science
plus
.abes.fr
|
explorer
À propos de :
Lu Yi
Goto
Sponge
NotDistinct
Permalink
An Entity of Type :
foaf:Person
, within Data Space :
scienceplus.abes.fr
associated with source
document(s)
Type:
Person
New Facet based on Instances of this Class
Attributs
Valeurs
type
Person
name
Lu Yi
familyName
Lu
Given name
Yi
is
relates
of
http://hub.abes.fr/acs/periodical/ancham/2007/volume_79/issue_11/101021ac070055k/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/2001/volume_40/issue_49/101021bi011400h/authorship/4
http://hub.abes.fr/acs/periodical/cmatex/2004/volume_16/issue_17/101021cm049453j/authorship/2
http://hub.abes.fr/acs/periodical/ancham/2004/volume_76/issue_6/101021ac0351769/authorship/2
http://hub.abes.fr/acs/periodical/inocaj/2005/volume_44/issue_17/101021ic050285m/authorship/5
http://hub.abes.fr/acs/periodical/jacsat/2000/volume_122/issue_34/101021ja0015343/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/2003/volume_125/issue_29/101021ja029699u/authorship/5
http://hub.abes.fr/acs/periodical/jacsat/2002/volume_124/issue_27/101021ja012514j/authorship/8
http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_16/101021ja042459p/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/2005/volume_44/issue_17/101021bi047465c/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/2000/volume_122/issue_42/101021ja0021316/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/2002/volume_124/issue_10/101021ja0169163/authorship/5
http://hub.abes.fr/acs/periodical/jacsat/2003/volume_125/issue_22/101021ja034775u/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/2006/volume_128/issue_49/101021ja062732i/authorship/7
http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_20/101021ja0501114/authorship/4
http://hub.abes.fr/acs/periodical/achre4/2007/volume_40/issue_5/101021ar600053g/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/2005/volume_44/issue_4/101021bi0479151/authorship/5
http://hub.abes.fr/acs/periodical/jpcbfk/2007/volume_111/issue_24/101021jp0672555/authorship/3
http://hub.abes.fr/acs/periodical/inocaj/2006/volume_45/issue_1/101021ic051375u/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/2001/volume_123/issue_24/101021ja004109i/authorship/6
http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_44/101021ja054983h/authorship/6
http://hub.abes.fr/acs/periodical/bcches/2008/volume_19/issue_2/101021bc7003928/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/2003/volume_42/issue_23/101021bi027332w/authorship/4
http://hub.abes.fr/acs/periodical/esthag/2005/volume_39/issue_10/101021es040505f/authorship/6
http://hub.abes.fr/acs/periodical/jacsat/2004/volume_126/issue_39/101021ja046628h/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_35/101021ja0541581/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/2007/volume_129/issue_32/101021ja0717358/authorship/2
http://hub.abes.fr/acs/periodical/ancham/2005/volume_77/issue_2/101021ac0401016/authorship/4
http://hub.abes.fr/acs/periodical/jacsat/2008/volume_130/issue_43/101021ja803607z/authorship/4
http://hub.abes.fr/acs/periodical/jacsat/2004/volume_126/issue_35/101021ja046908x/authorship/9
http://hub.abes.fr/acs/periodical/jacsat/2008/volume_130/issue_15/101021ja7102668/authorship/8
http://hub.abes.fr/acs/periodical/langd5/2007/volume_23/issue_18/101021la701303k/authorship/4
http://hub.abes.fr/acs/periodical/ancham/2003/volume_75/issue_23/101021ac034924r/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_36/101021ja053567u/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/2006/volume_128/issue_21/101021ja058822p/authorship/5
http://hub.abes.fr/acs/periodical/chreay/2001/volume_101/issue_10/101021cr0000574/authorship/1
http://hub.abes.fr/acs/periodical/jacsat/2008/volume_130/issue_12/101021ja076495a/authorship/7
http://hub.abes.fr/acs/periodical/jacsat/2008/volume_130/issue_26/101021ja711026r/authorship/4
http://hub.abes.fr/acs/periodical/jacsat/2002/volume_124/issue_51/101021ja027647z/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/2007/volume_129/issue_27/101021ja072075/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_47/101021ja052659g/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/2007/volume_129/issue_21/101021ja0712625/authorship/7
is
Author
of
Spectroscopic Characterizations of Bridging Cysteine Ligand Variants ofan Engineered Cu2(SCys)2 CuA Azurin
