Prof. Dr. Marina Mikhaylova
Profil
Forschungsthemen4
EXC 2049/1: Neurocure Applying RDoC’s Social Processes Domain to Autism and Social Anxiety Disorder: The Role of Neurobiology, Social Stress/Support, Oxytocin, and Immunological Markers
Quelle ↗Förderer: DFG Exzellenzstrategie Cluster Zeitraum: 06/2020 - 12/2025 Projektleitung: Prof. Dr. Marina Mikhaylova
FOR 5228/2: Die Rolle von Myosin VI bei der Regulierung der Positionierung und Sekretion degradativer Organellen in Axonen (TP 04)
Quelle ↗Förderer: DFG Forschungsgruppe Zeitraum: 06/2026 - 05/2030 Projektleitung: Prof. Dr. Marina Mikhaylova
SFB 1315/2: Die Rolle von mTORC1 und der Proteintranslation bei der Gedächtniskonsolidierung im Neokortex (TP A10)
Quelle ↗Förderer: DFG Sonderforschungsbereich Zeitraum: 07/2022 - 06/2026 Projektleitung: Prof. Dr. Matthew Larkum, Prof. Dr. Marina Mikhaylova
SFB 1315/2: Ein komparativer Forschungsansatz zur Konsolidierung des Verwandtschaftsgedächtnisses (TP A03)
Quelle ↗Förderer: DFG Sonderforschungsbereich Zeitraum: 07/2022 - 06/2026 Projektleitung: Prof. Dr. Michael Brecht, Prof. Dr. Marina Mikhaylova
Mögliche Industrie-Partner10
Stand: 26.4.2026, 19:48:44 (Top-K=20, Min-Cosine=0.4)
- 88 Treffer57.6%
- SFB 1315/2: Mechanismen und Störungen der Gedächtniskonsolidierung: Von Synapsen zur SystemebeneP57.6%
- DFG-Sachbeihilfe: Aufmerksamkeit und sensorische Integration im aktiven Sehen von bewegten ObjektenT49.1%
- SFB 1315/2: Mechanismen und Störungen der Gedächtniskonsolidierung: Von Synapsen zur Systemebene
- 5 Treffer55.1%
- Zuwendung im Rahmen des Programms „exist – Existenzgründungen aus der Wissenschaft“ aus dem Bundeshaushalt, Einzelplan 09, Kapitel 02, Titel 68607, Haushaltsjahr 2026, sowie aus Mitteln des Europäischen Strukturfonds (hier Euro-päischer Sozialfonds Plus – ESF Plus) Förderperiode 2021-2027 – Kofinanzierung für das Vorhaben: „exist Women“T55.1%
- Zuwendung im Rahmen des Programms „exist – Existenzgründungen aus der Wissenschaft“ aus dem Bundeshaushalt, Einzelplan 09, Kapitel 02, Titel 68607, Haushaltsjahr 2026, sowie aus Mitteln des Europäischen Strukturfonds (hier Euro-päischer Sozialfonds Plus – ESF Plus) Förderperiode 2021-2027 – Kofinanzierung für das Vorhaben: „exist Women“
- DYnamic control in hybrid plasmonic NAnopores: road to next generation multiplexed single MOlecule detectionP55.1%
- DYnamic control in hybrid plasmonic NAnopores: road to next generation multiplexed single MOlecule detection
NVIDIA GmbH
PT30 Treffer54.7%- EU: Simulation in Multiscale Physical and Biological Systems (STIMULATE)P54.7%
- EU: Simulation in Multiscale Physical and Biological Systems (STIMULATE)
- 49 Treffer54.7%
- EU: Simulation in Multiscale Physical and Biological Systems (STIMULATE)P54.7%
- EU: Bottom-Up Generation of atomicalLy Precise syntheTIc 2D MATerials for High Performance in Energy and Electronic Applications – A Multi-Site Innovative Training Action (ULTIMATE)P48.4%
- EU: Simulation in Multiscale Physical and Biological Systems (STIMULATE)
- 31 Treffer54.7%
- EU: Simulation in Multiscale Physical and Biological Systems (STIMULATE)P54.7%
- EU: Simulation in Multiscale Physical and Biological Systems (STIMULATE)
- 51 Treffer54.4%
- Engineering of New-Generation Protein Secretion SystemsP54.4%
- Engineering of New-Generation Protein Secretion Systems
- 53 Treffer54.4%
- Engineering of New-Generation Protein Secretion SystemsP54.4%
- Engineering of New-Generation Protein Secretion Systems
- 50 Treffer54.4%
- Engineering of New-Generation Protein Secretion SystemsP54.4%
- Engineering of New-Generation Protein Secretion Systems
- 32 Treffer54.0%
- Lösung gekoppelter Probleme in der Nanoelektronik (nanoCOPS)P54.0%
- Lösung gekoppelter Probleme in der Nanoelektronik (nanoCOPS)
Publikationen25
Top 25 nach Zitationen — Quelle: OpenAlex (BAAI/bge-m3 embedded für Matching).
