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  1. Article: Protoporphyrin IX Binds to Iron(II)-Loaded and to Zinc-Loaded Human Frataxin.

    Bernardo-Seisdedos, Ganeko / Schedlbauer, Andreas / Pereira-Ortuzar, Tania / Mato, José M / Millet, Oscar

    Life (Basel, Switzerland)

    2023  Volume 13, Issue 1

    Abstract: 1) Background: Human frataxin is an iron binding protein that participates in the biogenesis of iron sulfur clusters and enhances ferrochelatase activity. While frataxin association to other proteins has been extensively characterized up to the ... ...

    Abstract (1) Background: Human frataxin is an iron binding protein that participates in the biogenesis of iron sulfur clusters and enhances ferrochelatase activity. While frataxin association to other proteins has been extensively characterized up to the structural level, much less is known about the putative capacity of frataxin to interact with functionally related metabolites. In turn, current knowledge about frataxin's capacity to coordinate metal ions is limited to iron (II and III); (2) Methods: here, we used NMR spectroscopy, Molecular Dynamics, and Docking approaches to demonstrate new roles of frataxin; (3) Results: We demonstrate that frataxin also binds Zn
    Language English
    Publishing date 2023-01-12
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2662250-6
    ISSN 2075-1729
    ISSN 2075-1729
    DOI 10.3390/life13010222
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  2. Article: Characterizing ligand-induced conformational changes in clinically relevant galectin-1 by HN/H2O (D2O) exchange

    Schedlbauer, Andreas / Gilles, Ulrich / Ludwig, Anna-Kristin / Adler, Andreas / Kaltner, Herbert / Lindner, Ingo / Mayo, Kevin H / Diercks, Tammo / Reusch, Dietmar / Gabius, Hans-Joachim

    Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM) Biochimie. 2021 Aug., v. 187

    2021  

    Abstract: Glycans of cellular glycoconjugates serve as biochemical signals for a multitude of (patho)physiological processes via binding to their receptors (e.g. lectins). In the case of human adhesion/growth-regulatory galectin-1 (Gal-1), small angle neutron ... ...

    Abstract Glycans of cellular glycoconjugates serve as biochemical signals for a multitude of (patho)physiological processes via binding to their receptors (e.g. lectins). In the case of human adhesion/growth-regulatory galectin-1 (Gal-1), small angle neutron scattering and fluorescence correlation spectroscopy have revealed a significant decrease of its gyration radius and increase of its diffusion coefficient upon binding lactose, posing the pertinent question on the nature and region(s) involved in the underlying structural alterations. Requiring neither a neutron source nor labeling, diffusion measurements by ¹H NMR spectroscopy are shown here to be sufficiently sensitive to detect this ligand-induced change. In order to figure out which region(s) of Gal-1 is (are) affected at the level of peptides, we first explored the use of H/D exchange mass spectrometry (HDX MS). Hereby, we found a reduction in proton exchange kinetics beyond the lactose-binding site. The measurement of fast Hᴺ/H₂O exchange by phase-modulated NMR clean chemical exchange (CLEANEX) NMR on ¹⁵N-labeled Gal-1 then increased the spatial resolution to the level of individual amino acids. The mapped regions with increased protection from Hᴺ/H₂O (D₂O) exchange that include the reduction of solvent exposure around the interface can underlie the protein's compaction. These structural changes have potential to modulate this galectin's role in lattice formation on the cell surface and its interaction(s) with protein(s) at the F-face.
    Keywords diffusivity ; fluorescence correlation spectroscopy ; galectins ; glycoconjugates ; humans ; lactose ; mass spectrometry ; neutrons ; nuclear magnetic resonance spectroscopy ; peptides ; polysaccharides ; solvents
    Language English
    Dates of publication 2021-08
    Size p. 48-56.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 120345-9
    ISSN 0300-9084
    ISSN 0300-9084
    DOI 10.1016/j.biochi.2021.05.008
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 72/375: Show issues

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  3. Article ; Online: Backbone and sidechain NMR assignments for the ribosome maturation factor RimP from Escherichia coli.

    Schedlbauer, Andreas / Ochoa-Lizarralde, Borja / Iturrioz, Idoia / Çapuni, Retina / Diercks, Tammo / de Astigarraga, Elisa / Fucini, Paola / Connell, Sean R

    Biomolecular NMR assignments

    2020  Volume 14, Issue 2, Page(s) 189–193

    Abstract: Ribosome biogenesis is an energetically expensive and complex cellular process that involves the coordinated folding of the ribosomal RNA and dozens of ribosomal proteins. It proceeds along multiple parallel pathways and is guided by trans-acting factors ...

