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  1. Book ; Thesis: Role of DEAD-box RNA helicases in protein kinase regulation

    Švorinić, Andrea / Sinning, Irmgard

    2023  

    Institution Universität Heidelberg
    Author's details presented by Andrea Švorinić ; referees: Prof. Dr. Irmgard Sinning, Prof. Dr. Christof Niehrs
    Language English
    Size xiii, 118 Blätter, Illustrationen, Diagramme
    Publishing place Heidelberg
    Publishing country Germany
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Dissertation, Ruprecht-Karls-University Heidelberg, 2023
    Note Text Englisch, Zusammenfassung in englischer und deutscher Sprache
    HBZ-ID HT030344130
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2023 E 1258 order for loan Magazin

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  2. Book ; Thesis: Investigation and characterization of N-terminal aminopeptidase activity and degradation signal generation in yeast Saccharomyces cerevisiae

    Reinbold, Christian / Knop, Michael / Sinning, Irmgard

    2023  

    Institution Universität Heidelberg
    Author's details presented by M.Sc. Christain Reinbold ; referees: Prof. Dr. Michael Knop, Prof. Dr. Irmgard Sinning
    Subject code 570
    Language English
    Size xxi, 105 Seiten, Illustrationen, Diagramme
    Publishing place Heidelberg
    Publishing country Germany
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Dissertation, Ruperto Carola University Heidelberg, 2023
    Note Text Englisch, Zusammenfassung in englischer und deutscher Sprache
    HBZ-ID HT030638926
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2024 E 246 order for loan Magazin

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  3. Book ; Thesis: Tail-anchored membrane protein biogenesis by the GET insertase complex

    Heimes, Michael / Sinning, Irmgard

    2023  

    Institution Universität Heidelberg
    Author's details presented by M. Sc. Michael Heimes ; referees: Prof. Dr. Irmgard Sinning, Prof. Dr. Britta Brügger
    Subject code 570
    Language English
    Size VII, 167 Seiten, Illustrationen, Diagramme
    Publishing place Heidelberg
    Publishing country Germany
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Dissertation, Ruprechts-Karls-University Heidelberg, 2023
    Note Text Englisch, Zusammenfassung in englischer und deutscher Sprache ; References: 128-152
    HBZ-ID HT030626260
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2024 E 76 order for loan Magazin

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  4. Book ; Thesis: Studying the nascent polypeptide interactome of the ribosome-associated factor NAC by selective ribosome profiling

    Merker, Dorina / Bukau, Bernd / Sinning, Irmgard

    2020  

    Institution Universität Heidelberg
    Author's details presented by Dorina Merker ; referees : Prof. Dr. Bernd Bukau, Prof. Dr. Irmgard Sinning
    Subject code 570
    Language English
    Size II, 113 Seiten, Illustrationen, Diagramme, 30 cm
    Publishing place Heidelberg
    Publishing country Germany
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Dissertation, Ruperto Carola University Heidelberg, Germany, 2020
    Note Zusammenfassungen in deutscher und englischer Sprache
    HBZ-ID HT020893638
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2021 E 465 order for loan Magazin

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  5. Article ; Online: Methionine aminopeptidase 2 and its autoproteolysis product have different binding sites on the ribosome.

    Klein, Marius A / Wild, Klemens / Kišonaitė, Miglė / Sinning, Irmgard

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 716

    Abstract: Excision of the initiator methionine is among the first co-translational processes that occur at the ribosome. While this crucial step in protein maturation is executed by two types of methionine aminopeptidases in eukaryotes (MAP1 and MAP2), additional ... ...

    Abstract Excision of the initiator methionine is among the first co-translational processes that occur at the ribosome. While this crucial step in protein maturation is executed by two types of methionine aminopeptidases in eukaryotes (MAP1 and MAP2), additional roles in disease and translational regulation have drawn more attention to MAP2. Here, we report several cryo-EM structures of human and fungal MAP2 at the 80S ribosome. Irrespective of nascent chains, MAP2 can occupy the tunnel exit. On nascent chain displaying ribosomes, the MAP2-80S interaction is highly dynamic and the MAP2-specific N-terminal extension engages in stabilizing interactions with the long rRNA expansion segment ES27L. Loss of this extension by autoproteolytic cleavage impedes interactions at the tunnel, while promoting MAP2 to enter the ribosomal A-site, where it engages with crucial functional centers of translation. These findings reveal that proteolytic remodeling of MAP2 severely affects ribosome binding, and set the stage for targeted functional studies.
    MeSH term(s) Humans ; Aminopeptidases/genetics ; Ribosomes ; Binding Sites ; Methionine ; Metalloendopeptidases
    Chemical Substances methionine aminopeptidase 2 (EC 3.4.11.18) ; Aminopeptidases (EC 3.4.11.-) ; Methionine (AE28F7PNPL) ; Metalloendopeptidases (EC 3.4.24.-)
    Language English
    Publishing date 2024-01-24
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-44862-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Cryo-EM insights into tail-anchored membrane protein biogenesis in eukaryotes.

    Sinning, Irmgard / McDowell, Melanie A

    Current opinion in structural biology

    2022  Volume 75, Page(s) 102428

    Abstract: Tail-anchored (TA) proteins are a biologically significant class of membrane proteins, which require specialised cellular pathways to insert their single C-terminal transmembrane domain into the correct membrane. Cryo-electron microscopy has recently ... ...

