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  1. Book ; Online ; E-Book: Praxisbuch Kontrastmittelsonografie

    Teichgräber, Ulf / Fischer, Thomas / Clevert, Dirk-André

    Kursbuch des CEUS-Kurs-Zertifikats der DRG

    2022  

    Author's details Ulf Teichgräber, Thomas Fischer, Dirk-André Clevert Hrsg
    Keywords Electronic books
    Language German
    Size 1 Online-Ressource (XIV, 273 Seiten), Illustrationen
    Publisher Springer
    Publishing place Berlin
    Publishing country Germany
    Document type Book ; Online ; E-Book
    Note Description based on publisher supplied metadata and other sources
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    HBZ-ID HT021461859
    ISBN 978-3-662-61686-4 ; 9783662616857 ; 3-662-61686-6 ; 3662616858
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Article: Optimizing EPI Image Quality Beyond Linear Phase Corrections with Dual-Polarity GRAPPA¹

    Fischer, André

    Magnetom flash

    2023  Volume 2 = Nr, Issue 84, Page(s) 26

    Language English
    Document type Article
    ZDB-ID 2465783-9
    Database Current Contents Medicine

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  3. Article: The Role of Dynamic Histone Modifications in Learning Behavior.

    Fischer, Andre

    Current topics in behavioral neurosciences

    2019  Volume 42, Page(s) 127–157

    Abstract: Epigenetic mechanisms have been linked to memory formation under physiological and pathological conditions. Therapeutic strategies that target the epigenetic machinery have been successfully used in preclinical studies investigating cognitive phenotypes ... ...

    Abstract Epigenetic mechanisms have been linked to memory formation under physiological and pathological conditions. Therapeutic strategies that target the epigenetic machinery have been successfully used in preclinical studies investigating cognitive phenotypes linked to neuropsychiatric and neurodegenerative diseases. This chapter will specifically discuss the role of histone modification in the adult brain with a focus on learning and memory processes in the healthy and diseased brain. Data on dynamic changes in histone modification during memory processes as well as the most current knowledge on the corresponding enzymatic machinery in the adult brain will be summarized and discussed in the context of potential therapeutic opportunities to treat brain diseases.
    MeSH term(s) Animals ; Brain/physiology ; DNA Methylation ; Epigenesis, Genetic ; Histone Code ; Humans ; Learning ; Memory
    Language English
    Publishing date 2019-08-26
    Publishing country Germany
    Document type Journal Article
    ISSN 1866-3370
    ISSN 1866-3370
    DOI 10.1007/7854_2019_108
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: [No title information]

    Fischer, André

    Drug research

    2017  Volume 67, Issue S 01, Page(s) S9

    Title translation Epigenetische Prozesse als Drug Targets.
    MeSH term(s) Epigenesis, Genetic/drug effects ; Humans ; Mental Disorders/drug therapy ; Mental Disorders/genetics ; Nervous System Diseases/drug therapy ; Nervous System Diseases/genetics ; Neurodegenerative Diseases/drug therapy ; Neurodegenerative Diseases/genetics ; Psychotropic Drugs/pharmacology ; Psychotropic Drugs/therapeutic use
    Chemical Substances Psychotropic Drugs
    Language German
    Publishing date 2017-10-25
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2703847-6
    ISSN 2194-9387 ; 2194-9379
    ISSN (online) 2194-9387
    ISSN 2194-9379
    DOI 10.1055/s-0043-118154
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: A Conserved Allosteric Site on Drug-Metabolizing CYPs: A Systematic Computational Assessment.

    Fischer, André / Smieško, Martin

    International journal of molecular sciences

    2021  Volume 22, Issue 24

    Abstract: Cytochrome P450 enzymes (CYPs) are the largest group of enzymes involved in human drug metabolism. Ligand tunnels connect their active site buried at the core of the membrane-anchored protein to the surrounding solvent environment. Recently, evidence of ... ...

