LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 8 of total 8

Search options

  1. Article ; Online: Reply to: How Many SARS-CoV-2 "Viroporins" Are Really Ion Channels?

    Toft-Bertelsen, Trine L / Jeppesen, Mads Gravers / Landbrug, Asante / Mujezinovic, Amer / Bentzen, Bo Hjorth / Kledal, Thomas Nitschke / Rosenkilde, Mette Marie

    Communications biology

    2022  Volume 5, Issue 1, Page(s) 860

    MeSH term(s) COVID-19 ; Humans ; Ion Channels ; SARS-CoV-2 ; Viral Proteins/metabolism ; Viroporin Proteins
    Chemical Substances Ion Channels ; Viral Proteins ; Viroporin Proteins
    Language English
    Publishing date 2022-08-25
    Publishing country England
    Document type Letter ; Comment
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-022-03670-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  2. Article ; Online: Publisher Correction: Reply to: How many SARS-CoV-2 "viroporins" are really ion channels?

    Toft-Bertelsen, Trine L / Jeppesen, Mads Gravers / Landbrug, Asante / Mujezinovic, Amer / Bentzen, Bo Hjorth / Kledal, Thomas Nitschke / Rosenkilde, Mette Marie

    Communications biology

    2022  Volume 5, Issue 1, Page(s) 1017

    Language English
    Publishing date 2022-09-27
    Publishing country England
    Document type Published Erratum
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-022-03982-w
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  3. Article ; Online: Author Correction: Amantadine inhibits known and novel ion channels encoded by SARS-CoV-2 in vitro.

    Toft-Bertelsen, Trine Lisberg / Jeppesen, Mads Gravers / Tzortzini, Eva / Xue, Kai / Giller, Karin / Becker, Stefan / Mujezinovic, Amer / Bentzen, Bo Hjorth / Andreas, Loren B / Kolocouris, Antonios / Kledal, Thomas Nitschke / Rosenkilde, Mette Marie

    Communications biology

    2021  Volume 4, Issue 1, Page(s) 1402

    Language English
    Publishing date 2021-12-10
    Publishing country England
    Document type Published Erratum
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-021-02940-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  4. Article ; Online: Amantadine has potential for the treatment of COVID-19 because it inhibits known and novel ion channels encoded by SARS-CoV-2.

    Toft-Bertelsen, Trine Lisberg / Jeppesen, Mads Gravers / Tzortzini, Eva / Xue, Kai / Giller, Karin / Becker, Stefan / Mujezinovic, Amer / Bentzen, Bo Hjorth / B Andreas, Loren / Kolocouris, Antonios / Kledal, Thomas Nitschke / Rosenkilde, Mette Marie

    Communications biology

    2021  Volume 4, Issue 1, Page(s) 1347

    Abstract: The dire need for COVID-19 treatments has inspired strategies of repurposing approved drugs. Amantadine has been suggested as a candidate, and cellular as well as clinical studies have indicated beneficial effects of this drug. We demonstrate that ... ...

    Abstract The dire need for COVID-19 treatments has inspired strategies of repurposing approved drugs. Amantadine has been suggested as a candidate, and cellular as well as clinical studies have indicated beneficial effects of this drug. We demonstrate that amantadine and hexamethylene-amiloride (HMA), but not rimantadine, block the ion channel activity of Protein E from SARS-CoV-2, a conserved viroporin among coronaviruses. These findings agree with their binding to Protein E as evaluated by solution NMR and molecular dynamics simulations. Moreover, we identify two novel viroporins of SARS-CoV-2; ORF7b and ORF10, by showing ion channel activity in a X. laevis oocyte expression system. Notably, amantadine also blocks the ion channel activity of ORF10, thereby providing two ion channel targets in SARS-CoV-2 for amantadine treatment in COVID-19 patients. A screen of known viroporin inhibitors on Protein E, ORF7b, ORF10 and Protein 3a from SARS-CoV-2 revealed inhibition of Protein E and ORF7b by emodin and xanthene, the latter also blocking Protein 3a. This illustrates a general potential of well-known ion channel blockers against SARS-CoV-2 and specifically a dual molecular basis for the promising effects of amantadine in COVID-19 treatment. We therefore propose amantadine as a novel, cheap, readily available and effective way to treat COVID-19.
    MeSH term(s) Amantadine/pharmacology ; Amiloride/analogs & derivatives ; Amiloride/pharmacology ; Antiviral Agents/pharmacology ; Ion Channels/physiology ; Rimantadine/pharmacology ; SARS-CoV-2/drug effects ; Viral Proteins/physiology
    Chemical Substances Antiviral Agents ; Ion Channels ; Viral Proteins ; Rimantadine (0T2EF4JQTU) ; 5-(N,N-hexamethylene)amiloride (1428-95-1) ; Amiloride (7DZO8EB0Z3) ; Amantadine (BF4C9Z1J53)
    Language English
    Publishing date 2021-12-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-021-02866-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  5. Article: Crystal structure of the bovine mitochondrial elongation factor Tu.Ts complex.

