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@ARTICLE{Schwarten:4477,
author = {Schwarten, M. and Stoldt, M. and Mohrlüder, J. and
Willbold, D.},
title = {{S}equence-specific 1{H}, 13{C} and 15{N} resonance
assignment of the autophagy-related protein {A}tg 8.},
journal = {Biomolecular NMR assignments},
volume = {3},
issn = {1874-2718},
address = {Dordrecht [u.a.]},
publisher = {Springer Netherlands},
reportid = {PreJuSER-4477},
pages = {137 - 139},
year = {2009},
note = {We would like to thank Sven Schunke for helpful
discussions. This study was supported by a research grant
from the Deutsche Forschungsgemeinschaft (DFG) to D. W.
(Wi1472/5) and a fellowship from the International Helmholtz
Research School on Biophysics and Soft Matter ("BioSoft'')
to M. Sch.},
abstract = {The autophagy-related protein Atg8 is important for the
formation of autophagosomes as it mediates membrane fusion.
To elucidate the solution structure of Atg8 backbone and
side chain chemical shifts of Atg8 were assigned as far as
possible.},
keywords = {Amino Acid Sequence / Autophagy / Carbon Isotopes:
chemistry / Magnetic Resonance Spectroscopy: methods /
Microtubule-Associated Proteins: chemistry / Molecular
Sequence Data / Nitrogen Isotopes: chemistry / Protein
Structure, Tertiary / Protein Subunits / Protons /
Saccharomyces cerevisiae Proteins: chemistry / ATG8 protein,
S cerevisiae (NLM Chemicals) / Carbon Isotopes (NLM
Chemicals) / Microtubule-Associated Proteins (NLM Chemicals)
/ Nitrogen Isotopes (NLM Chemicals) / Protein Subunits (NLM
Chemicals) / Protons (NLM Chemicals) / Saccharomyces
cerevisiae Proteins (NLM Chemicals) / J (WoSType)},
cin = {ISB-3},
ddc = {570},
cid = {I:(DE-Juel1)VDB942},
pnm = {Funktion und Dysfunktion des Nervensystems},
pid = {G:(DE-Juel1)FUEK409},
shelfmark = {Biophysics / Spectroscopy},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:19636965},
UT = {WOS:000266006900033},
doi = {10.1007/s12104-009-9159-3},
url = {https://juser.fz-juelich.de/record/4477},
}