Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Tamantha K. Littlejohn"'
Publikováno v:
International Congress Series. 1233:157-160
Indoleamine 2,3-dioxygenase (IDO), the first enzyme of the kynurenine pathway of tryptophan metabolism, has been implicated in numerous disease states. Site-directed mutagenesis was undertaken using the expression plasmid pQE9-IDO, to incorporate a s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8e9d622c5336c19a4237ffa5195ee835
https://doi.org/10.1016/s0531-5131(02)00312-6
https://doi.org/10.1016/s0531-5131(02)00312-6
Autor:
Roland Stocker, Osamu Takikawa, Tamantha K. Littlejohn, Syun Ru Yeh, Robert S. Armstrong, Roger J.W. Truscott, Shane R. Thomas, Andrew C. Terentis
Publikováno v:
Journal of Biological Chemistry. 277:15788-15794
Indoleamine 2,3-dioxygenase is a heme enzyme that catalyzes the oxidative degradation of L-Trp and other indoleamines. We have used resonance Raman spectroscopy to characterize the heme environment of purified recombinant human indoleamine 2,3-dioxyg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e5332af5d0207e6197b4fa68eab44cc2
https://doi.org/10.1074/jbc.m200457200
https://doi.org/10.1074/jbc.m200457200
Autor:
Tamantha K. Littlejohn, Joanne F. Jamie, Daniel Skylas, Roger J.W. Truscott, Mark J. Walker, Osamu Takikawa
Publikováno v:
Protein Expression and Purification. 19:22-29
Indoleamine 2,3-dioxygenase, the first and rate-limiting enzyme in human tryptophan metabolism, has been implicated in the pathogenesis of many diseases. The human enzyme was expressed in Escherichia coli EC538 (pREP4) as a fusion protein to a hexahi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1773e2b241a55173ee9227e31097f889
https://doi.org/10.1006/prep.2000.1214
https://doi.org/10.1006/prep.2000.1214
Autor:
Robert D. Willows, Perminder S. Sachdev, George A. Smythe, Christopher J.D. Austin, Mark J. Walker, Roger J.W. Truscott, Ross Grant, Tamantha K. Littlejohn, Joanne F. Jamie, Osamu Takikawa, Anne Poljak
Indoleamine 2,3-dioxygenase is the first and rate limiting enzyme of the kynurenine pathway of tryptophan metabolism, has potent effects on cell proliferation and mediates antimicrobial, antitumorogenic, and immuno suppressive effects. As a potent cy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8652d7842fb79a260f58a368f0fefe15
https://acuresearchbank.acu.edu.au/item/85x70/inhibition-of-indoleamine-2-3-dioxygenase-activity-by-h2o2
https://acuresearchbank.acu.edu.au/item/85x70/inhibition-of-indoleamine-2-3-dioxygenase-activity-by-h2o2
Publikováno v:
The Journal of biological chemistry. 278(32)
L-Tryptophan is the least abundant essential amino acid in humans. Indoleamine 2,3-dioxgyenase (IDO) is a cytosolic heme protein which, together with the hepatic enzyme tryptophan 2,3-dioxygenase, catalyzes the first and rate-limiting step in the maj
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e50b0f5849c871260b7ad56bf3647a0c
https://pubmed.ncbi.nlm.nih.gov/12766158
https://pubmed.ncbi.nlm.nih.gov/12766158
Autor:
Andrew C, Terentis, Shane R, Thomas, Osamu, Takikawa, Tamantha K, Littlejohn, Roger J W, Truscott, Robert S, Armstrong, Syun-Ru, Yeh, Roland, Stocker
Publikováno v:
The Journal of biological chemistry. 277(18)
Indoleamine 2,3-dioxygenase is a heme enzyme that catalyzes the oxidative degradation of L-Trp and other indoleamines. We have used resonance Raman spectroscopy to characterize the heme environment of purified recombinant human indoleamine 2,3-dioxyg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a3c3079c4e077b96d5452e1003de3fcd
https://pubmed.ncbi.nlm.nih.gov/11867636
https://pubmed.ncbi.nlm.nih.gov/11867636
Publikováno v:
Experimental eye research. 72(3)
Tryptophan-derived UV filters have recently been shown to bind to human lens proteins. These UV filter adducts increase in amount with age and appear to be mainly responsible for the yellowing of the lens in man. On the basis of research performed in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::faddbb6f63ab7740fe290aa19dda5935
https://pubmed.ncbi.nlm.nih.gov/11180976
https://pubmed.ncbi.nlm.nih.gov/11180976
Autor:
Najla Nasr, Vimal Kapoor, Hassan M. Naif, Sophie J. Thuruthyil, Ross Grant, Osamu Takikawa, Tamantha K. Littlejohn
Publikováno v:
Journal of virology. 74(9)
Increased kynurenine pathway metabolism has been implicated in the etiology of AIDS dementia complex (ADC). The rate-limiting enzyme for this pathway is indolamine 2,3-dioxygenase (IDO). We tested the efficacy of different strains of human immunodefi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cfd61f953cd8754b6a59d5e4e0e8db6
https://pubmed.ncbi.nlm.nih.gov/10756023
https://pubmed.ncbi.nlm.nih.gov/10756023
Autor:
Najla Nasr, Tamantha K. Littlejohn, Vimal Kapoor, Sophie J. Thuruthyil, Ross Grant, Osamu Takikawa, Hassan M. Naif
Publikováno v:
Redox report : communications in free radical research. 5(2-3)
Increased kynurenine pathway metabolism has been implicated in the aetiology of the AIDS dementia complex (ADC). The rate limiting enzyme for this pathway is indoleamine 2,3- dioxygenase (IDO). We tested the efficacy of different strains of HIV-1 (HI
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0cd7c04a8c413044b26d7a158005338
https://pubmed.ncbi.nlm.nih.gov/10939284
https://pubmed.ncbi.nlm.nih.gov/10939284
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781461371335
3-Hydroxykynurenine (3OHKyn), the precursor of UV filters in human lens, is highly autooxidizable, generates H2O2, and binds to lens proteins, yielding a tanned/yellow product resembling senile nuclear cataractous materials. Thus, if 3OHkyn can be sh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8cad21101f4e843837fa87611cc1c514
https://doi.org/10.1007/978-1-4615-4709-9_31
https://doi.org/10.1007/978-1-4615-4709-9_31