Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Brett W. Lennon"'
Autor:
Rowena G. Matthews, Martha L. Ludwig, Brian D. Guenther, Elizabeth M. Campbell, Brett W. Lennon, Robert Pejchal
Publikováno v:
Biochemistry. 45:4808-4818
In human methylenetetrahydrofolate reductase (MTHFR) the Ala222Val (677C-->T) polymorphism encodes a heat-labile gene product that is associated with elevated levels of homocysteine and possibly with risk for cardiovascular disease. Generation of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c66e0df78c4188464806b56a28e23416
https://doi.org/10.1021/bi052294c
https://doi.org/10.1021/bi052294c
Autor:
Katherine A. Pattridge, Vahe Bandarian, Brett W. Lennon, Rowena G. Matthews, Donald P. Huddler, Martha L. Ludwig
Publikováno v:
Nature Structural Biology. 9:53-56
B(12)-dependent methionine synthase (MetH) from Escherichia coli is a large modular protein that uses bound cobalamin as an intermediate methyl carrier. Major domain rearrangements have been postulated to explain how cobalamin reacts with three diffe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46a034045e712b57dff79ab9f38251eb
https://doi.org/10.1038/nsb738
https://doi.org/10.1038/nsb738
Publikováno v:
Science. 289:1190-1194
In thioredoxin reductase (TrxR) from Escherichia coli , cycles of reduction and reoxidation of the flavin adenine dinucleotide (FAD) cofactor depend on rate-limiting rearrangements of the FAD and NADPH (reduced form of nicotinamide adenine dinucleoti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::560a811e6fc831a0a9b7b8fddea8c995
https://doi.org/10.1126/science.289.5482.1190
https://doi.org/10.1126/science.289.5482.1190
Autor:
Brett W. Lennon, Charles H. Williams
Publikováno v:
Biochemistry. 35:4704-4712
Thioredoxin reductase from Escherichia coli is a member of the pyridine nucleotide-disulfide oxidoreductase family, and contains one FAD and one redox-active disulfide per subunit. It is known that two other well-studied members of this family, lipoa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed2c9ea7f1232865f8f800fb59cd98fb
https://doi.org/10.1021/bi952521i
https://doi.org/10.1021/bi952521i
Autor:
Charles H. Williams, Brett W. Lennon
Publikováno v:
Biochemistry. 34:3670-3677
The kinetics of the oxidative half-reaction between reduced thioredoxin reductase and oxidized thioredoxin measured in the presence and absence of pyridine nucleotide show a significant difference in the rates of the main phase of oxidation. When 1 e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44ff07470d4b4eab8b26f75cabfb38ab
https://doi.org/10.1021/bi00011a023
https://doi.org/10.1021/bi00011a023
Publikováno v:
Toxicon. 28:718-722
Crotoxin was cross-linked using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride. Cross-linked crotoxin had the expected amino-terminal amino acids, amino acid composition, behavior on SDS-PAGE and an 80% reduction of reactable lysine res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::855706fb2c72571b4c24395f7092b9b6
https://doi.org/10.1016/0041-0101(90)90261-5
https://doi.org/10.1016/0041-0101(90)90261-5
Autor:
Pan-Fen Wang, Donna M. Veine, Martha L. Ludwig, Charles H. Williams, Sylke Müller, Katja Becker, Brett W. Lennon, R.H. Schirmer, Arscott Ld
Publikováno v:
European journal of biochemistry. 267(20)
Thioredoxin reductase (EC 1.6.4.5) is a widely distributed flavoprotein that catalyzes the NADPH-dependent reduction of thioredoxin. Thioredoxin plays several key roles in maintaining the redox environment of the cell. Like all members of the enzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47305126da3e761a20e89678cf6be520
https://pubmed.ncbi.nlm.nih.gov/11012662
https://pubmed.ncbi.nlm.nih.gov/11012662
Publikováno v:
Protein science : a publication of the Protein Society. 8(11)
Catalysis by thioredoxin reductase (TrxR) from Escherichia coli requires alternation between two domain arrangements. One of these conformations has been observed by X-ray crystallography (Waksman G, Krishna TSR, Williams CH Jr, Kuriyan J, 1994, J Mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0330fef117ac6d0e8f83b5313b5f937d
https://pubmed.ncbi.nlm.nih.gov/10595539
https://pubmed.ncbi.nlm.nih.gov/10595539
Autor:
Charles H. Williams, Brett W. Lennon
Publikováno v:
Biochemistry. 36(31)
Thioredoxin reductase is a homodimeric flavoenzyme containing a flavin adenine dinucleotide (FAD) and a redox-active disulfide in each subunit. Structural work on the enzyme from Escherichia coli suggests that thioredoxin reductase exists in two conf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::919fb3dfeec7aa6054423f7363e82e47
https://pubmed.ncbi.nlm.nih.gov/9235991
https://pubmed.ncbi.nlm.nih.gov/9235991
Autor:
Ivan I. Kaiser, Brett W. Lennon
Publikováno v:
Comparative biochemistry and physiology. B, Comparative biochemistry. 97(4)
1. 1. A crotoxin-like protein was isolated from the venom of a South American rattlesnake Crotalus durissus collilineatus. 2. 2. Many of its properties are similar to those of crotoxin, including its non-covalent heterodimeric structure, electrophore
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b0f4cfbb91f129db94d0316268f89ed
https://pubmed.ncbi.nlm.nih.gov/2085953
https://pubmed.ncbi.nlm.nih.gov/2085953