Search Results - "Mauro, J.M."

Self-assembled nanoscale biosensors based on quantum dot FRET donors by Mattoussi, Hedi, Mauro, J. Matthew, Medintz, Igor L, Clapp, Aaron R, Goldman, Ellen R, Fisher, Brent

“…The potential of luminescent semiconductor quantum dots (QDs) to enable development of hybrid inorganic-bioreceptor sensing materials has remained largely…”
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Avidin:  A Natural Bridge for Quantum Dot-Antibody Conjugates by Goldman, Ellen R, Balighian, Eric D, Mattoussi, Hedi, Kuno, M. Kenneth, Mauro, J. Matthew, Tran, Phan T, Anderson, George P

“…We describe the preparation and characterization of bioinorganic conjugates in which luminescent semiconductor CdSe−ZnS core−shell nanocrystal quantum dots…”
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Use of Luminescent CdSe-ZnS Nanocrystal Bioconjugates in Quantum Dot-Based Nanosensors by Tran, P.T., Anderson, G.P., Mauro, J.M., Mattoussi, H.

“…Biomolecules labeled with luminescent colloidal semiconductor quantum dots (QDs) have potential for use in numerous applications, including fluoro‐immunoassays…”
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Bioconjugation of Highly Luminescent Colloidal CdSe-ZnS Quantum Dots with an Engineered Two-Domain Recombinant Protein by Mattoussi, H., Mauro, J.M., Goldman, E.R., Green, T.M., Anderson, G.P., Sundar, V.C., Bawendi, M.G.

“…We present a novel approach, based on molecular self‐assembly driven by electrostatic attractions, for conjugating inorganic colloidal semiconductor…”
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General Strategy for Biosensor Design and Construction Employing Multifunctional Surface-Tethered Components by Medintz, Igor L, Anderson, George P, Lassman, Michael E, Goldman, Ellen R, Bettencourt, Laura A, Mauro, J. Matthew

“…Biosensors function by reversibly linking bioreceptor−target analyte binding with closely integrated signal generation and can either continuously monitor…”
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Luminescent Quantum Dot-Adaptor Protein-Antibody Conjugates for Use in Fluoroimmunoassays by Goldman, E.R., Balighian, E.D., Kuno, M.K., Labrenz, S., Anderson, G.P., Mauro, J.M., Mattoussi, H.

“…A method for the preparation and characterization of bioinorganic conjugates made with highly luminescent semiconductor CdSe–ZnS core‐shell quantum dots (QDs)…”
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Construction and expression of functional multi-domain polypeptides in Escherichia coli: expression of the Neurospora crassa metallothionein gene by Mauro, J.M, Pazirandeh, M

“…J.M. MAURO and M. PAZIRANDEH.2000. A system for the construction of polymeric peptides in Escherichia coli was utilized to prepare a library of plasmids coding…”
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Expression of the Neurospora crassa metallothionein gene in Escherichia coli and its effect on heavy-metal uptake by Pazirandeh, M, Chrisey, L.A, Mauro, J.M, Campbell, J.R, Gaber, B.P

“…The gene coding for the Neurospora crassa metallothionein protein was chemically synthesized and cloned into the fusion expression vectors pMa1-c and pMa1-p…”
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X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis by Wang, Jimin, Mauro, J. Matthew, Edwards, Steven L, Oatley, Stuart J, Fishel, Laurence A, Ashford, Victor A, Nguyen Huu Xuong, Kraut, Joseph

“…The 2.2-A X-ray structure for CCP(MI), a plasmid-encoded form of Saccharomyces cerevisiae cytochrome c peroxidase (CCP) expressed in Escherichia coli [Fishel,…”
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Yeast cytochrome c peroxidase: mutagenesis and expression in Escherichia coli show tryptophan-51 is not the radical site in compound I by Fishel, Laurence A, Villafranca, Jesus E, Mauro, J. Matthew, Kraut, Joseph

“…Using oligonucleotide-directed site-specific mutagenesis, we have constructed a system for the mutation and expression of yeast cytochrome c peroxidase (CCP,…”
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Structure of plant and fungal peroxidases by Welinder, K G, Mauro, J M, Nørskov-Lauritsen, L

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Conversion of the proximal histidine ligand to glutamine restores activity to an inactive mutant of cytochrome c peroxidase by CHOUDHURY, K, SUNDARAMOORTHY, M, MAURO, J. M, POULOS, T. L

“…Using site-directed mutagenesis, a double mutant in yeast cytochrome c peroxidase (CCP) has been constructed where the proximal ligand, His175, has been…”
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Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235 yields Asn-235 mutant by Satterlee, J.D., Erman, J.E., Mauro, J.M., Kraut, J.

“…Proton NMR spectra of cytochrome c peroxidase (CcP) isolated from yeast (wild type) and two Escherichia coli expressed proteins, the parent expressed protein…”
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Site-directed mutagenesis of yeast cytochrome c peroxidase shows histidine 181 is not required for oxidation of ferrocytochrome c by Miller, Mark A, Hazzard, James T, Mauro, J. Matthew, Edwards, Steven L, Simons, Peter C, Tollin, Gordon, Kraut, Joseph

“…The long-distance electron transfer observed in the complex formed between ferrocytochrome c and compound I, the peroxide-oxidized form of cytochrome c…”
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effect of the Asn82 to Asp mutation in yeast cytochrome c peroxidase studied by proton NMR spectroscopy by Satterlee, J.D, Alam, S.L, Mauro, J.M, Erman, J.E, Poulos, T.L

“…Proton NMR studies of the mutant of baker's yeast cytochrome c peroxidase-cyanide with the Asn 82 leads to Asp mutation ([N82D]cytochrome c peroxidase-CN) are…”
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