Neuron · 449 Zitationen · DOI
Neurobiology of Aging · 240 Zitationen · DOI
Microtubule Minus-End Binding Protein CAMSAP2 Controls Axon Specification and Dendrite Development
2014Neuron · 225 Zitationen · DOI
Nature Communications · 216 Zitationen · DOI
Microtubules are hollow biopolymers of 25-nm diameter and are key constituents of the cytoskeleton. In neurons, microtubules are organized differently between axons and dendrites, but their precise organization in different compartments is not completely understood. Super-resolution microscopy techniques can detect specific structures at an increased resolution, but the narrow spacing between neuronal microtubules poses challenges because most existing labelling strategies increase the effective microtubule diameter by 20-40 nm and will thereby blend neighbouring microtubules into one structure. Here we develop single-chain antibody fragments (nanobodies) against tubulin to achieve super-resolution imaging of microtubules with a decreased apparent diameter. To test the resolving power of these novel probes, we generate microtubule bundles with a known spacing of 50-70 nm and successfully resolve individual microtubules. Individual bundled microtubules can also be resolved in different mammalian cells, including hippocampal neurons, allowing novel insights into fundamental mechanisms of microtubule organization in cell- and neurobiology.
Cell · 193 Zitationen · DOI
PLoS Biology · 184 Zitationen · DOI
NMDA (N-methyl-D-aspartate) receptors and calcium can exert multiple and very divergent effects within neuronal cells, thereby impacting opposing occurrences such as synaptic plasticity and neuronal degeneration. The neuronal Ca2+ sensor Caldendrin is a postsynaptic density component with high similarity to calmodulin. Jacob, a recently identified Caldendrin binding partner, is a novel protein abundantly expressed in limbic brain and cerebral cortex. Strictly depending upon activation of NMDA-type glutamate receptors, Jacob is recruited to neuronal nuclei, resulting in a rapid stripping of synaptic contacts and in a drastically altered morphology of the dendritic tree. Jacob's nuclear trafficking from distal dendrites crucially requires the classical Importin pathway. Caldendrin binds to Jacob's nuclear localization signal in a Ca2+-dependent manner, thereby controlling Jacob's extranuclear localization by competing with the binding of Importin-alpha to Jacob's nuclear localization signal. This competition requires sustained synapto-dendritic Ca2+ levels, which presumably cannot be achieved by activation of extrasynaptic NMDA receptors, but are confined to Ca2+ microdomains such as postsynaptic spines. Extrasynaptic NMDA receptors, as opposed to their synaptic counterparts, trigger the cAMP response element-binding protein (CREB) shut-off pathway, and cell death. We found that nuclear knockdown of Jacob prevents CREB shut-off after extrasynaptic NMDA receptor activation, whereas its nuclear overexpression induces CREB shut-off without NMDA receptor stimulation. Importantly, nuclear knockdown of Jacob attenuates NMDA-induced loss of synaptic contacts, and neuronal degeneration. This defines a novel mechanism of synapse-to-nucleus communication via a synaptic Ca2+-sensor protein, which links the activity of NMDA receptors to nuclear signalling events involved in modelling synapto-dendritic input and NMDA receptor-induced cellular degeneration.
