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44 results for “Threonine”

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zenodo44/100

X-ray diffraction images for L-threonine dehydrogenase from Trypanosoma brucei with NAD and pyruvate bound.

<p>X-ray diffraction images which were collected at ESRF (Grenoble) using an ADSC 315r CCD detector on beamline ID29 on 11th November 2009. More details are given in the uploaded notes. </p>

opencc-by-4.0Dec 2016View details →
zenodo40/100

Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (Proline-serine-threonine phosphatase-interacting protein 1) mutant G258A (PDB entry 7AAL)

<p>Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (residues 1-289), mutant G258A.</p> <p>Data were collected on a single crystal at the beamline i03 of the Diamond Light Source synchrotron (Didcot, UK) using radiation of 0.9999 &Aring; wavelength and a PILATUS3 6M detector. The dataset consists of 2400 images (0.15 degree oscillation per image). Crystals belong to the space group P2(1)2(1)2(1) with unit cell dimensions a=48.19 &Aring;, b=73.02 &Aring;, c=205.25 &Aring;. The asymmetric unit contains an homodimer of the F-BAR domain (~53% solvent content), which is the biological unit.</p> <p>Diffraction data was notably anisotropic. The lowest resolution limit was 2.92 &Aring; in the direction b* and the highest limits were 1.97 &Aring; and 2.09 in the directions a* and c*, respectively.</p> <p>&nbsp;</p> <p>The structure derived form these data is published in:</p> <p>Manso, J.A., Marcos, T., Ruiz-Mart&iacute;n, V. Casas J, Alc&oacute;n P, S&aacute;nchez Crespo M, Bay&oacute;n Y, de Pereda JM, Alonso A <em>PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders</em>. <strong>Cell. Mol. Life Sci</strong>. 79, 131 (2022). <a href="https://doi.org/10.1007/s00018-022-04173-w">https://doi.org/10.1007/s00018-022-04173-w</a></p> <p>The structure is available at the PDB under the code 7AAL:</p> <p><a href="https://www.ebi.ac.uk/pdbe/entry/pdb/7aal">https://www.ebi.ac.uk/pdbe/entry/pdb/7aal</a></p>

opencc-by-sa-4.0Jun 2020View details →
zenodo40/100

Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (Proline-serine-threonine phosphatase-interacting protein 1) bound to the C-terminal homology (CTH) segment of the phosphatase LYP (PTPN22) (PDB entry 7AAM)

<p>Diffraction images of a crystal of the F-BAR domain of human PSTPIP1 (residues 1-289, Uniprot reference O43586-1) in complex with the CTH of LYP (residues 787-807, Uniprot Q9Y2R2-1).</p> <p>Data were collected on a single crystal at the beamline i03 of the Diamond Light Source synchrotron (Didcot, UK) using radiation of 0.99987 &Aring; wavelength and a PILATUS3 6M detector. The dataset consists of 3 groups, each containing of 1800 images (0.1 degree oscillation per image), collected at three different positions of the same crystal. Crystal belongs to the space group P2(1)2(1)2(1) with unit cell dimensions a=48.0 &Aring;, b=72.0 &Aring;, c=205.0 &Aring;. The asymmetric unit contains an homodimer of the F-BAR domain bound to a LYP-CTH (~53% solvent content), which is the biological complex.</p> <p>Diffraction data was notably anisotropic. The lowest resolution limit was 4.05 &Aring; in the direction b* and the highest limits were 2.11 &Aring; and 2.10 in the directions a* and c*, respectively.</p> <p>&nbsp;</p> <p>The structure derived form these data is published in:</p> <p>Manso, J.A., Marcos, T., Ruiz-Mart&iacute;n, V. Casas J, Alc&oacute;n P, S&aacute;nchez Crespo M, Bay&oacute;n Y, de Pereda JM, Alonso A <em>PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders</em>. <strong>Cell. Mol. Life Sci</strong>. 79, 131 (2022). <a href="https://doi.org/10.1007/s00018-022-04173-w">https://doi.org/10.1007/s00018-022-04173-w</a></p> <p>The structure is available at the PDB under the code <strong>7AAM</strong>:</p> <p><a href="https://www.ebi.ac.uk/pdbe/entry/pdb/7aam">https://www.ebi.ac.uk/pdbe/entry/pdb/7aam</a></p>

opencc-by-4.0Jun 2020View details →
zenodo40/100

Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (Proline-serine-threonine phosphatase-interacting protein 1) (PDB entry 7AAN)

