Add to ORKG[[sponsorship]]農業生物科技研究中心[[note]]已出版;[SCI];有審查制度;具代表性[[note]]http://gateway.isiknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=Drexel&SrcApp=hagerty_opac&KeyRecord=0021-9258&DestApp=JCR&RQ=IF_CAT_BOXPLOT[[note]]http://gateway.isiknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=RID&SrcApp=RID&DestLinkType=FullRecord&DestApp=ALL_WOS&KeyUT=A1997YB1390003
Fructose-1,6-bisphosphatase (FBPase) plays a crucial role in the regulation of gluconeogenesis. It i...
AbstractRat liver fructose-1,6-bisphosphatase was partially phosphorylated in vitro and separated in...
Fructose-1, 6-bisphosphate (D-fructose-1, 6-bisphosphate 1-phosphohydrolase; EC 3. 1. 3; FBPase) is ...
AbstractAdenosine 5′-monophosphate (AMP) inhibits muscle fructose 1,6-bisphosphatase (FBPase) about ...
International audienceBackgroundFructose-1,6-bisphosphatase, a major enzyme of gluconeogenesis, is i...
Porcine Fructose-1,6-bisphosphatase is a homotetramer with four identical subunits. It plays a centr...
Loop 52–72 of porcine fructose-1,6-bisphosphatase may play a central role in the mechanism of cataly...
Fructose 1,6-bisphosphatase (FBPase) is a key enzyme in gluconeogenesis. It is a potential drug targ...
Fructose-1,6-bisphosphatase, a key enzyme in gluconeogenesis, is subject to metabolic regulation. Th...
AMP transforms fructose-1,6-bisphosphatase from its active R-state to its inactive T-state. This qua...
Fructose-1,6-bisphosphatase, a key enzyme in gluconeogenesis, is subject to metabolic regulation. Th...
Residues 1–10 of porcine fructose-1,6-bisphosphatase (FBPase) are poorly ordered or are in different...
Arg-136, Glu-137, Arg-138 and Arg-139 are conserved in all sequences of the 2-kinase domain of 6-pho...
Fructose-1,6-bisphosphatase (FBPase) catalyzes the reaction of fructose-1,6-bisphosphate to fructose...
The roles of Arg-104 and Arg-225 located in the 2-kinase domain of the bifunctional enzyme 6-phospho...
Fructose-1,6-bisphosphatase (FBPase) plays a crucial role in the regulation of gluconeogenesis. It i...
AbstractRat liver fructose-1,6-bisphosphatase was partially phosphorylated in vitro and separated in...
Fructose-1, 6-bisphosphate (D-fructose-1, 6-bisphosphate 1-phosphohydrolase; EC 3. 1. 3; FBPase) is ...
AbstractAdenosine 5′-monophosphate (AMP) inhibits muscle fructose 1,6-bisphosphatase (FBPase) about ...
International audienceBackgroundFructose-1,6-bisphosphatase, a major enzyme of gluconeogenesis, is i...
Porcine Fructose-1,6-bisphosphatase is a homotetramer with four identical subunits. It plays a centr...
Loop 52–72 of porcine fructose-1,6-bisphosphatase may play a central role in the mechanism of cataly...
Fructose 1,6-bisphosphatase (FBPase) is a key enzyme in gluconeogenesis. It is a potential drug targ...
Fructose-1,6-bisphosphatase, a key enzyme in gluconeogenesis, is subject to metabolic regulation. Th...
AMP transforms fructose-1,6-bisphosphatase from its active R-state to its inactive T-state. This qua...
Fructose-1,6-bisphosphatase, a key enzyme in gluconeogenesis, is subject to metabolic regulation. Th...
Residues 1–10 of porcine fructose-1,6-bisphosphatase (FBPase) are poorly ordered or are in different...
Arg-136, Glu-137, Arg-138 and Arg-139 are conserved in all sequences of the 2-kinase domain of 6-pho...
Fructose-1,6-bisphosphatase (FBPase) catalyzes the reaction of fructose-1,6-bisphosphate to fructose...
The roles of Arg-104 and Arg-225 located in the 2-kinase domain of the bifunctional enzyme 6-phospho...
Fructose-1,6-bisphosphatase (FBPase) plays a crucial role in the regulation of gluconeogenesis. It i...
AbstractRat liver fructose-1,6-bisphosphatase was partially phosphorylated in vitro and separated in...
Fructose-1, 6-bisphosphate (D-fructose-1, 6-bisphosphate 1-phosphohydrolase; EC 3. 1. 3; FBPase) is ...