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  1. Article ; Online: A lens-shaped supramolecule based on the bulky pentaphosphaferrocene [Cp

    Heinl, Sebastian / Peresypkina, Eugenia / Kremer, Werner / Scheer, Manfred

    Chemical communications (Cambridge, England)

    2023  Volume 59, Issue 68, Page(s) 10263–10266

    Abstract: Besides inherent fullerene-like hollow spheres, the metallasupramolecular chemistry of pentaphosphaferrocenes and ... ...

    Abstract Besides inherent fullerene-like hollow spheres, the metallasupramolecular chemistry of pentaphosphaferrocenes and CuBr
    Language English
    Publishing date 2023-08-22
    Publishing country England
    Document type Journal Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d3cc03244b
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  2. Book ; Online ; Thesis: Kernresonanz-basierte Lipoproteinanalyse bei diabetischer Stoffwechsellage

    Kalbitzer, Tina [Verfasser] / Kremer, Werner [Akademischer Betreuer]

    2023  

    Author's details Tina Kalbitzer ; Betreuer: Werner Kremer
    Keywords Medizin, Gesundheit ; Medicine, Health
    Subject code sg610
    Language German
    Publisher Universitätsbibliothek Regensburg
    Publishing place Regensburg
    Document type Book ; Online ; Thesis
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  3. Article ; Online: Insights into the Structure of Invisible Conformations of Large Methyl Group Labeled Molecular Machines from High Pressure NMR

    Krempl, Christina / Wurm, Jan Philip / Beck Erlach, Markus / Kremer, Werner / Sprangers, Remco

    Journal of Molecular Biology. 2023 June, v. 435, no. 11 p.167922-

    2023  

    Abstract: Most proteins are highly flexible and can adopt conformations that deviate from the energetically most favorable ground state. Structural information on these lowly populated, alternative conformations is often lacking, despite the functional importance ... ...

    Abstract Most proteins are highly flexible and can adopt conformations that deviate from the energetically most favorable ground state. Structural information on these lowly populated, alternative conformations is often lacking, despite the functional importance of these states. Here, we study the pathway by which the Dcp1:Dcp2 mRNA decapping complex exchanges between an autoinhibited closed and an open conformation. We make use of methyl Carr–Purcell–Meiboom–Gill (CPMG) NMR relaxation dispersion (RD) experiments that report on the population of the sparsely populated open conformation as well as on the exchange rate between the two conformations. To obtain volumetric information on the open conformation as well as on the transition state structure we made use of RD measurements at elevated pressures. We found that the open Dcp1:Dcp2 conformation has a lower molecular volume than the closed conformation and that the transition state is close in volume to the closed state. In the presence of ATP the volume change upon opening of the complex increases and the volume of the transition state lies in-between the volumes of the closed and open state. These findings show that ATP has an effect on the volume changes that are associated with the opening-closing pathway of the complex. Our results highlight the strength of pressure dependent NMR methods to obtain insights into structural features of protein conformations that are not directly observable. As our work makes use of methyl groups as NMR probes we conclude that the applied methodology is also applicable to high molecular weight complexes.
    Keywords dispersions ; exhibitions ; journals ; measurement ; molecular biology ; molecular weight ; pressure ; protein conformation ; structural proteins ; volume ; methyl TROSY ; CPMG relaxation dispersion ; protein dynamics ; high pressure ; Dcp1:Dcp2 mRNA decapping complex
    Language English
    Dates of publication 2023-06
    Publishing place Elsevier Ltd
    Document type Article ; Online
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2022.167922
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    In stock of ZB MED Bonn / Germany

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  4. Article ; Online: NMR derived changes of lipoprotein particle concentrations related to impaired fasting glucose, impaired glucose tolerance, or manifest type 2 diabetes mellitus.

    Kalbitzer, Tina / Lobenhofer, Kristina / Martin, Silke / Beck Erlach, Markus / Kremer, Werner / Kalbitzer, Hans Robert

    Lipids in health and disease

    2023  Volume 22, Issue 1, Page(s) 42

    Abstract: Background: Type 2 diabetes mellitus (T2D) and corresponding borderline states, impaired fasting glucose (IFG) and/or glucose tolerance (IGT), are associated with dyslipoproteinemia. It is important to distinguish between factors that cause T2D and that ...

