LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Back to previous search Search history
Advanced search

Your last searches

  1. AU="Vesper, Oliver"
  2. AU="Langley, Avery A"

Search results

Result 1 - 10 of total 18

Search options

  1. Article ; Online: Mechanism of AAA+ ATPase-mediated RuvAB-Holliday junction branch migration.

    Wald, Jiri / Fahrenkamp, Dirk / Goessweiner-Mohr, Nikolaus / Lugmayr, Wolfgang / Ciccarelli, Luciano / Vesper, Oliver / Marlovits, Thomas C

    Nature

    2022  Volume 609, Issue 7927, Page(s) 630–639

    Abstract: The Holliday junction is a key intermediate formed during DNA recombination across all kingdoms of ... ...

    Abstract The Holliday junction is a key intermediate formed during DNA recombination across all kingdoms of life
    MeSH term(s) ATPases Associated with Diverse Cellular Activities/chemistry ; ATPases Associated with Diverse Cellular Activities/metabolism ; ATPases Associated with Diverse Cellular Activities/ultrastructure ; Adenosine Triphosphate/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Bacterial Proteins/ultrastructure ; Cryoelectron Microscopy ; DNA Helicases/chemistry ; DNA Helicases/metabolism ; DNA Helicases/ultrastructure ; DNA, Cruciform/chemistry ; DNA, Cruciform/metabolism ; DNA, Cruciform/ultrastructure ; DNA, Single-Stranded/chemistry ; DNA, Single-Stranded/metabolism ; DNA, Single-Stranded/ultrastructure ; Homologous Recombination ; Hydrolysis ; Multienzyme Complexes/chemistry ; Multienzyme Complexes/metabolism ; Multienzyme Complexes/ultrastructure ; Nucleotides ; Protein Conformation ; Rotation
    Chemical Substances Bacterial Proteins ; DNA, Cruciform ; DNA, Single-Stranded ; Multienzyme Complexes ; Nucleotides ; RuvB protein, Bacteria ; Adenosine Triphosphate (8L70Q75FXE) ; ATPases Associated with Diverse Cellular Activities (EC 3.6.4.-) ; DNA Helicases (EC 3.6.4.-)
    Language English
    Publishing date 2022-08-24
    Publishing country England
    Document type Journal Article
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-022-05121-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 26: 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)
    Zs.MG 9: Show issues
    Zs.MO 244: Show issues

    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.

  2. Article ; Online: Substrate-engaged type III secretion system structures reveal gating mechanism for unfolded protein translocation.

    Miletic, Sean / Fahrenkamp, Dirk / Goessweiner-Mohr, Nikolaus / Wald, Jiri / Pantel, Maurice / Vesper, Oliver / Kotov, Vadim / Marlovits, Thomas C

    Nature communications

    2021  Volume 12, Issue 1, Page(s) 1546

    Abstract: Many bacterial pathogens rely on virulent type III secretion systems (T3SSs) or injectisomes to translocate effector proteins in order to establish infection. The central component of the injectisome is the needle complex which assembles a continuous ... ...

    Abstract Many bacterial pathogens rely on virulent type III secretion systems (T3SSs) or injectisomes to translocate effector proteins in order to establish infection. The central component of the injectisome is the needle complex which assembles a continuous conduit crossing the bacterial envelope and the host cell membrane to mediate effector protein translocation. However, the molecular principles underlying type III secretion remain elusive. Here, we report a structure of an active Salmonella enterica serovar Typhimurium needle complex engaged with the effector protein SptP in two functional states, revealing the complete 800Å-long secretion conduit and unraveling the critical role of the export apparatus (EA) subcomplex in type III secretion. Unfolded substrates enter the EA through a hydrophilic constriction formed by SpaQ proteins, which enables side chain-independent substrate transport. Above, a methionine gasket formed by SpaP proteins functions as a gate that dilates to accommodate substrates while preventing leaky pore formation. Following gate penetration, a moveable SpaR loop first folds up to then support substrate transport. Together, these findings establish the molecular basis for substrate translocation through T3SSs and improve our understanding of bacterial pathogenicity and motility.
    MeSH term(s) Antigens, Bacterial/chemistry ; Antigens, Bacterial/genetics ; Antigens, Bacterial/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cryoelectron Microscopy ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Models, Molecular ; Protein Conformation, alpha-Helical ; Protein Transport/physiology ; Salmonella enterica/metabolism ; Salmonella typhimurium/genetics ; Salmonella typhimurium/metabolism ; Type III Secretion Systems/chemistry ; Type III Secretion Systems/genetics ; Type III Secretion Systems/metabolism
    Chemical Substances Antigens, Bacterial ; Bacterial Proteins ; Membrane Proteins ; SpaQ protein, Salmonella ; Type III Secretion Systems
    Language English
    Publishing date 2021-03-09
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-021-21143-1
    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.

