Larion, Mioara; Salinas, Roberto Kopke 
; Bruschweiler Li, Lei; Miller, Brian G; Brüschweiler, Rafael
Source: PLOS Biology. Unidade: IQ
Subjects: ENZIMAS, BIOQUÍMICA
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LARION, Mioara et al. Order-disorder transitions govern kinetic cooperativity and allostery of monomeric human glucokinase. PLOS Biology, v. 10, n. 12, p. 1-9 art. e1001452, 2012Tradução . . Disponível em: https://doi.org/10.1371/journal.pbio.1001452. Acesso em: 08 out. 2024.APA
Larion, M., Salinas, R. K., Bruschweiler Li, L., Miller, B. G., & Brüschweiler, R. (2012). Order-disorder transitions govern kinetic cooperativity and allostery of monomeric human glucokinase. PLOS Biology, 10( 12), 1-9 art. e1001452. doi:10.1371/journal.pbio.1001452NLM
Larion M, Salinas RK, Bruschweiler Li L, Miller BG, Brüschweiler R. Order-disorder transitions govern kinetic cooperativity and allostery of monomeric human glucokinase [Internet]. PLOS Biology. 2012 ; 10( 12): 1-9 art. e1001452.[citado 2024 out. 08 ] Available from: https://doi.org/10.1371/journal.pbio.1001452Vancouver
Larion M, Salinas RK, Bruschweiler Li L, Miller BG, Brüschweiler R. Order-disorder transitions govern kinetic cooperativity and allostery of monomeric human glucokinase [Internet]. PLOS Biology. 2012 ; 10( 12): 1-9 art. e1001452.[citado 2024 out. 08 ] Available from: https://doi.org/10.1371/journal.pbio.1001452
