Getting Newly Synthesized Proteins Minireview into Shape
By Bernd Bukau, E. Deuerling, C. Pfund, E. Craig. 2000
436 citations recorded by the source corpus.
View Paper: https://www.semanticscholar.org/paper/88b3763d41741290ecc8a25f882f7e636bcf4e5f
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Citations in the corpus
- Hsp90: a specialized but essential protein-folding tool. (2001, background): “Chaperone proteins often cooperate in folding: a polypeptide that is bound by Hsp70 at an early stage of folding can be transferred to a chaperonin to reach its final native state (Hartl, 1996; Bukau et al., 2000).”
- Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli (2007, background): “400" language="eng" publish="issue" relation="no"> Introduction Polypeptide chains emerging from the ribosomes often depend on molecular helpers to reach their native conformation and to maintain it under stress condition”