2014
Lanthanide ion (III) complexes of 1,4,7,10‐tetraazacyclododecane‐1,4,7,10‐tetraaminophosphonate for dual biosensing of pH with chemical exchange saturation transfer (CEST) and biosensor imaging of redundant deviation in shifts (BIRDS)
Huang Y, Coman D, Ali MM, Hyder F. Lanthanide ion (III) complexes of 1,4,7,10‐tetraazacyclododecane‐1,4,7,10‐tetraaminophosphonate for dual biosensing of pH with chemical exchange saturation transfer (CEST) and biosensor imaging of redundant deviation in shifts (BIRDS). Contrast Media & Molecular Imaging 2014, 10: 51-58. PMID: 24801742, PMCID: PMC4222994, DOI: 10.1002/cmmi.1604.Peer-Reviewed Original ResearchConceptsChemical exchange saturation transferLanthanide complexesExchangeable protonsProton resonancesPH imagingLanthanide ion complexesRedundant deviationChemical shift differencesChemical exchange saturation transfer contrastCEST contrastIon complexesChemical shiftsQuantitative pH imagingShift differencesSingle-proton resonancesChemical shift imaging methodsMagnetic resonanceCEST experimentsWater protonsNonexchangeable protonsParamagnetic effectSaturation transferBiosensorComplexesWater resonance
2011
A lanthanide complex with dual biosensing properties: CEST (chemical exchange saturation transfer) and BIRDS (biosensor imaging of redundant deviation in shifts) with europium DOTA–tetraglycinate
Coman D, Kiefer GE, Rothman DL, Sherry AD, Hyder F. A lanthanide complex with dual biosensing properties: CEST (chemical exchange saturation transfer) and BIRDS (biosensor imaging of redundant deviation in shifts) with europium DOTA–tetraglycinate. NMR In Biomedicine 2011, 24: 1216-1225. PMID: 22020775, PMCID: PMC3267016, DOI: 10.1002/nbm.1677.Peer-Reviewed Original ResearchConceptsResponsive contrast agentsChemical exchange saturation transferMolecular imagingNonexchangeable proton resonancesMolecular imaging agentsLanthanide complexesCEST characteristicsIon complexesBiosensing propertiesBulk waterProton exchangeProton resonancesTetraacetate derivativeNonexchangeable protonsQuantitative molecular imagingRedundant deviationExchangeable sitesInner sphereSaturation transferImaging agentCEST methodComplexesIonsContrast agentsGreat potential
1996
Base-Catalysis of Imino Proton Exchange in DNA: Effects of Catalyst upon DNA Structure and Dynamics
Folta-Stogniew E, Russu I. Base-Catalysis of Imino Proton Exchange in DNA: Effects of Catalyst upon DNA Structure and Dynamics. Biochemistry 1996, 35: 8439-8449. PMID: 8679602, DOI: 10.1021/bi952932z.Peer-Reviewed Original ResearchConceptsDNA dodecamerProton exchangeExchange catalystImino proton exchangeDQF-COSY experimentsImino protonsEffect of catalystNon-exchangeable protonsSelf-complementary DNA dodecamerNucleic acid moleculesNMR spectroscopyDNA structureOverall correlation timeAcid moleculesSolution conformationBase catalysisCatalystProton resonancesWater protonsProton relaxationRate of exchangeNucleic acidsProtonsDodecamerCorrelation time
1985
1H-Observe/13C-decouple spectroscopic measurements of lactate and glutamate in the rat brain in vivo.
Rothman D, Behar K, Hetherington H, Hollander J, Bendall M, Petroff O, Shulman R. 1H-Observe/13C-decouple spectroscopic measurements of lactate and glutamate in the rat brain in vivo. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 1633-1637. PMID: 2858850, PMCID: PMC397326, DOI: 10.1073/pnas.82.6.1633.Peer-Reviewed Original Research
1984
Homonuclear 1H double-resonance difference spectroscopy of the rat brain in vivo.
Rothman D, Behar K, Hetherington H, Shulman R. Homonuclear 1H double-resonance difference spectroscopy of the rat brain in vivo. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 6330-6334. PMID: 6149543, PMCID: PMC391917, DOI: 10.1073/pnas.81.20.6330.Peer-Reviewed Original Research1H NMR (500 MHz) of gene 32 protein--oligonucleotide complexes.
Prigodich R, Casas-Finet J, Williams K, Konigsberg W, Coleman J. 1H NMR (500 MHz) of gene 32 protein--oligonucleotide complexes. Biochemistry 1984, 23: 522-9. PMID: 6367821, DOI: 10.1021/bi00298a019.Peer-Reviewed Original ResearchConceptsN-terminal B-domainGene 32 proteinC-terminal domainCore proteinComplex formationGene 32Bacteriophage T4Bacteriophage fdC-terminalOligonucleotide bindingChemical shift changesTyr residuesB domainAromatic residuesNucleotide basesProteinResiduesLong rotational correlation timeOligonucleotide complexesHigh affinityComplexesShift changesDomainProton resonancesRotational correlation time
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