Journal of Neuroscience · 163 Zitationen · DOI
Expression of synaptic plasticity involves the translation of mRNA into protein and, probably, active protein degradation via the proteasome pathway. Here, we report on the rapid activation of synthesis and degradation of a probe protein with the induction of long-term potentiation (LTP) in the hippocampal Schaffer collateral CA1 pathway. The proteasome inhibitor MG132 significantly reduced the field EPSP slope potentiation and LTP maintenance without acutely affecting basal synaptic transmission. To visualize protein dynamics, CA1 pyramidal cells of hippocampal slices were transfected with Semliki Forest virus particles expressing a recombinant RNA. This RNA contained the coding sequence for a degradable green fluorescence protein with a nuclear localization signal (NLS-d1EGFP) followed by a 3'- untranslated region dendritic targeting sequence. NLS-d1EGFP fluorescence remained stable in the low-frequency test stimulation but increased with LTP induction in the cell body and in most dendritic compartments of CA1 neurons. Applying anisomycin, a protein synthesis inhibitor, caused NLS-d1EGFP levels to decline; a proteasome inhibitor MG132 reversed this effect. In the presence of anisomycin, LTP induction accelerated the degradation of NLS-d1EGFP. When both inhibitors were present, NLS-d1EGFP levels remained unaffected by LTP induction. Moreover, LTP-induced acceleration of NLS-d1EGFP synthesis was blocked by rapamycin, which is consistent with the involvement of dendritic mammalian target of rapamycin in LTP-triggered translational activity. Our results clearly demonstrate that LTP induction not only leads to a rapid increase in the rate of protein synthesis but also accelerates protein degradation via the proteasome system.
Frontiers in Cellular Neuroscience · 161 Zitationen · DOI
Actin is a versatile and ubiquitous cytoskeletal protein that plays a major role in both the establishment and the maintenance of neuronal polarity. For a long time, the most prominent roles that were attributed to actin in neurons were the movement of growth cones, polarized cargo sorting at the axon initial segment, and the dynamic plasticity of dendritic spines, since those compartments contain large accumulations of actin filaments (F-actin) that can be readily visualized using electron- and fluorescence microscopy. With the development of super-resolution microscopy in the past few years, previously unknown structures of the actin cytoskeleton have been uncovered: a periodic lattice consisting of actin and spectrin seems to pervade not only the whole axon, but also dendrites and even the necks of dendritic spines. Apart from that striking feature, patches of F-actin and deep actin filament bundles have been described along the lengths of neurites. So far, research has been focused on the specific roles of actin in the axon, while it is becoming more and more apparent that in the dendrite, actin is not only confined to dendritic spines, but serves many additional and important functions. In this review, we focus on recent developments regarding the role of actin in dendrite morphology, the regulation of actin dynamics by internal and external factors, and the role of F-actin in dendritic protein trafficking.
Scientific Reports · 109 Zitationen · DOI
Most of the excitatory synapses on principal neurons of the forebrain are located on specialized structures called dendritic spines. Their morphology, comprising a spine head connected to the dendritic branch via a thin neck, provides biochemical and electrical compartmentalization during signal transmission. Spine shape is defined and tightly controlled by the organization of the actin cytoskeleton. Alterations in synaptic strength correlate with changes in the morphological appearance of the spine head and neck. Therefore, it is important to get a better understanding of the nanoscale organization of the actin cytoskeleton in dendritic spines. A periodic organization of the actin/spectrin lattice was recently discovered in axons and a small fraction of dendrites using super-resolution microscopy. Here we use a small probe phalloidin-Atto647N, to label F-actin in mature hippocampal primary neurons and in living hippocampal slices. STED nanoscopy reveals that in contrast to β-II spectrin antibody labelling, phalloidin-Atto647N stains periodic actin structures in all dendrites and the neck of nearly all dendritic spines, including filopodia-like spines. These findings extend the current view on F-actin organization in dendritic spines and may provide new avenues for understanding the structural changes in the spine neck during induction of synaptic plasticity, active organelle transport or tethering.
Cell Reports · 106 Zitationen · DOI
The local synthesis of transmembrane proteins underlies functional specialization of dendritic microdomains in neuronal plasticity. It is unclear whether these proteins have access to the complete machinery of the secretory pathway following local synthesis. In this study, we describe a probe called pGolt that allows visualization of Golgi-related organelles for live imaging in neurons. We show that pGolt labels a widespread microsecretory Golgi satellite (GS) system that is, in contrast to Golgi outposts, present throughout basal and apical dendrites of all pyramidal neurons. The GS system contains glycosylation machinery and is localized between ERGIC and retromer. Synaptic activity restrains lateral movement of ERGIC, GS, and retromer close to one another, allowing confined processing of secretory cargo. Several synaptic transmembrane proteins pass through and recycle back to the GS system. Thus, the presence of an ER-ERGIC-GS-retromer microsecretory system in all neuronal dendrites enables autonomous local control of transmembrane protein synthesis and processing.
