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418 results for “Dimerization”
Is USP5 Zf-UBD a dimer?
<p>Determination of the molar mass of USP5 zinc finger ubiquitin binding domain (Zf-UBD) using size exclusion chromatography with multiple angle light scattering (SEC-MALS). </p>
Real-time dynamics of nanoplasmonic dimer, distance d = 0.5 nm
<p>In Ref. <a href="http://doi.org/10.5281/zenodo.1476721">http://doi.org/10.5281/zenodo.1476721 </a>we provide a movie that shows the real-time dynamics of the nanoplasmonic dimer with distance $ d_1=0.5 $ nm. The time-evolution in the movie corresponds to the runs that we discuss in section VI. In the figure, we show a frame of the movie at time 8.33 fs. The upper two panels show contour plots of matter variables, the absolute value of the current density and the electron localized function (ELF). The most relevant Maxwell field variables, the electric field along the laser polarization direction z and the total Maxwell energy are presented in the lower panels. In the top of the figure, we show the incident laser pulse and at the center the geometry of the nanoplasmonic dimer.</p>
Real-time dynamics of nanoplasmonic dimer, distance d = 0.1 nm
<p>In Ref. <a href="http://dx.doi.org/10.5281/zenodo.1476719">http://doi.org/10.5281/zenodo.1476719 </a>we provide a movie that shows the real-time dynamics of the nanoplasmonic dimer with distance $ d_1=0.1 $ nm. The time-evolution in the movie corresponds to the runs that we discuss in section VI. In the figure, we show a frame of the movie at time 6.89 fs. The upper two panels show contour plots of matter variables, the absolute value of the current density and the electron localized function (ELF). The most relevant Maxwell field variables, the electric field along the laser polarization direction z and the total Maxwell energy are presented in the lower panels. In the top of the figure, we show the incident laser pulse and at the center the geometry of the nanoplasmonic dimer.</p>
Real-time dynamics of nanoplasmonic dimer, distance d = 0.5 nm
<p>In Ref. we provide a movie that shows the real-time dynamics of the nanoplasmonic dimer with distance $ d_1=0.5 $ nm. The time-evolution in the movie corresponds to the runs that we discuss in section VI. In the figure, we show a frame of the movie at time 8.33 fs. The upper two panels show contour plots of matter variables, the absolute value of the current density and the electron localized function (ELF). The most relevant Maxwell field variables, the electric field along the laser polarization direction z and the total Maxwell energy are presented in the lower panels. In the top of the figure, we show the incident laser pulse and at the center the geometry of the nanoplasmonic dimer.</p>
Real-time dynamics of nanoplasmonic dimer, distance d = 0.1 nm
<p>In http://dx.doi.org/10.5281/zenodo.1482739 we provide a movie that shows the real-time dynamics of the nanoplasmonic dimer with distance $ d_1=0.1 $ nm. The time-evolution in the movie corresponds to the runs that we discuss in section VI. In the figure, we show a frame of the movie at time 6.89 fs. The upper two panels show contour plots of matter variables, the absolute value of the current density and the electron localized function (ELF). The most relevant Maxwell field variables, the electric field along the laser polarization direction z and the total Maxwell energy are presented in the lower panels. In the top of the figure, we show the incident laser pulse and at the center the geometry of the nanoplasmonic dimer.</p>
Data for Nguyen Le at al. ""Topological phases of a dimerized Fermi-Hubbard model for semiconductor nano-lattices"
<p>Codes and simulation data used in Nguyen Le at al. "“Topological phases of a dimerized Fermi-Hubbard model for semiconductor nano-lattices."</p>
Assessing many-body methods on the potential energy surface of the H2_2 hydrogen dimer
<p>Density functional theory, RPA, and quantum Monte Carlo datasets produced for the "Assessing many-body methods on the potential energy surface of the H2_2 hydrogen dimer" paper submitted to the Journal of Chemical Physics and to the arXiv (https://arxiv.org).</p>
Real-time solution of coupled Ehrenfest-Maxwell-Pauli-Kohn-Sham equations for a nanoplasmonic dimer, distance d = 0.5 nm
<p>Here we provide the movie mentioned in https://arxiv.org/abs/1812.05049 that shows the real-time dynamics of the nanoplasmonic dimer with distance $ d_1=0.5 $ nm. The time-evolution in the movie corresponds to the runs that we discuss in section VI. In the figure, we show a frame of the movie at time 8.33 fs. The upper two panels show contour plots of matter variables, the absolute value of the current density and the electron localized function (ELF). The most relevant Maxwell field variables, the electric field along the laser polarization direction z and the total Maxwell energy are presented in the lower panels. In the top of the figure, we show the incident laser pulse and at the center the geometry of the nanoplasmonic dimer.</p>
Real-time solution of coupled Ehrenfest-Maxwell-Pauli-Kohn-Sham equations for a nanoplasmonic dimer, distance d = 0.1 nm
<p>Here we provide the movie mentioned in https://arxiv.org/abs/1812.05049 that shows the real-time dynamics of the nanoplasmonic dimer with distance $ d_1=0.1 $ nm. The time-evolution in the movie corresponds to the runs that we discuss in section VI. In the figure, we show a frame of the movie at time 6.89 fs. The upper two panels show contour plots of matter variables, the absolute value of the current density and the electron localized function (ELF). The most relevant Maxwell field variables, the electric field along the laser polarization direction z and the total Maxwell energy are presented in the lower panels. In the top of the figure, we show the incident laser pulse and at the center the geometry of the nanoplasmonic dimer.</p>
Data for: The conserved centrosomin motif, γTuNA, forms a dimer that directly activates microtubule nucleation by the γ-tubulin ring complex (γTuRC)
<p>To establish the microtubule cytoskeleton, the cell must tightly regulate when and where microtubules are nucleated. This regulation involves controlling the initial nucleation template, the γ-tubulin ring complex (γTuRC). Although γTuRC is present throughout the cytoplasm, its activity is restricted to specific sites including the centrosome and Golgi. The well-conserved γ-tubulin nucleation activator (γTuNA) domain has been reported to increase the number of microtubules (MTs) generated by γTuRCs. However, previously we and others observed that γTuNA had a minimal effect on the activity of antibody-purified Xenopus γTuRCs in vitro (Thawani et al., eLife, 2020; Liu et al., 2020). Here we instead report, based on improved versions of γTuRC, γTuNA, and our TIRF assay, the first real-time observation that γTuNA directly increases γTuRC activity in vitro, which is thus a bona fide γTuRC activator. We further validate this effect in Xenopus egg extract. Via mutation analysis, we find that γTuNA is an obligate dimer. Moreover, efficient dimerization as well as γTuNA's L70, F75, and L77 residues are required for binding to and activation of γTuRC. Finally, we find that γTuNA's activating effect opposes inhibitory regulation by stathmin. In sum, our improved assays prove that direct γTuNA binding strongly activates γTuRCs, explaining previously observed effects of γTuNA expression in cells and illuminating how γTuRC-mediated microtubule nucleation is regulated.</p>
Original Data for Publication: Exceptionally Stable Dimers and Trimers of Au25 Clusters Linked with a Bidentate Dithiol: Synthesis, Structure and Chirality Study.
