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@ARTICLE{Cehlar:144121,
author = {Cehlar, O. and Skrabana, R. and Kovac, A. and Kovacech, B.
and Novak, M. and DESY},
title = {{C}rystallization and preliminary {X}-ray diffraction
analysis of tau protein microtubule-binding motifs in
complex with {T}au5 and {DC}25 antibody {F}ab fragments},
journal = {Acta crystallographica / F},
volume = {68},
issn = {1744-3091},
address = {Oxford [u.a.]},
publisher = {Blackwell},
reportid = {PHPPUBDB-25816},
pages = {1181},
year = {2012},
abstract = {The Alzheimer's disease-associated protein tau is an
intrinsically disordered protein with no preferred structure
in solution. Under physiological conditions, tau binds to
microtubules and regulates their dynamics, whereas during
the development of neurodegeneration tau dissociates from
microtubules, misfolds and creates highly insoluble
deposits. To elucidate the determinants of tau-protein
misfolding, tau peptides from microtubule-binding motifs
were crystallized in complexes with Fab fragments of
specific monoclonal antibodies. The crystals diffracted to
1.69 Å resolution and gave complete data sets using a
synchrotron X-ray source. Molecular replacement was used to
solve the phase problem.},
keywords = {Amino Acid Motifs / Antibodies, Monoclonal /
Crystallization / Crystallography, X-Ray / Immunoglobulin
Fab Fragments: chemistry / Immunoglobulin Fab Fragments:
immunology / Microtubules: chemistry / Microtubules:
metabolism / Protein Structure, Tertiary / tau Proteins:
chemistry / tau Proteins: immunology / tau Proteins:
metabolism / Antibodies, Monoclonal (NLM Chemicals) /
Immunoglobulin Fab Fragments (NLM Chemicals) / tau Proteins
(NLM Chemicals)},
cin = {HASYLAB},
ddc = {530},
cid = {$I:(DE-H253)HASYLAB_-2012_-20130307$},
pnm = {DORIS Beamline K1.2 (POF2-54G13)},
pid = {G:(DE-H253)POF2-K1.2-20130405},
experiment = {EXP:(DE-H253)D-K1.2-20150101},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:23027743},
pmc = {pmc:PMC3497975},
UT = {WOS:000309357200008},
doi = {10.1107/S1744309112030382},
url = {https://bib-pubdb1.desy.de/record/144121},
}