Current Biology · 105 Zitationen · DOI
Autophagy · 99 Zitationen · DOI
CTSD (cathepsin D) is one of the major lysosomal proteases indispensable for the maintenance of cellular proteostasis by turning over substrates of endocytosis, phagocytosis and autophagy. Consequently, CTSD deficiency leads to a strong impairment of the lysosomal-autophagy machinery. In mice and humans CTSD dysfunction underlies the congenital variant (CLN10) of neuronal ceroid lipofuscinosis (NCL). NCLs are distinct lysosomal storage disorders (LSDs) sharing various hallmarks, namely accumulation of protein aggregates and ceroid lipofuscin leading to neurodegeneration and blindness. The most established and clinically approved approach to treat LSDs is enzyme replacement therapy (ERT) aiming to replace the defective hydrolase with an exogenously applied recombinant protein. Here we reveal that recombinant human pro-CTSD produced in a mammalian expression system can be efficiently taken up by a variety of cell models, is correctly targeted to lysosomes and processed to the active mature form of the protease. In proof-of-principle experiments we provide evidence that recombinant human CTSD (rhCTSD) can improve the biochemical phenotype of CTSD-deficient hippocampal slice cultures <i>in vitro</i> and retinal cells <i>in vivo</i>. Furthermore, we demonstrate that dosing of rhCTSD in the murine CLN10 model leads to a correction of lysosomal hypertrophy, storage accumulation and impaired autophagic flux in the viscera and central nervous system (CNS). We establish that direct delivery of the recombinant protease to the CNS is required for improvement of neuropathology and lifespan extension. Together these data support the continuation of the pre-clinical studies for the application of rhCTSD in the treatment of NCL.<b>Abbreviations:</b> AIF1/IBA1: allograft inflammatory factor 1; BBB: blood brain barrier; CNS: central nervous system; CTSB: cathepsin B; CTSD: cathepsin D; CTSL: cathepsin L; ERT: enzyme replacement therapy; GFAP: glial fibrillary acidic protein; INL: inner nuclear layer; LAMP1: lysosomal-associated membrane protein 1; LAMP2: lysosomal-associated membrane protein 2; MAP1LC3/LC3: microtubule-associated protein 1 light chain 3; LDL: low-density lipoprotein; LRP1: low density lipoprotein receptor-related protein 1; LSD: lysosomal storage disorder; MEFs: mouse embryonic fibroblasts; M6P: mannose 6-phosphate; mCTSD: mature CTSD; NCL: neuronal ceroid lipofuscinosis; ONL: outer nuclear layer; PB: phosphate buffer; proCTSD: pro-cathepsin D; LRPAP1: low density lipoprotein receptor-related protein associated protein 1; rhCTSD: human recombinant CTSD; SAPC: saposin C; SAPD: saposin D; ATP5G1: ATP synthase, H+ transporting, mitochondrial F0 complex, subunit C1 (subunit 9); SQSTM1/p62: sequestosome 1; TPP1: tripeptidyl peptidase I.
Cell Reports · 99 Zitationen · DOI
Neuronal differentiation is a multistep process that shapes and re-shapes neurons by progressing through several typical stages, including axon outgrowth, dendritogenesis, and synapse formation. To systematically profile proteome dynamics throughout neuronal differentiation, we took cultured rat hippocampal neurons at different developmental stages and monitored changes in protein abundance using a combination of stable isotope labeling and high-resolution liquid chromatography-tandem mass spectrometry (LC-MS/MS). Almost one third of all 4,500 proteins quantified underwent a more than 2-fold expression change during neuronal differentiation, indicating extensive remodeling of the neuron proteome. To highlight the strength of our resource, we studied the neural-cell-adhesion molecule 1 (NCAM1) and found that it stimulates dendritic arbor development by promoting actin filament growth at the dendritic growth cone. We anticipate that our quantitative map of neuronal proteome dynamics is a rich resource for further analyses of the many identified proteins in various neurodevelopmental processes.
