lance-c documents

[IEEE 2012 IEEE International Conference on RFID (IEEE RFID 2012) - Orlando, FL, USA (2012.04.3-2012.04.5)] 2012 IEEE International Conference on RFID (RFID) - A real-time RFID localization
Documents [IEEE 2012 IEEE International Conference on RFID (IEEE RFID 2012) - Orlando, FL, USA (2012.04.3-2012.04.5)] 2012 IEEE International Conference on RFID (RFID) - A real-time RFID localization
Climbing Nitrogenase: Toward a Mechanism of Enzymatic Nitrogen Fixation
Documents Climbing Nitrogenase: Toward a Mechanism of Enzymatic Nitrogen Fixation
M ECHANISTIC F EATURES OF THE M O -C ONTAINING N ITROGENASE
Documents M ECHANISTIC F EATURES OF THE M O -C ONTAINING N ITROGENASE
Restoration of Congenitally Missing Lateral Incisors After Orthodontic Treatment
Documents Restoration of Congenitally Missing Lateral Incisors After Orthodontic Treatment
Dynamic Force Generation within the Immune Synapse
Documents Dynamic Force Generation within the Immune Synapse
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Documents Reply
Microscale Colocalization of CD3 and CD28 is Required for Activation of Human CD4+ T Cells
Documents Microscale Colocalization of CD3 and CD28 is Required for Activation of Human CD4+ T Cells
Emerging Advances in Rapid Diagnostics of Respiratory Infections
Documents Emerging Advances in Rapid Diagnostics of Respiratory Infections
Elucidating the Mechanism of Nucleotide-Dependent Changes in the Redox Potential of the [4Fe-4S] Cluster in Nitrogenase Iron Protein:  The Role of Phenylalanine 135 †
Documents Elucidating the Mechanism of Nucleotide-Dependent Changes in the Redox Potential of the [4Fe-4S] Cluster in Nitrogenase Iron Protein:  The Role of Phenylalanine 135 †
Synthesis of Biodiesel from Mixed Feedstocks and Longer Chain Alcohols Using an Acid-Catalyzed Method
Documents Synthesis of Biodiesel from Mixed Feedstocks and Longer Chain Alcohols Using an Acid-Catalyzed Method
The [4Fe-4S] Cluster Domain of the Nitrogenase Iron Protein Facilitates Conformational Changes Required for the Cooperative Binding of Two Nucleotides †
Documents The [4Fe-4S] Cluster Domain of the Nitrogenase Iron Protein Facilitates Conformational Changes Required for the Cooperative Binding of Two Nucleotides †
Elucidation of a MgATP Signal Transduction Pathway in the Nitrogenase Iron Protein:  Formation of a Conformation Resembling the MgATP-Bound State by Protein Engineering †
Documents Elucidation of a MgATP Signal Transduction Pathway in the Nitrogenase Iron Protein:  Formation of a Conformation Resembling the MgATP-Bound State by Protein Engineering †
Trapping a Hydrazine Reduction Intermediate on the Nitrogenase Active Site †
Documents Trapping a Hydrazine Reduction Intermediate on the Nitrogenase Active Site †
Changes in the Midpoint Potentials of the Nitrogenase Metal Centers as a Result of Iron Protein−Molybdenum-Iron Protein Complex Formation †
Documents Changes in the Midpoint Potentials of the Nitrogenase Metal Centers as a Result of Iron Protein−Molybdenum-Iron Protein Complex Formation †
Evidence for Coupled Electron and Proton Transfer in the [8Fe-7S] Cluster of Nitrogenase †
Documents Evidence for Coupled Electron and Proton Transfer in the [8Fe-7S] Cluster of Nitrogenase †
Uncoupling Nitrogenase: Catalytic Reduction of Hydrazine to Ammonia by a MoFe Protein in the Absence of Fe Protein-ATP
Documents Uncoupling Nitrogenase: Catalytic Reduction of Hydrazine to Ammonia by a MoFe Protein in the Absence of Fe Protein-ATP
Substrate Channel in Nitrogenase Revealed by a Molecular Dynamics Approach
Documents Substrate Channel in Nitrogenase Revealed by a Molecular Dynamics Approach
Improving energetics of triacylglyceride extraction from wet oleaginous microbes
Documents Improving energetics of triacylglyceride extraction from wet oleaginous microbes
Electron Transfer within Nitrogenase: Evidence for a Deficit-Spending Mechanism
Documents Electron Transfer within Nitrogenase: Evidence for a Deficit-Spending Mechanism
Nucleotide Hydrolysis and Protein Conformational Changes in Azotobacter vinelandii Nitrogenase Iron Protein: Defining the Function of Aspartate 129
Documents Nucleotide Hydrolysis and Protein Conformational Changes in Azotobacter vinelandii Nitrogenase Iron Protein: Defining the Function of Aspartate 129
Proton NMR investigation of the [4Fe-4S]1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes
Documents Proton NMR investigation of the [4Fe-4S]1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes