Results 11 to 20 of about 13,839 (206)

Alteration of de novo glucose production contributes to fasting hypoglycaemia in Fyn deficient mice. [PDF]

open access: yesPLoS ONE, 2013
Previous studies have demonstrated that glucose disposal is increased in the Fyn knockout (FynKO) mice due to increased insulin sensitivity. FynKO mice also display fasting hypoglycaemia despite decreased insulin levels, which suggested that hepatic ...
Yingjuan Yang   +7 more
doaj   +4 more sources

ALDOB (aldolase B, fructose-bisphosphate) [PDF]

open access: yesAtlas of Genetics and Cytogenetics in Oncology and Haematology, 2011
Review on ALDOB (aldolase B, fructose-bisphosphate), with data on DNA, on the protein encoded, and where the gene is implicated.
Peng, SY, Hsu, HC
openaire   +4 more sources

The metabolic enzyme fructose-1,6-bisphosphate aldolase acts as a transcriptional regulator in pathogenic Francisella [PDF]

open access: yesNature Communications, 2017
The enzyme fructose-bisphosphate aldolase (FBA) plays central roles in glycolysis and gluconeogenesis. Here, Ziveri et al. show that FBA of the pathogen Francisella novicida acts, in addition, as a transcriptional regulator and is important for bacterial
Jason Ziveri   +11 more
doaj   +2 more sources

Cooperative effect of fructose bisphosphate and glyceraldehyde-3-phosphate dehydrogenase on aldolase action [PDF]

open access: yesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
The combination of binding and kinetic approaches is suggested to study (i) the mechanism of substrate-modulated dynamic enzyme associations; (ii) the specificity of enzyme interactions. The effect of complex formation between aldolase and glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating), EC 1.
J, Neuzil   +3 more
openaire   +3 more sources

Fructose biphosphate aldolase: A new cassava allergen [PDF]

open access: yesWorld Allergy Organization Journal, 2023
Background: Food allergy has considerably increased in recent years and this situation has been aggravated mainly by the consumption of more processed and complex foods, since minor or potentially allergenic foods are not required to be labeled.
Anne K.R.M. Ventura, Ph.D   +10 more
doaj   +2 more sources

Characterization of the genes for fructose-bisphosphate aldolase in Trypanosoma brucei [PDF]

open access: yesMolecular and Biochemical Parasitology, 1988
In Trypanosoma brucei stock 427 the glycolytic enzyme fructose-bisphosphate aldolase is encoded by two tandemly linked genes of identical sequence. Such a tandem arrangement of aldolase genes is also present in other T. brucei stocks of unrelated origin.
M, Marchand   +5 more
openaire   +3 more sources

Kinetic properties of fructose bisphosphate aldolase from Trypanosoma brucei compared to aldolase from rabbit muscle and Staphylococcus aureus [PDF]

open access: yesMolecular and Biochemical Parasitology, 1991
The kinetic properties of aldolase from Trypanosoma brucei were studied in comparison with aldolase from rabbit muscle and Staphylococcus aureus. The 3 enzymes displayed a similar broad pH optimum for the cleavage of fructose 1,6-bisphosphate (Fru(1,6)P2) and a similar narrow pH optimum for the cleavage of fructose 1-phosphate (Fru-1-P). However, small
M, Callens, D A, Kuntz, F R, Opperdoes
openaire   +3 more sources

Chemical modification of fructose bisphosphate aldolase from Trypanosoma brucei compared to aldolase from rabbit muscle and Staphylococcus aureus [PDF]

open access: yesMolecular and Biochemical Parasitology, 1991
Chemical modifications of Class I aldolases from Trypanosoma brucei, rabbit muscle and Staphylococcus aureus with carboxypeptidase A, glyceraldehyde 3-phosphate and cysteine-specific reagents revealed the following differences between the three homologous enzymes. Aldolase from S. aureus was not affected by any of these reagents.
M, Callens, F R, Opperdoes
openaire   +3 more sources

Molecular modeling of inhibitors against fructose bisphosphate aldolase from Candida albicans. [PDF]

open access: yesIn Silico Pharmacol, 2018
Candida albicans is an opportunistic pathogen that causes from vulvovaginal and oropharyngeal candidiasis to systemic infections. The enzyme 1,6-fructose bisphosphate aldolase class II (FBA II), is a macromolecule existing only in lower organisms, being essential for the survival of the pathogen due to its function of maintaining the glycolysis process.
de Amorim AL   +5 more
europepmc   +4 more sources

Multifunctional Fructose 1,6-Bisphosphate Aldolase as a Therapeutic Target

open access: yesFrontiers in Molecular Biosciences, 2021
Fructose 1,6-bisphosphate aldolase is a ubiquitous cytosolic enzyme that catalyzes the fourth step of glycolysis. Aldolases are classified into three groups: Class-I, Class-IA, and Class-II; all classes share similar structural features but low amino ...
David B. Pirovich   +2 more
doaj   +1 more source

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