Nature Communications · 84 Zitationen · DOI
The cytoplasm is a highly complex and heterogeneous medium that is structured by the cytoskeleton. How local transport depends on the heterogeneous organization and dynamics of F-actin and microtubules is poorly understood. Here we use a novel delivery and functionalization strategy to utilize quantum dots (QDs) as probes for active and passive intracellular transport. Rapid imaging of non-functionalized QDs reveals two populations with a 100-fold difference in diffusion constant, with the faster fraction increasing upon actin depolymerization. When nanobody-functionalized QDs are targeted to different kinesin motor proteins, their trajectories do not display strong actin-induced transverse displacements, as suggested previously. Only kinesin-1 displays subtle directional fluctuations, because the subset of microtubules used by this motor undergoes prominent undulations. Using actin-targeting agents reveals that F-actin suppresses most microtubule shape remodelling, rather than promoting it. These results demonstrate how the spatial heterogeneity of the cytoskeleton imposes large variations in non-equilibrium intracellular dynamics.
F‐actin patches associated with glutamatergic synapses control positioning of dendritic lysosomes
2019The EMBO Journal · 82 Zitationen · DOI
Organelle positioning within neurites is required for proper neuronal function. In dendrites, with their complex cytoskeletal organization, transport of organelles is guided by local specializations of the microtubule and actin cytoskeleton, and by coordinated activity of different motor proteins. Here, we focus on the actin cytoskeleton in the dendritic shaft and describe dense structures consisting of longitudinal and branched actin filaments. These actin patches are devoid of microtubules and are frequently located at the base of spines, or form an actin mesh around excitatory shaft synapses. Using lysosomes as an example, we demonstrate that the presence of actin patches has a strong impact on dendritic organelle transport, as lysosomes frequently stall at these locations. We provide mechanistic insights on this pausing behavior, demonstrating that actin patches form a physical barrier for kinesin-driven cargo. In addition, we identify myosin Va as an active tether which mediates long-term stalling. This correlation between the presence of actin meshes and halting of organelles could be a generalized principle by which synapses control organelle trafficking.
Proceedings of the National Academy of Sciences · 68 Zitationen · DOI
Phosphatidylinositol 4-OH kinase IIIbeta (PI-4Kbeta) is involved in the regulated local synthesis of phospholipids that are crucial for trans-Golgi network (TGN)-to-plasma membrane trafficking. In this study, we show that the calcium sensor proteins calneuron-1 and calneuron-2 physically associate with PI-4Kbeta, inhibit the enzyme profoundly at resting and low calcium levels, and negatively interfere with Golgi-to-plasma membrane trafficking. At high calcium levels this inhibition is released and PI-4Kbeta is activated via a preferential association with neuronal calcium sensor-1 (NCS-1). In accord to its supposed function as a filter for subthreshold Golgi calcium transients, neuronal overexpression of calneuron-1 enlarges the size of the TGN caused by a build-up of vesicle proteins and reduces the number of axonal Piccolo-Bassoon transport vesicles, large dense core vesicles that carry a set of essential proteins for the formation of the presynaptic active zone during development. A corresponding protein knockdown has the opposite effect. The opposing roles of calneurons and NCS-1 provide a molecular switch to decode local calcium transients at the Golgi and impose a calcium threshold for PI-4Kbeta activity and vesicle trafficking.
Caldendrin Directly Couples Postsynaptic Calcium Signals to Actin Remodeling in Dendritic Spines
2018Neuron · 59 Zitationen · DOI
Journal of Cancer Research and Clinical Oncology · 59 Zitationen · DOI
Brain Communications · 56 Zitationen · DOI
Regulation of actin cytoskeleton dynamics in dendritic spines is crucial for learning and memory formation. Hence, defects in the actin cytoskeleton pathways are a biological trait of several brain diseases, including Alzheimer's disease. Here, we describe a novel synaptic mechanism governed by the cyclase-associated protein 2, which is required for structural plasticity phenomena and completely disrupted in Alzheimer's disease. We report that the formation of cyclase-associated protein 2 dimers through its Cys<sup>32</sup> is important for cyclase-associated protein 2 binding to cofilin and for actin turnover. The Cys<sup>32</sup>-dependent cyclase-associated protein 2 homodimerization and association to cofilin are triggered by long-term potentiation and are required for long-term potentiation-induced cofilin translocation into spines, spine remodelling and the potentiation of synaptic transmission. This mechanism is specifically affected in the hippocampus, but not in the superior frontal gyrus, of both Alzheimer's disease patients and APP/PS1 mice, where cyclase-associated protein 2 is down-regulated and cyclase-associated protein 2 dimer synaptic levels are reduced. Notably, cyclase-associated protein 2 levels in the cerebrospinal fluid are significantly increased in Alzheimer's disease patients but not in subjects affected by frontotemporal dementia. In Alzheimer's disease hippocampi, cofilin association to cyclase-associated protein 2 dimer/monomer is altered and cofilin is aberrantly localized in spines. Taken together, these results provide novel insights into structural plasticity mechanisms that are defective in Alzheimer's disease.
