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  <url>
    <loc>http://www.thelowlab.org/dynamin</loc>
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    <lastmod>2014-01-30</lastmod>
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  <url>
    <loc>http://www.thelowlab.org/membrane-remodelling-dynamin</loc>
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    <lastmod>2021-12-21</lastmod>
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      <image:loc>https://images.squarespace-cdn.com/content/v1/52e79cb5e4b0b77fb0239620/b57d5cbd-2f45-440d-a8fc-7ba7e23d619f/cjy_xtal_packing.png</image:loc>
      <image:title>Membrane remodelling- Dynamin</image:title>
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    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/52e79cb5e4b0b77fb0239620/7d99eeb5-66c0-44b7-999d-dfd11bbe370b/DNM1_BDLP.png</image:loc>
      <image:title>Membrane remodelling- Dynamin</image:title>
      <image:caption>X-ray crystal structures of the mitochondrial fission dynamin DNM1 from the algae Cyanidioschyzon merolae (left) and the bacterial dynamin BDLP1 from the cyanobacteria Nostoc punctiforme (right). Unexpectedly, both are observed in a closed conformation, which has implication for how dynamin-family members couple large scale conformational changes with membrane fission and fusion.</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/52e79cb5e4b0b77fb0239620/198dd60d-20f6-40a6-b828-db9504735303/CmDNM1_mechanism.png</image:loc>
      <image:title>Membrane remodelling- Dynamin - Make it stand out</image:title>
      <image:caption>Model for CmDnm1 activation and polymerization on membrane templates.</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/52e79cb5e4b0b77fb0239620/26d0808f-63c9-43fe-820d-52207ab13d17/CJY1_2.png</image:loc>
      <image:title>Membrane remodelling- Dynamin - Make it stand out</image:title>
      <image:caption>The crystal structure of Cj-DLP1/2 tetramer in the apo state. Cj-DLP2 forms a central back-to-back dimer flanked on each side by Cj-DLP1 subunits.</image:caption>
    </image:image>
    <image:image>
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      <image:title>Membrane remodelling- Dynamin - Make it stand out</image:title>
      <image:caption>Membrane tethering by a bacterial DLP. Cj-DLP1 is connected to Cj-DLP2 by a linker that is likely highly flexible in solution.</image:caption>
    </image:image>
    <image:image>
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      <image:title>Membrane remodelling- Dynamin - Make it stand out</image:title>
      <image:caption>Cartoon superposition of Cj-DLP1 and Mitofusin 1 partial structure.</image:caption>
    </image:image>
  </url>
  <url>
    <loc>http://www.thelowlab.org/hlow</loc>
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    <priority>0.75</priority>
    <lastmod>2025-09-11</lastmod>
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      <image:title>Harry Low CV</image:title>
    </image:image>
  </url>
  <url>
    <loc>http://www.thelowlab.org/overview</loc>
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    <priority>0.75</priority>
    <lastmod>2023-01-20</lastmod>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/52e79cb5e4b0b77fb0239620/1391172858175-475JB13VA72IOQ4O9P41/bdlp_gdpdimer_slim.png</image:loc>
      <image:title>Overview</image:title>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/52e79cb5e4b0b77fb0239620/997de3d6-1cb3-4c7a-86f3-a2cbb9fd05b5/T2SS_OMC_6second_for_gif_360frames_medium.gif</image:loc>
      <image:title>Overview - Make it stand out</image:title>
      <image:caption>Klebsiella pneumoniae type II secretion system outer membrane complex comprising the secretin PulD (blue and red), the pilotin PulS (cyan) and PulC HR domain (orange).</image:caption>
    </image:image>
  </url>
  <url>
    <loc>http://www.thelowlab.org/bacterial-secretion-systems</loc>
    <changefreq>daily</changefreq>
    <priority>0.75</priority>
    <lastmod>2021-12-21</lastmod>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/52e79cb5e4b0b77fb0239620/8ac897bc-007b-47a5-ae20-7e48f57731c1/mech_schematic.png</image:loc>
      <image:title>Bacterial secretion systems</image:title>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/52e79cb5e4b0b77fb0239620/c5d0afd4-2c19-4d7d-bed1-96817dd4446e/T2SS_secretin.png</image:loc>
      <image:title>Bacterial secretion systems</image:title>