    Jeppesen, Mads Gravers / Navratil, Tomas / Spremulli, Linda Lucy / Nyborg, Jens

    The Journal of biological chemistry

    2004  Volume 280, Issue 6, Page(s) 5071–5081

    Abstract: The three-dimensional structure of the bovine mitochondrial elongation factor (EF)-Tu.Ts complex (EF-Tumt.Tsmt) has been determined to 2.2-A resolution using the multi-wavelength anomalous dispersion experimental method. This complex provides the first ... ...

    Abstract The three-dimensional structure of the bovine mitochondrial elongation factor (EF)-Tu.Ts complex (EF-Tumt.Tsmt) has been determined to 2.2-A resolution using the multi-wavelength anomalous dispersion experimental method. This complex provides the first insight into the structure of EF-Tsmt. EF-Tsmt is similar to Escherichia coli and Thermus thermophilus EF-Ts in the amino-terminal domain. However, the structure of EF-Tsmt deviates considerably in the core domain with a five-stranded beta-sheet forming a portion of subdomain N of the core. In E. coli EF-Ts, this region is composed of a three-stranded sheet. The coiled-coil domain of the E. coli EF-Ts is largely eroded in EF-Tsmt, in which it consists of a large loop packed against subdomain C of the core. The conformation of bovine EF-Tumt in complex with EF-Tsmt is distinct from its conformation in the EF-Tumt.GDP complex. When domain III of bovine EF-Tumt.GDP is superimposed on domain III of EF-Tumt in the EF-Tumt.Tsmt complex, helix B from domain I is also almost superimposed. However, the rest of domain I is rotated relative to this helix toward domain II, which itself is rotated toward domain I relative to domain III. Extensive contacts are observed between the amino-terminal domain of EF-Tsmt and domain I of EF-Tumt. Furthermore, the conserved TDFV sequence of EF-Tsmt also contacts domain I with the side chain of Asp139 contacting helix B of EF-Tumt and inserting the side chain of Phe140 between helices B and C. The structure of the EF-Tumt.Tsmt complex provides new insights into the nucleotide exchange mechanism and provides a framework for explaining much of the mutational data obtained for this complex.
    MeSH term(s) Amino Acid Sequence ; Animals ; Cattle ; Cloning, Molecular ; Crystallography, X-Ray/methods ; Escherichia coli/metabolism ; Guanine/chemistry ; Models, Molecular ; Molecular Sequence Data ; Peptide Elongation Factor Tu/chemistry ; Peptide Elongation Factors/chemistry ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Thermus thermophilus/metabolism
    Chemical Substances Peptide Elongation Factors ; elongation factor Ts ; Guanine (5Z93L87A1R) ; Peptide Elongation Factor Tu (EC 3.6.1.-)
    Language English
    Publishing date 2004-11-22
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M411782200
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article: Mg2+ and a key lysine modulate exchange activity of eukaryotic translation elongation factor 1B alpha.

    Pittman, Yvette R / Valente, Louis / Jeppesen, Mads Gravers / Andersen, Gregers Rom / Patel, Smita / Kinzy, Terri Goss

    The Journal of biological chemistry

    2006  Volume 281, Issue 28, Page(s) 19457–19468

    Abstract: To sustain efficient translation, eukaryotic elongation factor B alpha (eEF1B alpha) functions as the guanine nucleotide exchange factor for eEF1A. Stopped-flow kinetics using 2'-(or 3')-O-N-methylanthraniloyl (mant)-GDP showed spontaneous release of ... ...

    Abstract To sustain efficient translation, eukaryotic elongation factor B alpha (eEF1B alpha) functions as the guanine nucleotide exchange factor for eEF1A. Stopped-flow kinetics using 2'-(or 3')-O-N-methylanthraniloyl (mant)-GDP showed spontaneous release of nucleotide from eEF1A is extremely slow and accelerated 700-fold by eEF1B alpha. The eEF1B alpha-stimulated reaction was inhibited by Mg2+ with a K(1/2) of 3.8 mM. Previous structural studies predicted the Lys-205 residue of eEF1B alpha plays an important role in promoting nucleotide exchange by disrupting the Mg2+ binding site. Co-crystal structures of the lethal K205A mutant in the catalytic C terminus of eEF1B alpha with eEF1A and eEF1A.GDP established that the lethality was not due to a structural defect. Instead, the K205A mutant drastically reduced the nucleotide exchange activity even at very low concentrations of Mg2+. A K205R eEF1B alpha mutant on the other hand was functional in vivo and showed nearly wild-type nucleotide dissociation rates but almost no sensitivity to Mg2+. These results indicate the significant role of Mg2+ in the nucleotide exchange reaction by eEF1B alpha and establish the catalytic function of Lys-205 in displacing Mg2+ from its binding site.
    MeSH term(s) Catalysis ; Eukaryotic Initiation Factor-1/metabolism ; Fungal Proteins/chemistry ; Guanosine Diphosphate/chemistry ; Kinetics ; Lysine/chemistry ; Magnesium/chemistry ; Models, Molecular ; Mutation ; Nucleotides/chemistry ; Peptide Elongation Factor 1/chemistry ; Peptide Elongation Factor 1/genetics ; Peptide Elongation Factors/chemistry ; Protein Structure, Tertiary ; Saccharomyces cerevisiae/metabolism
    Chemical Substances Eukaryotic Initiation Factor-1 ; Fungal Proteins ; Nucleotides ; Peptide Elongation Factor 1 ; Peptide Elongation Factors ; Guanosine Diphosphate (146-91-8) ; Magnesium (I38ZP9992A) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2006-05-04
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M601076200
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article: Crystallization and preliminary X-ray diffraction study of mammalian mitochondrial seryl-tRNA synthetase.

