% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Pacheco:14240,
      author       = {Pacheco, V. and Ma, P. and Thielmann, Y. and Hartmann, R.
                      and Weiergräber, O.H. and Mohrlüder, J. and Willbold, D.},
      title        = {{A}ssessment of {GABARAP} self-association by its diffusion
                      properties},
      journal      = {Journal of biomolecular NMR},
      volume       = {48},
      issn         = {0925-2738},
      address      = {Dordrecht [u.a.]},
      publisher    = {Springer Science + Business Media B.V},
      reportid     = {PreJuSER-14240},
      pages        = {49 - 58},
      year         = {2010},
      note         = {O. 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.},
      abstract     = {Gamma-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.},
      keywords     = {Adaptor Proteins, Signal Transducing: chemistry / Adaptor
                      Proteins, Signal Transducing: metabolism / Diffusion /
                      Humans / Microtubule-Associated Proteins: chemistry /
                      Microtubule-Associated Proteins: metabolism / Models,
                      Molecular / Nuclear Magnetic Resonance, Biomolecular:
                      methods / Protein Multimerization / Temperature / Adaptor
                      Proteins, Signal Transducing (NLM Chemicals) / GABARAP
                      protein, human (NLM Chemicals) / Microtubule-Associated
                      Proteins (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-3 / JARA-HPC / ICS-5},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB942 / $I:(DE-82)080012_20140620$ /
                      I:(DE-Juel1)ICS-5-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Spectroscopy},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20665069},
      UT           = {WOS:000282102300005},
      doi          = {10.1007/s10858-010-9437-5},
      url          = {https://juser.fz-juelich.de/record/14240},
}