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  1. Article ; Online: Ultrasound and antibodies - a potentially powerful combination for Alzheimer disease therapy.

    Götz, Jürgen / Padmanabhan, Pranesh

    Nature reviews. Neurology

    2024  

    Language English
    Publishing date 2024-02-20
    Publishing country England
    Document type Journal Article
    ZDB-ID 2491514-2
    ISSN 1759-4766 ; 1759-4758
    ISSN (online) 1759-4766
    ISSN 1759-4758
    DOI 10.1038/s41582-024-00943-1
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    Zs.A 6257: Show issues Location:
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  2. Book ; Thesis: Ganganalytische Untersuchung an unilateral hüfttotalendoprothisch versorgten Patienten im Vergleich mit einem gleichaltrigen gesunden Probandenkollektiv

    Götz, Jürgen

    2008  

    Author's details vorgelegt von Jürgen Götz
    Language German
    Size VI, 192 S., Ill., graph. Darst., 21 cm
    Publishing country Germany
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Regensburg, Univ., Diss., 2009
    HBZ-ID HT016103238
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    2009 D 1036 order for loan Magazin

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  3. Article ; Online: Clinical relevance of animal models in aging-related dementia research.

    Padmanabhan, Pranesh / Götz, Jürgen

    Nature aging

    2023  Volume 3, Issue 5, Page(s) 481–493

    Abstract: Alzheimer's disease (AD) and other, less prevalent dementias are complex age-related disorders that exhibit multiple etiologies. Over the past decades, animal models have provided pathomechanistic insight and evaluated countless therapeutics; however, ... ...

    Abstract Alzheimer's disease (AD) and other, less prevalent dementias are complex age-related disorders that exhibit multiple etiologies. Over the past decades, animal models have provided pathomechanistic insight and evaluated countless therapeutics; however, their value is increasingly being questioned due to the long history of drug failures. In this Perspective, we dispute this criticism. First, the utility of the models is limited by their design, as neither the etiology of AD nor whether interventions should occur at a cellular or network level is fully understood. Second, we highlight unmet challenges shared between animals and humans, including impeded drug transport across the blood-brain barrier, limiting effective treatment development. Third, alternative human-derived models also suffer from the limitations mentioned above and can only act as complementary resources. Finally, age being the strongest AD risk factor should be better incorporated into the experimental design, with computational modeling expected to enhance the value of animal models.
    MeSH term(s) Animals ; Humans ; Clinical Relevance ; Alzheimer Disease/genetics ; Treatment Outcome ; Aging ; Models, Animal
    Language English
    Publishing date 2023-05-18
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ISSN 2662-8465
    ISSN (online) 2662-8465
    DOI 10.1038/s43587-023-00402-4
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  4. Article ; Online: Special issue on "Cytoskeletal proteins in health and neurodegenerative disease: Concepts and methods".

    Brandt, Roland / Götz, Jürgen

    Brain research bulletin

    2023  Volume 198, Page(s) 50–52

    Abstract: Since 2016, when we compiled a very well-received special issue on "Cytoskeletal Proteins in Health and Neurodegenerative Disease" for Brain Research Bulletin, the field has rapidly evolved, to a large part thanks to the development and maturation of new ...

    Abstract Since 2016, when we compiled a very well-received special issue on "Cytoskeletal Proteins in Health and Neurodegenerative Disease" for Brain Research Bulletin, the field has rapidly evolved, to a large part thanks to the development and maturation of new methods including super-resolution microscopy. Being asked to create a sequel, we therefore decided to keep the main topic, but focus on emerging concepts and novel methods. As before, we compiled nine articles on the role of the neuronal cytoskeleton in both physiological and pathological conditions. Seven of the contributions present current concepts and discuss how cytoskeletal components develop and are maintained throughout a neuron's long lifespan, and also, how they may contribute to physiology and neurodegenerative diseases. Two contributions focus on novel methodological developments and how these techniques can be used to analyze the structure and function of the neuronal cytoskeleton in new ways. The compilation of the articles makes it clear that future approaches must consider the functional relationships between the individual filament systems and the influence different signal transduction mechanisms have on the cytoskeleton and vice versa, in order to adequately explore the causes and consequences of the role of cytoskeletal proteins in health and disease. We hope that this compilation will help in the design of appropriate experiments, aided by new methods, to test critical hypotheses in the field.
    MeSH term(s) Humans ; Cytoskeletal Proteins ; Neurodegenerative Diseases/metabolism ; Cytoskeleton/metabolism ; Brain/metabolism ; Signal Transduction
    Chemical Substances Cytoskeletal Proteins
    Language English
    Publishing date 2023-04-20
    Publishing country United States
    Document type Editorial
    ZDB-ID 197620-5
    ISSN 1873-2747 ; 0361-9230
    ISSN (online) 1873-2747
    ISSN 0361-9230
    DOI 10.1016/j.brainresbull.2023.04.007
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  5. Book ; Online ; Thesis: Zusammenhang von depressiven Symptomen und riskantem Gesundheitsverhalten bei Patienten der medizinischen Basisversorgung