  3. Article ; Online: Correction for Kumar et al., "Escherichia coli Quorum-Sensing EDF, A Peptide Generated by Novel Multiple Distinct Mechanisms and Regulated by

    Kumar, Sathish / Kolodkin-Gal, Ilana / Vesper, Oliver / Alam, Nawsad / Schueler-Furman, Ora / Moll, Isabella / Engelberg-Kulka, Hanna

    mBio

    2021  Volume 12, Issue 1

    Language English
    Publishing date 2021-02-02
    Publishing country United States
    Document type Journal Article ; Published Erratum
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mBio.03436-20
    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.

  4. Article: Marktorientiertes Controlling in den USA und Deutschland

    Link, Jörg / Vesper, Oliver

    Herausforderungen der internationalen marktorientierten Unternehmensführung : Festschrift für Reinhard Hünerberg , p. 325-349

    2011  , Page(s) 325–349

    Author's details Jörg Link; Oliver Vesper
    Keywords Controlling ; Marketingmanagement ; Vergleich ; Deutschland ; USA
    Language German
    Size graph. Darst.
    Publisher Gabler
    Publishing place Wiesbaden
    Document type Article
    ISBN 978-3-8349-2403-2 ; 3-8349-2403-2
    Database ECONomics Information System

    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: Insights into the Stress Response Triggered by Kasugamycin in Escherichia coli.

    Müller, Christian / Sokol, Lena / Vesper, Oliver / Sauert, Martina / Moll, Isabella

    Antibiotics (Basel, Switzerland)

    2016  Volume 5, Issue 2

    Abstract: The bacteriostatic aminoglycoside antibiotic kasugamycin inhibits protein synthesis at an initial step without affecting translation elongation. It binds to the mRNA track of the ribosome and prevents formation of the translation initiation complex on ... ...

    Abstract The bacteriostatic aminoglycoside antibiotic kasugamycin inhibits protein synthesis at an initial step without affecting translation elongation. It binds to the mRNA track of the ribosome and prevents formation of the translation initiation complex on canonical mRNAs. In contrast, translation of leaderless mRNAs continues in the presence of the drug in vivo. Previously, we have shown that kasugamycin treatment in E. coli stimulates the formation of protein-depleted ribosomes that are selective for leaderless mRNAs. Here, we provide evidence that prolonged kasugamycin treatment leads to selective synthesis of specific proteins. Our studies indicate that leaderless and short-leadered mRNAs are generated by different molecular mechanisms including alternative transcription and RNA processing. Moreover, we provide evidence for ribosome heterogeneity in response to kasugamycin treatment by alteration of the modification status of the stalk proteins bL7/L12.
    Language English
    Publishing date 2016-06-01
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2681345-2
    ISSN 2079-6382
    ISSN 2079-6382
    DOI 10.3390/antibiotics5020019
    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.

  6. Book ; Online ; Thesis: Analyse funktioneller Komplexe des Ribosoms in Regulations- und Teriminationsprozessen

    Vesper, Oliver [Verfasser]

    2007  

    Author's details vorgelegt von Oliver Vesper
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language German
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

    Full text online

    More links

    Kategorien

    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.