    Chimnaronk, Sarin / Jeppesen, Mads Gravers / Shimada, Nobukazu / Suzuki, Tsutomu / Nyborg, Jens / Watanabe, Kimitsuna

    Acta crystallographica. Section D, Biological crystallography

    2004  Volume 60, Issue Pt 7, Page(s) 1319–1322

    Abstract: The mitochondrial seryl-tRNA synthetase (mt SerRS) from Bos taurus was overexpressed in Escherichia coli and crystallized using the sitting-drop vapour-diffusion method. Crystals grew in a very narrow range of conditions using PEG 8000 as precipitant at ... ...

    Abstract The mitochondrial seryl-tRNA synthetase (mt SerRS) from Bos taurus was overexpressed in Escherichia coli and crystallized using the sitting-drop vapour-diffusion method. Crystals grew in a very narrow range of conditions using PEG 8000 as precipitant at room temperature. An appropriate concentration of lithium sulfate was critical for crystal nucleation. Crystals diffracted well beyond a resolution of 1.6 A and were found to belong to the orthorhombic space group C222(1), with unit-cell parameters a = 79.89, b = 230.42, c = 135.60 A. There is one dimer (M(r) approximately 113 kDa) in the asymmetric unit, with a solvent content of 55%. Efforts to solve the phase problem by molecular replacement are under way.
    MeSH term(s) Animals ; Base Sequence ; Cattle ; Crystallization ; Crystallography, X-Ray ; Gene Expression ; Mitochondria/enzymology ; Mitochondria/genetics ; Nucleic Acid Conformation ; Serine-tRNA Ligase/chemistry ; Serine-tRNA Ligase/genetics ; Serine-tRNA Ligase/isolation & purification
    Chemical Substances Serine-tRNA Ligase (EC 6.1.1.11)
    Language English
    Publishing date 2004-07
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2020492-9
    ISSN 2059-7983 ; 1399-0047 ; 0907-4449
    ISSN (online) 2059-7983 ; 1399-0047
    ISSN 0907-4449
    DOI 10.1107/S0907444904011217
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  8. Article: The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae.

    Jeppesen, Mads Gravers / Ortiz, Pedro / Shepard, William / Kinzy, Terri Goss / Nyborg, Jens / Andersen, Gregers Rom

    The Journal of biological chemistry

    2003  Volume 278, Issue 47, Page(s) 47190–47198

    Abstract: The crystal structure of the N-terminal 219 residues (domain 1) of the conserved eukaryotic translation elongation factor 1Bgamma (eEF1Bgamma), encoded by the TEF3 gene in Saccharomyces cerevisiae, has been determined at 3.0 A resolution by the single ... ...

    Abstract The crystal structure of the N-terminal 219 residues (domain 1) of the conserved eukaryotic translation elongation factor 1Bgamma (eEF1Bgamma), encoded by the TEF3 gene in Saccharomyces cerevisiae, has been determined at 3.0 A resolution by the single wavelength anomalous dispersion technique. The structure is overall very similar to the glutathione S-transferase proteins and contains a pocket with architecture highly homologous to what is observed in glutathione S-transferase enzymes. The TEF3-encoded form of eEF1Bgamma has no obvious catalytic residue. However, the second form of eEF1Bgamma encoded by the TEF4 gene contains serine 11, which may act catalytically. Based on the x-ray structure and gel filtration studies, we suggest that the yeast eEF1 complex is organized as an [eEF1A.eEF1Balpha.eEF1Bgamma]2 complex. A 23-residue sequence in the middle of eEF1Bgamma is essential for the stable dimerization of eEF1Bgamma and the quaternary structure of the eEF1 complex.
    MeSH term(s) Amino Acid Sequence ; Crystallography, X-Ray ; Dimerization ; Glutathione Transferase/chemistry ; Molecular Structure ; Peptide Elongation Factor 1/chemistry ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Saccharomyces cerevisiae Proteins/chemistry
    Chemical Substances Peptide Elongation Factor 1 ; Saccharomyces cerevisiae Proteins ; Glutathione Transferase (EC 2.5.1.18)
    Language English
    Publishing date 2003-09-12
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M306630200
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top