Aerobic fermentation of glucose by trypanosomatids

The consumption of glucose by trypanosomatid protozoa such as Trypanosoma brucei, Trypanosoma cruzi, Leishmania spp., and Crithidia spp. is characterized by the excretion of reduced products such as succinate, pyruvate, ethanol, L-alanine, or lactate (depending on the species) not only in anaerobios...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autor principal:	Cazzulo, J.-J.
Formato:	JOUR
Materias:	anaerobic carbohydrate glucose catabolism glycolytic enzymes leishmanias Pasteur effect amino acid glucose malic acid reduced nicotinamide adenine dinucleotide enzyme activity fermentation glucose utilization glycolysis leishmania nonhuman oxidation priority journal protein degradation review trypanosoma brucei trypanosoma cruzi Aerobiosis Amino Acids Animal Carbohydrates Fermentation Glucose NAD Support, Non-U.S. Gov't Trypanosomatina Crithidia Protozoa Trypanosoma Trypanosoma brucei Trypanosoma cruzi Trypanosomatidae
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_08926638_v6_n13_p3153_Cazzulo
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

Ejemplares similares

Aerobic fermentation of glucose by trypanosomatids
Publicado: (1992)

Intermediate metabolism in Trypanosoma cruzi
por: Cazzulo, J.J.

Evolution of non-LTR retrotransposons in the trypanosomatid genomes: Leishmania major has lost the active elements
Publicado: (2006)

Evolution of non-LTR retrotransposons in the trypanosomatid genomes: Leishmania major has lost the active elements
por: Bringaud, F., et al.

Intermediate metabolism in Trypanosoma cruzi
Publicado: (1994)

Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids
por: Pereira, Claudio Alejandro, et al.
Publicado: (2002)

Arginine kinase: A common feature for management of energy reserves in African and American flagellated trypanosomatids
por: Pereira, C.A., et al.

Arginine kinase in Phytomonas, a trypanosomatid parasite of plants
por: Canepa, Gaspar Exequiel, et al.
Publicado: (2011)

Arginine kinase in Phytomonas, a trypanosomatid parasite of plants
por: Canepa, G.E., et al.

Amino acid and carbohydrate composition of a lysosomal cysteine proteinase from Trypanosoma cruzi. Absence of phosphorylated mannose residues
por: Cazzulo, J.J., et al.

Amino acid and carbohydrate composition of a lysosomal cysteine proteinase from Trypanosoma cruzi. Absence of phosphorylated mannose residues
por: Couso, Roberto O., et al.
Publicado: (1990)

Lysine transporters in human trypanosomatid pathogens
por: Canepa, Gaspar Exequiel, et al.
Publicado: (2012)

Lysine transporters in human trypanosomatid pathogens
por: Inbar, E., et al.

Phosphoenolpyruvate carboxykinase from Trypanosoma cruzi. Purification and physicochemical and kinetic properties
por: Cymeryng, C., et al.

Phosphoenolpyruvate carboxykinase from Trypanosoma cruzi. Purification and physicochemical and kinetic properties
por: Cymeryng, Cora Beatriz, et al.
Publicado: (1995)

Transporte de riboflavina en tripanosomátidos : novedoso blanco terapéutico
por: Balcazar, Darío Emmanuel
Publicado: (2017)

Transporte de riboflavina en tripanosomátidos : novedoso blanco terapéutico
por: Balcazar, Darío E.
Publicado: (2017)

Transporte de riboflavina en tripanosomátidos : novedoso blanco terapéutico
por: Balcazar, Darío Emmanuel
Publicado: (2017)

Differential regulation of putrescine uptake in trypanosoma cruzi and other trypanosomatids
por: González, Nélida Susana, et al.
Publicado: (1992)

Differential regulation of putrescine uptake in trypanosoma cruzi and other trypanosomatids
por: Gonzalez, N.S., et al.

Self-proteolysis of the cysteine proteinase, cruzipain, from Trypanosoma cruzi gives a major fragment corresponding to its carboxy-terminal domain
por: Hellman, U., et al.

A new twist in trypanosome RNA metabolism: Cis-splicing of pre-mRNA
Publicado: (2000)

A new twist in trypanosome RNA metabolism: Cis-splicing of pre-mRNA
por: Mair, G., et al.

Inositolphosphoceramide metabolism in Trypanosoma cruzi as compared with other trypanosomatids
por: Muchnik de Lederkremer, Rosa María, et al.
Publicado: (2011)

Inositolphosphoceramide metabolism in Trypanosoma cruzi as compared with other trypanosomatids
por: De Lederkremer, R.M., et al.

Carbon‐13 nuclear magnetic resonance analysis of [1‐13C]glucose metabolism in Trypanosoma cruzi Evidence of the presence of two alanine pools and of two CO2 fixation reactions
por: FRYDMAN, B., et al.

Self-proteolysis of the cysteine proteinase, cruzipain, from Trypanosoma cruzi gives a major fragment corresponding to its carboxy-terminal domain
Publicado: (1991)

Purification and partial structural and kinetic characterization of an aromatic L-α-hydroxy acid dehydrogenase from epimastigotes of Trypanosoma cruzi
por: Montemartini, M., et al.

Transporte de riboflavina en tripanosomátidos : novedoso blanco terapéutico
por: Balcazar, Darío Emmanuel, et al.
Publicado: (2017)

Carbon‐13 nuclear magnetic resonance analysis of [1‐13C]glucose metabolism in Trypanosoma cruzi Evidence of the presence of two alanine pools and of two CO2 fixation reactions
por: Frydman, Benjamín Jaime, et al.
Publicado: (1990)

Purification and partial structural and kinetic characterization of an aromatic L-α-hydroxy acid dehydrogenase from epimastigotes of Trypanosoma cruzi
Publicado: (1994)

Relative efficacy of lactose-related donors for Trypanosoma cruzi trans-sialidase [2]
por: Muchnik de Lederkremer, Rosa María
Publicado: (2004)

Relative efficacy of lactose-related donors for Trypanosoma cruzi trans-sialidase [2]
por: de Lederkremer, R.M., et al.

Protein glycosylation in Trypanosoma cruzi. II. Partial characterization of protein-bound oligosaccharides labeled 'in vivo'
por: Parodi, A.J., et al.

Sensitivity of trypanosomatid protozoa to DFMO and metabolic turnover of ornithine decarboxylase
por: Carrillo, Carolina, et al.
Publicado: (2000)

Sensitivity of trypanosomatid protozoa to DFMO and metabolic turnover of ornithine decarboxylase
por: Carrillo, C., et al.

Production of aromatic α-hydroxyacids by epimastigotes of Trypanosoma cruzi, and its possible role in NADH reoxidation
por: Montemartini, M., et al.

New heterobimetallic ferrocenyl derivatives are promising antitrypanosomal agents
por: Rodríguez Arce, Esteban, et al.
Publicado: (2019)

L-arginine uptake and L-phosphoarginine synthesis in Trypanosoma cruzi
por: Pereira, Claudio Alejandro, et al.
Publicado: (1999)

L-arginine uptake and L-phosphoarginine synthesis in Trypanosoma cruzi
por: Pereira, C.A., et al.