% 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{Kadavath:138080, author = {Kadavath, Harindranath and Jaremko, Mariusz and Jaremko, Lukasz and Biernat, Jacek and Mandelkow, Eckhard and Zweckstetter, Markus}, title = {{F}olding of the {T}au {P}rotein on {M}icrotubules.}, journal = {Angewandte Chemie / International edition}, volume = {54}, number = {35}, issn = {1433-7851}, address = {Weinheim}, publisher = {Wiley-VCH}, reportid = {DZNE-2020-04402}, pages = {10347-10351}, year = {2015}, abstract = {Microtubules are regulated by microtubule-associated proteins. However, little is known about the structure of microtubule-associated proteins in complex with microtubules. Herein we show that the microtubule-associated protein Tau, which is intrinsically disordered in solution, locally folds into a stable structure upon binding to microtubules. While Tau is highly flexible in solution and adopts a β-sheet structure in amyloid fibrils, in complex with microtubules the conserved hexapeptides at the beginning of the Tau repeats two and three convert into a hairpin conformation. Thus, binding to microtubules stabilizes a unique conformation in Tau.}, keywords = {Amyloid: chemistry / Humans / Magnetic Resonance Spectroscopy / Microtubules: chemistry / Protein Conformation / Protein Folding / tau Proteins: chemistry / Amyloid (NLM Chemicals) / tau Proteins (NLM Chemicals)}, cin = {AG Zweckstetter / AG Mandelkow 1 ; AG Mandelkow 1}, ddc = {540}, cid = {I:(DE-2719)1410001 / I:(DE-2719)1013014}, pnm = {342 - Disease Mechanisms and Model Systems (POF3-342)}, pid = {G:(DE-HGF)POF3-342}, typ = {PUB:(DE-HGF)16}, pubmed = {pmid:26094605}, doi = {10.1002/anie.201501714}, url = {https://pub.dzne.de/record/138080}, }