Results 1 to 10 of about 69 (69)

Roscovitine Targets, Protein Kinases and Pyridoxal Kinase [PDF]

open access: yesJournal of Biological Chemistry, 2005
(R)-Roscovitine (CYC202) is often referred to as a "selective inhibitor of cyclin-dependent kinases." Besides its use as a biological tool in cell cycle, neuronal functions, and apoptosis studies, it is currently evaluated as a potential drug to treat cancers, neurodegenerative diseases, viral infections, and glomerulonephritis.
Bach, S.   +21 more
openaire   +7 more sources

Brain pyridoxal kinase [PDF]

open access: yesEuropean Journal of Biochemistry, 1986
Pyridoxal kinase has been purified 9000‐fold from sheep brain. The purification procedure involves ammonium sulphate fractionation, DEAE‐cellulose chromatography, affinity chromatography and Sephadex G‐100 gel filtration. The final chromatography step yields a homogeneous preparation of high specific activity with a pI of 5.
Manfred Rohde   +2 more
openaire   +3 more sources

NRF2 signalling in cytoprotection and metabolism

open access: yesBritish Journal of Pharmacology, EarlyView., 2023
The KEAP1‐NRF2 system plays a central role in cytoprotection in defence mechanisms against oxidative stress. The KEAP1‐NRF2 system has been regarded as a sulfur‐utilizing cytoprotective mechanism, because KEAP1 serves as a biosensor for electrophiles by using its reactive thiols and NRF2 is a transcriptional factor regulating genes involved in sulfur ...
Shohei Murakami   +4 more
wiley   +1 more source

Inhibiting Pyridoxal Kinase of Entamoeba histolytica Is Lethal for This Pathogen [PDF]

open access: yesFrontiers in Cellular and Infection Microbiology, 2021
Pyridoxal 5’-phosphate (PLP) functions as a cofactor for hundreds of different enzymes that are crucial to the survival of microorganisms. PLP-dependent enzymes have been extensively characterized and proposed as drug targets in Entamoeba histolytica.
Samudrala Gourinath   +4 more
openaire   +4 more sources

Conformational Changes in the Reaction of Pyridoxal Kinase [PDF]

open access: yesJournal of Biological Chemistry, 2004
To understand the processes involved in the catalytic mechanism of pyridoxal kinase (PLK),1 we determined the crystal structures of PLK.AMP-PCP-pyridoxamine, PLK.ADP.PLP, and PLK.ADP complexes. Comparisons of these structures have revealed that PLK exhibits different conformations during its catalytic process.
Francis Kwok   +7 more
openaire   +3 more sources

Crystal Structure of Pyridoxal Kinase from the Escherichia coli pdxK Gene: Implications for the Classification of Pyridoxal Kinases [PDF]

open access: yesJournal of Bacteriology, 2006
ABSTRACT The pdxK and pdxY genes have been found to code for pyridoxal kinases, enzymes involved in the pyridoxal phosphate salvage pathway. Two pyridoxal kinase structures have recently been published, including Escherichia coli pyridoxal kinase 2 (ePL ...
M. K. Safo   +5 more
openaire   +3 more sources

Pyridoxal Kinase Inhibition by Artemisinins Downregulates Inhibitory Neurotransmission [PDF]

open access: yesProceedings of the National Academy of Sciences, 2020
ABSTRACTThe anti-malarial artemisinins have also been implicated in the regulation of various other cellular pathways. Despite their widespread application, the cellular specificities and molecular mechanisms of target recognition by artemisinins remain poorly characterized.
Vikram Babu Kasaragod   +7 more
openaire   +3 more sources

Reversible unfolding of pyridoxal kinase.

open access: yesJournal of Biological Chemistry, 1993
The unfolding of brain pyridoxal kinase by guanidinium HCl has been investigated at equilibrium. The overall process was reversible as judged from the complete recovery of catalytic activity after removal of guanidinium HCl. Unfolding of pyridoxal kinase was monitored by circular dichroism and fluorescence spectroscopy.
T Pineda, Jorge E. Churchich
openaire   +3 more sources

Brain Pyridoxal Kinase. Mobility of the Substrate Pyridoxal and Binding of Inhibitors to the Nucleotide Site [PDF]

open access: yesEuropean Journal of Biochemistry, 1979
Pyridoxal kinase has been purified 2000‐fold from pig brain. The enzyme preparation migrates as a single protein and activity band on analytical gel electrophoresis. The interactions of the substrate pyridoxal and the inhibitor N‐dansyl‐2‐oxopyrrolidine (dansyl = 5‐dimethylaminonaph‐thalene‐1‐sulfonyl) with the catalytic site were examined by means of ...
Jorge E. Churchich, Francis Kwok
openaire   +3 more sources

Study on the Pyridoxal Kinase of Mouse Brain

open access: yesTHE JOURNAL OF VITAMINOLOGY, 1969
The properties of the pyridoxal kinase of mouse brain were studied and the following results were obtained.1. It was concluded that toxopyrimidine seemed to be phosphorylated by the same phosphokinase as pyridoxal based on the following reasons: the mutual competitive inhibition, the coincidence of the metal requirements, the denaturation effects of ...
Katashi Makino, Michiko Tsubosaka
openaire   +4 more sources

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