作者: Gregory L Blatch , Addmore Shonhai , Keoagile W Modisakeng , Fritha Hennessy , Graeme Bradley
DOI:
关键词: Cell biology 、 Heat shock protein 、 Biotechnology 、 Hsp70 、 Hsp90 、 Target protein 、 Chemical chaperone 、 Co-chaperone 、 Protein folding 、 Biology 、 Chaperone (protein)
摘要: Molecular chaperones consist of several highly conserved families of proteins, many which heat shock proteins. The primary function molecular is to facilitate the folding or refolding and therefore they play an important role in diverse cellular processes including protein synthesis, translocation, or degradation proteins after cell stress. Cells are often exposed different stressors, resulting protein misfolding aggregation. It now well established that the levels certain elevated during stress provide protection cell. focus this review on impact biology, medicine biotechnology, thus covers both fundamental applied aspects chaperone biology. Attention paid functions and applications from bacterial eukaryotic cells, focusing 90 (Hsp90), 70 (Hsp70) 40 (Hsp40) classes chaperones, respectively. role these human diseases discussed, as as parts played by produced causative agents malaria trypanosomiasis. Recent advances have seen application improving yields a particular target recombinant production. prospects for targeted use over-production critically reviewed, current research at Rhodes University also discussed.