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  1. Book ; Thesis: Oxidativer Stress durch neutrophile Granulozyten als Pathomechanismus im kardiopulmonalen System

    Hammerschmidt, Stefan

    2003  

    Author's details vorgelegt von Stefan Hammerschmidt
    Language German
    Size 166 S. : graph. Darst.
    Publishing country Germany
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Leipzig, Univ., Diss., 2003
    HBZ-ID HT013949772
    Database Catalogue ZB MED Medicine, Health

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  2. Book ; Thesis: Modifikation von Plasmaproteinen durch die Hypochlorsäure aktivierter neutrophiler Granulozyten

    Hammerschmidt, Stefan

    1994  

    Author's details eingereicht von Stefan Hammerschmidt
    Language German
    Size 77, 4 Bl. : Ill., graph. Darst.
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Leipzig, Univ., Diss., 1994
    HBZ-ID HT006308305
    Database Catalogue ZB MED Medicine, Health

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  3. Article: [No title information]

    Hammerschmidt, Stefan Josef / Müller, Patrick / Schirmeister, Tanja

    Biospektrum : Zeitschrift der Gesellschaft fur Biologishe Chemie (GBCH) und der Vereinigung fur Allgemeine und Angewandte Mikrobiologie (VAAM)

    2021  Volume 27, Issue 3, Page(s) 254–256

    Abstract: The SARS-CoV-encoded papain-like cysteine protease ( ... ...

    Title translation SARS-CoV-PL
    Abstract The SARS-CoV-encoded papain-like cysteine protease (PL
    Language German
    Publishing date 2021-05-11
    Publishing country Germany
    Document type English Abstract ; Journal Article ; Review
    ZDB-ID 2203536-9
    ISSN 1868-6249 ; 0947-0867
    ISSN (online) 1868-6249
    ISSN 0947-0867
    DOI 10.1007/s12268-021-1576-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Improving binding entropy by higher ligand symmetry? - A case study with human matriptase.

    Hammerschmidt, Stefan J / Maus, Hannah / Weldert, Annabelle C / Gütschow, Michael / Kersten, Christian

    RSC medicinal chemistry

    2023  Volume 14, Issue 5, Page(s) 969–982

    Abstract: Understanding different contributions to the binding entropy of ligands is of utmost interest to better predict affinity and the thermodynamic binding profiles of protein-ligand interactions and to develop new strategies for ligand optimization. To these ...

    Abstract Understanding different contributions to the binding entropy of ligands is of utmost interest to better predict affinity and the thermodynamic binding profiles of protein-ligand interactions and to develop new strategies for ligand optimization. To these means, the largely neglected effects of introducing higher ligand symmetry, thereby reducing the number of energetically distinguishable binding modes on binding entropy using the human matriptase as a model system, were investigated. A set of new trivalent phloroglucinol-based inhibitors that address the roughly symmetric binding site of the enzyme was designed, synthesized, and subjected to isothermal titration calorimetry. These highly symmetric ligands that can adopt multiple indistinguishable binding modes exhibited high entropy-driven affinity in line with affinity-change predictions.
    Language English
    Publishing date 2023-04-27
    Publishing country England
    Document type Journal Article
    ISSN 2632-8682
    ISSN (online) 2632-8682
    DOI 10.1039/d3md00125c
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Book ; Online: Organverantwortlichkeit für Finanzanlagegeschäfte in der AG

    Hammerschmidt, Stefan

    2016  

    Abstract: ... Die Zielgruppen · Dozierende und Studierende der Rechtswissenschaften · Rechtsanwälte, Juristen Der Autor Stefan ... Hammerschmidt ist Rechtsanwaltsanwärter in einer Linzer Wirtschaftskanzlei ...