    Abstract Ribosome biogenesis is an energetically expensive and complex cellular process that involves the coordinated folding of the ribosomal RNA and dozens of ribosomal proteins. It proceeds along multiple parallel pathways and is guided by trans-acting factors called ribosome assembly factors. Although this process has been studied for decades, there are still many open questions regarding the role of the ribosome assembly factors in directing the folding of ribosome biogenesis intermediates. RimP is one of the early acting factors and guides the assembly of the small 30S ribosomal subunit by facilitating the binding of ribosomal proteins uS5 and uS12. Here we report the virtually complete
    MeSH term(s) Carbon-13 Magnetic Resonance Spectroscopy ; Escherichia coli/metabolism ; Escherichia coli Proteins/chemistry ; Nitrogen Isotopes ; Nuclear Magnetic Resonance, Biomolecular ; Protein Structure, Secondary ; Ribosomal Proteins/chemistry
    Chemical Substances Escherichia coli Proteins ; Nitrogen Isotopes ; Nitrogen-15 ; Ribosomal Proteins ; RimP protein, E coli
    Language English
    Publishing date 2020-04-17
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2388861-1
    ISSN 1874-270X ; 1874-2718
    ISSN (online) 1874-270X
    ISSN 1874-2718
    DOI 10.1007/s12104-020-09943-w
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  4. Article ; Online: A conserved rRNA switch is central to decoding site maturation on the small ribosomal subunit.

    Schedlbauer, Andreas / Iturrioz, Idoia / Ochoa-Lizarralde, Borja / Diercks, Tammo / López-Alonso, Jorge Pedro / Lavin, José Luis / Kaminishi, Tatsuya / Çapuni, Retina / Dhimole, Neha / de Astigarraga, Elisa / Gil-Carton, David / Fucini, Paola / Connell, Sean R

    Science advances

    2021  Volume 7, Issue 23

    Abstract: While a structural description of the molecular mechanisms guiding ribosome assembly in eukaryotic systems is emerging, bacteria use an unrelated core set of assembly factors for which high-resolution structural information is still missing. To address ... ...

    Abstract While a structural description of the molecular mechanisms guiding ribosome assembly in eukaryotic systems is emerging, bacteria use an unrelated core set of assembly factors for which high-resolution structural information is still missing. To address this, we used single-particle cryo-electron microscopy to visualize the effects of bacterial ribosome assembly factors RimP, RbfA, RsmA, and RsgA on the conformational landscape of the 30
    MeSH term(s) Cryoelectron Microscopy ; RNA, Ribosomal, 16S/genetics ; Ribosome Subunits, Small ; Ribosome Subunits, Small, Bacterial ; Ribosomes
    Chemical Substances RNA, Ribosomal, 16S
    Language English
    Publishing date 2021-06-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2810933-8
    ISSN 2375-2548 ; 2375-2548
    ISSN (online) 2375-2548
    ISSN 2375-2548
    DOI 10.1126/sciadv.abf7547
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  5. Article ; Online: Characterizing ligand-induced conformational changes in clinically relevant galectin-1 by H

    Schedlbauer, Andreas / Gilles, Ulrich / Ludwig, Anna-Kristin / Adler, Andreas / Kaltner, Herbert / Lindner, Ingo / Mayo, Kevin H / Diercks, Tammo / Reusch, Dietmar / Gabius, Hans-Joachim

    Biochimie

    2021  Volume 187, Page(s) 48–56

    Abstract: Glycans of cellular glycoconjugates serve as biochemical signals for a multitude of (patho)physiological processes via binding to their receptors (e.g. lectins). In the case of human adhesion/growth-regulatory galectin-1 (Gal-1), small angle neutron ... ...

    Abstract Glycans of cellular glycoconjugates serve as biochemical signals for a multitude of (patho)physiological processes via binding to their receptors (e.g. lectins). In the case of human adhesion/growth-regulatory galectin-1 (Gal-1), small angle neutron scattering and fluorescence correlation spectroscopy have revealed a significant decrease of its gyration radius and increase of its diffusion coefficient upon binding lactose, posing the pertinent question on the nature and region(s) involved in the underlying structural alterations. Requiring neither a neutron source nor labeling, diffusion measurements by
    MeSH term(s) Deuterium Exchange Measurement ; Galectin 1/chemistry ; Humans ; Nuclear Magnetic Resonance, Biomolecular
    Chemical Substances Galectin 1 ; LGALS1 protein, human
    Language English
    Publishing date 2021-05-19
    Publishing country France
    Document type Journal Article
    ZDB-ID 120345-9
    ISSN 1638-6183 ; 0300-9084
    ISSN (online) 1638-6183
    ISSN 0300-9084
    DOI 10.1016/j.biochi.2021.05.008
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.135: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  6. Article ; Online: What is the Sugar Code?