      <image:caption>Cryo-EM structure of the T2SS outer membrane complex, which includes the PulD secretin (light blue) and PulS pilotin (cyan) with C15 symmetry. PulC HR domain (orange) is positioned at the base of the secretin.</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/52e79cb5e4b0b77fb0239620/2654c068-9fba-437b-8210-f4b414c6d404/schematic.png</image:loc>
      <image:title>Bacterial secretion systems - Make it stand out</image:title>
      <image:caption>(Left) Negative stain class averages of the PulCDELMNS complex showing the first glimpse of the assembled inner membrane platform. (Right) Stoichiometric model of an assembled T2SS core apparatus. Inner membrane platform components comprise a hexameric hub. PulC connects the inner membrane platform to the outer membrane complex by binding to the secretin base. Substrate may be loaded through the PulC cage in positions where PulC is absent.</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/52e79cb5e4b0b77fb0239620/9fa967f7-c25c-4160-9b46-e02264f7b8f7/T2SS_review_2020.png</image:loc>
      <image:title>Bacterial secretion systems - Make it stand out</image:title>
      <image:caption>A model of the bacterial Type II secretion system. Substrates include the cholera and LT toxins which are secreted by Vibrio cholerae and entertoxigenic Escherichia coli (ETEC), respectively.</image:caption>
    </image:image>
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    <lastmod>2026-03-29</lastmod>
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    <loc>http://www.thelowlab.org/lab-members</loc>
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    <lastmod>2025-10-08</lastmod>
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      <image:caption>Whatever it is, the way you tell your story online can make all the difference.</image:caption>
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      <image:caption>Whatever it is, the way you tell your story online can make all the difference.</image:caption>
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      <image:title>Lab members - Make it stand out</image:title>
      <image:caption>Whatever it is, the way you tell your story online can make all the difference.</image:caption>
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      <image:title>Lab members</image:title>
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      <image:caption>Whatever it is, the way you tell your story online can make all the difference.</image:caption>
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  </url>
  <url>
    <loc>http://www.thelowlab.org/membrane-remodelling-vipp1</loc>
    <changefreq>daily</changefreq>
    <priority>0.75</priority>
    <lastmod>2021-12-21</lastmod>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/52e79cb5e4b0b77fb0239620/685007f4-5ff6-47f0-afc8-047aafe36b35/vipp1_collage.png</image:loc>
      <image:title>Membrane remodelling- Vipp1/ESCRT-III-like - Make it stand out</image:title>
      <image:caption>Whatever it is, the way you tell your story online can make all the difference.</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/52e79cb5e4b0b77fb0239620/33ed43c6-3a3b-40d5-b9bf-ac99c1ce8ddc/evo_tree.png</image:loc>
      <image:title>Membrane remodelling- Vipp1/ESCRT-III-like - Make it stand out</image:title>
      <image:caption>Tree of the PspA/ESCRT-III superfamily colored according to phylogenetic groups. A long branch separates the PspA/Vipp1 (left) and ESCRT-III (right) subfamilies. Scale bar represents expected substitutions per site. Study undertaken by Diorge Souza, Tom Williams and Buzz Baum.</image:caption>
    </image:image>
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      <image:loc>https://images.squarespace-cdn.com/content/v1/52e79cb5e4b0b77fb0239620/c65235de-4ce8-48fa-8625-7f580dab09e0/ezgif.com-gif-maker.gif</image:loc>
      <image:title>Membrane remodelling- Vipp1/ESCRT-III-like - Make it stand out</image:title>
      <image:caption>C14 symmetry Vipp1 ring showing dome-shaped curvature. The membrane binding Helix 0 can be seen lining the inner lumen.</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/52e79cb5e4b0b77fb0239620/1e07aaf4-049c-4af8-a63b-4c31b5e531d9/vipp1_chmp1B.png</image:loc>
      <image:title>Membrane remodelling- Vipp1/ESCRT-III-like - Make it stand out</image:title>
      <image:caption>Vipp1 has the same helical domain organization as ESCRT-III proteins, such as human CHMP1B shown here. In addition, Vipp1 and CHMP1B form similar polymers based on hairpin packing (blue and purple helices) and helix α5 (orange) domain swap.</image:caption>
    </image:image>
  </url>
</urlset>

