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Cofilin-1 and phosphoglycerate kinase 1 as promising indicators for glioma radiosensibility and prognosis. [PDF]
Oncotarget, 2017 Sun W +8 more
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Characterization of filarial phosphoglycerate kinase
Biochimie, 2019Phosphoglycerate kinase (PGK) is a key enzyme of glycolysis which also acts as a mediator of DNA replication and repair in the nucleus. We have cloned and expressed PGK in Brugia malayi. The rBmPGK was found to be 415 amino acid residues long having 45 kDa subunit molecular weight.
Faiyaz Ahmad
exaly +3 more sources
FEBS Letters, 1988 Rabbit muscle glyceraldehyde-3-phosphate dehydrogenase covalently bound to Sepharose was shown to form a complex with soluble 3-phosphoglycerate kinase. The strength of the association appeared to depend upon the functional state of both enzymes.
Vladimir I Muronetz, Natalia K Nagradova
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Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1981
Abstract Phosphoglycerate kinase catalyses the high-energy phosphoryl transfer of the acyl phosphate of 1,3-bisphosphoglycerate to ADP to produce ATP, a reaction requiring magnesium ions. The enzyme is widely distributed and apparently highly conserved as a monomer of molecular mass 45000.
C C, Blake, D W, Rice
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Abstract Phosphoglycerate kinase catalyses the high-energy phosphoryl transfer of the acyl phosphate of 1,3-bisphosphoglycerate to ADP to produce ATP, a reaction requiring magnesium ions. The enzyme is widely distributed and apparently highly conserved as a monomer of molecular mass 45000.
C C, Blake, D W, Rice
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Flexibility and folding of phosphoglycerate kinase
Biochimie, 1990Flexibility and folding of phosphoglycerate kinase, a two-domain monomeric enzyme, have been studied using a wide variety of methods including theoretical approaches. Mutants of yeast phosphoglycerate kinase have been prepared in order to introduce cysteinyl residues as local probes throughout the molecule without perturbating significantly the ...
J M, Yon +8 more
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Inhibition of phosphoglycerate kinase by salicylates
Biochimica et Biophysica Acta (BBA) - Enzymology, 1978A kinetic analysis has been performed on the inhibition of the yeast phosphoglycerate kinase (APT:3-phospho-D-glycerate 1-phosphotransferase, EC 2.7.2.3) reaction by 2-hydroxybenzoate (salicylate) and two of its iododerivatives, 2-hydroxy-5-iodobenzoate and 2-hydroxy-3,5-diiodobenzoate.
M, Larsson-Raźnikiewicz, E, Wiksell
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On the “phosphoryl-enzyme” of phosphoglycerate kinase
Biochemical and Biophysical Research Communications, 1975The ‘phosphoryl-enzyme’ prepared from phosphoglycerate kinase and ATP in the presence of an ADP trap, is shown to be a complex between the enzyme and 1,3-diphosphoglycerate. The capricious variation in the extent of phosphorylation is due to varying amounts of contaminating 3-phosphoglycerate.
P E, Johnson +4 more
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A Sandwich ELISA for Phosphoglycerate Kinase
Journal of Immunoassay and Immunochemistry, 2008Phosphoglycerate kinase (PGK1) is a key enzyme in glycolysis that can also be released from certain cells. In the extracellular milieu, PGK1 reportedly acts as a disulphide reductase to activate plasmin, resulting in the production of angiostatin, a potent angiogenesis inhibitor.
Weilin, Zhao +5 more
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Structure of Yeast Phosphoglycerate Kinase
Nature, 1974A 3.5 A resolution electron density map of yeast phosphoglycerate mutase has been calculated which shows that much of the tertiary structure of this enzyme resembles that found in a number of nucleotide binding enzymes although the mutase itself has no known nucleotide binding requirement.
T N, Bryant, H C, Watson, P L, Wendell
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