    Gabius, Hans-Joachim / Cudic, Maré / Diercks, Tammo / Kaltner, Herbert / Kopitz, Jürgen / Mayo, Kevin H / Murphy, Paul V / Oscarson, Stefan / Roy, René / Schedlbauer, Andreas / Toegel, Stefan / Romero, Antonio

    Chembiochem : a European journal of chemical biology

    2021  Volume 23, Issue 13, Page(s) e202100327

    Abstract: A code is defined by the nature of the symbols, which are used to generate information-storing combinations (e. g. oligo- and polymers). Like nucleic acids and proteins, oligo- and polysaccharides are ubiquitous, and they are a biochemical platform for ... ...

    Abstract A code is defined by the nature of the symbols, which are used to generate information-storing combinations (e. g. oligo- and polymers). Like nucleic acids and proteins, oligo- and polysaccharides are ubiquitous, and they are a biochemical platform for establishing molecular messages. Of note, the letters of the sugar code system (third alphabet of life) excel in coding capacity by making an unsurpassed versatility for isomer (code word) formation possible by variability in anomery and linkage position of the glycosidic bond, ring size and branching. The enzymatic machinery for glycan biosynthesis (writers) realizes this enormous potential for building a large vocabulary. It includes possibilities for dynamic editing/erasing as known from nucleic acids and proteins. Matching the glycome diversity, a large panel of sugar receptors (lectins) has developed based on more than a dozen folds. Lectins 'read' the glycan-encoded information. Hydrogen/coordination bonding and ionic pairing together with stacking and C-H/π-interactions as well as modes of spatial glycan presentation underlie the selectivity and specificity of glycan-lectin recognition. Modular design of lectins together with glycan display and the nature of the cognate glycoconjugate account for the large number of post-binding events. They give an entry to the glycan vocabulary its functional, often context-dependent meaning(s), hereby building the dictionary of the sugar code.
    MeSH term(s) Carbohydrates/chemistry ; Lectins/metabolism ; Nucleic Acids ; Polysaccharides/chemistry ; Sugars
    Chemical Substances Carbohydrates ; Lectins ; Nucleic Acids ; Polysaccharides ; Sugars
    Language English
    Publishing date 2021-09-22
    Publishing country Germany
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2020469-3
    ISSN 1439-7633 ; 1439-4227
    ISSN (online) 1439-7633
    ISSN 1439-4227
    DOI 10.1002/cbic.202100327
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  7. Article ; Online: Backbone and sidechain NMR assignments for the ribosome maturation factor RbfA from Escherichia coli.

    Schedlbauer, Andreas / Iturrioz, Idoia / Ochoa-Lizarralde, Borja / Çapuni, Retina / Han, Xu / de Astigarraga, Elisa / Diercks, Tammo / Fucini, Paola / Connell, Sean R

    Biomolecular NMR assignments

    2020  Volume 14, Issue 2, Page(s) 317–321

    Abstract: RbfA (ribosome binding factor A; 15.2 kDa) is a protein involved in ribosome biogenesis and has been shown to be important for growth at low temperatures and to act as a suppressor for a cold-sensitive mutation (C23U) in the ribosomal RNA of the small ... ...

    Abstract RbfA (ribosome binding factor A; 15.2 kDa) is a protein involved in ribosome biogenesis and has been shown to be important for growth at low temperatures and to act as a suppressor for a cold-sensitive mutation (C23U) in the ribosomal RNA of the small 30S ribosomal subunit. The 3D structure of isolated RbfA has been determined from several organisms showing that RbfA has type-II KH-domain fold topology similar to the KH domain of another assembly factor, Era, whose overexpression can compensate for the deletion of rbfA, suppressing both the cold sensitivity and abnormal accumulation of 17S rRNA in rbfA knockout stains. Interestingly, a RbfAΔ25 variant used in previous NMR studies, truncated at the C-terminal domain to remove 25 unstructured residues causing aggregation at room temperature, was biologically active in the sense that it could complement a knock-out of wildtype RbfA, although it did not act as a suppressor for a 16S cold-sensitive mutation (C23U), nor did it interact stably with the 30S subunit. To complement this work, we report the
    MeSH term(s) Amino Acid Sequence ; Escherichia coli/metabolism ; Escherichia coli Proteins/analysis ; Escherichia coli Proteins/chemistry ; Nuclear Magnetic Resonance, Biomolecular ; Protein Structure, Secondary ; Ribosomal Proteins/analysis ; Ribosomal Proteins/chemistry ; Ribosomes/metabolism
    Chemical Substances Escherichia coli Proteins ; RbfA protein, E coli ; Ribosomal Proteins
    Language English
    Publishing date 2020-07-15
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2388861-1
    ISSN 1874-270X ; 1874-2718
    ISSN (online) 1874-270X
    ISSN 1874-2718
    DOI 10.1007/s12104-020-09969-0
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  8. Article ; Online: Binding of the protein ICln to α-integrin contributes to the activation of ICl