    Goetz, Svea-Lies [Verfasser] / Rumpf, Hans-Jürgen [Akademischer Betreuer] / Götz, Katja [Akademischer Betreuer]

    Ausmaß und Bedeutung spezifischer depressiver Symptome

    2024  

    Author's details Svea-Lies Goetz ; Akademische Betreuer: Hans-Jürgen Rumpf, Katja Götz
    Keywords Medizin, Gesundheit ; Medicine, Health
    Subject code sg610
    Language German
    Publisher Zentrale Hochschulbibliothek Lübeck
    Publishing place Lübeck
    Document type Book ; Online ; Thesis
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  6. Article: Experimental Models of Tauopathy - From Mechanisms to Therapies.

    Götz, Julika J / Götz, Jürgen

    Advances in experimental medicine and biology

    2020  Volume 1184, Page(s) 381–391

    Abstract: Animal models have been instrumental in reproducing key aspects of human tauopathy. In pursuing these efforts, the mouse continues to have a prominent role. In this chapter, we focus on models that overexpress wild-type or mutant forms of tau, the latter ...

    Abstract Animal models have been instrumental in reproducing key aspects of human tauopathy. In pursuing these efforts, the mouse continues to have a prominent role. In this chapter, we focus on models that overexpress wild-type or mutant forms of tau, the latter being based on mutations found in familial cases of frontotemporal dementia. We review some of these models in more detail and discuss what they have revealed about the underlying pathomechanisms, as well as highlighting new developments that exploit gene editing tools such as TALEN and CRISPR. Interestingly, when investigating the role of tau in impairing cellular functions, common themes emerge. Because tau is a scaffolding protein that aggregates in the somatodendritic domain under pathological conditions, it traps proteins such as parkin and JIP1, preventing them from executing their normal function in mitophagy and axonal transport, respectively. Another aspect is the emerging role of tau in the translational machinery and the finding that the somatodendritic accumulation of tau in Alzheimer's disease may in part be due to the induction of the de novo synthesis of tau by amyloid-β via the Fyn/ERK/S6 pathway. We further discuss treatment strategies such as tau-based vaccinations and therapeutic ultrasound and conclude by discussing whether there is a future for animal models of tauopathies.
    MeSH term(s) Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Animals ; Disease Models, Animal ; Humans ; Tauopathies/genetics ; Tauopathies/metabolism ; Tauopathies/pathology ; Tauopathies/therapy ; Ultrasonography, Interventional ; Vaccines/therapeutic use ; tau Proteins/genetics ; tau Proteins/metabolism
    Chemical Substances Vaccines ; tau Proteins
    Language English
    Publishing date 2020-02-20
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 2214-8019 ; 0065-2598
    ISSN (online) 2214-8019
    ISSN 0065-2598
    DOI 10.1007/978-981-32-9358-8_28
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  7. Article ; Online: Single-molecule imaging of Tau reveals how phosphorylation affects its movement and confinement in living cells.

    Padmanabhan, Pranesh / Kneynsberg, Andrew / Cruz, Esteban / Briner, Adam / Götz, Jürgen

    Molecular brain

    2024  Volume 17, Issue 1, Page(s) 7

    Abstract: Tau is a microtubule-associated protein that is regulated by post-translational modifications. The most studied of these modifications is phosphorylation, which affects Tau's aggregation and loss- and gain-of-functions, including the interaction with ... ...

    Abstract Tau is a microtubule-associated protein that is regulated by post-translational modifications. The most studied of these modifications is phosphorylation, which affects Tau's aggregation and loss- and gain-of-functions, including the interaction with microtubules, in Alzheimer's disease and primary tauopathies. However, little is known about how Tau's phosphorylation state affects its dynamics and organisation at the single-molecule level. Here, using quantitative single-molecule localisation microscopy, we examined how mimicking or abrogating phosphorylation at 14 disease-associated serine and threonine residues through mutagenesis influences the behaviour of Tau in live Neuro-2a cells. We observed that both pseudohyperphosphorylated Tau (Tau
    MeSH term(s) Humans ; Phosphorylation ; tau Proteins/metabolism ; Single Molecule Imaging ; Alzheimer Disease/pathology ; Microtubules/metabolism
    Chemical Substances tau Proteins
    Language English
    Publishing date 2024-02-12
    Publishing country England
    Document type Journal Article
    ZDB-ID 2436057-0
    ISSN 1756-6606 ; 1756-6606
    ISSN (online) 1756-6606
    ISSN 1756-6606
    DOI 10.1186/s13041-024-01078-6
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  8. Article ; Online: Ultrasound as a versatile tool for short- and long-term improvement and monitoring of brain function.

    Blackmore, Daniel G / Razansky, Daniel / Götz, Jürgen

    Neuron

    2023  Volume 111, Issue 8, Page(s) 1174–1190

    Abstract: Treating the brain with focused ultrasound (FUS) at low intensities elicits diverse responses in neurons, astroglia, and the extracellular matrix. In combination with intravenously injected microbubbles, FUS also opens the blood-brain barrier (BBB) and ... ...

