Výsledky vyhledávání - "D M, Mueller"

Partial assembly of the yeast mitochondrial ATP synthase

Autor: D M, Mueller

Publikováno v: Journal of bioenergetics and biomembranes. 32(4)

The mitochondrial ATP synthase is a molecular motor that drives the phosphorylation of ADP to ATP. The yeast mitochondrial ATP synthase is composed of at least 19 different peptides, which comprise the F1 catalytic domain, the F0 proton pore, and two

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4ddce66f68ab7b0e25b34af2843588ec
https://pubmed.ncbi.nlm.nih.gov/11768301

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Production of brominating intermediates by myeloperoxidase. A transhalogenation pathway for generating mutagenic nucleobases during inflammation

Autor: J P, Henderson, J, Byun, M V, Williams, D M, Mueller, M L, McCormick, J W, Heinecke

Publikováno v: The Journal of biological chemistry. 276(11)

The existence of interhalogen compounds was proposed more than a century ago, but no biological roles have been attributed to these highly oxidizing intermediates. In this study, we determined whether the peroxidases of white blood cells can generate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e7e38364ba281d3a6b3ef11e644fe873
https://pubmed.ncbi.nlm.nih.gov/11096071

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Complementation of deletion mutants in the genes encoding the F1-ATPase by expression of the corresponding bovine subunits in yeast S. cerevisiae

Autor: J, Lai-Zhang, D M, Mueller

Publikováno v: European journal of biochemistry. 267(8)

The F1F0 ATP synthase is composed of the F1-ATPase which is bound to F0, in the inner membrane of the mitochondrion. Assembly and function of the enzyme is a complicated task requiring the interactions of many proteins for the folding, import, assemb

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2b44ce3017dbd71bb1726e6f780133b2
https://pubmed.ncbi.nlm.nih.gov/10759867

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The role of the amino-terminal beta-barrel domain of the alpha and beta subunits in the yeast F1-ATPase

Autor: B, Yao, D M, Mueller

Publikováno v: Journal of bioenergetics and biomembranes. 31(2)

The crystal structure of mitochondrial F1-ATPase indicates that the alpha and beta subunits fold into a structure defined by three domains: the top beta-barrel domain, the middle nucleotide-binding domain, and the C-terminal alpha-helix bundle domain

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4ae9a20a122a3094a9b985ab96890b88
https://pubmed.ncbi.nlm.nih.gov/10449236

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Detecting oxidative modification of biomolecules with isotope dilution mass spectrometry: sensitive and quantitative assays for oxidized amino acids in proteins and tissues

Autor: J W, Heinecke, F F, Hsu, J R, Crowley, S L, Hazen, C, Leeuwenburgh, D M, Mueller, J E, Rasmussen, J, Turk

Publikováno v: Methods in enzymology. 300

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::75a26868785ba54c8c8ce52876b4139f
https://pubmed.ncbi.nlm.nih.gov/9919517

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Mass spectrometric quantification of 3-chlorotyrosine in human tissues with attomole sensitivity: a sensitive and specific marker for myeloperoxidase-catalyzed chlorination at sites of inflammation

Autor: S L, Hazen, J R, Crowley, D M, Mueller, J W, Heinecke

Publikováno v: Free radical biologymedicine. 23(6)

Oxidative modification of proteins has been implicated in a variety of processes ranging from atherosclerosis to aging. Identifying the underlying oxidation pathways has proven difficult, however, due to the lack of specific markers for distinct oxid

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::31d59bd462fdd804c6c190beee7edf14
https://pubmed.ncbi.nlm.nih.gov/9378370

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Tyrosyl radical generated by myeloperoxidase is a physiological catalyst for the initiation of lipid peroxidation in low density lipoprotein

Autor: M L, Savenkova, D M, Mueller, J W, Heinecke

Publikováno v: The Journal of biological chemistry. 269(32)

Myeloperoxidase, a heme protein secreted by activated phagocytes, is expressed in human atherosclerotic lesions. The enzyme uses H2O2 generated by the cells to oxidize L-tyrosine to tyrosyl radical, a catalyst for protein dityrosine synthesis. We hav

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a83f0ce1049708873f031bf7576f6325
https://pubmed.ncbi.nlm.nih.gov/8051134

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Primary structural constraints of P-loop of mitochondrial F1-ATPase from yeast

Autor: H, Shen, B Y, Yao, D M, Mueller

Publikováno v: The Journal of biological chemistry. 269(13)

Nucleotide binding proteins, including ras, elongation factor Tu, adenylate kinase, and the mitochondrial F1-ATPase have a glycine-rich motif known as the P-loop or the Walker A sequence (Walker, J. E., Saraste, M., Runswick, M. J., and Gay, N. J. (1

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d8a1cf53adbcfe8f2847305cbbd522b6
https://pubmed.ncbi.nlm.nih.gov/8144526

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Heterologous expression, purification, and biochemistry of the oligomycin sensitivity conferring protein (OSCP) from yeast

Autor: A, Mukhopadhyay, X Q, Zhou, M, Uh, D M, Mueller

Publikováno v: The Journal of biological chemistry. 267(36)

Yeast Saccharomyces cerevisiae oligomycin sensitivity conferring proteins (OSCP) have been expressed in Escherichia coli. Heterologous expression results in production of a protein that is identical to yeast mature OSCP, including the absence of the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ff307439b4d38bea99df2c676bda7a9f
https://pubmed.ncbi.nlm.nih.gov/1464586

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The gene coding for the yeast oligomycin sensitivity-conferring protein

Autor: M, Uh, D, Jones, D M, Mueller

Publikováno v: The Journal of biological chemistry. 265(31)

The gene coding for the yeast Saccharomyces cerevisiae mitochondrial oligomycin sensitivity-conferring protein (OSCP) has been sequenced, and the gene products have been characterized. The OSCP is subunit 5 of the mitochondrial ATP synthase, a multim

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::37deb81a87d1f77262dbdbb08c02d98b
https://pubmed.ncbi.nlm.nih.gov/2146269

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