Co-overexpression of bacterial GroESL chaperonins partly overcomes non-productive folding and tetramer assembly of E. coli-expressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation.

MLA

Bross, P., et al. “Co-Overexpression of Bacterial GroESL Chaperonins Partly Overcomes Non-Productive Folding and Tetramer Assembly of E. Coli-Expressed Human Medium-Chain Acyl-CoA Dehydrogenase (MCAD) Carrying the Prevalent Disease-Causing K304E Mutation.” Biochimica et Biophysica Acta, vol. 1182, no. 3, Oct. 1993, pp. 264–74. EBSCOhost, https://doi.org/10.1016/0925-4439(93)90068-c.

APA

Bross, P., Andresen, B. S., Winter, V., Kräutle, F., Jensen, T. G., Nandy, A., Kølvraa, S., Ghisla, S., Bolund, L., & Gregersen, N. (1993). Co-overexpression of bacterial GroESL chaperonins partly overcomes non-productive folding and tetramer assembly of E. coli-expressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation. Biochimica et Biophysica Acta, 1182(3), 264–274. https://doi.org/10.1016/0925-4439(93)90068-c

Chicago

Bross, P, B S Andresen, V Winter, F Kräutle, T G Jensen, A Nandy, S Kølvraa, S Ghisla, L Bolund, and N Gregersen. 1993. “Co-Overexpression of Bacterial GroESL Chaperonins Partly Overcomes Non-Productive Folding and Tetramer Assembly of E. Coli-Expressed Human Medium-Chain Acyl-CoA Dehydrogenase (MCAD) Carrying the Prevalent Disease-Causing K304E Mutation.” Biochimica et Biophysica Acta 1182 (3): 264–74. doi:10.1016/0925-4439(93)90068-c.