    Author's details von Stefan Hammerschmidt
    Abstract Der Autor prüft, welches Maß an Sorgfalt die Organe einer Aktiengesellschaft beim An- und Verkauf von Finanztiteln an den Tag zu legen haben. Das Kernstück der Studie bildet eine Untersuchung, inwieweit die an einen professionellen Vermögensverwalter zu stellenden Sorgfaltsanforderungen zur Präzisierung der Vorstandspflichten beim Wertpapiererwerb herangezogen werden können. Verstoßen Mitglieder des Vorstands gegen diese Verhaltensstandards, so besteht die Gefahr, im Falle verlustreicher Anlagegeschäfte Regressforderungen der eigenen Gesellschaft ausgesetzt zu sein. Anschließend wird auch die Überwachungstätigkeit des Aufsichtsrats bei derartigen Geschäften näher beleuchtet. Der Inhalt · Der Vorstand als Vermögensverwalter der AG? · Der Ermessensspielraum des Vorstands im Zusammenhang mit Wertpapiergeschäften · Beiziehung externer Wertpapierdienstleister · Die Veranlagungsstrategie bzw. der Wertpapiererwerbals zustimmungspflichtiges Geschäft? Die Zielgruppen · Dozierende und Studierende der Rechtswissenschaften · Rechtsanwälte, Juristen Der Autor Stefan Hammerschmidt ist Rechtsanwaltsanwärter in einer Linzer Wirtschaftskanzlei
    Keywords Commercial law ; International law ; Law ; Trade
    Language German
    Size Online-Ressource (XV, 124 S), online resource
    Edition 1. Aufl. 2016
    Publisher Springer Fachmedien Wiesbaden
    Publishing place Wiesbaden ;s.l
    Document type Book ; Online
    ISBN 9783658113919 ; 9783658113926 ; 365811391X ; 3658113928
    DOI 10.1007/978-3-658-11392-6
    Database Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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  6. Article ; Online: A competition smFRET assay to study ligand-induced conformational changes of the dengue virus protease.

    Maus, Hannah / Hinze, Gerald / Hammerschmidt, Stefan Josef / Basché, Thomas / Schirmeister, Tanja

    Protein science : a publication of the Protein Society

    2022  Volume 32, Issue 1, Page(s) e4526

    Abstract: Ligand binding to proteins often is accompanied by conformational transitions. Here, we describe a competition assay based on single molecule Förster resonance energy transfer (smFRET) to investigate the ligand-induced conformational changes of the ... ...

    Abstract Ligand binding to proteins often is accompanied by conformational transitions. Here, we describe a competition assay based on single molecule Förster resonance energy transfer (smFRET) to investigate the ligand-induced conformational changes of the dengue virus (DENV) NS2B-NS3 protease, which can adopt at least two different conformations. First, a competitive ligand was used to stabilize the closed conformation of the protease. Subsequent addition of the allosteric inhibitor reduced the fraction of the closed conformation and simultaneously increased the fraction of the open conformation, demonstrating that the allosteric inhibitor stabilizes the open conformation. In addition, the proportions of open and closed conformations at different concentrations of the allosteric inhibitor were used to determine its binding affinity to the protease. The K
    MeSH term(s) Dengue Virus/metabolism ; Peptide Hydrolases/metabolism ; Ligands ; Fluorescence Resonance Energy Transfer ; Viral Nonstructural Proteins/chemistry ; Antiviral Agents/chemistry
    Chemical Substances Peptide Hydrolases (EC 3.4.-) ; Ligands ; Viral Nonstructural Proteins ; Antiviral Agents
    Language English
    Publishing date 2022-12-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1106283-6
    ISSN 1469-896X ; 0961-8368
    ISSN (online) 1469-896X
    ISSN 0961-8368
    DOI 10.1002/pro.4526
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: The effects of allosteric and competitive inhibitors on ZIKV protease conformational dynamics explored through smFRET, nanoDSF, DSF, and

    Maus, Hannah / Hammerschmidt, Stefan J / Hinze, Gerald / Barthels, Fabian / Pérez Carrillo, Victor H / Hellmich, Ute A / Basché, Thomas / Schirmeister, Tanja

    European journal of medicinal chemistry

    2023  Volume 258, Page(s) 115573

    Abstract: Zika and dengue viruses cause mosquito-borne diseases of high epidemic relevance. The viral NS2B-NS3 proteases play crucial roles in the pathogen replication cycle and are validated drug targets. They can adopt at least two conformations depending on the ...

    Abstract Zika and dengue viruses cause mosquito-borne diseases of high epidemic relevance. The viral NS2B-NS3 proteases play crucial roles in the pathogen replication cycle and are validated drug targets. They can adopt at least two conformations depending on the position of the NS2B cofactor. Recently, we reported ligand-induced conformational changes of dengue virus NS2B-NS3 protease by single-molecule Förster resonance energy transfer (smFRET). Here, we investigated the conformational dynamics of the homologous Zika virus protease through an integrated methodological approach combining smFRET, thermal shift assays (DSF and nanoDSF) and
    MeSH term(s) Animals ; Zika Virus ; Zika Virus Infection ; Peptide Hydrolases ; Fluorescence Resonance Energy Transfer ; Serine Endopeptidases/metabolism ; Viral Nonstructural Proteins ; Protein Conformation ; Magnetic Resonance Spectroscopy ; Protease Inhibitors/pharmacology ; Protease Inhibitors/chemistry
    Chemical Substances Peptide Hydrolases (EC 3.4.-) ; Serine Endopeptidases (EC 3.4.21.-) ; Viral Nonstructural Proteins ; Protease Inhibitors
    Language English
    Publishing date 2023-06-21
    Publishing country France
    Document type Journal Article
    ZDB-ID 188597-2
    ISSN 1768-3254 ; 0009-4374 ; 0223-5234
    ISSN (online) 1768-3254
    ISSN 0009-4374 ; 0223-5234
    DOI 10.1016/j.ejmech.2023.115573
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Thermodynamic characterization of a macrocyclic Zika virus NS2B/NS3 protease inhibitor and its acyclic analogs.