    Abstract Background: Type 2 diabetes mellitus (T2D) and corresponding borderline states, impaired fasting glucose (IFG) and/or glucose tolerance (IGT), are associated with dyslipoproteinemia. It is important to distinguish between factors that cause T2D and that are the direct result of T2D.
    Methods: The lipoprotein subclass patterns of blood donors with IFG, IGT, with IFG combined with IGT, and T2D are analyzed by nuclear magnetic resonance (NMR) spectroscopy. The development of lipoprotein patterns with time is investigated by using samples retained for an average period of 6 years. In total 595 blood donors are classified by oral glucose tolerance test (oGTT) and their glycosylated hemoglobin (HbA1c) concentrations. Concentrations of lipoprotein particles of 15 different subclasses are analyzed in the 10,921 NMR spectra recorded under fasting and non-fasting conditions. The subjects are assumed healthy according to the strict regulations for blood donors before performing the oGTT.
    Results: Under fasting conditions manifest T2D exhibits a significant concentration increase of the smallest HDL particles (HDL A) combined with a decrease in all other HDL subclasses. In contrast to other studies reviewed in this paper, a general concentration decrease of all LDL particles is observed that is most prominent for the smallest LDL particles (LDL A). Under normal nutritional conditions a large, significant increase of the concentrations of VLDL and chylomicrons is observed for all groups with IFG and/or IGT and most prominently for manifest T2D. As we show it is possible to obtain an estimate of the concentrations of the apolipoproteins Apo-A1, Apo-B100, and Apo-B48 from the NMR data. In the actual study cohort, under fasting conditions the concentrations of the lipoproteins are not increased significantly in T2D, under non-fasting conditions only Apo-B48 increases significantly.
    Conclusion: In contrast to other studies, in our cohort of "healthy" blood donors the T2D associated dyslipoproteinemia does not change the total concentrations of the lipoprotein particles produced in the liver under fasting and non-fasting conditions significantly but only their subclass distributions. Compared to the control group, under non-fasting conditions participants with IGT and IFG or T2D show a substantial increase of plasma concentrations of those lipoproteins that are produced in the intestinal tract. The intestinal insulin resistance becomes strongly observable.
    MeSH term(s) Humans ; Glucose Intolerance ; Diabetes Mellitus, Type 2 ; Blood Glucose ; Prediabetic State ; Lipoproteins ; Magnetic Resonance Spectroscopy
    Chemical Substances Blood Glucose ; Lipoproteins
    Language English
    Publishing date 2023-03-24
    Publishing country England
    Document type Journal Article
    ZDB-ID 2091381-3
    ISSN 1476-511X ; 1476-511X
    ISSN (online) 1476-511X
    ISSN 1476-511X
    DOI 10.1186/s12944-023-01801-7
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  5. Article ; Online: Insights into the Structure of Invisible Conformations of Large Methyl Group Labeled Molecular Machines from High Pressure NMR.

    Krempl, Christina / Wurm, Jan Philip / Beck Erlach, Markus / Kremer, Werner / Sprangers, Remco

    Journal of molecular biology

    2023  Volume 435, Issue 11, Page(s) 167922

    Abstract: Most proteins are highly flexible and can adopt conformations that deviate from the energetically most favorable ground state. Structural information on these lowly populated, alternative conformations is often lacking, despite the functional importance ... ...

    Abstract Most proteins are highly flexible and can adopt conformations that deviate from the energetically most favorable ground state. Structural information on these lowly populated, alternative conformations is often lacking, despite the functional importance of these states. Here, we study the pathway by which the Dcp1:Dcp2 mRNA decapping complex exchanges between an autoinhibited closed and an open conformation. We make use of methyl Carr-Purcell-Meiboom-Gill (CPMG) NMR relaxation dispersion (RD) experiments that report on the population of the sparsely populated open conformation as well as on the exchange rate between the two conformations. To obtain volumetric information on the open conformation as well as on the transition state structure we made use of RD measurements at elevated pressures. We found that the open Dcp1:Dcp2 conformation has a lower molecular volume than the closed conformation and that the transition state is close in volume to the closed state. In the presence of ATP the volume change upon opening of the complex increases and the volume of the transition state lies in-between the volumes of the closed and open state. These findings show that ATP has an effect on the volume changes that are associated with the opening-closing pathway of the complex. Our results highlight the strength of pressure dependent NMR methods to obtain insights into structural features of protein conformations that are not directly observable. As our work makes use of methyl groups as NMR probes we conclude that the applied methodology is also applicable to high molecular weight complexes.
    MeSH term(s) Adenosine Triphosphate/chemistry ; Magnetic Resonance Spectroscopy ; Nuclear Magnetic Resonance, Biomolecular/methods ; Protein Conformation ; Proteins/chemistry
    Chemical Substances Adenosine Triphosphate (8L70Q75FXE) ; Proteins
    Language English
    Publishing date 2023-06-16
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2022.167922
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 867: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  6. Article ; Online: A suite of

    Overbeck, Jan H / Kremer, Werner / Sprangers, Remco

    Journal of biomolecular NMR

    2020  Volume 74, Issue 12, Page(s) 753–766

    Abstract: Proteins and nucleic acids are highly dynamic bio-molecules that can populate a variety of conformational states. NMR relaxation dispersion (RD) methods are uniquely suited to quantify the associated kinetic and thermodynamic parameters. Here, we present ...

