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  1. Article: Halide Perovskites Breathe Too: The Iodide-Iodine Equilibrium and Self-Doping in Cs

    Vigil, Julian A / Wolf, Nathan R / Slavney, Adam H / Matheu, Roc / Saldivar Valdes, Abraham / Breidenbach, Aaron / Lee, Young S / Karunadasa, Hemamala I

    ACS central science

    2024  Volume 10, Issue 4, Page(s) 907–919

    Abstract: The response of an oxide crystal to the atmosphere can be personified as breathing-a dynamic equilibrium between ... ...

    Abstract The response of an oxide crystal to the atmosphere can be personified as breathing-a dynamic equilibrium between O
    Language English
    Publishing date 2024-04-02
    Publishing country United States
    Document type Journal Article
    ISSN 2374-7943
    ISSN 2374-7943
    DOI 10.1021/acscentsci.4c00056
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Coumarin as a structural component of substrates and probes for serine and cysteine proteases.

    Breidenbach, Julian / Bartz, Ulrike / Gütschow, Michael

    Biochimica et biophysica acta. Proteins and proteomics

    2020  Volume 1868, Issue 9, Page(s) 140445

    Abstract: Coumarins represent well-established structures to introduce fluorescence into tool compounds for biochemical investigations. They are valued for their small size, chemical stability and accessibility as well as their tunable photochemical properties. As ...

    Abstract Coumarins represent well-established structures to introduce fluorescence into tool compounds for biochemical investigations. They are valued for their small size, chemical stability and accessibility as well as their tunable photochemical properties. As components of fluorophore/quencher pairs or FRET donor/acceptor pairs, coumarins have frequently been applied in substrate mapping approaches for serine and cysteine proteases. This review also focuses on the incorporation of coumarins into the side chain of amino acids and the exploitation of the resulting fluorescent amino acids for the positional profiling of protease substrates. The protease-inhibiting properties of certain coumarin derivatives and the utilization of coumarin moieties to assemble activity-based probes for serine and cysteine proteases are discussed as well.
    MeSH term(s) Catalytic Domain ; Coumarins/chemistry ; Coumarins/metabolism ; Coumarins/pharmacology ; Cysteine Proteases/drug effects ; Cysteine Proteases/metabolism ; Fluorescence ; Fluorescence Resonance Energy Transfer/methods ; Fluorescent Dyes/chemistry ; Serine/metabolism ; Serine Proteases/drug effects ; Serine Proteases/metabolism ; Substrate Specificity
    Chemical Substances Coumarins ; Fluorescent Dyes ; Serine (452VLY9402) ; coumarin (A4VZ22K1WT) ; Cysteine Proteases (EC 3.4.-) ; Serine Proteases (EC 3.4.-)
    Keywords covid19
    Language English
    Publishing date 2020-05-13
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 2918798-9
    ISSN 1878-1454 ; 1570-9639
    ISSN (online) 1878-1454
    ISSN 1570-9639
    DOI 10.1016/j.bbapap.2020.140445
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 7161: Show issues Location:
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  3. Article ; Online: Correction to "Cathepsin-Targeting SARS-CoV-2 Inhibitors: Design, Synthesis, and Biological Activity".

    Flury, Philipp / Breidenbach, Julian / Krüger, Nadine / Voget, Rabea / Schäkel, Laura / Si, Yaoyao / Krasniqi, Vesa / Calistri, Sara / Olfert, Matthias / Sylvester, Katharina / Rocha, Cheila / Ditzinger, Raphael / Rasch, Alexander / Pöhlmann, Stefan / Kronenberger, Thales / Poso, Antti / Rox, Katharina / Laufer, Stefan A / Müller, Christa E /
    Gütschow, Michael / Pillaiyar, Thanigaimalai

    ACS pharmacology & translational science

    2024  Volume 7, Issue 4, Page(s) 1195–1196

    Abstract: This corrects the article DOI: 10.1021/acsptsci.3c00313.]. ...

    Abstract [This corrects the article DOI: 10.1021/acsptsci.3c00313.].
    Language English
    Publishing date 2024-03-06
    Publishing country United States
    Document type Published Erratum
    ISSN 2575-9108
    ISSN (online) 2575-9108
    DOI 10.1021/acsptsci.4c00095
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Cell Type-Specific Anti-Viral Effects of Novel SARS-CoV-2 Main Protease Inhibitors.

    Geiger, Nina / Diesendorf, Viktoria / Roll, Valeria / König, Eva-Maria / Obernolte, Helena / Sewald, Katherina / Breidenbach, Julian / Pillaiyar, Thanigaimalai / Gütschow, Michael / Müller, Christa E / Bodem, Jochen

    International journal of molecular sciences

    2023  Volume 24, Issue 4

    Abstract: Recently, we have described novel pyridyl indole esters and peptidomimetics as potent inhibitors of the severe acute respiratory syndrome coronavirus type 2 (SARS-CoV-2) main protease. Here, we analysed the impact of these compounds on viral replication. ...

