Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Milton J. Axley"'
Autor:
Maureen Sampson, Edward B. Neufeld, Emily Hillman, Lita A. Freeman, Boris L. Vaisman, Milton J. Axley, Sotirios K. Karathanasis, Milton Pryor, Alan T. Remaley, Scott M. Gordon
Publikováno v:
Journal of Pharmacology and Experimental Therapeutics. 368:423-434
Familial LCAT deficiency (FLD) is due to mutations in lecithin:cholesterol acyltransferase (LCAT), a plasma enzyme that esterifies cholesterol on lipoproteins. FLD is associated with markedly reduced levels of plasma high-density lipoprotein and chol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1eb8f1178500f03930b896318f51a521
https://doi.org/10.1124/jpet.118.251876
https://doi.org/10.1124/jpet.118.251876
Autor:
Joomi Ahn, John J.G. Tesmer, Wenmin Yuan, Alisa Glukhova, Anna Schwendeman, Louise Chang, Milton J. Axley, Taylor D. Manett, Christopher Larkin, Kelly A. Manthei, James A. Shayman
Publikováno v:
Journal of Biological Chemistry. 292:20313-20327
Lecithin:cholesterol acyltransferase (LCAT) plays a key role in reverse cholesterol transport by transferring an acyl group from phosphatidylcholine to cholesterol, promoting the maturation of high-density lipoproteins (HDL) from discoidal to spheric
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6087b227c87c8f1c286d90d862ee1fc
https://doi.org/10.1074/jbc.m117.802736
https://doi.org/10.1074/jbc.m117.802736
Autor:
Milton J Axley, Peter Barker, Lorin Roskos, Magnus Aurivillius, Rainard Fuhr, Ubaldo J. Martin, Pablo Forte, Li Yan
Publikováno v:
The Journal of asthma : official journal of the Association for the Care of Asthma. 58(1)
We compared the pharmacokinetic exposure following a single subcutaneous dose of benralizumab 30 mg using either autoinjectors (AI) or accessorized prefilled syringes (APFS). APFS and AI functionality and reliability for at-home benralizumab delivery
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33af716821d4ac9d710d4dae51a625ce
https://pubmed.ncbi.nlm.nih.gov/31539289
https://pubmed.ncbi.nlm.nih.gov/31539289
Autor:
Li Yan, Ubaldo J. Martin, Pablo Forte, Rainard Fuhr, Magnus Aurivillius, Peter Barker, Milton J. Axley
Publikováno v:
Journal of Allergy and Clinical Immunology. 143:AB95
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aee49cecd09f9e6588b2a87cd147cd63
https://doi.org/10.1016/j.jaci.2018.12.291
https://doi.org/10.1016/j.jaci.2018.12.291
Autor:
Mauro Abbate, Alice Ossoli, Sotirios K. Karathanasis, Seth G. Thacker, Irina N. Baranova, Carlamaria Zoja, Christine A. Brantner, Boris L. Vaisman, Milton Pryor, Alan T. Remaley, Laura Calabresi, Edward B. Neufeld, Lita A. Freeman, Guido Franceschini, Cecilia Vitali, Nicolás O. Francone, Monica Locatelli, Milton J. Axley, Stephen J. Demosky
Publikováno v:
Arteriosclerosis, Thrombosis, and Vascular Biology. 36
Familial lecithin:cholesterol acyltransferase (LCAT) deficiency (FLD) is characterized by low HDL, accumulation of an abnormal cholesterol-rich multilamellar particle called lipoprotein-X (LpX) in plasma, and renal disease. The aim of our study was t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::93795d4f13fa5e1498e979ea235c6407
https://doi.org/10.1161/atvb.36.suppl_1.230
https://doi.org/10.1161/atvb.36.suppl_1.230
Autor:
Milton J. Axley, Milton Pryor, Boris L. Vaisman, Alan T. Remaley, Sotirios K. Karathanasis, Maureen Sampson, Edward B. Neufeld, Lita A. Freeman
Publikováno v:
Arteriosclerosis, Thrombosis, and Vascular Biology. 36
Familial LCAT Deficiency (FLD) is associated with the gradual development of severe kidney dysfunction from the renal deposition of LpX, an abnormal lipoprotein that accumulates in this disorder. The aim of our study was to develop an efficient mouse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::193a513399c4477c90b1d09332d887ea
https://doi.org/10.1161/atvb.36.suppl_1.234
https://doi.org/10.1161/atvb.36.suppl_1.234
Publikováno v:
Biochemistry. 36:812-822
Purified uridine diphosphate N-acetylenolpyruvylglucosamine reductase (E.C. 1.1.1.158) was analyzed by circular dichroism (CD) and UV-visible spectroscopy to establish the spectral properties of its tightly bound flavin adenine dinucleotide (FAD) cof
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5429646f7a4d2e90ed759c95cdc8e843
https://doi.org/10.1021/bi962260s
https://doi.org/10.1021/bi962260s
Publikováno v:
Proceedings of the National Academy of Sciences. 91:7708-7711
Formate dehydrogenase H from Escherichia coli contains multiple redox centers, which include a molybdopterin cofactor, an iron-sulfur center, and a selenocysteine residue (SeCys-140 in the polypeptide chain) that is essential for catalytic activity.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::244f6f87e1d40970738e11ede76815d4
https://doi.org/10.1073/pnas.91.16.7708
https://doi.org/10.1073/pnas.91.16.7708
Publikováno v:
Quality by Design for Biopharmaceuticals
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::506ff0d96f309114420b84f4c7f1d454
https://doi.org/10.1002/9780470466315.ch4
https://doi.org/10.1002/9780470466315.ch4
Publikováno v:
Proceedings of the National Academy of Sciences. 88:8450-8454
Formate dehydrogenase H of Escherichia coli contains selenocysteine as an integral amino acid. We have purified a mutant form of the enzyme in which cysteine replaces selenocysteine. To elucidate the essential catalytic role of selenocysteine, kineti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::794535574d89f550686a935e1d99ffb2
https://doi.org/10.1073/pnas.88.19.8450
https://doi.org/10.1073/pnas.88.19.8450