From Myoglobin to Heme-Copper Oxidase: Design and Engineeringof a CuB Center into Sperm Whale Myoglobin
Accelerated Color Change of Gold Nanoparticles Assembledby DNAzymes for Simple and Fast Colorimetric Pb2+Detection
Highly Active and Stable DNAzyme−Carbon Nanotube Hybrids
Blue Ferrocenium Azurin: An Organometalloprotein with Tunable RedoxProperties
Probing the Role of Axial Methionine in the Blue CopperCenter of Azurin with Unnatural Amino Acids
Role of Heme Types in Heme-Copper Oxidases: Effects ofReplacing a Heme b with a Heme o Mimic in an EngineeredHeme-Copper Center in Myoglobin§
Perturbations to the Geometric and Electronic Structure of the CuA Site: Factors that Influence Delocalization and Their Contributions to Electron Transfer
Effects of Metal Ions in the CuB Center on the Redox Properties of Heme inHeme-Copper Oxidases: Spectroelectrochemical Studies of an EngineeredHeme-Copper Center in Myoglobin
FRET Study of a Trifluorophore-Labeled DNAzyme
Axial Methionine Has Much Less Influence on Reduction Potentials in a CuACenter than in a Blue Copper Center
MRI Detection of Thrombin with Aptamer Functionalized Superparamagnetic Iron Oxide Nanoparticles
Redox-Dependent Structural Changes in an Engineered Heme−Copper Center inMyoglobin: Insights into Chloride Binding to CuB in Heme Copper Oxidases
An Engineered Azurin Variant Containing a Selenocysteine Copper Ligand
Stimuli-Responsive Disassembly of Nanoparticle Aggregatesfor Light-Up Colorimetric Sensing
A Quantitative Description of the Ground-State Wave Function ofCuA by X-ray Absorption Spectroscopy: Comparison to Plastocyaninand Relevance to Electron Transfer
Improving Fluorescent DNAzyme Biosensors byCombining Inter- and Intramolecular Quenchers
Immobilization of a Catalytic DNA MolecularBeacon on Au for Pb(II) Detection
A Site-Selective Dual Anchoring Strategy for Artificial Metalloprotein Design
Surface Immobilization of Catalytic Beacons Based on RatiometricFluorescent DNAzyme Sensors: A Systematic Study
Miniaturized Lead Sensor Based onLead-Specific DNAzyme in aNanocapillary InterconnectedMicrofluidic Device
A Colorimetric Lead Biosensor Using DNAzyme-Directed Assembly of GoldNanoparticles
Non-Base Pairing DNA Provides a New Dimension forControlling Aptamer-Linked Nanoparticles and Sensors
Spectroscopic and Density Functional Theory Studies of theBlue−Copper Site in M121SeM and C112SeC Azurin: Cu−Se Versus Cu−S Bonding
Smart Nanomaterials Inspired by Biology: Dynamic Assemblyof Error-Free Nanomaterials in Response to Multiple Chemical and BiologicalStimuli
Quantum Dot Encoding of Aptamer-LinkedNanostructures for One-Pot SimultaneousDetection of Multiple Analytes
Engineering Novel Metalloproteins: Design of Metal-Binding Sites into NativeProtein Scaffolds
Optimization of a Pb2+-Directed Gold Nanoparticle/DNAzyme Assembly and Its Application as aColorimetric Biosensor for Pb2+
Reorganization Energy of the CuA Center in Purple Azurin: Impact of the MixedValence-to-Trapped Valence State Transition
A Highly Sensitive and Selective Catalytic DNABiosensor for Lead Ions
Catalytic Reduction of NO to N2O by a Designed Heme Copper Center inMyoglobin: Implications for the Role of Metal Ions
Highly Sensitive and Selective Colorimetric Sensors for Uranyl (UO22+): Development and Comparison of Labeled and Label-Free DNAzyme-Gold Nanoparticle Systems
Metal-Dependent Global Folding and Activity of the 8-17DNAzyme Studied by Fluorescence Resonance EnergyTransfer
DNA and DNAzyme-Mediated 2D Colloidal Assembly
Adenosine-Dependent Assembly ofAptazyme-Functionalized Gold Nanoparticles andIts Application as a Colorimetric Biosensor
The Role of Redox-Active Amino Acids on Compound I Stability, SubstrateOxidation, and Protein Cross-Linking in Yeast Cytochrome c Peroxidase
Disulfide Bond Cleavage Induced by a Platinum(II) Methionine Complex
Electron-Mediating CuA Centers in Proteins: A ComparativeHigh Field 1H ENDOR Study
A DNAzyme Catalytic Beacon Sensor for Paramagnetic Cu2+ Ions in AqueousSolution with High Sensitivity and Selectivity
A Lead-Dependent DNAzyme with a Two-Step Mechanism
Reduction Potential Tuning of the Blue Copper Center inPseudomonas aeruginosa Azurin by the Axial Methionine asProbed by Unnatural Amino Acids
Hopping in the Electron-Transfer Photocycle of the 1:1 Complex ofZn−Cytochrome c Peroxidase with Cytochrome c
Alternative Linked Data Documents:
ODE
Content Formats:
RDF
ODATA
Microdata