<p>Original Data for Publication: Exceptionally Stable Dimers and Trimers of Au25 Clusters Linked with a Bidentate Dithiol: Synthesis, Structure and Chirality Study. Angewandte Chemie, 2023</p>
The kinetics and energetics of electron transfer to dimer radical cations
<p>Data files associated with publication titled "The kinetics and energetics of electron transfer to dimer radical cations" <em>J. Phys. Chem. B</em> 2023, 127, 13, 2881–2886</p>
3D structure model of the TgREMIND F-BAR dimer
<p>Coordinates of the AlphaFold2 3D structure model of TgREMIND F-BAR domain dimer (amino acids 80 to 345, UniProt S7W754_TOXGG). The model of the dimer was made using ColabFold v1.5.2 (Mirdita, M., Schütze, K., Moriwaki, Y. <em>et al.</em> ColabFold: making protein folding accessible to all. <em>Nat Methods</em> <strong>19</strong>, 679–682 (2022). https://doi.org/10.1038/s41592-022-01488-1; https://colab.research.google.com/github/sokrypton/ColabFold/blob/main/AlphaFold2.ipynb)</p> <pre> </pre>
ISOLDE model and validation statistics to support: Guanine-containing ssDNA and RNA induce dimeric and tetrameric SAMHD1 in cryo-EM and binding studies
<p>These files provide the pdb atom coordinates and structural validation of the ISOLDE structural model (Fig. 6) contained in the manuscript "Guanine-containing ssDNA and RNA induce dimeric and tetrameric SAMHD1 in cryo-EM and binding studies" </p>
Supplemental data for 'Biophysical analysis reveals autophosphorylation as an important negative regulator of LRRK2 dimerization''
<p><strong>Supplemental mass photomerty raw data used in Figure 3</strong> of 'Guaitoli, G., Zhang, X., Saitta, F., Miglionico, P., Silbermann, L.M., Ho, F.Y., Zweydorf, F.v., Signorelli, M., Tych, K., Fessas, D., Raimondi, F., Kortholt, A., and Gloeckner, C.J. (2023). Biophysical analysis reveals autophosphorylation as an important negative regulator of LRRK2 dimerization. <em>bioRxiv</em>, 2023.2008.2011.549911 doi: 10.1101/2023.08.11.549911'</p> <p><strong>Raw data Figure 3A:</strong> Mass photometry raw data for LRRK2 wild-type in presence of different G-nucleotides at different LRRK2 concentrations. Three biological replicates have been considered for the statistical analysis.</p> <p><strong>Raw data Figure 3B: </strong>Mass photometry raw data for LRRK2 WT (left panel), LRRK2 WT + MLi-2 (middle panel) and kinase-dead LRRK2 (right panel) without and with ATP pre-incubation (-/+ ATP). Two biological and three technical replicates have been considered for the statistical analysis.</p> <p><strong>Raw data Figure 3C</strong><strong>:</strong> Mass photometry raw data for pathogenic LRRK2 variants in presence of different G-nucleotides. Two biological and two technical replicates have been considered for the statistical analysis<strong>.</strong></p> <p> </p>
D-Dimer Determined Anticoagulation INTENSITY in Patients With Mechanical Valve Replacement
ClinicalTrials.gov study NCT01996657. IPD Sharing: UNDECIDED. Countries: 1. Publications: 2.
D-dimer Assay for the Exclusion of Intra-atrial Thrombus Risk Before Ablation of Atrial Fibrillation
ClinicalTrials.gov study NCT02199080. IPD Sharing: Not stated. Countries: 1. Publications: 1.
Attenuation of D-dimer Using Vorapaxar to Target Inflammatory and Coagulation Endpoints
ClinicalTrials.gov study NCT02394730. IPD Sharing: UNDECIDED. Countries: 2. Publications: 1.
D-dimer to Predict Recurrence in Patients With Multiple Episodes of Venous Thromboembolism
ClinicalTrials.gov study NCT00428441. IPD Sharing: Not stated. Countries: 1. Publications: 2.
Evolutionary variation in MADS-box dimerization affects floral development and protein abundance in maize
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