Zobrazeno 1 - 10 of 44 pro vyhledávání: '"B E Haley"'
1
Oxidatively Induced Structural Alteration of Glutamine Synthetase Assessed by Analysis of Spin Label Incorporation Kinetics: Relevance to Alzheimer's Disease
Autor: Ram Subramaniam, P. Cole, D A Butterfield, P. Bummer, Marina V. Aksenova, B E Haley, Kenneth Hensley, John M. Carney, Michael Y. Aksenov
Publikováno v: Journal of Neurochemistry. 68:2451-2457
The activity of the astrocytic enzyme glutamine synthetase (GS) is decreased in the Alzheimer's disease brain, which may have relevance to mechanisms of chronic excitotoxicity. The molecular perturbation(s) that results in GS inactivation is not know
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec826922e4c90c405a0f32ab67e53428
https://doi.org/10.1046/j.1471-4159.1997.68062451.x
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2
HgEDTA Complex Inhibits GTP Interactions with the E-Site of Brain β-Tubulin
Autor: B E Haley, J C Pendergrass, J T Slevin, E F Duhr
Publikováno v: Toxicology and Applied Pharmacology. 122:273-280
We have found that EDTA and EGTA complexes of Hg2+, which conventional wisdom has assumed are biologically inert, are potentially injurious to the neuronal cytoskeleton. Tubulin, a major protein component of the neuronal cytoskeleton, is the target o
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34b3c457d29b2a8f1374fd48c9906f03
https://doi.org/10.1006/taap.1993.1196
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3
Photoaffinity labeling of ribulose-1,5-bisphosphate carboxylase/oxygenase activase with ATP gamma-benzophenone. Identification of the ATP gamma-phosphate binding domain
Autor: G. Sievert, B. E. Haley, Michael E. Salvucci, K. Rajagopalan, David S. Watt
Publikováno v: Journal of Biological Chemistry. 268:14239-14244
The phosphate-binding domain of the ATP-binding site of tobacco Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) activase was elucidated by photo-affinity labeling with a monoanhydride of ADP with N-(4-(benzoyl)phenylmethyl)phosphoramide ([g
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::064c7e12290818ce4b3a58bd6d82e7c1
https://doi.org/10.1016/s0021-9258(19)85232-8
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5
Synthesis and characterization of 5-azido-UDP-glucuronic acid. A new photoaffinity probe for UDP-glucuronic acid-utilizing proteins
Autor: R Lester, B E Haley, Piotr Zimniak, Richard R. Drake, Anna Radominska, Alan D. Elbein
Publikováno v: Journal of Biological Chemistry. 266:23257-23260
A new active site-directed photoaffinity analogue, [beta-32P]5-azido-UDP-glucuronic acid (UDP-GlcA), was enzymatically synthesized from [beta-32P]5-N3UDP-Glc using UDP-glucose dehydrogenase. The product was characterized by its mobility on ion exchan
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1ed5adebda61c6034504c78fcad85a57
https://doi.org/10.1016/s0021-9258(18)54490-2
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6
Identification of the uridine 5'-diphosphoglucose (UDP-Glc) binding subunit of cellulose synthase in Acetobacter xylinum using the photoaffinity probe 5-azido-UDP-Glc
Autor: Fong Chyr Lin, R. R. Drake, B. E. Haley, R. M. Brown
Publikováno v: Journal of Biological Chemistry. 265:4782-4784
Photoaffinity labeling of purified cellulose synthase with [beta-32P]5-azidouridine 5'-diphosphoglucose (UDP-Glc) has been used to identify the UDP-Glc binding subunit of the cellulose synthase from Acetobacter xylinum strain ATCC 53582. The results
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::dd0ea85578b80e9009f3bf7d8f9b8d55
https://doi.org/10.1016/s0021-9258(19)34039-6
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8
Mercury vapor inhalation inhibits binding of GTP to tubulin in rat brain: similarity to a molecular lesion in Alzheimer diseased brain
Autor: J C, Pendergrass, B E, Haley, M J, Vimy, S A, Winfield, F L, Lorscheider
Publikováno v: Neurotoxicology. 18(2)
Hg2+ interacts with brain tubulin and disassembles microtubules that maintain neurite structure. Since it is well known that Hg vapor (Hg0) is continuously released from "silver" amalgam tooth fillings and is absorbed into brain, rats were exposed to
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::20436f7a06b49028c909751b62dc960a
https://pubmed.ncbi.nlm.nih.gov/9291481
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9
Identification of peptides within the base binding domains of the GTP- and ATP-specific binding sites of tubulin
Autor: B, Jayaram, B E, Haley
Publikováno v: The Journal of biological chemistry. 269(5)
Using gamma-32P-labeled 8-azidopurine nucleotide photoaffinity probes of GTP and ATP, the respective purine ring binding domain peptides of tubulin have been identified. First, the location of the GTP-specific binding site was shown to be on the beta
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3348c013b5be3e9f7b884817384b187d
https://pubmed.ncbi.nlm.nih.gov/8106359
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10
Photoaffinity labeling of human placental NAD(+)-linked 15-hydroxyprostaglandin dehydrogenase with [alpha-32P]2N3NAD+. Identification of a peptide in the adenine ring binding domain
Autor: A J, Chavan, C M, Ensor, P, Wu, B E, Haley, H H, Tai
Publikováno v: The Journal of biological chemistry. 268(22)
Oxidation of many prostaglandins at C-15 results in the formation of 15-keto metabolites, which have reduced biological activity. This reaction is catalyzed by NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase. Using the photoaffinity analog of
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f499348cad6735a260b574c799250160
https://pubmed.ncbi.nlm.nih.gov/8344929
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