AZURIN
AZURIN结构式
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常用名 | AZURIN | 英文名 | AZURIN |
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| CAS号 | 12284-43-4 | 分子量 | N/A | |
| 密度 | N/A | 沸点 | N/A | |
| 分子式 | N/A | 熔点 | N/A | |
| MSDS | 美版 | 闪点 | N/A |
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Understanding the mechanism of short-range electron transfer using an immobilized cupredoxin.
J. Am. Chem. Soc. 134(29) , 11848-51, (2012) The hydrophobic patch of azurin (AZ) from Pseudomonas aeruginosa is an important recognition surface for electron transfer (ET) reactions. The influence of changing the size of this region, by mutating the C-terminal copper-binding loop, on the ET reactivity ... |
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A first-in-class, first-in-human, phase I trial of p28, a non-HDM2-mediated peptide inhibitor of p53 ubiquitination in patients with advanced solid tumours.
Br. J. Cancer 108(5) , 1061-70, (2013) This first-in-human, phase I clinical trial of p28 (NSC745104), a 28-amino-acid fragment of the cupredoxin azurin, investigated the safety, tolerability, pharmacokinetics and preliminary activity of p28 in patients with p53(+) metastatic solid tumours.A total... |
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Structural and functional effects of Cu metalloprotein-driven silver nanoparticle dissolution.
Environ. Sci. Technol. 46(11) , 6355-62, (2012) Interactions of a model Cu-metalloprotein, azurin, with 10-100 nm silver nanoparticles (NPs) were examined to elucidate the role of oxidative dissolution and protein interaction on the biological reactivity of NPs. Although minimal protein and NP structural c... |
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Effects of the protein environment on the spectral properties of tryptophan radicals in Pseudomonas aeruginosa azurin.
J. Am. Chem. Soc. 135(12) , 4822-33, (2013) Many biological electron-transfer reactions involve short-lived tryptophan radicals as key reactive intermediates. While these species are difficult to investigate, the recent photogeneration of a long-lived neutral tryptophan radical in two Pseudomonas aerug... |
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Escherichia coli Nissle 1917 targets and restrains mouse B16 melanoma and 4T1 breast tumors through expression of azurin protein.
Appl. Environ. Microbiol. 78(21) , 7603-10, (2012) Many studies have demonstrated that intravenously administered bacteria can target and proliferate in solid tumors and then quickly be released from other organs. Here, we employed the tumor-targeting property of Escherichia coli Nissle 1917 to inhibit mouse ... |
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p28, a first in class peptide inhibitor of cop1 binding to p53.
Br. J. Cancer 108(12) , 2495-504, (2013) A 28 amino-acid (aa) cell-penetrating peptide (p28) derived from azurin, a redox protein secreted from the opportunistic pathogen Pseudomonas aeruginosa, produces a post-translational increase in p53 in cancer cells by inhibiting its ubiquitination.In silico ... |
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Outer-sphere contributions to the electronic structure of type zero copper proteins.
J. Am. Chem. Soc. 134(19) , 8241-53, (2012) Bioinorganic canon states that active-site thiolate coordination promotes rapid electron transfer (ET) to and from type 1 copper proteins. In recent work, we have found that copper ET sites in proteins also can be constructed without thiolate ligation (called... |
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Axial interactions in the mixed-valent CuA active site and role of the axial methionine in electron transfer.
Proc. Natl. Acad. Sci. U. S. A. 110(36) , 14658-63, (2013) Within Cu-containing electron transfer active sites, the role of the axial ligand in type 1 sites is well defined, yet its role in the binuclear mixed-valent CuA sites is less clear. Recently, the mutation of the axial Met to Leu in a CuA site engineered into... |
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Azurin as a protein scaffold for a low-coordinate nonheme iron site with a small-molecule binding pocket.
J. Am. Chem. Soc. 134(48) , 19746-57, (2012) The apoprotein of Pseudomonas aeruginosa azurin binds iron(II) to give a 1:1 complex, which has been characterized by electronic absorption, Mössbauer, and NMR spectroscopies, as well as X-ray crystallography and quantum-chemical computations. Despite potenti... |
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Periplasmic response upon disruption of transmembrane Cu transport in Pseudomonas aeruginosa.
Metallomics 5(2) , 144-51, (2013) Pseudomonas aeruginosa, an opportunistic pathogen, has two transmembrane Cu(+) transport ATPases, CopA1 and CopA2. Both proteins export cytoplasmic Cu(+) into the periplasm and mutation of either gene leads to attenuation of virulence. CopA1 is required for m... |