PLoS ONE · 52 Zitationen · DOI
Taken together, these findings suggest that the two major forms of NMDA-receptor dependent synaptic plasticity, LTP and LTD, elicit the transition of different synapto-nuclear messengers albeit in both cases importin-mediated retrograde transport and NMDA-receptor activation is required.
Cytoskeleton · 51 Zitationen · DOI
The ability of neurons to communicate and store information depends on the activity of synapses which can be located on small protrusions (dendritic spines) or directly on the dendritic shaft. The formation, plasticity, and stability of synapses are regulated by the neuronal cytoskeleton. Actin filaments together with microtubules, neurofilaments, septins, and scaffolding proteins orchestrate the structural organization of both shaft and spine synapses, enabling their efficacy in response to synaptic activation. Synapses critically depend on several factors, which are also mediated by the cytoskeleton, including transport and delivery of proteins from the soma, protein synthesis, as well as surface diffusion of membrane proteins. In this minireview, we focus on recent progress made in the field of cytoskeletal elements of the postsynapse and discuss the differences and similarities between synapses located in the spines versus dendritic shaft.
Molecular Psychiatry · 51 Zitationen · DOI
Cellular and Molecular Life Sciences · 50 Zitationen · DOI
Journal of Neurochemistry · 50 Zitationen · DOI
In recent years, substantial progress has been made towards an understanding of the physiological function of EF-hand calcium sensor proteins of the Calmodulin (CaM) superfamily in neurons. This deeper appreciation is based on the identification of novel target interactions, structural studies and the discovery of novel signalling mechanisms in protein trafficking and synaptic plasticity, in which CaM-like sensor proteins appear to play a role. However, not all interactions are of plausible physiological relevance and in many cases it is not yet clear how the CaM signaling network relates to the proposed function of other EF-hand sensors. In this review, we will summarize these findings and address some of the open questions on the functional role of EF-hand calcium binding proteins in neurons.
Chemistry & Biology · 48 Zitationen · DOI
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Bestätigte Forscher↔Partner-Paare aus HU-FIS — Gold-Standard-Positive für das Matching.
FOR 5228/2: Die Rolle von Myosin VI bei der Regulierung der Positionierung und Sekretion degradativer Organellen in Axonen (TP 04)
university
FOR 5228/2: Die Rolle von Myosin VI bei der Regulierung der Positionierung und Sekretion degradativer Organellen in Axonen (TP 04)
university
FOR 5228/2: Die Rolle von Myosin VI bei der Regulierung der Positionierung und Sekretion degradativer Organellen in Axonen (TP 04)
other
FOR 5228/2: Die Rolle von Myosin VI bei der Regulierung der Positionierung und Sekretion degradativer Organellen in Axonen (TP 04)
other
FOR 5228/2: Die Rolle von Myosin VI bei der Regulierung der Positionierung und Sekretion degradativer Organellen in Axonen (TP 04)
other
FOR 5228/2: Die Rolle von Myosin VI bei der Regulierung der Positionierung und Sekretion degradativer Organellen in Axonen (TP 04)
university
FOR 5228/2: Die Rolle von Myosin VI bei der Regulierung der Positionierung und Sekretion degradativer Organellen in Axonen (TP 04)
university
Stammdaten
Identität, Organisation und Kontakt aus HU-FIS.
- Name
- Prof. Dr. Marina Mikhaylova
- Titel
- Prof. Dr.
- Fakultät
- Lebenswissenschaftliche Fakultät
- Institut
- Institut für Biologie
- Arbeitsgruppe
- Optobiologie
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- +49 30 2093-8466
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- 26.4.2026, 01:09:25