Výsledky vyhledávání - "Timothy Geddes"

Akademický článek

Leukemia Mediated Endothelial Cell Activation Modulates Leukemia Cell Susceptibility to Chemotherapy through a Positive Feedback Loop Mechanism.

Autor: Bahareh Pezeshkian, Christopher Donnelly, Kelley Tamburo, Timothy Geddes, Gerard J Madlambayan

Publikováno v: PLoS ONE, Vol 8, Iss 4, p e60823 (2013)

In acute myeloid leukemia (AML), the chances of achieving disease-free survival are low. Studies have demonstrated a supportive role of endothelial cells (ECs) in normal hematopoiesis. Here we show that similar intercellular relationships exist in le

Externí odkaz: https://doaj.org/article/0089922bdd53409588f16f42b535e1e7

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Changes in renal markers and acute kidney injury after marathon running

Autor: Peter A, McCullough, Kavitha M, Chinnaiyan, Michael J, Gallagher, James M, Colar, Timothy, Geddes, Jeffrey M, Gold, Justin E, Trivax

Publikováno v: Nephrology (Carlton, Vic.). 16(2)

The impact of marathon running on kidney function has not been previously described.From 425 marathon runners, 13 women and 12 men were randomly selected and cardiovascular magnetic resonance imaging (MRI) and blood/urine biomarkers were performed 4

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::84237d5334a7fd9b367f3280bd829c23
https://pubmed.ncbi.nlm.nih.gov/21272132

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Dopamine biosynthesis is regulated by S-glutathionylation. Potential mechanism of tyrosine hydroxylast inhibition during oxidative stress

Autor: Chad R, Borges, Timothy, Geddes, J Throck, Watson, Donald M, Kuhn

Publikováno v: The Journal of biological chemistry. 277(50)

Tyrosine hydroxylase (TH), the initial and rate-limiting enzyme in the biosynthesis of the neurotransmitter dopamine, is inhibited by the sulfhydryl oxidant diamide in a concentration-dependent manner. The inhibitory effect of diamide on TH catalytic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5b3521646a28d21a78399d54d8a15a7f
https://pubmed.ncbi.nlm.nih.gov/12376535

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Peroxynitrite-induced nitration of tyrosine hydroxylase: identification of tyrosines 423, 428, and 432 as sites of modification by matrix-assisted laser desorption ionization time-of-flight mass spectrometry and tyrosine-scanning mutagenesis

Autor: Donald M, Kuhn, Mahdieh, Sadidi, Xiuli, Liu, Christian, Kreipke, Timothy, Geddes, Chad, Borges, J Throck, Watson

Publikováno v: The Journal of biological chemistry. 277(16)

Tyrosine hydroxylase (TH), the initial and rate-limiting enzyme in the biosynthesis of the neurotransmitter dopamine, is inactivated by peroxynitrite. The sites of peroxynitrite-induced tyrosine nitration in TH have been identified by matrix-assisted

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::697a122dedcbe205ae8434afbc2bdd0f
https://pubmed.ncbi.nlm.nih.gov/11834745

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