PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10729259-9 2000 At all powers it is proven that the instantaneous reduced coupling constant acting on the S spins is J cosφ, where φ is the polar angle of the I-spin magnetizations, thus establishing the central tenet of the semi-classical model applicable at moderate power. Adenosine Monophosphate 107-110 spindlin 1 Homo sapiens 92-96 31519012-8 2020 Finally, by creating a one-dimensional 3d<sup>2</sup>-4d<sup>4</sup> hybrid system that involves orbital pairing terms, it is possible to obtain an insulating spin-orbital model where the orbital part after fermionization maps to a non-uniform Kitaev model. Adenosine Monophosphate 42-45 spindlin 1 Homo sapiens 247-251 31519012-8 2020 Finally, by creating a one-dimensional 3d<sup>2</sup>-4d<sup>4</sup> hybrid system that involves orbital pairing terms, it is possible to obtain an insulating spin-orbital model where the orbital part after fermionization maps to a non-uniform Kitaev model. Adenosine Monophosphate 46-49 spindlin 1 Homo sapiens 247-251 31519012-8 2020 Finally, by creating a one-dimensional 3d<sup>2</sup>-4d<sup>4</sup> hybrid system that involves orbital pairing terms, it is possible to obtain an insulating spin-orbital model where the orbital part after fermionization maps to a non-uniform Kitaev model. Adenosine Monophosphate 46-49 spindlin 1 Homo sapiens 247-251 31519012-8 2020 Finally, by creating a one-dimensional 3d<sup>2</sup>-4d<sup>4</sup> hybrid system that involves orbital pairing terms, it is possible to obtain an insulating spin-orbital model where the orbital part after fermionization maps to a non-uniform Kitaev model. Adenosine Monophosphate 46-49 spindlin 1 Homo sapiens 247-251 31519012-8 2020 Finally, by creating a one-dimensional 3d<sup>2</sup>-4d<sup>4</sup> hybrid system that involves orbital pairing terms, it is possible to obtain an insulating spin-orbital model where the orbital part after fermionization maps to a non-uniform Kitaev model. Adenosine Monophosphate 46-49 spindlin 1 Homo sapiens 247-251 31519012-8 2020 Finally, by creating a one-dimensional 3d<sup>2</sup>-4d<sup>4</sup> hybrid system that involves orbital pairing terms, it is possible to obtain an insulating spin-orbital model where the orbital part after fermionization maps to a non-uniform Kitaev model. Adenosine Monophosphate 46-49 spindlin 1 Homo sapiens 247-251 31519012-8 2020 Finally, by creating a one-dimensional 3d<sup>2</sup>-4d<sup>4</sup> hybrid system that involves orbital pairing terms, it is possible to obtain an insulating spin-orbital model where the orbital part after fermionization maps to a non-uniform Kitaev model. Adenosine Monophosphate 46-49 spindlin 1 Homo sapiens 247-251 31519012-8 2020 Finally, by creating a one-dimensional 3d<sup>2</sup>-4d<sup>4</sup> hybrid system that involves orbital pairing terms, it is possible to obtain an insulating spin-orbital model where the orbital part after fermionization maps to a non-uniform Kitaev model. Adenosine Monophosphate 46-49 spindlin 1 Homo sapiens 247-251 31519012-8 2020 Finally, by creating a one-dimensional 3d<sup>2</sup>-4d<sup>4</sup> hybrid system that involves orbital pairing terms, it is possible to obtain an insulating spin-orbital model where the orbital part after fermionization maps to a non-uniform Kitaev model. Adenosine Monophosphate 46-49 spindlin 1 Homo sapiens 247-251 31519012-8 2020 Finally, by creating a one-dimensional 3d<sup>2</sup>-4d<sup>4</sup> hybrid system that involves orbital pairing terms, it is possible to obtain an insulating spin-orbital model where the orbital part after fermionization maps to a non-uniform Kitaev model. Adenosine Monophosphate 46-49 spindlin 1 Homo sapiens 247-251 31519012-8 2020 Finally, by creating a one-dimensional 3d<sup>2</sup>-4d<sup>4</sup> hybrid system that involves orbital pairing terms, it is possible to obtain an insulating spin-orbital model where the orbital part after fermionization maps to a non-uniform Kitaev model. Adenosine Monophosphate 46-49 spindlin 1 Homo sapiens 247-251 31519012-8 2020 Finally, by creating a one-dimensional 3d<sup>2</sup>-4d<sup>4</sup> hybrid system that involves orbital pairing terms, it is possible to obtain an insulating spin-orbital model where the orbital part after fermionization maps to a non-uniform Kitaev model. Adenosine Monophosphate 46-49 spindlin 1 Homo sapiens 247-251 31519012-8 2020 Finally, by creating a one-dimensional 3d<sup>2</sup>-4d<sup>4</sup> hybrid system that involves orbital pairing terms, it is possible to obtain an insulating spin-orbital model where the orbital part after fermionization maps to a non-uniform Kitaev model. Adenosine Monophosphate 46-49 spindlin 1 Homo sapiens 247-251 31519012-8 2020 Finally, by creating a one-dimensional 3d<sup>2</sup>-4d<sup>4</sup> hybrid system that involves orbital pairing terms, it is possible to obtain an insulating spin-orbital model where the orbital part after fermionization maps to a non-uniform Kitaev model. Adenosine Monophosphate 46-49 spindlin 1 Homo sapiens 247-251 31519012-8 2020 Finally, by creating a one-dimensional 3d<sup>2</sup>-4d<sup>4</sup> hybrid system that involves orbital pairing terms, it is possible to obtain an insulating spin-orbital model where the orbital part after fermionization maps to a non-uniform Kitaev model. Adenosine Monophosphate 46-49 spindlin 1 Homo sapiens 247-251 31519012-8 2020 Finally, by creating a one-dimensional 3d<sup>2</sup>-4d<sup>4</sup> hybrid system that involves orbital pairing terms, it is possible to obtain an insulating spin-orbital model where the orbital part after fermionization maps to a non-uniform Kitaev model. Adenosine Monophosphate 46-49 spindlin 1 Homo sapiens 247-251 31491770-1 2020 A spin-rotation mode emerging in a quantum Hall ferromagnet due to excitation by a laser pulse