<p>Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (residues 1-289).</p> <p>Data were collected on a single crystal at the beamline i03 of the Diamond Light Source synchrotron (Didcot, UK) using radiation of 0.99987 &Aring; wavelength and a PILATUS3 6M detector. The dataset consists of 3600 images (0.15 degree oscillation per image) that were collected: 2400 at one position and the other 1200 at a second site in the same crystal. Crystal belongs to the space group P2(1)2(1)2(1) with unit cell dimensions a=48.3 &Aring;, b=71.9 &Aring;, c=204.6 &Aring;. The asymmetric unit contains an homodimer of the F-BAR domain (~53% solvent content), which is the biological unit.</p> <p>Diffraction data was notably anisotropic. The lowest resolution limit was 4.32 &Aring; in the direction b* and the highest limits were 2.12 &Aring; and 2.17 in the directions a* and c*, respectively.</p> <p>The structure derived form these data is published in:</p> <p>Manso, J.A., Marcos, T., Ruiz-Mart&iacute;n, V. Casas J, Alc&oacute;n P, S&aacute;nchez Crespo M, Bay&oacute;n Y, de Pereda JM, Alonso A <em>PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders</em>. <strong>Cell. Mol. Life Sci</strong>. 79, 131 (2022). <a href="https://doi.org/10.1007/s00018-022-04173-w">https://doi.org/10.1007/s00018-022-04173-w</a></p> <p>The structure is available at the PDB under the code <strong>7AAN</strong>:</p> <p><a href="https://www.ebi.ac.uk/pdbe/entry/pdb/7aan">https://www.ebi.ac.uk/pdbe/entry/pdb/7aan</a></p>

opencc-by-sa-4.0Jun 2020View details →
zenodo32/100

Trypanosoma brucei L-threonine dehydrogenase diffraction images.

<p>Diffraction images for apo-L-threonine dehydrogenase from <em>T. brucei</em>.&nbsp;</p>

opencc-zeroJun 2016View details →
zenodo32/100

Fig. 4 in A pair of threonines mark ent-kaurene synthases for phytohormone biosynthesis

Fig. 4. TT motif is not required for the production of ent-kaurene (1). Extracted ion (m/z = 272) chromatograms demonstrating the production of 1 by all mutants (as indicated) by comparison to wild-type (WT) AtKS.

opennotspecifiedApr 2021View details →
zenodo32/100

Fig. 5 in A pair of threonines mark ent-kaurene synthases for phytohormone biosynthesis

Fig. 5. TT motif has minimal effect on catalytic efficiency. Curve fit of Michaelis-Menton equation to data for wild-type (WT) and indicated mutants of AtKS.

opennotspecifiedApr 2021View details →
zenodo32/100

Fig. 3 in A pair of threonines mark ent-kaurene synthases for phytohormone biosynthesis

Fig. 3. Identification of the TT motif. A) Representative alignment of KSs spanning plant evolution with the KS specific pair of threonines (TT motif) indicated by asterisks (*) above the alignment. B) Sequence logos demonstrating the absolute conservation of this TT motif in KS (bottom) relative to the derived KS(L)/TPS-e subfamily more generally (top). C) Location of TT motif in active site from model of AtKS (blue) containing 2-fluoroGGPP (green) and Mg2+ co-factors (magenta) derived from the template co-crystal structure of taxadiene synthase (Koksal et al., 2011).

opennotspecifiedApr 2021View details →
zenodo32/100

Fig. 2 in A pair of threonines mark ent-kaurene synthases for phytohormone biosynthesis

