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4. Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding. van der Vies SM, Gatenby AA, Georgopoulos C. Nature; 1994 Apr 14; 368(6472):654-6. PubMed ID: 7908418 [Abstract] [Full Text] [Related]
5. Substrate mutations that bypass a specific Cpn10 chaperonin requirement for protein folding. Andreadis JD, Black LW. J Biol Chem; 1998 Dec 18; 273(51):34075-86. PubMed ID: 9852065 [Abstract] [Full Text] [Related]
8. Chaperonin complexes monitored by ion mobility mass spectrometry. van Duijn E, Barendregt A, Synowsky S, Versluis C, Heck AJ. J Am Chem Soc; 2009 Feb 04; 131(4):1452-9. PubMed ID: 19138114 [Abstract] [Full Text] [Related]
9. Watching and weighting--chaperone complexes in action. Robinson CV. Nat Methods; 2005 May 04; 2(5):331-2. PubMed ID: 15846358 [No Abstract] [Full Text] [Related]
10. On the role of symmetrical and asymmetrical chaperonin complexes in assisted protein folding. Hayer-Hartl MK, Ewalt KL, Hartl FU. Biol Chem; 1999 May 04; 380(5):531-40. PubMed ID: 10384959 [Abstract] [Full Text] [Related]
17. Inter-ring communication allows the GroEL chaperonin complex to distinguish between different substrates. van Duijn E, Heck AJ, van der Vies SM. Protein Sci; 2007 May 02; 16(5):956-65. PubMed ID: 17456746 [Abstract] [Full Text] [Related]