Zobrazeno 1 - 10
of 225
pro vyhledávání: '"Roberta F. Colman"'
Publikováno v:
Protein Science. 20:834-848
Human GSTpi, an important detoxification enzyme, has been shown to modulate the activity of JNKs by inhibiting apoptosis and by causing cell proliferation and tumor growth. In this work, we describe a detailed analysis of the interaction in vitro bet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cf12666958a01acb792d7b7d25856498
https://doi.org/10.1002/pro.609
https://doi.org/10.1002/pro.609
Publikováno v:
Protein Expression and Purification. 75:138-146
c-Jun N-terminal kinases (JNKs) are part of the mitogen-activated protein kinase (MAPK) signaling cascade. They are activated through dual phosphorylation of two residues in the activation loop, a threonine and a tyrosine, by MAP2 kinases (MKK4 and 7
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e108c51d271c19f05e12f3430b56dff9
https://doi.org/10.1016/j.pep.2010.08.002
https://doi.org/10.1016/j.pep.2010.08.002
Autor:
Mayura Dange, Roberta F. Colman
Publikováno v:
Journal of Biological Chemistry. 285:20520-20525
The human NAD-dependent isocitrate dehydrogenase (IDH) is a heterotetrameric mitochondrial enzyme with 2alpha:1beta:1gamma subunit ratio. The three subunits share 40-52% identity in amino acid sequence and each includes a tyrosine in a comparable pos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f57e163abc3dfa89bec98711640f9cd
https://doi.org/10.1074/jbc.m110.115386
https://doi.org/10.1074/jbc.m110.115386
Autor:
Luis A. Ralat, Roberta F. Colman
Publikováno v:
Protein Science. 12:2575-2587
Monobromobimane (mBBr), functions as a substrate of porcine glutathione S-transferase pi (GST pi): The enzyme catalyzes the reaction of mBBr with glutathione. S-(Hydroxyethyl)bimane, a nonreactive analog of monobromobimane, acts as a competitive inhi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19248b19abb4ed8612d8f6347e31296f
https://doi.org/10.1110/ps.03249303
https://doi.org/10.1110/ps.03249303
Publikováno v:
Journal of Biological Chemistry. 283:32880-32888
Human glutathione transferase pi (GST pi) has been crystallized as a homodimer, with a subunit molecular mass of approximately 23 kDa; however, in solution the average molecular mass depends on protein concentration, approaching that of monomer at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4588c254b6a530e6a5a76b57fab3b478
https://doi.org/10.1074/jbc.m805484200
https://doi.org/10.1074/jbc.m805484200
Autor:
Sharmila Sivendran, Roberta F. Colman
Publikováno v:
Protein Science. 17:1162-1174
Adenylosuccinate lyase (ASL) catalyzes two beta-elimination reactions in purine biosynthesis, leading to the question of whether the two substrates occupy the same or different active sites. Kinetic studies of Bacillus subtilis and human ASL with a n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b104ef9588eff00e3443b4cc753df794
https://doi.org/10.1110/ps.034777.108
https://doi.org/10.1110/ps.034777.108
Publikováno v:
Biochemistry. 47:2923-2934
Adenylosuccinate lyase (ASL) of Bacillus subtilis is a homotetramer in which three subunits contribute to each of four active sites. We sought to evaluate the types of interactions responsible for subunit association by studying the enzyme's oligomer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a289b8248dc201c3cc642323a6f9e654
https://doi.org/10.1021/bi701400c
https://doi.org/10.1021/bi701400c
Publikováno v:
Journal of Molecular Biology. 370:541-554
Adenylosuccinate lyase (ADL) catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR) to 5-aminoimidazole-4-carboxamide ribotide (AICAR) and fumarate, and of adenylosuccinate (ADS) to adenosine monophosphate (AMP) and f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::690ab01bbdf680b7d95497bcac038c03
https://doi.org/10.1016/j.jmb.2007.04.052
https://doi.org/10.1016/j.jmb.2007.04.052
Autor:
Krzysztof P Bzymek, Roberta F. Colman
Publikováno v:
Biochemistry. 46:5391-5397
Human NAD-dependent isocitrate dehydrogenase (IDH) is allosterically activated by ADP by lowering the Km for isocitrate. The enzyme has three subunit types with distinguishable sequences present in the approximate ratio 2alpha:1beta:1gamma and, per t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ae18a744e8e7f3f85ba45bf4d0e86a0
https://doi.org/10.1021/bi700061t
https://doi.org/10.1021/bi700061t
Autor:
Roberta F. Colman, Luis A. Ralat
Publikováno v:
Biochemistry. 45:12491-12499
Alpha-tocopherol, the most abundant form of vitamin E present in humans, is a noncompetitive inhibitor of glutathione S-transferase pi (GST pi), but its binding site had not been located. Tocopherol iodoacetate (TIA), a reactive analogue, produces a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d57a67224c9c3013a992278ba914b3ec
https://doi.org/10.1021/bi061330k
https://doi.org/10.1021/bi061330k