    Schedlbauer, Andreas / Tamma, Grazia / Rodighiero, Simona / Civello, Davide Antonio / Tamplenizza, Margherita / Ledolter, Karin / Nofziger, Charity / Patsch, Wolfgang / Konrat, Robert / Paulmichl, Markus / Dossena, Silvia

    Scientific reports

    2019  Volume 9, Issue 1, Page(s) 12195

    Abstract: ... ...

    Abstract ICl
    MeSH term(s) Animals ; Blood Platelets/metabolism ; Cell Membrane/genetics ; Cell Membrane/metabolism ; Chloride Channels/genetics ; Chloride Channels/metabolism ; Dogs ; HEK293 Cells ; Humans ; Integrin alpha Chains/genetics ; Integrin alpha Chains/metabolism ; Ion Transport ; Madin Darby Canine Kidney Cells
    Chemical Substances Chloride Channels ; Integrin alpha Chains
    Language English
    Publishing date 2019-08-21
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-019-48496-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Author Correction: Binding of the protein ICln to α-integrin contributes to the activation of ICl

    Schedlbauer, Andreas / Tamma, Grazia / Rodighiero, Simona / Civello, Davide Antonio / Tamplenizza, Margherita / Ledolter, Karin / Nofziger, Charity / Patsch, Wolfgang / Konrat, Robert / Paulmichl, Markus / Dossena, Silvia

    Scientific reports

    2019  Volume 9, Issue 1, Page(s) 17107

    Abstract: An amendment to this paper has been published and can be accessed via a link at the top of the paper. ...

    Abstract An amendment to this paper has been published and can be accessed via a link at the top of the paper.
    Language English
    Publishing date 2019-11-14
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-019-53690-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: The Novel Aminomethylcycline Omadacycline Has High Specificity for the Primary Tetracycline-Binding Site on the Bacterial Ribosome.

    Heidrich, Corina G / Mitova, Sanya / Schedlbauer, Andreas / Connell, Sean R / Fucini, Paola / Steenbergen, Judith N / Berens, Christian

    Antibiotics (Basel, Switzerland)

    2016  Volume 5, Issue 4

    Abstract: Omadacycline is an aminomethylcycline antibiotic with potent activity against many Gram-positive and Gram-negative pathogens, including strains carrying the major efflux and ribosome protection resistance determinants. This makes it a promising candidate ...

    Abstract Omadacycline is an aminomethylcycline antibiotic with potent activity against many Gram-positive and Gram-negative pathogens, including strains carrying the major efflux and ribosome protection resistance determinants. This makes it a promising candidate for therapy of severe infectious diseases. Omadacycline inhibits bacterial protein biosynthesis and competes with tetracycline for binding to the ribosome. Its interactions with the 70S ribosome were, therefore, analyzed in great detail and compared with tigecycline and tetracycline. All three antibiotics are inhibited by mutations in the 16S rRNA that mediate resistance to tetracycline in Brachyspira hyodysenteriae, Helicobacter pylori, Mycoplasma hominis, and Propionibacterium acnes. Chemical probing with dimethyl sulfate and Fenton cleavage with iron(II)-complexes of the tetracycline derivatives revealed that each antibiotic interacts in an idiosyncratic manner with the ribosome. X-ray crystallography had previously revealed one primary binding site for tetracycline on the ribosome and up to five secondary sites. All tetracyclines analyzed here interact with the primary site and tetracycline also with two secondary sites. In addition, each derivative displays a unique set of non-specific interactions with the 16S rRNA.
    Language English
    Publishing date 2016-09-22
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2681345-2
    ISSN 2079-6382
    ISSN 2079-6382
    DOI 10.3390/antibiotics5040032
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