    Abstract Recently, we have described novel pyridyl indole esters and peptidomimetics as potent inhibitors of the severe acute respiratory syndrome coronavirus type 2 (SARS-CoV-2) main protease. Here, we analysed the impact of these compounds on viral replication. It has been shown that some antivirals against SARS-CoV-2 act in a cell line-specific way. Thus, the compounds were tested in Vero, Huh-7, and Calu-3 cells. We showed that the protease inhibitors at 30 µM suppress viral replication by up to 5 orders of magnitude in Huh-7 cells, while in Calu-3 cells, suppression by 2 orders of magnitude was achieved. Three pyridin-3-yl indole-carboxylates inhibited viral replication in all cell lines, indicating that they might repress viral replication in human tissue as well. Thus, we investigated three compounds in human precision-cut lung slices and observed donor-dependent antiviral activity in this patient-near system. Our results provide evidence that even direct-acting antivirals may act in a cell line-specific manner.
    MeSH term(s) Humans ; Antiviral Agents/pharmacology ; SARS-CoV-2 ; COVID-19 ; Hepatitis C, Chronic ; Protease Inhibitors/pharmacology ; Indoles/pharmacology
    Chemical Substances Antiviral Agents ; 3C-like proteinase, SARS-CoV-2 (EC 3.4.22.-) ; Protease Inhibitors ; Indoles
    Language English
    Publishing date 2023-02-16
    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/ijms24043972
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Cathepsin-Targeting SARS-CoV-2 Inhibitors: Design, Synthesis, and Biological Activity.

    Flury, Philipp / Breidenbach, Julian / Krüger, Nadine / Voget, Rabea / Schäkel, Laura / Si, Yaoyao / Krasniqi, Vesa / Calistri, Sara / Olfert, Matthias / Sylvester, Katharina / Rocha, Cheila / Ditzinger, Raphael / Rasch, Alexander / Pöhlmann, Stefan / Kronenberger, Thales / Poso, Antti / Rox, Katharina / Laufer, Stefan A / Müller, Christa E /
    Gütschow, Michael / Pillaiyar, Thanigaimalai

    ACS pharmacology & translational science

    2024  Volume 7, Issue 2, Page(s) 493–514

    Abstract: Cathepsins (Cats) are proteases that mediate the successful entry of SARS-CoV-2 into host cells. We designed and synthesized a tailored series of 21 peptidomimetics and evaluated their inhibitory activity against human cathepsins L, B, and S. Structural ... ...

    Abstract Cathepsins (Cats) are proteases that mediate the successful entry of SARS-CoV-2 into host cells. We designed and synthesized a tailored series of 21 peptidomimetics and evaluated their inhibitory activity against human cathepsins L, B, and S. Structural diversity was realized by combinations of different C-terminal warhead functions and N-terminal capping groups, while a central Leu-Phe fragment was maintained. Several compounds were identified as promising cathepsin L and S inhibitors with
    Language English
    Publishing date 2024-01-19
    Publishing country United States
    Document type Journal Article
    ISSN 2575-9108
    ISSN (online) 2575-9108
    DOI 10.1021/acsptsci.3c00313
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Targeting the Main Protease of SARS-CoV-2: From the Establishment of High Throughput Screening to the Design of Tailored Inhibitors.

    Breidenbach, Julian / Lemke, Carina / Pillaiyar, Thanigaimalai / Schäkel, Laura / Al Hamwi, Ghazl / Diett, Miriam / Gedschold, Robin / Geiger, Nina / Lopez, Vittoria / Mirza, Salahuddin / Namasivayam, Vigneshwaran / Schiedel, Anke C / Sylvester, Katharina / Thimm, Dominik / Vielmuth, Christin / Phuong Vu, Lan / Zyulina, Maria / Bodem, Jochen / Gütschow, Michael /
    Müller, Christa E

    Angewandte Chemie (International ed. in English)

    2021  Volume 60, Issue 18, Page(s) 10423–10429

    Abstract: The main protease of SARS-CoV-2 ( ... ...

    Abstract The main protease of SARS-CoV-2 (M
    MeSH term(s) Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; COVID-19/drug therapy ; COVID-19/metabolism ; COVID-19/virology ; Coronavirus 3C Proteases/antagonists & inhibitors ; Coronavirus 3C Proteases/metabolism ; Drug Design ; Drug Discovery ; HEK293 Cells ; High-Throughput Screening Assays ; Humans ; Molecular Docking Simulation ; Nitriles/chemistry ; Nitriles/pharmacology ; Protease Inhibitors/chemistry ; Protease Inhibitors/pharmacology ; Pyridines/chemistry ; Pyridines/pharmacology ; SARS-CoV-2/drug effects ; SARS-CoV-2/enzymology ; SARS-CoV-2/physiology ; Virus Internalization/drug effects
    Chemical Substances Antiviral Agents ; Nitriles ; Protease Inhibitors ; Pyridines ; 3C-like proteinase, SARS-CoV-2 (EC 3.4.22.-) ; Coronavirus 3C Proteases (EC 3.4.22.28)
    Language English
    Publishing date 2021-03-24
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2011836-3
    ISSN 1521-3773 ; 1433-7851
    ISSN (online) 1521-3773
    ISSN 1433-7851
    DOI 10.1002/anie.202016961
    Database MEDical Literature Analysis and Retrieval System OnLINE

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