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Conference Paper: Metal binding profiles of H. pylori metallochaperone HypA and HspA in cells

TitleMetal binding profiles of H. pylori metallochaperone HypA and HspA in cells
Authors
Issue Date2013
Citation
The 12th International Symposium on Applied Bioinorganic Chemistry (ISABC12), Guangzhou, China, 3-6 December 2013. How to Cite?
AbstractMetal 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 …
DescriptionPoster-80
Persistent Identifierhttp://hdl.handle.net/10722/203961

 

DC FieldValueLanguage
dc.contributor.authorWang, Yen_US
dc.contributor.authorHu, Len_US
dc.contributor.authorHu, Xen_US
dc.contributor.authorChang, YYen_US
dc.contributor.authorYang, Xen_US
dc.contributor.authorLi, Hen_US
dc.contributor.authorSun, Hen_US
dc.date.accessioned2014-09-19T19:30:34Z-
dc.date.available2014-09-19T19:30:34Z-
dc.date.issued2013en_US
dc.identifier.citationThe 12th International Symposium on Applied Bioinorganic Chemistry (ISABC12), Guangzhou, China, 3-6 December 2013.en_US
dc.identifier.urihttp://hdl.handle.net/10722/203961-
dc.descriptionPoster-80-
dc.description.abstractMetal 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.languageengen_US
dc.relation.ispartof12th International Symposium on Applied Bioinorganic Chemistry 2013en_US
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.titleMetal binding profiles of H. pylori metallochaperone HypA and HspA in cellsen_US
dc.typeConference_Paperen_US
dc.identifier.emailHu, L: liganghu@hku.hken_US
dc.identifier.emailLi, H: hylichem@hku.hken_US
dc.identifier.emailSun, H: hsun@hku.hken_US
dc.identifier.authoritySun, H=rp00777en_US
dc.description.naturepostprint-
dc.identifier.hkuros239796en_US

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