Search Results - "Kaminski Schierle, Gabriele S."

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  1. 1

    Fluorescent Nanoparticles for Super-Resolution Imaging by Li, Wei, Kaminski Schierle, Gabriele S., Lei, Bingfu, Liu, Yingliang, Kaminski, Clemens F.

    Published in Chemical reviews (10-08-2022)
    “…Super-resolution imaging techniques that overcome the diffraction limit of light have gained wide popularity for visualizing cellular structures with…”
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    The Cellular Environment Affects Monomeric α-Synuclein Structure by Stephens, Amberley D., Zacharopoulou, Maria, Kaminski Schierle, Gabriele S.

    “…The presynaptic protein α-synuclein (aSyn) is an ‘intrinsically disordered protein’ that is highly dynamic in conformation. Transient intramolecular…”
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    Structural basis of synaptic vesicle assembly promoted by α-synuclein by Fusco, Giuliana, Pape, Tillmann, Stephens, Amberley D., Mahou, Pierre, Costa, Ana Rita, Kaminski, Clemens F., Kaminski Schierle, Gabriele S., Vendruscolo, Michele, Veglia, Gianluigi, Dobson, Christopher M., De Simone, Alfonso

    Published in Nature communications (19-09-2016)
    “…α-synuclein (αS) is an intrinsically disordered protein whose fibrillar aggregates are the major constituents of Lewy bodies in Parkinson’s disease. Although…”
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    Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity by Stephens, Amberley D., Zacharopoulou, Maria, Moons, Rani, Fusco, Giuliana, Seetaloo, Neeleema, Chiki, Anass, Woodhams, Philippa J., Mela, Ioanna, Lashuel, Hilal A., Phillips, Jonathan J., De Simone, Alfonso, Sobott, Frank, Schierle, Gabriele S. Kaminski

    Published in Nature communications (04-06-2020)
    “…As an intrinsically disordered protein, monomeric alpha-synuclein (aSyn) occupies a large conformational space. Certain conformations lead to aggregation prone…”
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    The role of water in amyloid aggregation kinetics by Stephens, Amberley D, Kaminski Schierle, Gabriele S

    Published in Current opinion in structural biology (01-10-2019)
    “…[Display omitted] •Water and protein mobility are inextricably linked and therefore water itself plays an essential role in protein function.•IDPs have a…”
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  8. 8

    Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry Approach to Correlate Local Structure and Aggregation in α‑Synuclein by Seetaloo, Neeleema, Zacharopoulou, Maria, Stephens, Amberley D., Kaminski Schierle, Gabriele S., Phillips, Jonathan J.

    Published in Analytical chemistry (Washington) (06-12-2022)
    “…In Parkinson’s disease and other synucleinopathies, α-synuclein misfolds and aggregates. Its intrinsically disordered nature, however, causes it to adopt…”
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    Direct Observation of Heterogeneous Amyloid Fibril Growth Kinetics via Two-Color Super-Resolution Microscopy by Pinotsi, Dorothea, Buell, Alexander K, Galvagnion, Celine, Dobson, Christopher M, Kaminski Schierle, Gabriele S, Kaminski, Clemens F

    Published in Nano letters (08-01-2014)
    “…The self-assembly of normally soluble proteins into fibrillar amyloid structures is associated with a range of neurodegenerative disorders, such as Parkinson’s…”
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    Fluorescence Self-Quenching from Reporter Dyes Informs on the Structural Properties of Amyloid Clusters Formed in Vitro and in Cells by Chen, WeiYue, Young, Laurence J, Lu, Meng, Zaccone, Alessio, Ströhl, Florian, Yu, Na, Kaminski Schierle, Gabriele S, Kaminski, Clemens F

    Published in Nano letters (11-01-2017)
    “…The characterization of the aggregation kinetics of protein amyloids and the structural properties of the ensuing aggregates are vital in the study of the…”
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    A Label-Free, Quantitative Assay of Amyloid Fibril Growth Based on Intrinsic Fluorescence by Pinotsi, Dorothea, Buell, Alexander K., Dobson, Christopher M., Kaminski Schierle, Gabriele S., Kaminski, Clemens F.

    “…Kinetic assay of seeded growth: The graph shows the variation in intrinsic fluorescence intensity of amyloid fibrils. Fluorescence increases during the seeded…”
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    Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox by Avezov, Edward, Cross, Benedict C S, Kaminski Schierle, Gabriele S, Winters, Mikael, Harding, Heather P, Melo, Eduardo Pinho, Kaminski, Clemens F, Ron, David

    Published in The Journal of cell biology (15-04-2013)
    “…Interfering with disulfide bond formation impedes protein folding and promotes endoplasmic reticulum (ER) stress. Due to limitations in measurement techniques,…”
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    Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons by Pinotsi, Dorothea, Michel, Claire H., Buell, Alexander K., Laine, Romain F., Mahou, Pierre, Dobson, Christopher M., Kaminski, Clemens F., Schierle, Gabriele S. Kaminski

    “…New strategies for visualizing self-assembly processes at the nanoscale give deep insights into the molecular origins of disease. An example is the…”
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    A safety mechanism enables tissue-specific resistance to protein aggregation during aging in C. elegans by Jung, Raimund, Lechler, Marie C, Fernandez-Villegas, Ana, Chung, Chyi Wei, Jones, Harry C, Choi, Yoon Hee, Thompson, Maximilian A, Rödelsperger, Christian, Röseler, Waltraud, Kaminski Schierle, Gabriele S, Sommer, Ralf J, David, Della C

    Published in PLoS biology (14-09-2023)
    “…During aging, proteostasis capacity declines and distinct proteins become unstable and can accumulate as protein aggregates inside and outside of cells. Both…”
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    CYK4 promotes antiparallel microtubule bundling by optimizing MKLP1 neck conformation by Davies, Tim, Kodera, Noriyuki, Kaminski Schierle, Gabriele S, Rees, Eric, Erdelyi, Miklos, Kaminski, Clemens F, Ando, Toshio, Mishima, Masanori

    Published in PLoS biology (01-04-2015)
    “…Centralspindlin, a constitutive 2:2 heterotetramer of MKLP1 (a kinesin-6) and the non-motor subunit CYK4, plays important roles in cytokinesis. It is crucial…”
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