    Abstract Treating the brain with focused ultrasound (FUS) at low intensities elicits diverse responses in neurons, astroglia, and the extracellular matrix. In combination with intravenously injected microbubbles, FUS also opens the blood-brain barrier (BBB) and facilitates focal drug delivery. However, an incompletely understood cellular specificity and a wide parameter space currently limit the optimal application of FUS in preclinical and human studies. In this perspective, we discuss how different FUS modalities can be utilized to achieve short- and long-term improvements, thereby potentially treating brain disorders. We review the ongoing efforts to determine which parameters induce neuronal inhibition versus activation and how mechanoreceptors and signaling cascades are activated to induce long-term changes, including memory improvements. We suggest that optimal FUS treatments may require different FUS modalities and devices, depending on the targeted brain area or local pathology, and will be greatly enhanced by new techniques for monitoring FUS efficacy.
    MeSH term(s) Rats ; Animals ; Humans ; Rats, Sprague-Dawley ; Blood-Brain Barrier/diagnostic imaging ; Brain/diagnostic imaging ; Ultrasonography ; Biological Transport ; Drug Delivery Systems/methods
    Language English
    Publishing date 2023-03-13
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 808167-0
    ISSN 1097-4199 ; 0896-6273
    ISSN (online) 1097-4199
    ISSN 0896-6273
    DOI 10.1016/j.neuron.2023.02.018
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    Zs.A 2496: Show issues Location:
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    Zs.MG 92: Show issues

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  9. Article ; Online: Three methods for examining the de novo proteome of microglia using BONCAT bioorthogonal labeling and FUNCAT click chemistry.

    Carlisle, Alison Keolani / Götz, Jürgen / Bodea, Liviu-Gabriel

    STAR protocols

    2023  Volume 4, Issue 3, Page(s) 102418

    Abstract: Bioorthogonal labeling and click chemistry techniques allow the detailed examination of cellular physiology through tagging and visualizing newly synthesized proteins. Here, we describe three methods applying bioorthogonal non-canonical amino acid ... ...

    Abstract Bioorthogonal labeling and click chemistry techniques allow the detailed examination of cellular physiology through tagging and visualizing newly synthesized proteins. Here, we describe three methods applying bioorthogonal non-canonical amino acid tagging and fluorescent non-canonical amino acid tagging to quantify protein synthesis in microglia. We describe steps for cell seeding and labeling. We then detail microscopy, flow cytometry, and Western blotting techniques. These methods can be easily adapted for other cell types to explore cellular physiology in health and disease. For complete details on the use and execution of this protocol, please refer to Evans et al. (2021).
    MeSH term(s) Proteome/chemistry ; Click Chemistry/methods ; Microglia/metabolism ; Amino Acids/metabolism ; Protein Biosynthesis
    Chemical Substances Proteome ; Amino Acids
    Language English
    Publishing date 2023-07-10
    Publishing country United States
    Document type Journal Article
    ISSN 2666-1667
    ISSN (online) 2666-1667
    DOI 10.1016/j.xpro.2023.102418
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  10. Article ; Online: Break and accelerator-The mechanics of Tau (and amyloid) toxicity.

    Cruz, Esteban / Nisbet, Rebecca M / Götz, Jürgen

    Cytoskeleton (Hoboken, N.J.)

    2023  Volume 81, Issue 1, Page(s) 24–29

    Abstract: Aggregates of the microtubule-associated protein Tau define more than a dozen primary tauopathies, and together with amyloid-β, the secondary tauopathy Alzheimer's disease (AD). Historically, Tau has been viewed as executor of amyloid-β toxicity, with ... ...

    Abstract Aggregates of the microtubule-associated protein Tau define more than a dozen primary tauopathies, and together with amyloid-β, the secondary tauopathy Alzheimer's disease (AD). Historically, Tau has been viewed as executor of amyloid-β toxicity, with the two molecules working together as "trigger and bullet." Given the two protein's opposing roles in protein translation, we wish to introduce another metaphor, borrowing from the mechanics of a car, with amyloid-β boosting Tau translation, whereas Tau puts a break on global translation. The underlying studies entail an alternative hypothesis regarding Tau's subcellular accumulation in AD, namely its de novo synthesis in the somatodendritic domain rather than the relocalization from the axon upon dissociation from microtubules. We contest that it may be worth (given Tau's 50th birthday) to revisit some entrenched dogmas about Tau's pathophysiology.
    MeSH term(s) Humans ; tau Proteins ; Alzheimer Disease/metabolism ; Axons ; Microtubules/metabolism ; Protein Binding ; Phosphorylation
    Chemical Substances tau Proteins
    Language English
    Publishing date 2023-08-26
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2534372-5
    ISSN 1949-3592 ; 1949-3584
    ISSN (online) 1949-3592
    ISSN 1949-3584
    DOI 10.1002/cm.21781
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