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          Institute: MPI für molekulare Physiologie     Collection: Abteilung IV - Chemische Biologie     Display Documents



  history
ID: 577056.0, MPI für molekulare Physiologie / Abteilung IV - Chemische Biologie
Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity despite close relationship to acyl protein thioesterase
Authors:Bürger, Marco; Zimmermann, Tobias J.; Kondoh, Yasumitsu; Stege, Patricia; Watanabe, Nobumoto; Osada, Hiroyuki; Waldmann, Herbert; Vetter, Ingrid R.
Language:English
Date of Publication (YYYY-MM-DD):2012
Title of Journal:Journal of Lipid Research
Volume:53
Issue / Number:1
Start Page:43
End Page:50
Sequence Number of Article:1
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Free Keywords:lysophospholipase; α/β hydrolase; chemical array screening; inhibitor
External Publication Status:published
Document Type:Article
Communicated by:Jürgen Block
Affiliations:MPI für molekulare Physiologie/Abteilung IV - Chemische Biologie/AG Prof. Dr. Herbert Waldmann
MPI für molekulare Physiologie/Abteilung I - Mechanistische Zellbiologie/AG Kristallographie-Dr. I. Vetter
External Affiliations:Faculty of Chemistry, Technical University of Dortmund, Dortmund, Germany
Chemical Biology Core Facility, RIKEN Advanced Science Institute, Wako, Japan
Bioprobe Application Team Riken-Max Planck Joint Research Center, RIKEN Advanced Science Institute, Wako, Japan
Identifiers:URL:http://dx.doi.org/10.1194/jlr.M019851 [article locator with full text links]
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