CBD reduced LPS-stimulated phosphorylation of NF-κB/p65 subunit and STAT3, but not MAP kinase in astrocytes and the inhibition of IL-6 did not involve PPARγ. 著者: Jun Wu (4002)

Conformational Substates of Myoglobin Intermediate Resolved by Picosecond X‑ray Solution Scattering 著者: Key Young Oang (1285278)

“…We attribute the biphasic kinetics to the involvement of two conformational substates of the first intermediate, which are generated by the interplay between the distal histidine and the photodissociated CO.…”

Data_Sheet_1_Quantitative Proteome Profiling of a S-Nitrosoglutathione Reductase (GSNOR) Null Mutant Reveals a New Class of Enzymes Involved in Nitric Oxide Homeostasis in Plants.X... 著者: Patrick Treffon (11815754)

“…<p>Nitric oxide (NO) is a short-lived radical gas that acts as a signaling molecule in all higher organisms, and that is involved in multiple plant processes, including germination, root growth, and fertility. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins 著者: Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins 著者: Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins 著者: Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins 著者: Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins 著者: Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins 著者: Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins 著者: Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins 著者: Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins 著者: Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins 著者: Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins 著者: Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins 著者: Olga B. Morozova (1521157)

“…The nuclear spin−lattice relaxation times in the radicals formed in these reactions have been determined from the CIDNP kinetics:  <i>T</i>₁ = 60 μs for H2,4,7 of Trp118, <i>T</i>₁ = 53 μs for H3,5 of Tyr103, <i>T</i>₁ = 16 μs for H3,5 of Tyr18, and <i>T</i>₁ = 10 μs for the H2 and H4 of His68. …”

Time-Resolved Chemical Bonding Structure Evolution by Direct-Dynamics Chemical Simulations 著者: Mario Piris (2054899)

Time-Resolved Chemical Bonding Structure Evolution by Direct-Dynamics Chemical Simulations 著者: Mario Piris (2054899)

Time-Resolved Chemical Bonding Structure Evolution by Direct-Dynamics Chemical Simulations 著者: Mario Piris (2054899)

Polarization-resolved microscopy—A method to determine actin order in biological systems. 著者: Olivier Loison (5150705)

“…<p>(A) Polarization-resolved microscopy provides information about F-actin molecular order Ψ and the average actin filament orientation ρ. …”

Predicting the Three-Dimensional Structure of the c-<i>KIT</i> Proto-Oncogene Promoter and the Dynamics of Its Strongly Coupled Guanine Quadruplexes 著者: Emmanuelle Bignon (3114651)

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