The surface protein Shr of Streptococcus pyogenes binds heme and transfers it to the streptococcal heme-binding protein Shp
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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1471-2180
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
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The surface protein Shr of Streptococcus pyogenes binds heme and transfers it to the streptococcal heme-binding protein Shp ; volume:8 ; number:1 ; day:23 ; month:1 ; year:2008 ; pages:1-8 ; date:12.2008
BMC microbiology ; 8, Heft 1 (23.1.2008), 1-8, 12.2008
- Creator
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Zhu, Hui
- Contributor
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Liu, Mengyao
Lei, Benfang
SpringerLink (Online service)
- DOI
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10.1186/1471-2180-8-15
- URN
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urn:nbn:de:1111-2016030222257
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:32 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Zhu, Hui
- Liu, Mengyao
- Lei, Benfang
- SpringerLink (Online service)
Other Objects (12)
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Spectro-Electrochemical Investigations on Immobilised Heme Proteins
Structural basis for the recognition of human hemoglobin by the heme-acquisition protein Shr from Streptococcus pyogenes
Histidine and Tyrosine-based Heme-binding Motifs for the Prediction of Heme-Regulated Proteins
Exploring the folding energy landscapes of heme proteins using a hybrid AWSEM-heme model
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Heme Newsletter
Identification and characterization of the heme-binding proteins SeShp and SeHtsA of Streptococcus equi subspecies equi
Engineering Escherichia coli for efficient assembly of heme proteins
Heme, Bernhard Wilhelm
Expanding heme-protein folding space using designed multi-heme β-sheet mini-proteins
Structural investigations on heme-interacting proteins
Characterization of transient heme-protein interactions as basis for the prediction of potential heme-regulated proteins
Spectro-Electrochemical Investigations on Immobilised Heme Proteins
Structural basis for the recognition of human hemoglobin by the heme-acquisition protein Shr from Streptococcus pyogenes
Histidine and Tyrosine-based Heme-binding Motifs for the Prediction of Heme-Regulated Proteins
Exploring the folding energy landscapes of heme proteins using a hybrid AWSEM-heme model
Development of heme protein based oxygen sensing indicators
Heme Newsletter
Identification and characterization of the heme-binding proteins SeShp and SeHtsA of Streptococcus equi subspecies equi
Engineering Escherichia coli for efficient assembly of heme proteins
Heme, Bernhard Wilhelm
Expanding heme-protein folding space using designed multi-heme β-sheet mini-proteins
Structural investigations on heme-interacting proteins
Characterization of transient heme-protein interactions as basis for the prediction of potential heme-regulated proteins
Spectro-Electrochemical Investigations on Immobilised Heme Proteins
Structural basis for the recognition of human hemoglobin by the heme-acquisition protein Shr from Streptococcus pyogenes
Histidine and Tyrosine-based Heme-binding Motifs for the Prediction of Heme-Regulated Proteins
Exploring the folding energy landscapes of heme proteins using a hybrid AWSEM-heme model
Development of heme protein based oxygen sensing indicators
Heme Newsletter
Identification and characterization of the heme-binding proteins SeShp and SeHtsA of Streptococcus equi subspecies equi
Engineering Escherichia coli for efficient assembly of heme proteins