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000014240 0247_ $$2DOI$$a10.1007/s10858-010-9437-5
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000014240 084__ $$2WoS$$aBiochemistry & Molecular Biology
000014240 084__ $$2WoS$$aSpectroscopy
000014240 1001_ $$0P:(DE-Juel1)VDB70443$$aPacheco, V.$$b0$$uFZJ
000014240 245__ $$aAssessment of GABARAP self-association by its diffusion properties
000014240 260__ $$aDordrecht [u.a.]$$bSpringer Science + Business Media B.V$$c2010
000014240 300__ $$a49 - 58
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000014240 440_0 $$09165$$aJournal of Biomolecular NMR$$v48$$x0925-2738$$y1
000014240 500__ $$aO. H. Weiergraber is grateful to Georg Buldt for continuous generous support. V. Pacheco appreciates support by Heike Schneider. This work was supported by a Deutsche Forschungsgemeinschaft (DFG) grant to D. W. (Wi1472/5) and a PhD scholarship from the Deutscher Akademischer Austauschdienst (DAAD) to P. M.
000014240 520__ $$aGamma-aminobutyric acid type A receptor-associated protein (GABARAP) belongs to a family of small ubiquitin-like adaptor proteins implicated in intracellular vesicle trafficking and autophagy. We have used diffusion-ordered nuclear magnetic resonance spectroscopy to study the temperature and concentration dependence of the diffusion properties of GABARAP. Our data suggest the presence of distinct conformational states and provide support for self-association of GABARAP molecules. Assuming a monomer-dimer equilibrium, a temperature-dependent dissociation constant could be derived. Based on a temperature series of (1)H(15)N heteronuclear single quantum coherence nuclear magnetic resonance spectra, we propose residues potentially involved in GABARAP self-interaction. The possible biological significance of these observations is discussed with respect to alternative scenarios of oligomerization.
000014240 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
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000014240 65320 $$2Author$$aDiffusion-ordered spectroscopy
000014240 65320 $$2Author$$aNMR spectroscopy
000014240 65320 $$2Author$$aProtein oligomerization
000014240 65320 $$2Author$$aGABARAP
000014240 650_2 $$2MeSH$$aAdaptor Proteins, Signal Transducing: chemistry
000014240 650_2 $$2MeSH$$aAdaptor Proteins, Signal Transducing: metabolism
000014240 650_2 $$2MeSH$$aDiffusion
000014240 650_2 $$2MeSH$$aHumans
000014240 650_2 $$2MeSH$$aMicrotubule-Associated Proteins: chemistry
000014240 650_2 $$2MeSH$$aMicrotubule-Associated Proteins: metabolism
000014240 650_2 $$2MeSH$$aModels, Molecular
000014240 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular: methods
000014240 650_2 $$2MeSH$$aProtein Multimerization
000014240 650_2 $$2MeSH$$aTemperature
000014240 650_7 $$00$$2NLM Chemicals$$aAdaptor Proteins, Signal Transducing
000014240 650_7 $$00$$2NLM Chemicals$$aGABARAP protein, human
000014240 650_7 $$00$$2NLM Chemicals$$aMicrotubule-Associated Proteins
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000014240 7001_ $$0P:(DE-Juel1)VDB84828$$aMa, P.$$b1$$uFZJ
000014240 7001_ $$0P:(DE-Juel1)VDB77156$$aThielmann, Y.$$b2$$uFZJ
000014240 7001_ $$0P:(DE-Juel1)VDB57647$$aHartmann, R.$$b3$$uFZJ
000014240 7001_ $$0P:(DE-Juel1)131988$$aWeiergräber, O.H.$$b4$$uFZJ
000014240 7001_ $$0P:(DE-Juel1)132012$$aMohrlüder, J.$$b5$$uFZJ
000014240 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b6$$uFZJ
000014240 773__ $$0PERI:(DE-600)2006645-4$$a10.1007/s10858-010-9437-5$$gVol. 48, p. 49 - 58$$p49 - 58$$q48<49 - 58$$tJournal of biomolecular NMR$$v48$$x0925-2738$$y2010
000014240 8567_ $$uhttp://dx.doi.org/10.1007/s10858-010-9437-5
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