  7. Article ; Online: Ribosome heterogeneity: another level of complexity in bacterial translation regulation.

    Byrgazov, Konstantin / Vesper, Oliver / Moll, Isabella

    Current opinion in microbiology

    2013  Volume 16, Issue 2, Page(s) 133–139

    Abstract: Translation of the mRNA-encoded genetic information into proteins is catalyzed by the intricate ribonucleoprotein machine, the ribosome. Historically, the bacterial ribosome is viewed as an unchangeable entity, constantly equipped with the entire ... ...

    Abstract Translation of the mRNA-encoded genetic information into proteins is catalyzed by the intricate ribonucleoprotein machine, the ribosome. Historically, the bacterial ribosome is viewed as an unchangeable entity, constantly equipped with the entire complement of RNAs and proteins. Conversely, several lines of evidence indicate the presence of functional selective ribosomal subpopulations that exhibit variations in the RNA or the protein components and modulate the translational program in response to environmental changes. Here, we summarize these findings, which raise the functional status of the ribosome from a protein synthesis machinery only to a regulatory hub that integrates environmental cues in the process of protein synthesis, thereby adding an additional level of complexity to the regulation of gene expression.
    MeSH term(s) Bacteria/genetics ; Bacteria/metabolism ; Gene Expression Regulation, Bacterial ; Genetic Variation ; Protein Biosynthesis ; Ribosomes/genetics ; Ribosomes/metabolism
    Language English
    Publishing date 2013-02-14
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1418474-6
    ISSN 1879-0364 ; 1369-5274
    ISSN (online) 1879-0364
    ISSN 1369-5274
    DOI 10.1016/j.mib.2013.01.009
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 5514: 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)
    Zs.MG 51: Show issues

    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 ; Online: The MazF-regulon: a toolbox for the post-transcriptional stress response in Escherichia coli.

    Sauert, Martina / Wolfinger, Michael T / Vesper, Oliver / Müller, Christian / Byrgazov, Konstantin / Moll, Isabella

    Nucleic acids research

    2016  Volume 44, Issue 14, Page(s) 6660–6675

    Abstract: Flexible adaptation to environmental stress is vital for bacteria. An energy-efficient post-transcriptional stress response mechanism in Escherichia coli is governed by the toxin MazF. After stress-induced activation the endoribonuclease MazF processes a ...

    Abstract Flexible adaptation to environmental stress is vital for bacteria. An energy-efficient post-transcriptional stress response mechanism in Escherichia coli is governed by the toxin MazF. After stress-induced activation the endoribonuclease MazF processes a distinct subset of transcripts as well as the 16S ribosomal RNA in the context of mature ribosomes. As these 'stress-ribosomes' are specific for the MazF-processed mRNAs, the translational program is changed. To identify this 'MazF-regulon' we employed Poly-seq (polysome fractionation coupled with RNA-seq analysis) and analyzed alterations introduced into the transcriptome and translatome after mazF overexpression. Unexpectedly, our results reveal that the corresponding protein products are involved in all cellular processes and do not particularly contribute to the general stress response. Moreover, our findings suggest that translational reprogramming serves as a fast-track reaction to harsh stress and highlight the so far underestimated significance of selective translation as a global regulatory mechanism in gene expression. Considering the reported implication of toxin-antitoxin (TA) systems in persistence, our results indicate that MazF acts as a prime effector during harsh stress that potentially introduces translational heterogeneity within a bacterial population thereby stimulating persister cell formation.
    MeSH term(s) Base Sequence ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Endoribonucleases/genetics ; Endoribonucleases/metabolism ; Escherichia coli/genetics ; Escherichia coli/physiology ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Polyribosomes/metabolism ; Protein Biosynthesis/genetics ; RNA/isolation & purification ; RNA Processing, Post-Transcriptional/genetics ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Regulon/genetics ; Reproducibility of Results ; Sequence Analysis, RNA ; Stress, Physiological/genetics ; Transcription, Genetic
    Chemical Substances DNA-Binding Proteins ; Escherichia coli Proteins ; MazF protein, E coli ; RNA, Messenger ; RNA (63231-63-0) ; Endoribonucleases (EC 3.1.-)
    Language English
    Publishing date 2016-02-22
    Publishing country England
    Document type Journal Article
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkw115
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1067: 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)

    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.