    Abstract Tail-anchored (TA) proteins are a biologically significant class of membrane proteins, which require specialised cellular pathways to insert their single C-terminal transmembrane domain into the correct membrane. Cryo-electron microscopy has recently provided new insights into the organelle-specific machineries for TA protein biogenesis. Structures of targeting and insertase complexes within the canonical guided entry of TA proteins (GET) pathway indicate how substrates are faithfully chaperoned into the endoplasmic reticulum (ER) membrane in metazoans. The core of the GET insertase is conserved within structures of the ER membrane protein complex (EMC), which acts in parallel to insert a different subset of TA proteins. Furthermore, structures of the dislocases Spf1 and Msp1 show how they remove mislocalised TA proteins from the ER and outer mitochondrial membranes respectively.
    MeSH term(s) ATP-Binding Cassette Transporters/metabolism ; Adenosine Triphosphatases/metabolism ; Cryoelectron Microscopy ; Endoplasmic Reticulum/metabolism ; Membrane Proteins/chemistry ; Protein Transport ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances ATP-Binding Cassette Transporters ; Membrane Proteins ; SPF1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Adenosine Triphosphatases (EC 3.6.1.-) ; MSP1 protein, S cerevisiae (EC 3.6.1.-)
    Language English
    Publishing date 2022-07-16
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2022.102428
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3206: 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: Structural and molecular mechanisms for membrane protein biogenesis by the Oxa1 superfamily.

    McDowell, Melanie A / Heimes, Michael / Sinning, Irmgard

    Nature structural & molecular biology

    2021  Volume 28, Issue 3, Page(s) 234–239

    Abstract: Members of the Oxa1 superfamily perform membrane protein insertion in bacteria, the eukaryotic endoplasmic reticulum (ER), and endosymbiotic organelles. Here, we review recent structures of the three ER-resident insertases and discuss the extent to which ...

    Abstract Members of the Oxa1 superfamily perform membrane protein insertion in bacteria, the eukaryotic endoplasmic reticulum (ER), and endosymbiotic organelles. Here, we review recent structures of the three ER-resident insertases and discuss the extent to which structure and function are conserved with their bacterial counterpart YidC.
    MeSH term(s) Binding Sites ; Electron Transport Complex IV/chemistry ; Electron Transport Complex IV/classification ; Electron Transport Complex IV/metabolism ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/metabolism ; Fungal Proteins/chemistry ; Fungal Proteins/metabolism ; Humans ; Membrane Proteins/biosynthesis ; Membrane Transport Proteins/chemistry ; Membrane Transport Proteins/metabolism ; Mitochondrial Proteins/chemistry ; Mitochondrial Proteins/classification ; Mitochondrial Proteins/metabolism ; Models, Molecular ; Nuclear Proteins/chemistry ; Nuclear Proteins/classification ; Nuclear Proteins/metabolism ; Protein Binding ; Protein Domains ; Substrate Specificity
    Chemical Substances Escherichia coli Proteins ; Fungal Proteins ; Membrane Proteins ; Membrane Transport Proteins ; Mitochondrial Proteins ; Nuclear Proteins ; OXA1 protein ; YIDC protein, E coli ; Electron Transport Complex IV (EC 1.9.3.1)
    Language English
    Publishing date 2021-03-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-021-00567-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4101: 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 56: Show issues

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  8. Article ; Online: High-resolution structures of a thermophilic eukaryotic 80S ribosome reveal atomistic details of translocation.

    Kišonaitė, Miglė / Wild, Klemens / Lapouge, Karine / Ruppert, Thomas / Sinning, Irmgard

    Nature communications

    2022  Volume 13, Issue 1, Page(s) 476

    Abstract: Ribosomes are complex and highly conserved ribonucleoprotein assemblies catalyzing protein biosynthesis in every organism. Here we present high-resolution cryo-EM structures of the 80S ribosome from a thermophilic fungus in two rotational states, which ... ...

    Abstract Ribosomes are complex and highly conserved ribonucleoprotein assemblies catalyzing protein biosynthesis in every organism. Here we present high-resolution cryo-EM structures of the 80S ribosome from a thermophilic fungus in two rotational states, which due to increased 80S stability provide a number of mechanistic details of eukaryotic translation. We identify a universally conserved 'nested base-triple knot' in the 26S rRNA at the polypeptide tunnel exit with a bulged-out nucleotide that likely serves as an adaptable element for nascent chain containment and handover. We visualize the structure and dynamics of the ribosome protective factor Stm1 upon ribosomal 40S head swiveling. We describe the structural impact of a unique and essential m
    MeSH term(s) Chaetomium/chemistry ; Chaetomium/metabolism ; Cryoelectron Microscopy/methods ; Peptide Elongation Factor 2/chemistry ; Peptide Elongation Factor 2/metabolism ; Protein Biosynthesis ; RNA, Ribosomal/chemistry ; RNA, Ribosomal/genetics ; RNA, Ribosomal/metabolism ; RNA, Transfer/metabolism ; Ribosomes/chemistry ; Ribosomes/metabolism
    Chemical Substances Peptide Elongation Factor 2 ; RNA, Ribosomal ; RNA, ribosomal, 26S ; RNA, Transfer (9014-25-9)
    Language English
    Publishing date 2022-01-25
    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/s41467-022-27967-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Book ; Online ; Thesis: In-cell structural biology of protein synthesis in Mycoplasma pneumoniae

    Xue, Liang [Verfasser] / Sinning, Irmgard [Akademischer Betreuer]

    2022  

    Author's details Liang Xue ; Betreuer: Irmgard Sinning
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Universitätsbibliothek Heidelberg
    Publishing place Heidelberg
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  10. Book ; Online ; Thesis: Structural studies of the human RNA polymerase I and the role of human RNA polymerase I and III in diseases.

    Misiaszek, Agata Dorota Verfasser] / [Sinning, Irmgard [Akademischer Betreuer]

    2022  

    Author's details Agata Dorota Misiaszek ; Betreuer: Irmgard Sinning
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Universitätsbibliothek Heidelberg
    Publishing place Heidelberg
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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