    Abstract Cytochrome P450 enzymes (CYPs) are the largest group of enzymes involved in human drug metabolism. Ligand tunnels connect their active site buried at the core of the membrane-anchored protein to the surrounding solvent environment. Recently, evidence of a superficial allosteric site, here denoted as hotspot 1 (H1), involved in the regulation of ligand access in a soluble prokaryotic CYP emerged. Here, we applied multi-scale computational modeling techniques to study the conservation and functionality of this allosteric site in the nine most relevant mammalian CYPs responsible for approximately 70% of drug metabolism. In total, we systematically analyzed over 44 μs of trajectories from conventional MD, cosolvent MD, and metadynamics simulations. Our bioinformatic analysis and simulations with organic probe molecules revealed the site to be well conserved in the CYP2 family with the exception of CYP2E1. In the presence of a ligand bound to the H1 site, we could observe an enlargement of a ligand tunnel in several members of the CYP2 family. Further, we could detect the facilitation of ligand translocation by H1 interactions with statistical significance in CYP2C8 and CYP2D6, even though all other enzymes except for CYP2C19, CYP2E1, and CYP3A4 presented a similar trend. As the detailed comprehension of ligand access and egress phenomena remains one of the most relevant challenges in the field, this work contributes to its elucidation and ultimately helps in estimating the selectivity of metabolic transformations using computational techniques.
    MeSH term(s) Allosteric Site ; Animals ; Camphor 5-Monooxygenase/chemistry ; Camphor 5-Monooxygenase/metabolism ; Catalytic Domain ; Computational Biology/methods ; Crystallography, X-Ray ; Cytochrome P-450 CYP2C8/chemistry ; Cytochrome P-450 CYP2C8/metabolism ; Cytochrome P-450 CYP2D6/chemistry ; Cytochrome P-450 CYP2D6/metabolism ; Cytochrome P-450 Enzyme System/chemistry ; Cytochrome P-450 Enzyme System/metabolism ; Humans ; Mammals/metabolism ; Models, Molecular ; Molecular Dynamics Simulation ; Protein Conformation ; Small Molecule Libraries/chemistry ; Small Molecule Libraries/pharmacology
    Chemical Substances Small Molecule Libraries ; Cytochrome P-450 Enzyme System (9035-51-2) ; Cytochrome P-450 CYP2C8 (EC 1.14.14.1) ; Cytochrome P-450 CYP2D6 (EC 1.14.14.1) ; Camphor 5-Monooxygenase (EC 1.14.15.1)
    Language English
    Publishing date 2021-12-08
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms222413215
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: A Conserved Allosteric Site on Drug-Metabolizing CYPs

    André Fischer / Martin Smieško

    International Journal of Molecular Sciences, Vol 22, Iss 13215, p

    A Systematic Computational Assessment

    2021  Volume 13215

    Abstract: Cytochrome P450 enzymes (CYPs) are the largest group of enzymes involved in human drug metabolism. Ligand tunnels connect their active site buried at the core of the membrane-anchored protein to the surrounding solvent environment. Recently, evidence of ... ...

    Abstract Cytochrome P450 enzymes (CYPs) are the largest group of enzymes involved in human drug metabolism. Ligand tunnels connect their active site buried at the core of the membrane-anchored protein to the surrounding solvent environment. Recently, evidence of a superficial allosteric site, here denoted as hotspot 1 (H1), involved in the regulation of ligand access in a soluble prokaryotic CYP emerged. Here, we applied multi-scale computational modeling techniques to study the conservation and functionality of this allosteric site in the nine most relevant mammalian CYPs responsible for approximately 70% of drug metabolism. In total, we systematically analyzed over 44 <math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mi mathvariant="sans-serif">μ</mi></semantics></math> s of trajectories from conventional MD, cosolvent MD, and metadynamics simulations. Our bioinformatic analysis and simulations with organic probe molecules revealed the site to be well conserved in the CYP2 family with the exception of CYP2E1. In the presence of a ligand bound to the H1 site, we could observe an enlargement of a ligand tunnel in several members of the CYP2 family. Further, we could detect the facilitation of ligand translocation by H1 interactions with statistical significance in CYP2C8 and CYP2D6, even though all other enzymes except for CYP2C19, CYP2E1, and CYP3A4 presented a similar trend. As the detailed comprehension of ligand access and egress phenomena remains one of the most relevant challenges in the field, this work contributes to its elucidation and ultimately helps in estimating the selectivity of metabolic transformations using computational techniques.
    Keywords Cytochrome P450 ; CYP ; allosteric ; ligand access ; tunnel ; molecular dynamics ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 500
    Language English
    Publishing date 2021-12-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Book ; Online ; Thesis: Epitranscriptomic Regulation in Synaptic Plasticity, Aging and Neurodegeneration

    Castro Hernandez, Ricardo [Verfasser] / Fischer, André [Akademischer Betreuer] / Fischer, André [Gutachter] / Outeiro, Tiago Fleming [Gutachter]

