% 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{Michel:280772,
author = {Michel, Max and Schwarten, Melanie and Decker, Christina
and Nagel-Steger, Luitgard and Willbold, Dieter and
Weiergräber, Oliver H.},
title = {{T}he mammalian autophagy initiator complex contains 2
{HORMA} domain proteins.},
journal = {Autophagy},
volume = {11},
number = {12},
issn = {1554-8635},
address = {Abingdon, Oxon},
publisher = {Taylor $\&$ Francis},
reportid = {FZJ-2016-00528},
pages = {2300 - 2308},
year = {2015},
abstract = {ATG101 is an essential component of the ULK complex
responsible for initiating cellular autophagy in mammalian
cells; its 3-dimensional structure and molecular function,
however, are currently unclear. Here we present the X-ray
structure of human ATG101. The protein displays an open
HORMA domain fold. Both structural properties and
biophysical evidence indicate that ATG101 is locked in this
conformation, in contrast to the prototypical HORMA domain
protein MAD2. Moreover, we discuss a potential mode of
dimerization with ATG13 as a fundamental aspect of ATG101
function.},
cin = {ICS-6},
ddc = {570},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {552 - Engineering Cell Function (POF3-552)},
pid = {G:(DE-HGF)POF3-552},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:26236954},
UT = {WOS:000367806300014},
doi = {10.1080/15548627.2015.1076605},
url = {https://juser.fz-juelich.de/record/280772},
}