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Conference Paper: Metal binding profiles of H. pylori metallochaperone HypA and HspA in cells
Title | Metal binding profiles of H. pylori metallochaperone HypA and HspA in cells |
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Authors | |
Issue Date | 2013 |
Citation | The 12th International Symposium on Applied Bioinorganic Chemistry (ISABC12), Guangzhou, China, 3-6 December 2013. How to Cite? |
Abstract | Metal ions play either catalytic or structural roles in a quarter to one-third of all proteins in biological systems. Bacterial metalloproteins have evolved an elaborate mechanism acting in concert to maintain cellular metal homeostasis[1]. The bacterial pathogen Helicobacter pylori is the leading risk factor for the development of human gastric cancer. Its infectious capacity relies heavily on two Ni-enyzmes urease and [Ni, Fe]-hydrogenase, which are denpendent on the intracelluar Ni2+ that is tightly controlled by a battery of metallochaperones. Bi-based antiulcer drugs have long been used for the treatment of H. pylori infection. Proteins are commonly believed … |
Description | Poster-80 |
Persistent Identifier | http://hdl.handle.net/10722/203961 |
DC Field | Value | Language |
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dc.contributor.author | Wang, Y | en_US |
dc.contributor.author | Hu, L | en_US |
dc.contributor.author | Hu, X | en_US |
dc.contributor.author | Chang, YY | en_US |
dc.contributor.author | Yang, X | en_US |
dc.contributor.author | Li, H | en_US |
dc.contributor.author | Sun, H | en_US |
dc.date.accessioned | 2014-09-19T19:30:34Z | - |
dc.date.available | 2014-09-19T19:30:34Z | - |
dc.date.issued | 2013 | en_US |
dc.identifier.citation | The 12th International Symposium on Applied Bioinorganic Chemistry (ISABC12), Guangzhou, China, 3-6 December 2013. | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/203961 | - |
dc.description | Poster-80 | - |
dc.description.abstract | Metal ions play either catalytic or structural roles in a quarter to one-third of all proteins in biological systems. Bacterial metalloproteins have evolved an elaborate mechanism acting in concert to maintain cellular metal homeostasis[1]. The bacterial pathogen Helicobacter pylori is the leading risk factor for the development of human gastric cancer. Its infectious capacity relies heavily on two Ni-enyzmes urease and [Ni, Fe]-hydrogenase, which are denpendent on the intracelluar Ni2+ that is tightly controlled by a battery of metallochaperones. Bi-based antiulcer drugs have long been used for the treatment of H. pylori infection. Proteins are commonly believed … | - |
dc.language | eng | en_US |
dc.relation.ispartof | 12th International Symposium on Applied Bioinorganic Chemistry 2013 | en_US |
dc.title | Metal binding profiles of H. pylori metallochaperone HypA and HspA in cells | en_US |
dc.type | Conference_Paper | en_US |
dc.identifier.email | Hu, L: liganghu@hku.hk | en_US |
dc.identifier.email | Li, H: hylichem@hku.hk | en_US |
dc.identifier.email | Sun, H: hsun@hku.hk | en_US |
dc.identifier.authority | Sun, H=rp00777 | en_US |
dc.description.nature | postprint | - |
dc.identifier.hkuros | 239796 | en_US |