Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected 
functional plasticity despite close relationship to acyl protein thioesterase

Bürger, Marco; Zimmermann, Tobias J.; Kondoh, Yasumitsu; Stege, Patricia; Watanabe, Nobumoto; Osada, Hiroyuki; Waldmann, Herbert; Vetter, Ingrid R.

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Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity despite close relationship to acyl protein thioesterase

Bürger, M., Zimmermann, T. J., Kondoh, Y., Stege, P., Watanabe, N., Osada, H., et al. (2012). Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity despite close relationship to acyl protein thioesterase. Journal of Lipid Research, 53(1): 1, pp. 43-50. Retrieved from http://dx.doi.org/10.1194/jlr.M019851.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0013-FF4C-6 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0013-FF4D-4

Genre: Journal Article

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Creators:
Bürger, Marco¹, Author
Zimmermann, Tobias J.¹, Author
Kondoh, Yasumitsu, Author
Stege, Patricia¹, Author
Watanabe, Nobumoto, Author
Osada, Hiroyuki, Author
Waldmann, Herbert², Author
Vetter, Ingrid R.³, Author

Affiliations:
1Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753286
2Abt. IV: Chemische Biologie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753290
3Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753287

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Free keywords: lysophospholipase; α/β hydrolase; chemical array screening; inhibitor

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Language(s): eng - English

Dates: Date issued: 2012

Publication Status: Issued

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Rev. Type: Peer

Identifiers: eDoc: 577056
URI: http://dx.doi.org/10.1194/jlr.M019851

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Title: Journal of Lipid Research

Source Genre: Journal

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Pages: - Volume / Issue: 53 (1) Sequence Number: 1 Start / End Page: 43 - 50 Identifier: -