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Journal of Biological Physics|January 25, 2013
Chaperonin-affected folding of globular proteinsK Kuwajima, T Makio, T InobeBiochimica Et Biophysica Acta|May 9, 2001
Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATPT Inobe, T Makio, E Takasu-Ishikawa, et al.Journal of Molecular Biology|October 8, 1999
Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroEST Makio, M Arai, K KuwajimaJournal of Molecular Biology|September 21, 2001
Nucleotide-induced transition of GroEL from the high-affinity to the low-affinity state for a target protein: effects of ATP and ADP on the GroEL-affected refolding of alpha-lactalbuminT Makio, E Takasu-Ishikawa, K KuwajimaJournal of Molecular Biology|May 23, 1998
Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroELG P Tsurupa, T Ikura, T Makio, et al.Biochemical and Biophysical Research Communications|February 16, 2000
Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide bindingF Motojima, T Makio, K Aoki, et al.FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology|January 1, 1996
The molten globule state of alpha-lactalbuminK KuwajimaBiophysical Chemistry|July 1, 1978
Equilibrium and kinetics of the thermal unfolding of alpha-lactalbumin. The relation to its folding mechanismK Kuwajima, S SugaiFolding & Design|January 1, 1996
Rapid formation of a molten globule intermediate in refolding of alpha-lactalbuminM Arai, K KuwajimaPageof 9