 is studied. Adenosine Monophosphate 95-98 spindlin 1 Homo sapiens 2-6 31491770-1 2020 A spin-rotation mode emerging in a quantum Hall ferromagnet due to excitation by a laser pulse
 is studied. Adenosine Monophosphate 99-102 spindlin 1 Homo sapiens 2-6 25974365-0 2015 Spin-state transition in unstrained & strained ultra-thin BiCoO3 films. Adenosine Monophosphate 37-40 spindlin 1 Homo sapiens 0-4 10729259-9 2000 At all powers it is proven that the instantaneous reduced coupling constant acting on the S spins is J cosφ, where φ is the polar angle of the I-spin magnetizations, thus establishing the central tenet of the semi-classical model applicable at moderate power. Adenosine Monophosphate 124-127 spindlin 1 Homo sapiens 92-96 9245366-0 1997 Spin Echoes after Arbitrary N Pulses Based on the Bloch equations, the general response of a nuclear spin-½ system to multiple RF pulses with arbitrary phases and flip angles is presented. Adenosine Monophosphate 107-110 spindlin 1 Homo sapiens 0-4 9245366-0 1997 Spin Echoes after Arbitrary N Pulses Based on the Bloch equations, the general response of a nuclear spin-½ system to multiple RF pulses with arbitrary phases and flip angles is presented. Adenosine Monophosphate 107-110 spindlin 1 Homo sapiens 101-105 6246972-13 1980 The changes in the mobility of the spin label of apophosphorylase I and its complex with the AMP analog--adenosine-5"-chloromethylphosphonate--during the choloenzyme reconstruction by pyridoxalphosphate are indicative of participation of AMP and the phosphate group of AMP in the formation of the enzyme active center. Adenosine Monophosphate 93-96 spindlin 1 Homo sapiens 35-39 6246972-13 1980 The changes in the mobility of the spin label of apophosphorylase I and its complex with the AMP analog--adenosine-5"-chloromethylphosphonate--during the choloenzyme reconstruction by pyridoxalphosphate are indicative of participation of AMP and the phosphate group of AMP in the formation of the enzyme active center. Adenosine Monophosphate 238-241 spindlin 1 Homo sapiens 35-39 6246972-13 1980 The changes in the mobility of the spin label of apophosphorylase I and its complex with the AMP analog--adenosine-5"-chloromethylphosphonate--during the choloenzyme reconstruction by pyridoxalphosphate are indicative of participation of AMP and the phosphate group of AMP in the formation of the enzyme active center. Adenosine Monophosphate 238-241 spindlin 1 Homo sapiens 35-39 177286-0 1976 Spin-labelled AMP - an activator of phosphorylase. Adenosine Monophosphate 14-17 spindlin 1 Homo sapiens 0-4 177286-2 1976 A spin-labelled AMP derivative and its diamagnetic analogue activate phosphorylase b in the same way, but do not activate phosphorylase a. Adenosine Monophosphate 16-19 spindlin 1 Homo sapiens 2-6 177286-4 1976 The electron-spin-resonance spectra of the spin-labelled AMP derivative bound to phosphorylase b and a have "powderlike" characteristics indicating that the spin label is immobilised on the protein. Adenosine Monophosphate 57-60 spindlin 1 Homo sapiens 13-17 177286-4 1976 The electron-spin-resonance spectra of the spin-labelled AMP derivative bound to phosphorylase b and a have "powderlike" characteristics indicating that the spin label is immobilised on the protein. Adenosine Monophosphate 57-60 spindlin 1 Homo sapiens 43-47 177286-4 1976 The electron-spin-resonance spectra of the spin-labelled AMP derivative bound to phosphorylase b and a have "powderlike" characteristics indicating that the spin label is immobilised on the protein. Adenosine Monophosphate 57-60 spindlin 1 Homo sapiens 43-47 177286-5 1976 From changes in the electron-spin-resonance spectrum of spin-labelled AMP as phosphorylase b or a is added, the dissociation constants were calculated. Adenosine Monophosphate 70-73 spindlin 1 Homo sapiens 29-33 177286-5 1976 From changes in the electron-spin-resonance spectrum of spin-labelled AMP as phosphorylase b or a is added, the dissociation constants were calculated. Adenosine Monophosphate 70-73 spindlin 1 Homo sapiens 56-60 177286-7 1976 The interactions of spin-labelled AMP and the diamagnetic analogue with phosphorylase b and a have been monitored by observing changes in the spectral properties of fluorescent and spin-label probes covalently attached to the enzyme. Adenosine Monophosphate 34-37 spindlin 1 Homo sapiens 20-24 177286-7 1976 The interactions of spin-labelled AMP and the diamagnetic analogue with phosphorylase b and a have been monitored by observing changes in the spectral properties of fluorescent and spin-label probes covalently attached to the enzyme. Adenosine Monophosphate 34-37 spindlin 1 Homo sapiens 181-185 177286-9 1976 The dissociation constants of spin-labelled AMP and phosphorylase b or a are 175 +/- 25 muM and 15 +/- 5 muM respectively. Adenosine Monophosphate 44-47 spindlin 1 Homo sapiens 30-34