2022-11-23 08:35 |
Detailed record - Similar records
|
2022-06-15 08:20 |
Detailed record - Similar records
|
2020-08-25 15:55 |
Detailed record - Similar records
|
2020-02-18 18:08 |
[DZNE-2020-07506]
Book/Journal Article
Wegmann, S. ; Muller, D. J. ; Mandelkow, E.
Investigating fibrillar aggregates of Tau protein by atomic force microscopy.
Atomic force microscopy (AFM) has been used in numerous studies to visualize and analyze the structure and conformation of biological samples, from single molecules to biopolymers to cells. The possibility to analyze native samples without fixation, staining and in physiological buffer conditions, combined with the sub-nanometer resolution, makes AFM a versatile tool for the analysis of protein aggregation and amyloid structures. [...]
Detailed record - Similar records
|
2020-02-18 17:38 |
[DZNE-2020-05651]
Book/Journal Article (Review Article)
Schultze, J.
Chromatin Remodeling in Monocyte and Macrophage Activation.
Increasing evidence collected during the last years supports the idea that monocyte and macrophage activation is not only associated with transcriptional changes but also changes in the chromatin landscape. Moreover, the introduction of a multidimensional model of macrophage activation allows a more precise description of monocytes and macrophages under homeostatic and pathophysiological conditions. [...]
Detailed record - Similar records
|
2020-02-18 17:28 |
[DZNE-2020-05038]
Book/Journal Article
Paquet, D. ; Plucińska, G. ; Misgeld, T.
In vivo imaging of mitochondria in intact zebrafish larvae.
Visualizing neuronal mitochondria in a living, intact mammalian organism is a challenge that can be overcome in zebrafish larvae, which are highly accessible for optical imaging and genetic manipulation. Here, we detail an approach to visualize neuronal mitochondria in sensory Rohon-Beard axons, which allows quantitatively measuring mitochondrial shape, dynamics, and transport in vivo. [...]
Detailed record - Similar records
|
2020-02-18 17:07 |
[DZNE-2020-04656]
Book/Journal Article
Wefers, B. ; Brandl, C. ; Ortiz, O. ; et al
Genome Editing in Mice Using TALE Nucleases.
Gene engineering for generating targeted mouse mutants is a key technology for biomedical research. Using TALENs as sequence-specific nucleases to induce targeted double-strand breaks, the mouse genome can be directly modified in zygotes in a single step without the need for embryonic stem cells. [...]
Detailed record - Similar records
|
2020-02-18 16:58 |
[DZNE-2020-04094]
Book/Journal Article (Review Article)
Berezin, V. ; Walmod, P. S. ; Filippov, M. ; et al
Targeting of ECM molecules and their metabolizing enzymes and receptors for the treatment of CNS diseases.
Extracellular matrix (ECM) molecules, their receptors at the cell surface, and cell adhesion molecules (CAMs) involved in cell-cell or cell-ECM interactions are implicated in processes related to major diseases of the central nervous system including Alzheimer's disease (AD), epilepsy, schizophrenia, addiction, multiple sclerosis, Parkinson's disease, and cancer. There are multiple strategies for targeting the ECM molecules and their metabolizing enzymes and receptors with antibodies, peptides, glycosaminoglycans, and other natural and synthetic compounds. [...]
Detailed record - Similar records
|
2020-02-18 16:58 |
Detailed record - Similar records
|
2020-02-18 16:28 |
[DZNE-2020-02777]
Book/Journal Article (Review Article)
Resenberger, U. K. ; Winklhofer, K. F. ; Tatzelt, J.
Neuroprotective and neurotoxic signaling by the prion protein.
2011Prion Proteins / Tatzelt, Jörg (Editor) ; Berlin, Heidelberg : Springer Berlin Heidelberg, 2012, Chapter 160 ; ISSN: 0340-1022=1436-5049 ; ISBN: 978-3-642-24066-9=978-3-642-24067-6 ; doi:10.1007/978-3-642-24067-6
Topics in current chemistry 305, 101-119 (2011) [10.1007/128_2011_160]2011
Prion diseases in humans and animals are characterized by progressive neurodegeneration and the formation of infectious particles called prions. Both features are intimately linked to a conformational transition of the cellular prion protein (PrP(C)) into aberrantly folded conformers with neurotoxic and self-replicating activities. [...]
Detailed record - Similar records
|
|
|