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86 results for “HTT”
Preliminary investigation of caspase6 cleavage of HTT and HTT-HAP40 2019/07/15
<p><strong>Project: </strong>Structural and functional analysis of huntingtin protein</p> <p><strong>Experiment: </strong>Preliminary investigation of caspase6 cleavage of HTT and HTT-HAP40</p> <p><strong>Date: </strong>2019/07/15</p> <p><strong>Background: </strong>HTT is cleaved by numerous enzymes to generate protein fragments, many of which have implications for disease pathogenesis (reviewed by Saudou et al (2016) Neuron). However, very few of these proteases have been assessed for their cleavage of purified HTT protein or HTT-HAP40 protein samples. Caspase-6 cleavage of HTT has been reported to generate a aa. 1-586 fragment. However, it is not clear how HAP40 binding of HTT might affect cleavage by caspase-6 or release of this fragment from the complex structure. The caspase-6 cleavage site is in the intrinsically disordered region, distal from the globular structure. How cleavage might release a 1-586 fragment from the remainder of the structure remains incompletely understood. </p> <p><strong>Rationale: </strong>In this experiments I am aiming to optimise conditions for caspase-6 cleavage to test how proteolytic cleavage of HTT affects “pathogenic” fragment formation for apo vs HAP40-bound HTT. </p>
Purification of HTT N-HEAT_81-1643
<p>The purification of huntingtin (HTT) fragments is a useful approach to learn more about the function of HTT in the cell. By obtaining soluble and monomeric samples of HTT domains namely the C-HEAT, N-HEAT and bridge domains, specific protein-protein interactions can be studied. Furthermore, domains of HTT in soluble monomeric form could enable crystallization studies. </p> <p>The first expression and purification of these fragments can be found on these posts <a href="https://zenodo.org/record/2600051#.XKU89aeZPOQ">https://zenodo.org/record/2600051#.XKU89aeZPOQ</a> and <a href="https://zenodo.org/record/2628060#.XULMtnspDb0">https://zenodo.org/record/2628060#.XULMtnspDb0</a> (performed by Dr. Rachel Harding). The latest post shows the purification of construct the HTT N-HEAT_81-1643 domain which elutes from Superdex 200 10/300 GL column in the void volume. The results here presented are a follow up of that purification.</p>
Nickel and FLAG Pull-Down Results From HTT With Putative Interaction Partners
<p>Huntington’s disease (HD) is a progressive neurological disorder caused by a mutation in the huntingtin gene, which encodes the huntingtin protein. Last year, the first structure of this protein was published. With a global resolution of approximately 4 Angstroms, this was a fantastic leap forward in our understanding of this protein. This structure helped our knowledge of Huntingtin, but there is still much more to find out. The structure published by this group is the only representative of about 75% of the protein, the other 25% being too mobile to capture using many high-resolution mapping techniques. One such mobile area is Exon 1, the location of the triplet repeat expansion responsible for HD. This critical region of the protein requires more structural information to understand. To obtain higher resolution images of this region, we are looking for huntingtin interaction partners that bind this region. These interaction partners will hopefully stabilize the structure enough to image the area. Interaction partners will be verified by a Pull-Down assay. Utilizing the FLAG-Tag and His-Tag present on HuntingtinPolyQ54+HAP40(HTT) complex used in this assay, we will look to identify reliable interaction partners. </p>
Mass spectrometry analysis of contaminating band in HTT samples 2019/10/31
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Mass spectrometry analysis of contaminating band in HTT samples</p> <p><strong>Date completed:­ </strong>2019/10/31</p> <p><strong>Rationale: </strong>To determine the identity of ~100 kDa band seen on SDS-PAGE in HTT preps – see <a href="https://zenodo.org/record/3555378">https://zenodo.org/record/3555378</a></p>
Purification of Q23 and Q54 HTT and HTT-HAP40 from Sf9 2019/10/07
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Purification of Q23 and Q54 HTT and HTT-HAP40 from Sf9 </p> <p><strong>Date completed:­ </strong>2019/10/07</p> <p><strong>Rationale: </strong>Purification of HTT and HTT-HAP40 Q23 and Q54 for different biophysical and functional analyses</p>
Purification of HTT Q23 and Q54 from EXPI293F for mass spectrometry analysis 2019/09/30
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Purification of Q23 and Q54 HTT from EXPI293F</p> <p><strong>Date completed:­ </strong>2019/09/30</p> <p><strong>Rationale: </strong>Purify HTT Q23 and Q54 for mass spectrometry analysis</p>
Large-scale purification of Q23 HTT from Sf9 2019/09/30
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Large-scale purification of Q23 HTT from Sf9 </p> <p><strong>Date completed:­ </strong>2019/09/30</p> <p><strong>Rationale: </strong>HTT samples are to be purified from different systems for subsequent biophysical and structural studies. </p>
Large-scale purification of Q23 HTT-HAP40 from Sf9 expression system with contaminating nucleic acid material 2019/09/16
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Large-scale purification of Q23 HTT-HAP40 from Sf9 expression system with contaminating nucleic acid material</p> <p><strong>Date completed:­ </strong>2019/09/16</p> <p><strong>Rationale:</strong> To purify HTT-HAP40 + Sf9 derived nucleic acid material for cryoEM analysis</p>
Large-scale purification of Q23 and Q54 HTT-HAP40 from Sf9 expression system in PBS 2019/09/16
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Large-scale purification of Q23 and Q54 HTT-HAP40 from Sf9 expression system in PBS.</p> <p><strong>Date completed:­ </strong>2019/09/16</p> <p><strong>Rationale: </strong>To purify HTT-HAP40 Q23 and Q54 in PBS to see if this reduces nucleic acid contamination.</p>
MS coverage HTT sequence and assessment of the data so far (2016/02/23)
<p>Open lab notebook for project: huntingtin structural studies</p> <p> </p>
Purification of full-length huntingtin (HTT) constructs (2017/03/14)
<p>Open lab notebook huntingtin structure function project.<br> </p>
Purification of full-length huntingtin (HTT) construct Q23 (2017/03/21)
<p>Open lab notebook huntingtin structure function project.<br> </p>
Purification of full-length huntingtin (HTT) constructs Q17 and Q46 from HEK293 cells
<p>Open lab notebook huntingtin structure function project.<br> </p>
Purification of full-length huntingtin (HTT) constructs Q23 and Q46 from insect sf9 cells and preparation of samples for electron microscopy (2017/03/30)
<p>Huntingtin structure-function open lab notebook project</p>
Preliminary PRC2-HTT interaction study 2017/06/02
<p>Huntingtin structure-function open lab notebook project.</p>
Cryo-EM HTT Q23 (+/- DNA) sample generation (2017/06/05)
<p>Huntingtin structure-function open lab notebook project</p>
Preliminary p53-HTT interaction study 20170719
<p>Huntingtin structure-function open lab notebook project</p>
PRC2-HTT interaction study 20170719
<p>Huntingtin structure-function open lab notebook project</p>
Cryo-EM HTT Q23 (+/- DNA) sample generation (2017/08/01)
<p>Huntingtin structure-function open lab notebook project</p>
Supplementary material 1 from: Linh NN, Hang PLB, Hue HTT, Ha NH, Hanh HH, Ton ND, Hien LTT (2022) Species discrimination of novel chloroplast DNA barcodes and their application for identification of Panax (Aralioideae, Araliaceae). PhytoKeys 188: 1-18. https://doi.org/10.3897/phytokeys.188.75937
NCBI accession numbers of DNA barcoding sequences, and complete chloroplast genomes used in this study.
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