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resolves. » resolved. (Espandi la ricerca), evolves. (Espandi la ricerca), resolveds. (Espandi la ricerca)
resolvent. » solvent. (Espandi la ricerca), resolved. (Espandi la ricerca), resolving. (Espandi la ricerca), resolvednt. (Espandi la ricerca)
resolve. » resolved. (Espandi la ricerca)
resolves. » resolved. (Espandi la ricerca), evolves. (Espandi la ricerca), resolveds. (Espandi la ricerca)
resolvent. » solvent. (Espandi la ricerca), resolved. (Espandi la ricerca), resolving. (Espandi la ricerca), resolvednt. (Espandi la ricerca)
resolve. » resolved. (Espandi la ricerca)
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Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins
Pubblicazione 2004“...The reaction mechanism and details of the formation of CIDNP (chemically induced dynamic nuclear polarization) in the photoreactions of two aromatic dyes (2,2‘-dipyridyl, DP, and flavin mononucleotide, FMN) with bovine and human α-lactalbumins (BLA and HLA) in aqueous solution have been studied using the time-resolved CIDNP technique. With DP as the photosensitizer, polarization in BLA is observed for the protons of Trp118, His68, Tyr18, and Tyr103. ...”
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122
Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins
Pubblicazione 2004“...The reaction mechanism and details of the formation of CIDNP (chemically induced dynamic nuclear polarization) in the photoreactions of two aromatic dyes (2,2‘-dipyridyl, DP, and flavin mononucleotide, FMN) with bovine and human α-lactalbumins (BLA and HLA) in aqueous solution have been studied using the time-resolved CIDNP technique. With DP as the photosensitizer, polarization in BLA is observed for the protons of Trp118, His68, Tyr18, and Tyr103. ...”
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123
Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins
Pubblicazione 2004“...The reaction mechanism and details of the formation of CIDNP (chemically induced dynamic nuclear polarization) in the photoreactions of two aromatic dyes (2,2‘-dipyridyl, DP, and flavin mononucleotide, FMN) with bovine and human α-lactalbumins (BLA and HLA) in aqueous solution have been studied using the time-resolved CIDNP technique. With DP as the photosensitizer, polarization in BLA is observed for the protons of Trp118, His68, Tyr18, and Tyr103. ...”
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124
Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins
Pubblicazione 2004“...The reaction mechanism and details of the formation of CIDNP (chemically induced dynamic nuclear polarization) in the photoreactions of two aromatic dyes (2,2‘-dipyridyl, DP, and flavin mononucleotide, FMN) with bovine and human α-lactalbumins (BLA and HLA) in aqueous solution have been studied using the time-resolved CIDNP technique. With DP as the photosensitizer, polarization in BLA is observed for the protons of Trp118, His68, Tyr18, and Tyr103. ...”
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125
Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins
Pubblicazione 2004“...The reaction mechanism and details of the formation of CIDNP (chemically induced dynamic nuclear polarization) in the photoreactions of two aromatic dyes (2,2‘-dipyridyl, DP, and flavin mononucleotide, FMN) with bovine and human α-lactalbumins (BLA and HLA) in aqueous solution have been studied using the time-resolved CIDNP technique. With DP as the photosensitizer, polarization in BLA is observed for the protons of Trp118, His68, Tyr18, and Tyr103. ...”
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126
Time-Resolved CIDNP Study of Native-State Bovine and Human α-Lactalbumins
Pubblicazione 2004“...The reaction mechanism and details of the formation of CIDNP (chemically induced dynamic nuclear polarization) in the photoreactions of two aromatic dyes (2,2‘-dipyridyl, DP, and flavin mononucleotide, FMN) with bovine and human α-lactalbumins (BLA and HLA) in aqueous solution have been studied using the time-resolved CIDNP technique. With DP as the photosensitizer, polarization in BLA is observed for the protons of Trp118, His68, Tyr18, and Tyr103. ...”
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Polarization-resolved microscopy—A method to determine actin order in biological systems.
Pubblicazione 2018“...<p>(A) Polarization-resolved microscopy provides information about F-actin molecular order Ψ and the average actin filament orientation ρ. ...”
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Key structural features involved in ion permeation and gating in C1C2.
Pubblicazione 2024“...Regions outside the permeation pathway that are involved in pore formation and cation conductance are (side views): <b>(D)</b> A highly conserved cluster of residues that borders the predicted channel entrance in cation ChRs. ...”
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Monotropic Transition Mechanism of <i>m</i>‑Hydroxybenzoic Acid Investigated by Temperature-Resolved Second Harmonic Generation
Pubblicazione 2013“...Temperature-resolved second harmonic generation (TR-SHG) and SHG microscopy were used to study under normal pressure the solid–solid transition mechanism occurring between the two monotropically related polymorphic forms (metastable <i>Pna</i>2<sub>1</sub> and stable <i>P</i>2<sub>1</sub>/<i>n</i>) of 3-hydroxybenzoic acid (MHBA). ...”
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138
Monotropic Transition Mechanism of <i>m</i>‑Hydroxybenzoic Acid Investigated by Temperature-Resolved Second Harmonic Generation
Pubblicazione 2013“...Temperature-resolved second harmonic generation (TR-SHG) and SHG microscopy were used to study under normal pressure the solid–solid transition mechanism occurring between the two monotropically related polymorphic forms (metastable <i>Pna</i>2<sub>1</sub> and stable <i>P</i>2<sub>1</sub>/<i>n</i>) of 3-hydroxybenzoic acid (MHBA). ...”
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139
The 161 genes coding for proteins forming ionic channels or involved in neurotransmitter release.
Pubblicazione 2014“...</p><p>The 161 genes coding for proteins forming ionic channels or involved in neurotransmitter release....”
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140
Widespread Involvement of Acetylation in the Retinal Metabolism of Form-Deprivation Myopia in Guinea Pigs
Pubblicazione 2023“...Although the pathogenesis of myopia remains controversial, proteomic studies suggest that dysregulation of retinal metabolism is potentially involved in the pathology of myopia. Lysine acetylation of proteins plays a key role in regulating cellular metabolism, but little is known about its role in the form-deprived myopic retina. ...”