Samadli S, Zhou Q, Zheng B, Gu W, Zhang A
Front Endocrinol (Lausanne). 2023; 14:1188301.
PMID: 37255971
PMC: 10226665.
DOI: 10.3389/fendo.2023.1188301.
Kum S, Ho J, Parikh A, Liedberg B
ACS Bio Med Chem Au. 2023; 2(1):73-83.
PMID: 37102179
PMC: 10114716.
DOI: 10.1021/acsbiomedchemau.1c00027.
Kosova K, Vitamvas P, Prasil I, Klima M, Renaut J
Front Plant Sci. 2021; 12:793113.
PMID: 34970290
PMC: 8712444.
DOI: 10.3389/fpls.2021.793113.
Lu W, Hsu P, Lin H
Antimicrob Agents Chemother. 2021; 65(9):e0032621.
PMID: 34228542
PMC: 8370199.
DOI: 10.1128/AAC.00326-21.
Wood H, Cruz-Navarrete F, Baxter N, Trevitt C, Robertson A, Dix S
Nat Commun. 2020; 11(1):5538.
PMID: 33139716
PMC: 7608592.
DOI: 10.1038/s41467-020-19215-9.
Systematic Evaluation of Imine-Reducing Enzymes: Common Principles in Imine Reductases, β-Hydroxy Acid Dehydrogenases, and Short-Chain Dehydrogenases/ Reductases.
Stockinger P, Roth S, Muller M, Pleiss J
Chembiochem. 2020; 21(18):2689-2695.
PMID: 32311225
PMC: 7540600.
DOI: 10.1002/cbic.202000213.
Molecular and cellular regulation of human glucokinase.
Sternisha S, Miller B
Arch Biochem Biophys. 2019; 663:199-213.
PMID: 30641049
PMC: 6377845.
DOI: 10.1016/j.abb.2019.01.011.
Conformational heterogeneity and intrinsic disorder in enzyme regulation: Glucokinase as a case study.
Larion M, Miller B, Bruschweiler R
Intrinsically Disord Proteins. 2017; 3(1):e1011008.
PMID: 28232887
PMC: 5314934.
DOI: 10.1080/21690707.2015.1011008.
Solution NMR Spectroscopy for the Study of Enzyme Allostery.
Lisi G, Loria J
Chem Rev. 2016; 116(11):6323-69.
PMID: 26734986
PMC: 4937494.
DOI: 10.1021/acs.chemrev.5b00541.
Allostery vs. "allokairy".
Hilser V, Anderson J, Motlagh H
Proc Natl Acad Sci U S A. 2015; 112(37):11430-1.
PMID: 26372953
PMC: 4577133.
DOI: 10.1073/pnas.1515239112.
Dual allosteric activation mechanisms in monomeric human glucokinase.
Whittington A, Larion M, Bowler J, Ramsey K, Bruschweiler R, Miller B
Proc Natl Acad Sci U S A. 2015; 112(37):11553-8.
PMID: 26283387
PMC: 4577146.
DOI: 10.1073/pnas.1506664112.
Kinetic Cooperativity in Human Pancreatic Glucokinase Originates from Millisecond Dynamics of the Small Domain.
Larion M, Hansen A, Zhang F, Bruschweiler-Li L, Tugarinov V, Miller B
Angew Chem Int Ed Engl. 2015; 54(28):8129-32.
PMID: 26013420
PMC: 4587531.
DOI: 10.1002/anie.201501204.
A general framework for thermodynamically consistent parameterization and efficient sampling of enzymatic reactions.
Saa P, Nielsen L
PLoS Comput Biol. 2015; 11(4):e1004195.
PMID: 25874556
PMC: 4397067.
DOI: 10.1371/journal.pcbi.1004195.
Acyl-ACP substrate recognition in Burkholderia mallei BmaI1 acyl-homoserine lactone synthase.
Montebello A, Brecht R, Turner R, Ghali M, Pu X, Nagarajan R
Biochemistry. 2014; 53(39):6231-42.
PMID: 25215658
PMC: 4188261.
DOI: 10.1021/bi5009529.
Role of connecting loop I in catalysis and allosteric regulation of human glucokinase.
Martinez J, Larion M, Conejo M, Porter C, Miller B
Protein Sci. 2014; 23(7):915-22.
PMID: 24723372
PMC: 4088975.
DOI: 10.1002/pro.2473.
Human 60-kDa lysophospholipase contains an N-terminal L-asparaginase domain that is allosterically regulated by L-asparagine.
Karamitros C, Konrad M
J Biol Chem. 2014; 289(19):12962-75.
PMID: 24657844
PMC: 4036312.
DOI: 10.1074/jbc.M113.545038.
Purification and characterization of sinapoylglucose:malate sinapoyltransferase from Raphanus sativus L.
Grawe W, Bachhuber P, Mock H, Strack D
Planta. 2013; 187(2):236-41.
PMID: 24178050
DOI: 10.1007/BF00201945.
Conformational transition pathway in the activation process of allosteric glucokinase.
Huang M, Lu S, Shi T, Zhao Y, Chen Y, Li X
PLoS One. 2013; 8(2):e55857.
PMID: 23409066
PMC: 3567010.
DOI: 10.1371/journal.pone.0055857.
Order-disorder transitions govern kinetic cooperativity and allostery of monomeric human glucokinase.
Larion M, Kopke Salinas R, Bruschweiler-Li L, Miller B, Bruschweiler R
PLoS Biol. 2012; 10(12):e1001452.
PMID: 23271955
PMC: 3525530.
DOI: 10.1371/journal.pbio.1001452.
Functional roles of slow enzyme conformational changes in network dynamics.
Wu Z, Xing J
Biophys J. 2012; 103(5):1052-9.
PMID: 23009855
PMC: 3433601.
DOI: 10.1016/j.bpj.2012.08.008.