains enzymes for N-linked glycosylation. The growing nascent polypeptide chain is in many cases modified co-translationally with N-linked sugars and begins to fold while still attached to the ribosome. Disulfide bond formation stabiliz
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Molecular chaperoning of steroid hormone receptors). For steroid receptors, the hsp90 chaperone system determines both repression of transcriptional activity in the absence of hormone and the proper folding of the hormone binding domain to produce the steroid binding conformation. Like steroid receptors, a number of other regulators of transcriptio
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Protein disulfide isomerase: A multifunctional protein of the endoplasmic reticulumhemical and molecular biology techniques have revealed that it is present in all eukaryotic cells studied and retained in the ER via a -KDEL or -HDEL sequence at its C-terminus. However, evidence is accumulating that, in certain cell types, PDI can be found in other subcellular compartments, despite
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