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024 7 _ |2 pmid
|a pmid:19462014
024 7 _ |2 DOI
|a 10.1039/b900425d
024 7 _ |2 WOS
|a WOS:000266269500002
037 _ _ |a PreJuSER-7139
041 _ _ |a eng
082 _ _ |a 540
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |0 P:(DE-Juel1)VDB77156
|a Thielmann, Y.
|b 0
|u FZJ
245 _ _ |a Structural characterization of GABARAP-ligand interactions
260 _ _ |a Cambridge
|b Royal Society of Chemistry
|c 2009
300 _ _ |a 575 - 579
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
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336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
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336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |0 20661
|a Molecular BioSystems
|v 5
|x 1742-206X
500 _ _ |a O.H.W. is grateful to Georg Buldt for continuous generous support. Moreover, assistance by the beamline staff at ESRF (Grenoble, France) is acknowledged. This study was supported by a research grant from the Deutsche Forschungsgemeinschaft to D. W. (Wi1472/5).
520 _ _ |a The GABA(A) receptor-associated protein (GABARAP) plays an important role in intracellular trafficking of several proteins. It undergoes a C-terminal lipidation process that enables anchoring in the cytosolic leaflet of cellular membranes. While the three-dimensional structure of GABARAP itself has been determined, structural investigation of complexes with its interaction partners has just commenced. Studies with indole derivatives revealed that GABARAP features two hydrophobic binding sites (hp1 and hp2). These also play an essential role in complex formation with the native ligand calreticulin. Furthermore, a model of hexameric N-ethylmaleimide-sensitive factor (NSF) suggests that binding of GABARAP to this molecular machine may involve a similar site. Since hp1 and hp2 are highly conserved throughout the GABARAP family, the relevance of the structural data presented here is likely to extend to GABARAP homologues.
536 _ _ |0 G:(DE-Juel1)FUEK409
|2 G:(DE-HGF)
|a Funktion und Dysfunktion des Nervensystems
|c P33
|x 0
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|2 G:(DE-HGF)
|a Programm Biosoft
|c N03
|x 1
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Amino Acid Sequence
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Calreticulin: chemistry
650 _ 2 |2 MeSH
|a Calreticulin: metabolism
650 _ 2 |2 MeSH
|a Clathrin Heavy Chains: chemistry
650 _ 2 |2 MeSH
|a Clathrin Heavy Chains: metabolism
650 _ 2 |2 MeSH
|a Humans
650 _ 2 |2 MeSH
|a Ligands
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary
650 _ 2 |2 MeSH
|a Receptors, GABA-A: chemistry
650 _ 2 |2 MeSH
|a Receptors, GABA-A: metabolism
650 _ 7 |0 0
|2 NLM Chemicals
|a Calreticulin
650 _ 7 |0 0
|2 NLM Chemicals
|a Ligands
650 _ 7 |0 0
|2 NLM Chemicals
|a Receptors, GABA-A
650 _ 7 |0 114899-12-6
|2 NLM Chemicals
|a Clathrin Heavy Chains
650 _ 7 |2 WoSType
|a J
700 1 _ |0 P:(DE-Juel1)131988
|a Weiergräber, O.H.
|b 1
|u FZJ
700 1 _ |0 P:(DE-Juel1)132012
|a Mohrlüder, J.
|b 2
|u FZJ
700 1 _ |0 P:(DE-Juel1)132029
|a Willbold, D.
|b 3
|u FZJ
773 _ _ |0 PERI:(DE-600)2188635-0
|a 10.1039/b900425d
|g Vol. 5, p. 575 - 579
|p 575 - 579
|q 5<575 - 579
|t Molecular BioSystems
|v 5
|x 1742-206X
|y 2009
856 7 _ |u http://dx.doi.org/10.1039/b900425d
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915 _ _ |0 StatID:(DE-HGF)0010
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