Results 21 to 30 of about 31,695 (232)

Phosphoglycerate kinase acts as a futile cycle at high temperature [PDF]

open access: yes, 2017
In (hyper)thermophilic organisms metabolic processes have to be adapted to function optimally at high temperature. We compared the gluconeogenic conversion of 3-phosphoglycerate via 1,3-bisphosphoglycerate to glyceraldehyde-3-phosphate at 30 C and at 70 ...
Snoep, J.L.   +8 more
core   +1 more source

Rethinking the evolution of eukaryotic metabolism: novel cellular partitioning of enzymes in stramenopiles links serine biosynthesis to glycolysis in mitochondria

open access: yesBMC Evolutionary Biology, 2017
Background An important feature of eukaryotic evolution is metabolic compartmentalization, in which certain pathways are restricted to the cytosol or specific organelles. Glycolysis in eukaryotes is described as a cytosolic process.
Melania Abrahamian   +3 more
doaj   +1 more source

Age-related modifications in rat cardiac phosphoglycerate kinase. Rejuvenation of the old enzyme by unfolding-refolding [PDF]

open access: yes, 1988
The occurrence of age-related modifications in functional and structural properties of several enzymes has been documented; however, the molecular basis of this phenomenon is still mostly unexplained.
Gafni, Ari, Zuniga, Alison
core   +1 more source

O-GlcNAcylation of PGK1 coordinates glycolysis and TCA cycle to promote tumor growth

open access: yesNature Communications, 2020
Post-translational modifications of phosphoglycerate kinase 1 (PGK1), a glycoytic enzyme, contribute to cancer progression. Here, the authors show that PGK1 is O-GlcNAcylated at T255, which induces its translocation into mitochondria to suppress the ...
Hao Nie   +8 more
doaj   +1 more source

Compartmentation of phosphoglycerate kinase in Trypanosoma brucei plays a critical role in parasite energy metabolism. [PDF]

open access: yes, 1998
African trypanosomes compartmentalize glycolysis in a microbody, the glycosome. When growing in the mammalian bloodstream, trypanosomes contain only a rudimentary mitochondrion, and the first seven glycolytic enzymes, including phosphoglycerate kinase ...
Blattner, J   +7 more
core   +1 more source

Genome-wide CRISPR/Cas9 library screening identified PHGDH as a critical driver for Sorafenib resistance in HCC

open access: yesNature Communications, 2019
Resistance to the tyrosine kinase inhibitor Sorafenib, which is the standard treatment for advanced hepatocellular carcinoma, is a major clinical challenge.
Lai Wei   +11 more
doaj   +1 more source

Trypanosoma evansi is alike to Trypanosoma brucei brucei in the subcellular localisation of glycolytic enzymes

open access: yesMemorias do Instituto Oswaldo Cruz, 2015
Trypanosoma evansi, which causes surra, is descended from Trypanosoma brucei brucei, which causes nagana. Although both parasites are presumed to be metabolically similar, insufficient knowledge of T. evansi precludes a full comparison.
S Andrea Moreno, Mayerly Nava
doaj   +1 more source

Insulin and mTOR Pathway Regulate HDAC3-Mediated Deacetylation and Activation of PGK1.

open access: yesPLoS Biology, 2015
Phosphoglycerate kinase 1 (PGK1) catalyzes the reversible transfer of a phosphoryl group from 1, 3-bisphosphoglycerate (1, 3-BPG) to ADP, producing 3-phosphoglycerate (3-PG) and ATP. PGK1 plays a key role in coordinating glycolytic energy production with
Shiwen Wang   +14 more
doaj   +1 more source

Molecular insights on pathogenic effects of mutations causing phosphoglycerate kinase deficiency.

open access: yesPLoS ONE, 2012
Phosphoglycerate kinase (PGK) catalyzes an important ATP-generating step in glycolysis. PGK1 deficiency is an uncommon X-linked inherited disorder, generally characterized by various combinations of non-spherocytic hemolytic anemia, neurological ...
Laurent R Chiarelli   +6 more
doaj   +1 more source

An allosteric signaling pathway of human 3-phosphoglycerate kinase from force distribution analysis. [PDF]

open access: yesPLoS Computational Biology, 2014
3-Phosphogycerate kinase (PGK) is a two domain enzyme, which transfers a phosphate group between its two substrates, 1,3-bisphosphoglycerate bound to the N-domain and ADP bound to the C-domain.
Zoltan Palmai   +3 more
doaj   +1 more source

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