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

MPS-Authors

Bürger,  Marco
Max Planck Institute of Molecular Physiology, Max Planck Society;

Zimmermann,  Tobias J.
Max Planck Institute of Molecular Physiology, Max Planck Society;

Stege,  Patricia
Max Planck Institute of Molecular Physiology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons98735

Waldmann,  Herbert
Abt. IV: Chemische Biologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons98734

Vetter,  Ingrid R.
Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0013-FF4C-6
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