    2023  

    Author's details Ricardo Castro Hernández ; Gutachter: André Fischer, Tiago Fleming Outeiro ; Betreuer: André Fischer
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Niedersächsische Staats- und Universitätsbibliothek Göttingen
    Publishing place Göttingen
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  8. Article: digitaler fortschrittsHUB LeMeDaRT – lean medical data gesundheitsdatenraum. Die richtigen Daten zur richtigen Zeit am richtigen Ort

    Fischer, Joachim E. / Baumgart, André

    Gesundhyte.de

    2022  Volume 15, Issue -, Page(s) 32

    Language German
    Document type Article
    ZDB-ID 3044168-7
    ISSN 2702-2544
    Database Current Contents Medicine

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6877: Show issues Location:
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  9. Article ; Online: Learning unseen coexisting attractors.

    Gauthier, Daniel J / Fischer, Ingo / Röhm, André

    Chaos (Woodbury, N.Y.)

    2022  Volume 32, Issue 11, Page(s) 113107

    Abstract: Reservoir computing is a machine learning approach that can generate a surrogate model of a dynamical system. It can learn the underlying dynamical system using fewer trainable parameters and, hence, smaller training data sets than competing approaches. ... ...

    Abstract Reservoir computing is a machine learning approach that can generate a surrogate model of a dynamical system. It can learn the underlying dynamical system using fewer trainable parameters and, hence, smaller training data sets than competing approaches. Recently, a simpler formulation, known as next-generation reservoir computing, removed many algorithm metaparameters and identified a well-performing traditional reservoir computer, thus simplifying training even further. Here, we study a particularly challenging problem of learning a dynamical system that has both disparate time scales and multiple co-existing dynamical states (attractors). We compare the next-generation and traditional reservoir computer using metrics quantifying the geometry of the ground-truth and forecasted attractors. For the studied four-dimensional system, the next-generation reservoir computing approach uses ∼ 1.7 × less training data, requires
    Language English
    Publishing date 2022-11-28
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1472677-4
    ISSN 1089-7682 ; 1054-1500
    ISSN (online) 1089-7682
    ISSN 1054-1500
    DOI 10.1063/5.0116784
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Allosteric Binding Sites On Nuclear Receptors: Focus On Drug Efficacy and Selectivity.

    Fischer, André / Smieško, Martin

    International journal of molecular sciences

    2020  Volume 21, Issue 2

    Abstract: Nuclear receptors (NRs) are highly relevant drug targets in major indications such as oncologic, metabolic, reproductive, and immunologic diseases. However, currently, marketed drugs designed towards the orthosteric binding site of NRs often suffer from ... ...

    Abstract Nuclear receptors (NRs) are highly relevant drug targets in major indications such as oncologic, metabolic, reproductive, and immunologic diseases. However, currently, marketed drugs designed towards the orthosteric binding site of NRs often suffer from resistance mechanisms and poor selectivity. The identification of two superficial allosteric sites, activation function-2 (AF-2) and binding function-3 (BF-3), as novel drug targets sparked the development of inhibitors, while selectivity concerns due to a high conservation degree remained. To determine important pharmacophores and hydration sites among AF-2 and BF-3 of eight hormonal NRs, we systematically analyzed over 10 μ s of molecular dynamics simulations including simulations in explicit water and solvent mixtures. In addition, a library of over 300 allosteric inhibitors was evaluated by molecular docking. Based on our results, we suggest the BF-3 site to offer a higher potential for drug selectivity as opposed to the AF-2 site that is more conserved among the selected receptors. Detected similarities among the AF-2 sites of various NRs urge for a broader selectivity assessment in future studies. In combination with the Supplementary Material, this work provides a foundation to improve both selectivity and potency of allosteric inhibitors in a rational manner and increase the therapeutic applicability of this promising compound class.
    MeSH term(s) Allosteric Regulation/drug effects ; Allosteric Site ; Binding Sites ; Ligands ; Molecular Conformation ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Protein Binding ; Quantitative Structure-Activity Relationship ; Receptors, Cytoplasmic and Nuclear/chemistry ; Receptors, Cytoplasmic and Nuclear/metabolism
    Chemical Substances Ligands ; Receptors, Cytoplasmic and Nuclear
    Language English
    Publishing date 2020-01-14
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms21020534
    Database MEDical Literature Analysis and Retrieval System OnLINE

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