Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Mireille M. A. E. Claessens"'
Autor:
Swarupa Chatterjee, Bram A. Schotpoort, Thieme Elbert, Jeroen J. L. M. Cornelissen, Mireille M. A. E. Claessens, Christian Blum
Publikováno v:
Molecules, Vol 26, Iss 19, p 5750 (2021)
Supramolecular protein complexes are the corner stone of biological processes; they are essential for many biological functions. Unraveling the interactions responsible for the (dis)assembly of these complexes is required to understand nature and to
Externí odkaz:
https://doaj.org/article/97ebdab57bad491e95b4253bae4422d8
Non-uniform self-assembly: On the anisotropic architecture of α-synuclein supra-fibrillar aggregates
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Abstract Although the function of biopolymer hydrogels in nature depends on structural anisotropy at mesoscopic length scales, the self-assembly of such anisotropic structures in vitro is challenging. Here we show that fibrils of the protein α-synuc
Externí odkaz:
https://doaj.org/article/1596bfc132534431bae186e64f01ebf2
Autor:
Gobert Heesink, Cécile Caron, Kirsten van Leijenhorst-Groener, Robert Molenaar, Theodorus W. J. Gadella, Mireille M. A. E. Claessens, Christian Blum
Publikováno v:
The journal of Physical Chemistry. B, 126(40), 7906-7915. American Chemical Society
Journal of physical chemistry B, 126(40), 7906-7915. American Chemical Society
Journal of physical chemistry B, 126(40), 7906-7915. American Chemical Society
Genetically encoded visible fluorescent proteins (VFPs) are a key tool used to visualize cellular processes. However, compared to synthetic fluorophores, VFPs are photophysically complex. This photophysical complexity includes the presence of non-emi
Autor:
Swarupa Chatterjee, Robert Molenaar, Wiebe M. de Vos, Hendrik D. W. Roesink, R. Martijn Wagterveld, Jeroen J. L. M. Cornelissen, Mireille M. A. E. Claessens, Christian Blum
Publikováno v:
ACS Applied Polymer Materials, 4(7), 5173-5179. American Chemical Society
Monitoring the performance of polymer-functionalized surfaces that aim at removing and inactivating viruses is typically labor-intensive and time-consuming. This hampers the development and optimization of such surfaces. Here we present experiments o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc8e87f451f86fa264d9ff18afa231d5
https://research.utwente.nl/en/publications/238a372f-9ed3-4431-8d73-e3a8dd75bf34
https://research.utwente.nl/en/publications/238a372f-9ed3-4431-8d73-e3a8dd75bf34
Publikováno v:
PLoS ONE, Vol 5, Iss 12, p e14292 (2010)
The question of how the aggregation of the neuronal protein α-synuclein contributes to neuronal toxicity in Parkinson's disease has been the subject of intensive research over the past decade. Recently, attention has shifted from the amyloid fibrils
Externí odkaz:
https://doaj.org/article/4a64d1945ed24396bbba0486107d6df3
Publikováno v:
The Giant Vesicle Book
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d999ef1cec90b8711b5a30f162d6046c
https://doi.org/10.1201/9781315152516-20
https://doi.org/10.1201/9781315152516-20
Autor:
Himanshu, Chaudhary, Ricardo M F, Fernandes, Vasantha, Gowda, Mireille M A E, Claessens, István, Furó, Christofer, Lendel
Publikováno v:
Journal of colloid and interface science. 556
The rich pool of protein conformations combined with the dimensions and properties of carbon nanotubes create new possibilities in functional materials and nanomedicine. Here, the intrinsically disordered protein α-synuclein is explored as a dispers
Autor:
Kai Uhrig, Florent Dalmas, Alexander Roth, Andreas R. Bausch, Wouter H. Roos, Camilla Mohrdieck, Erich Sackmann, Jennifer E. Curtis, Simon Schulz, Mireille M. A. E. Claessens, Christian Schmitz, Eduard Arzt, Joachim P. Spatz, Rainer Tharmann
Publikováno v:
Mohrdieck, C, Dalmas, F, Arzt, E, Tharmann, R, Claessens, M M A E, Bausch, A R, Schmitz, C, Curtis, J, Roos, W H, Schultz, S, Uhrig, K, Roth, A, Sackmann, E & Spatz, J P 2007, ' Biomimetic Models of the Actin Cytoskeleton ', Small, vol. 3, no. 6, pp. 1015-1022 . https://doi.org/10.1002/smll.200600565
Small
Small, 3(6), 1015-1022. Wiley-VCH Verlag
Small
Small, 3(6), 1015-1022. Wiley-VCH Verlag
The cytoskeleton is a complex polymer network that plays an essential role in the functionality of eukaryotic cells. It endows cells with mechanical stability, adaptability, and motility. To identify and understand the mechanisms underlying this larg
Publikováno v:
Journal of Biomechanics. 39:S240
Autor:
Enrico Zurlo, Pravin Kumar, Georg Meisl, Alexander J Dear, Dipro Mondal, Mireille M A E Claessens, Tuomas P J Knowles, Martina Huber
Publikováno v:
PLoS ONE, Vol 16, Iss 1, p e0245548 (2021)
Knowledge of the mechanisms of assembly of amyloid proteins into aggregates is of central importance in building an understanding of neurodegenerative disease. Given that oligomeric intermediates formed during the aggregation reaction are believed to
Externí odkaz:
https://doaj.org/article/e806670bc9994730b928f0b2e45f01bc