Results 11 to 20 of about 162,084 (246)

Thymidine Catabolism as a Metabolic Strategy for Cancer Survival [PDF]

open access: yesCell Reports, 2017
Thymidine phosphorylase (TP), a rate-limiting enzyme in thymidine catabolism, plays a pivotal role in tumor progression; however, the mechanisms underlying this role are not fully understood.
Sho Tabata   +20 more
doaj   +3 more sources

Synthesis of 5′-Thymidine-Conjugated Formylphenylboronic Acids as Potential Lysine Targeting Iminoboronate Reversible Covalent Enzyme Probes

open access: yes, 2022
The design of reversible-covalent molecules to selectively target the ε-amino functionality of lysine residues in enzymes or proteins is a highly desirable goal.
Katherine N. Robertson (841910)   +6 more
core   +1 more source

Relaxation Dynamics of Hydrated Thymine, Thymidine, and Thymidine Monophosphate Probed by Liquid Jet Time-Resolved Photoelectron Spectroscopy [PDF]

open access: yes, 2019
The relaxation dynamics of thymine and its derivatives thymidine and thymidine monophosphate were studied using time-resolved photoelectron spectroscopy applied to a water microjet. Two absorption bands were studied, the first is a bright ππ* state which
Erica, Liu   +5 more
core   +1 more source

Thymidine phosphorylase in cancer; Enemy or friend? [PDF]

open access: yes, 2016
Thymidine phosphorylase (TP) is a nucleoside metabolism enzyme that plays an important role in the pyrimidine pathway.TP catalyzes the conversion of thymidine to thymine and 2-deoxy-α-D-ribose-1-phosphate (dRib-1-P). Although this reaction is reversible,
Osman, Nemer   +4 more
core   +1 more source

Poor Outcome in a Mitochondrial Neurogastrointestinal Encephalomyopathy Patient with a Novel TYMP Mutation: The Need for Early Diagnosis. [PDF]

open access: yes, 2012
Mitochondrial neurogastrointestinal encephalomyopathy (MNGIE) is a devastating autosomal recessive disorder due to mutations in TYMP, which cause loss of function of thymidine phosphorylase (TP), nucleoside accumulation in plasma and tissues and ...
Padovani Alessandro   +40 more
core   +1 more source

Thymidine Kinase-Independent Click Chemistry DNADetect Probes for DNA Proliferation Assessment in Malaria Parasites

open access: yes, 2023
Metabolic chemical probes are small-molecule reagents that utilize naturally occurring biosynthetic enzymes for in situ incorporation into biomolecules of interest.
Hilko, David   +4 more
core   +1 more source

Nitrogen and carbon limitation of planktonic primary production and phytoplankton–bacterioplankton coupling in ponds on the McMurdo Ice Shelf, Antarctica

open access: yesEnvironmental Research Letters, 2013
We compared planktonic primary and secondary production across twenty meltwater ponds on the surface of the McMurdo Ice Shelf in January 2007, including some ponds with basal brines created by meromictic stratification.
Brian K Sorrell, Ian Hawes, Karl Safi
doaj   +1 more source

Clinical and biochemical improvements in a patient with MNGIE following enzyme replacement. [PDF]

open access: yes, 2013
Mitochondrial neurogastrointestinal encephalomyopathy (MNGIE) is a rare autosomal recessive metabolic disorder caused by a deficiency of thymidine phosphorylase (TP, EC2.4.2.4) due to mutations in the nuclear gene TYMP.
Bax, BE   +13 more
core   +1 more source

Anion exchange resins in phosphate form as versatile carriers for the reactions catalyzed by nucleoside phosphorylases

open access: yesBeilstein Journal of Organic Chemistry, 2020
In the present work, we suggested anion exchange resins in the phosphate form as a source of phosphate, one of the substrates of the phosphorolysis of uridine, thymidine, and 1-(β-ᴅ-arabinofuranosyl)uracil (Ara-U) catalyzed by recombinant E. coli uridine
Julia N. Artsemyeva   +7 more
doaj   +1 more source

Human Keratinocytes Catabolize Thymidine [PDF]

open access: yes, 1988
Human neonatal foreskin keratinocytes incorporate exogenous thymidine into DNA and proliferate in vitro even after reaching confluence. Keratinocytes also catabolize thymidine, as reported for the first time below.
Kugelman, Lisa C.   +4 more
core   +1 more source

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