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  An ancient enzyme domain hidden in the putative beta-glucan elicitor receptor of soybean may play an active part in the perception of pathogen-associated molecular patterns during broad host resistance

Fliegmann, J., Mithöfer, A., Wanner, G., & Ebel, J. (2004). An ancient enzyme domain hidden in the putative beta-glucan elicitor receptor of soybean may play an active part in the perception of pathogen-associated molecular patterns during broad host resistance. The Journal of Biological Chemistry, 279(2), 1132-1140. doi:10.1074/jbc.M308552200.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0012-A00B-B Version Permalink: https://hdl.handle.net/21.11116/0000-0009-4B25-A
Genre: Journal Article

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BOL150.pdf (Publisher version), 0B
 
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http://dx.doi.org/10.1074/jbc.M308552200 (Publisher version)
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 Creators:
Fliegmann, J., Author
Mithöfer, A.1, 2, Author           
Wanner, G., Author
Ebel, J., Author
Affiliations:
1Department of Bioorganic Chemistry, MPI for Chemical Ecology, Max Planck Society, ou_24028              
2Research Group Dr. A. Mithöfer, Plant Defense Physiology, Department of Bioorganic Chemistry, Prof. Dr. W. Boland, MPI for Chemical Ecology, Max Planck Society, Jena, DE, ou_421907              

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Free keywords: High-affinity binding Beta-1,3-glucan recognition protein Glycine-max l Disease-resistance Innate immunity Glucoside elicitor Defense responses Phytoalexin accumulation Bradyrhizobium-japonicum Aspergillus-fumigatus. Biochemistry & Biophysics in Current Contents(R)/Life Sciences.
 Abstract: A successful defense against potential pathogens requires that a host organism is able to discriminate between self and nonself structures. Soybean (Glycine max L.) exploits a specific molecular pattern, a 1,6-beta-linked and 1,3-beta-branched heptagluc

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 Dates: 2004
 Publication Status: Issued
 Pages: -
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 Rev. Type: -
 Identifiers: Other: BOL150
DOI: 10.1074/jbc.M308552200
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 279 (2) Sequence Number: - Start / End Page: 1132 - 1140 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1