Fig. 2. Representative phylogenetic tree for plant KS(L)/TPS-e subfamily. Green lines indicate KS activity, red lines KSL that mediate alternative product outcome. Green text indicates KS with known or assumed role in phytohormone biosynthesis, while blue text indicates enzymes known to produce 1 for secondary metabolism – i.e., in maize (Fu et al., 2016).

opennotspecifiedApr 2021View details →
zenodo32/100

Fig. 7 in A pair of threonines mark ent-kaurene synthases for phytohormone biosynthesis

Fig. 7. TT motif codons are not conserved. A) Exon sizes from KS with known genomic sequence. B) Sequence of TT motif containing exon from AtKS (codons for TT motif in larger blue text). C) Sequence logo indicating lack of conservation of the codons for the TT motif – i.e., in the variable third/'wobble' position.

opennotspecifiedApr 2021View details →
zenodo32/100

Fig. 6 in A pair of threonines mark ent-kaurene synthases for phytohormone biosynthesis

Fig. 6. TT motif has minimal effect on protein structure. CD spectra for wildtype (WT) and the T527 V/T528V (TT/VV) double mutant of AtKS (note that the minimal differences observed here are not reproducible).

opennotspecifiedApr 2021View details →
ClinicalTrials.gov32/100

A Physiological Study to Determine the Enteral Threonine Requirements in Infants Aged 1 to 6 Months

ClinicalTrials.gov study NCT02364843. IPD Sharing: NO. Countries: 1. Publications: 14.

closedIPD-NOFeb 2026View details →
ClinicalTrials.gov32/100

Length of Adaptation and Threonine Requirement

ClinicalTrials.gov study NCT04585087. IPD Sharing: NO. Countries: 1. Publications: 1.

closedIPD-NOFeb 2026View details →
zenodo28/100

Trypanosoma brucei L-threonine dehydrogenase high resolution diffraction images.

<p>Diffraction images obtained in the high resolution pass&nbsp;for apo-L-threonine dehydrogenase from&nbsp;<em>T. brucei</em>.&nbsp;</p>

openother-pdJul 2016View details →
zenodo28/100

Fig. 1 in A pair of threonines mark ent-kaurene synthases for phytohormone biosynthesis

Fig. 1. KS reaction mechanism.

opennotspecifiedApr 2021View details →
geo24/100

Threonine-4 of the budding yeast RNAP II CTD couples transcription with Htz1-mediated chromatin remodeling

GEO Series GSE60181. Saccharomyces cerevisiae. 4 samples. Type: Expression profiling by high throughput sequencing.

openGEO-OpenAug 2014View details →
geo24/100

Threonine Phosphorylation of STAT1 Restricts Interferon Signaling and Promotes Innate Inflammatory Responses

GEO Series GSE261824. Mus musculus. 16 samples. Type: Expression profiling by high throughput sequencing.

openGEO-OpenMar 2024View details →
geo24/100

Bisulfite sequencing with Daphnia highlights a role for epigenetics in regulating stress response to Microcystis through preferential differential methylation of serine and threonine amino acidsing bi

GEO Series GSE83407. Daphnia magna. 6 samples. Type: Methylation profiling by high throughput sequencing.

openGEO-OpenDec 2016View details →
geo24/100

Microarry and RNA-seq analysis of M. tuberculosis response to threonine auxotrophic starvation

GEO Series GSE119107. Mycobacterium tuberculosis H37Rv; Mycobacterium tuberculosis. 20 samples. Type: Expression profiling by array; Expression profiling by high throughput sequencing.

openGEO-OpenAug 2018View details →
geo24/100

Whole genome ChIP-seq of histone H3 threonine 11 phosphorylation in Saccharomyces cerevisiae

GEO Series GSE100564. Saccharomyces cerevisiae. 10 samples. Type: Genome binding/occupancy profiling by high throughput sequencing.

openGEO-OpenJun 2017View details →

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International Brain Laboratory public data

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