    Hammerschmidt, Stefan J / Huber, Simon / Braun, Niklas J / Lander, Marc / Steinmetzer, Torsten / Kersten, Christian

    Archiv der Pharmazie

    2022  Volume 356, Issue 4, Page(s) e2200518

    Abstract: Cyclization of small molecules is a widely applied strategy in drug design for ligand optimization to improve affinity, as it eliminates the putative need for structural preorganization of the ligand before binding, or to improve pharmacokinetic ... ...

    Abstract Cyclization of small molecules is a widely applied strategy in drug design for ligand optimization to improve affinity, as it eliminates the putative need for structural preorganization of the ligand before binding, or to improve pharmacokinetic properties. In this work, we provide a deeper insight into the binding thermodynamics of a macrocyclic Zika virus NS2B/NS3 protease inhibitor and its linear analogs. Characterization of the thermodynamic binding profiles by isothermal titration calorimetry experiments revealed an unfavorable entropy of the macrocycle compared to the open linear reference ligands. Molecular dynamic simulations and X-ray crystal structure analysis indicated only minor benefits from macrocyclization to fixate a favorable conformation, while linear ligands retained some flexibility even in the protein-bound complex structure, possibly explaining the initially surprising effect of a higher entropic penalty for the macrocyclic ligand.
    MeSH term(s) Humans ; Zika Virus/metabolism ; Ligands ; Viral Nonstructural Proteins ; Protein Conformation ; Structure-Activity Relationship ; Serine Endopeptidases/chemistry ; Serine Endopeptidases/metabolism ; Serine Endopeptidases/pharmacology ; Thermodynamics ; Protease Inhibitors/pharmacology ; Protease Inhibitors/chemistry ; Zika Virus Infection
    Chemical Substances Ligands ; Viral Nonstructural Proteins ; Serine Endopeptidases (EC 3.4.21.-) ; Protease Inhibitors
    Language English
    Publishing date 2022-12-08
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 6381-2
    ISSN 1521-4184 ; 0365-6233 ; 1437-1014
    ISSN (online) 1521-4184
    ISSN 0365-6233 ; 1437-1014
    DOI 10.1002/ardp.202200518
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Book ; Online ; Thesis: Retrospektive Analyse der leitliniengerechten Diagnostik und Therapie des nicht-kleinzelligen Bronchialkarzinoms in den Jahren 2015 und 2016 an der Klinik für Innere Medizin II des Krankenhauses Martha Maria Halle-Dölau

    Görke, Fabian [Verfasser] / Schütte, Wolfgang [Gutachter] / Vordermark, Dirk [Gutachter] / Hammerschmidt, Stefan [Gutachter]

    2022  

    Author's details Fabian Görke ; Gutachter: Wolfgang Schütte, Dirk Vordermark, Stefan Hammerschmidt
    Keywords Medizin, Gesundheit ; Medicine, Health
    Subject code sg610
    Language German
    Publisher Universitäts- und Landesbibliothek Sachsen-Anhalt
    Publishing place Halle (Saale)
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  10. Article: 2-Sulfonylpyrimidines as Privileged Warheads for the Development of

    Barthels, Fabian / Meyr, Jessica / Hammerschmidt, Stefan J / Marciniak, Tessa / Räder, Hans-Joachim / Ziebuhr, Wilma / Engels, Bernd / Schirmeister, Tanja

    Frontiers in molecular biosciences

    2022  Volume 8, Page(s) 804970

    Abstract: Staphylococcus ... ...

    Abstract Staphylococcus aureus
    Language English
    Publishing date 2022-01-03
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2814330-9
    ISSN 2296-889X
    ISSN 2296-889X
    DOI 10.3389/fmolb.2021.804970
    Database MEDical Literature Analysis and Retrieval System OnLINE

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