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- Publisher Website: 10.1007/s11426-014-5088-9
- Scopus: eid_2-s2.0-84902266824
- WOS: WOS:000336747700007
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Article: Urease inactivation by an unusual GroES chaperonin
Title | Urease inactivation by an unusual GroES chaperonin |
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Authors | |
Keywords | GroES chaperonin Helicobacter pylori metal binding microbial pathogenesis nickel urease inactivation |
Issue Date | 2014 |
Publisher | Science China Press, co-published with Springer. The Journal's web site is located at http://chem.scichina.com:8081/sciBe/EN/volumn/current.shtml |
Citation | Science China Chemistry, 2014, v. 57 n. 6, p. 842-848 How to Cite? |
Abstract | It remains uncovered yet how the common gastric pathogen, Helicobacter pylori, survives through the acidic barrier and the immune response simultaneously in the stomach. Herein we report a unique GroES chaperonin that effectively inactivates Helicobacter pylori urease in Escherichia coli model. Such a function depends on the quaternary structure as well as the metal binding at the C terminus. Surprisingly, the C-terminal metal capacity seems not closely relevant to the apparent urease inactivation. Our findings have possibly revealed a survival strategy of Helicobacter pylori after its gastric localization. © 2014 Science China Press and Springer-Verlag Berlin Heidelberg. |
Persistent Identifier | http://hdl.handle.net/10722/202608 |
ISSN | 2023 Impact Factor: 10.4 2023 SCImago Journal Rankings: 2.316 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Cun, SJ | - |
dc.contributor.author | Sun, H | - |
dc.date.accessioned | 2014-09-19T08:42:29Z | - |
dc.date.available | 2014-09-19T08:42:29Z | - |
dc.date.issued | 2014 | - |
dc.identifier.citation | Science China Chemistry, 2014, v. 57 n. 6, p. 842-848 | - |
dc.identifier.issn | 1674-7291 | - |
dc.identifier.uri | http://hdl.handle.net/10722/202608 | - |
dc.description.abstract | It remains uncovered yet how the common gastric pathogen, Helicobacter pylori, survives through the acidic barrier and the immune response simultaneously in the stomach. Herein we report a unique GroES chaperonin that effectively inactivates Helicobacter pylori urease in Escherichia coli model. Such a function depends on the quaternary structure as well as the metal binding at the C terminus. Surprisingly, the C-terminal metal capacity seems not closely relevant to the apparent urease inactivation. Our findings have possibly revealed a survival strategy of Helicobacter pylori after its gastric localization. © 2014 Science China Press and Springer-Verlag Berlin Heidelberg. | - |
dc.language | eng | - |
dc.publisher | Science China Press, co-published with Springer. The Journal's web site is located at http://chem.scichina.com:8081/sciBe/EN/volumn/current.shtml | - |
dc.relation.ispartof | Science China Chemistry | - |
dc.rights | The original publication is available at www.scichina.com and www.springerlink.com | - |
dc.subject | GroES chaperonin | - |
dc.subject | Helicobacter pylori | - |
dc.subject | metal binding | - |
dc.subject | microbial pathogenesis | - |
dc.subject | nickel | - |
dc.subject | urease inactivation | - |
dc.title | Urease inactivation by an unusual GroES chaperonin | - |
dc.type | Article | - |
dc.identifier.email | Sun, H: hsun@hku.hk | - |
dc.identifier.authority | Sun, H=rp00777 | - |
dc.identifier.doi | 10.1007/s11426-014-5088-9 | - |
dc.identifier.scopus | eid_2-s2.0-84902266824 | - |
dc.identifier.hkuros | 239334 | - |
dc.identifier.volume | 57 | - |
dc.identifier.issue | 6 | - |
dc.identifier.spage | 842 | - |
dc.identifier.epage | 848 | - |
dc.identifier.isi | WOS:000336747700007 | - |
dc.publisher.place | China | - |
dc.identifier.issnl | 1869-1870 | - |