  9. Article: [Ribosome recycling revisited].

    Vesper, Oliver / Wilson, Daniel N

    Molekuliarnaia biologiia

    2006  Volume 40, Issue 4, Page(s) 742–750

    Abstract: Ribosome recycling involves the coordinated action of the ribosome recycling factor (RRF), elongation factor EF-G and initiation factor IF3 to disassemble the post-termination complex, recycling the components for the next round of translation. The ... ...

    Abstract Ribosome recycling involves the coordinated action of the ribosome recycling factor (RRF), elongation factor EF-G and initiation factor IF3 to disassemble the post-termination complex, recycling the components for the next round of translation. The crystal structure of domain I of RRF (RRF-DI) in complex with the large ribosomal subunit from the eubacteria Deinococcus radiodurans at high resolution reveals the nature and details of the interactions between this protein factor and rRNA/protein components of the ribosome. Universally conserved arginine residues within the RRF-DI establish important interactions with nuleotides of the 23S rRNA, explaining why mutations at these positions abolish factor binding. Furthermore, in conjunction with cryo-EM reconstruction, the X-ray analysis provides a structural complement to the recent biochemical data, offering additional insight into the mechanism of ribosome recycling.
    MeSH term(s) Arginine/metabolism ; Bacteria/genetics ; Bacteria/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Deinococcus/metabolism ; Eukaryotic Initiation Factor-3/genetics ; Eukaryotic Initiation Factor-3/metabolism ; Models, Molecular ; Mutation ; Peptide Elongation Factor G/genetics ; Peptide Elongation Factor G/metabolism ; Protein Binding ; Protein Biosynthesis/genetics ; Protein Biosynthesis/physiology ; Protein Conformation ; Ribosomal Proteins/chemistry ; Ribosomal Proteins/genetics ; Ribosomal Proteins/metabolism ; Ribosomes/physiology
    Chemical Substances Bacterial Proteins ; Eukaryotic Initiation Factor-3 ; Peptide Elongation Factor G ; Ribosomal Proteins ; ribosome releasing factor ; Arginine (94ZLA3W45F)
    Language Russian
    Publishing date 2006-07
    Publishing country Russia (Federation)
    Document type English Abstract ; Journal Article ; Review
    ZDB-ID 213542-5
    ISSN 0026-8984
    ISSN 0026-8984
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.B 1796: 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.

  10. Article ; Online: In-depth interrogation of protein thermal unfolding data with MoltenProt.

    Kotov, Vadim / Mlynek, Georg / Vesper, Oliver / Pletzer, Marina / Wald, Jiri / Teixeira-Duarte, Celso M / Celia, Herve / Garcia-Alai, Maria / Nussberger, Stephan / Buchanan, Susan K / Morais-Cabral, João H / Loew, Christian / Djinovic-Carugo, Kristina / Marlovits, Thomas C

    Protein science : a publication of the Protein Society

    2020  Volume 30, Issue 1, Page(s) 201–217

    Abstract: Protein stability is a key factor in successful structural and biochemical research. However, the approaches for systematic comparison of protein stability are limited by sample consumption or compatibility with sample buffer components. Here we describe ...

    Abstract Protein stability is a key factor in successful structural and biochemical research. However, the approaches for systematic comparison of protein stability are limited by sample consumption or compatibility with sample buffer components. Here we describe how miniaturized measurement of intrinsic tryptophan fluorescence (NanoDSF assay) in combination with a simplified description of protein unfolding can be used to interrogate the stability of a protein sample. We demonstrate that improved protein stability measures, such as apparent Gibbs free energy of unfolding, rather than melting temperature T
    MeSH term(s) Crystallography, X-Ray ; Hot Temperature ; Membrane Proteins/chemistry ; Multiprotein Complexes/chemistry ; Protein Folding ; Protein Unfolding ; Software
    Chemical Substances Membrane Proteins ; Multiprotein Complexes
    Language English
    Publishing date 2020-11-21
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural ; 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.3986
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 3407: 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)
    Zs.MO 1: Show issues

    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