Výsledky vyhledávání - "Timothy J. Kirksey"

Class I MHC Is Stabilized Against Thermal Denaturation by Physiological Concentrations of NaCl

Autor: Rui Zhao, Ashwani Sharma, Jean-Pierre Abastado, Lihong Jiang, Timothy J. Kirksey, Edward J. Collins, Michael A. Batalia, Shuqin Yan

Publikováno v: Biochemistry. 39:9030-9038

Class I MHC molecules are ternary complexes composed of an allotype specific heavy chain, a noncovalently associated protein beta(2)-microglobulin (beta(2)m), and a peptide. The complexes are assembled in the endoplasmic reticulum by a complex series

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38ef351be9b428e2dd0a43696176a727
https://doi.org/10.1021/bi000442n

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The Structural Basis for the Increased Immunogenicity of Two HIV-Reverse Transcriptase Peptide Variant/Class I Major Histocompatibility Complexes

Autor: Jeffrey A. Frelinger, Timothy J. Kirksey, Rebecca R. Pogue-Caley, Edward J. Collins

Publikováno v: Journal of Biological Chemistry. 274:37259-37264

Designing altered peptide ligands to generate specific immunological reactivity when bound to class I major histocompatibility complexes is important for both therapeutic and prophylactic reasons. We have previously shown that two altered peptides, d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98e1da87a3baf957dd425224842c8175
https://doi.org/10.1074/jbc.274.52.37259

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Site-Directed Mutagenesis of a Highly Conserved Aspartate in the Putative 10-Formyl-Tetrahydrofolate Binding Site of Yeast C1-Tetrahydrofolate Synthase

Autor: Timothy J. Kirksey, Dean R. Appling

Publikováno v: Archives of Biochemistry and Biophysics. 333:251-259

C1-tetrahydrofolate (THF) synthase is a eukaryotic trifunctional protein possessing the activities 10-formyl-THF synthetase, 5,10-methenyl-THF cyclohydrolase, and 5,10-methylene-THF dehydrogenase. Although the 10-formyl-THF synthetase reaction (a rev

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7bfdcca10c1fbe31de40eee4ebae7a4
https://doi.org/10.1006/abbi.1996.0388

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Mutagenesis at a Highly Conserved Tyrosine in Monoamine Oxidase B Affects FAD Incorporation and Catalytic Activity

Autor: Creed W. Abell, Timothy J. Kirksey, Binhua P. Zhou, Duane A. Lewis, Sau-Wah Kwan

Publikováno v: Biochemistry. 34:9526-9531

Monoamine oxidase B (MAO B), an integral protein of the outer mitochondrial membrane, catalyzes the oxidative deamination of various neuroactive and vasoactive amines. A covalently bound FAD cofactor at Cys-397 of human MAO B is required for the oxid

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ceefd0dd662e9082816c290ad34d3533
https://doi.org/10.1021/bi00029a029

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