    Abstract Proteins and nucleic acids are highly dynamic bio-molecules that can populate a variety of conformational states. NMR relaxation dispersion (RD) methods are uniquely suited to quantify the associated kinetic and thermodynamic parameters. Here, we present a consistent suite of
    MeSH term(s) Bacterial Proteins/chemistry ; Fluorine/chemistry ; Kinetics ; Motion ; Nuclear Magnetic Resonance, Biomolecular ; Proteasome Endopeptidase Complex/chemistry ; Protein Folding ; Thermodynamics ; Thermotoga maritima/chemistry
    Chemical Substances Bacterial Proteins ; Fluorine (284SYP0193) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2020-09-30
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1081696-3
    ISSN 1573-5001 ; 0925-2738
    ISSN (online) 1573-5001
    ISSN 0925-2738
    DOI 10.1007/s10858-020-00348-4
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4132: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  7. Article ; Online: Correction to: A suite of

    Overbeck, Jan H / Kremer, Werner / Sprangers, Remco

    Journal of biomolecular NMR

    2020  Volume 74, Issue 12, Page(s) 767–768

    Abstract: In the original publication, Figures 3 and 6 were displayed incorrectly due to a mistake made by the publisher. The correct version of Figs. 3 and 6 are given below. ...

    Abstract In the original publication, Figures 3 and 6 were displayed incorrectly due to a mistake made by the publisher. The correct version of Figs. 3 and 6 are given below.
    Language English
    Publishing date 2020-11-25
    Publishing country Netherlands
    Document type Published Erratum
    ZDB-ID 1081696-3
    ISSN 1573-5001 ; 0925-2738
    ISSN (online) 1573-5001
    ISSN 0925-2738
    DOI 10.1007/s10858-020-00352-8
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4132: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  8. Book ; Online ; Thesis: Biophysical characterization of the VHP35 protein by NMR spectroscopy

    Becker, Paul [Verfasser] / Balbach, Jochen Gutachter] / [Hinderberger, Dariush [Gutachter] / Kremer, Werner [Gutachter]

    2022  

    Author's details Paul Becker ; Gutachter: Jochen Balbach, Dariush Hinderberger, Werner Kremer
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Universitäts- und Landesbibliothek Sachsen-Anhalt
    Publishing place Halle (Saale)
    Document type Book ; Online ; Thesis
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  9. Article ; Online: The accuracy limit of chemical shift predictions for species in aqueous solution.

    Maste, Stefan / Sharma, Bikramjit / Pongratz, Tim / Grabe, Bastian / Hiller, Wolf / Erlach, Markus Beck / Kremer, Werner / Kalbitzer, Hans Robert / Marx, Dominik / Kast, Stefan M

    Physical chemistry chemical physics : PCCP

    2024  Volume 26, Issue 7, Page(s) 6386–6395

    Abstract: Interpreting NMR experiments benefits from first-principles predictions of chemical shifts. Reaching the accuracy limit of theory is relevant for unambiguous structural analysis and dissecting theoretical approximations. Since accurate chemical shift ... ...

    Abstract Interpreting NMR experiments benefits from first-principles predictions of chemical shifts. Reaching the accuracy limit of theory is relevant for unambiguous structural analysis and dissecting theoretical approximations. Since accurate chemical shift measurements are based on using internal reference compounds such as trimethylsilylpropanesulfonate (DSS), a detailed comparison of experimental with theoretical data requires simultaneous consideration of both target and reference species ensembles in the same solvent environment. Here we show that
    Language English
    Publishing date 2024-02-14
    Publishing country England
    Document type Journal Article
    ZDB-ID 1476244-4
    ISSN 1463-9084 ; 1463-9076
    ISSN (online) 1463-9084
    ISSN 1463-9076
    DOI 10.1039/d3cp05471c
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  10. Article ; Online: RNA and DNA Binding Epitopes of the Cold Shock Protein TmCsp from the Hyperthermophile Thermotoga maritima.

    von König, Konstanze / Kachel, Norman / Kalbitzer, Hans Robert / Kremer, Werner

    The protein journal

    2020  Volume 39, Issue 5, Page(s) 487–500

    Abstract: Prokaryotic cold shock proteins (CSPs) are considered to play an important role in the transcriptional and translational regulation of gene expression, possibly by acting as transcription anti-terminators and "RNA chaperones". They bind with high ... ...

    Abstract Prokaryotic cold shock proteins (CSPs) are considered to play an important role in the transcriptional and translational regulation of gene expression, possibly by acting as transcription anti-terminators and "RNA chaperones". They bind with high affinity to single-stranded nucleic acids. Here we report the binding epitope of TmCsp from Thermotoga maritima for both single-stranded DNA and RNA, using heteronuclear 2D NMR spectroscopy. At "physiological" growth temperatures of TmCsp (≥ 343 K), all oligonucleotides studied have dissociation constants between 1.6 ((dT)
    MeSH term(s) Amino Acid Motifs ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Cold Shock Proteins and Peptides/chemistry ; Cold Shock Proteins and Peptides/genetics ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/genetics ; Epitopes/chemistry ; Epitopes/genetics ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/genetics ; Thermotoga maritima/chemistry ; Thermotoga maritima/genetics
    Chemical Substances Bacterial Proteins ; Cold Shock Proteins and Peptides ; DNA-Binding Proteins ; Epitopes ; RNA-Binding Proteins
    Language English
    Publishing date 2020-10-22
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2143071-8
    ISSN 1875-8355 ; 1572-3887
    ISSN (online) 1875-8355
    ISSN 1572-3887
    DOI 10.1007/s10930-020-09929-6
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