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  1. Book: Old-age provision and homeownership

    Dötsch, Jörg / Eckardt, Martina / Okruch, Stefan

    fiscal incentives and other public policy options

    2018  

    Institution Springer International Publishing AG
    Author's details Martina Eckardt, Jörg Dötsch, Stefan Okruch, editors
    Language English
    Size x, 251 Seiten, Illustrationen, 23.5 cm x 15.5 cm
    Edition 1st edition 2018
    Document type Book
    Note Enthält 8 Beiträge
    ISBN 3319752103 ; 9783319752105 ; 9783319752112 ; 3319752111
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  2. Book ; Thesis: Sozioökonomischer Hintergrund chronisch nierenkranker Kinder im Vergleich mit gleichaltriger Gesamtbevölkerung und anderen Gruppen chronisch kranker Kinder

    Kuder, Martin / Hoppe, Bernd / Dötsch, Jörg

    2011  

    Institution Klinik und Poliklinik für Kinder- und Jugendmedizin
    Author's details vorgelegt von Martin Kuder ; 1. Berichterstatter: Professor Dr. med. B. Hoppe, 2. Berichterstatter: Universitätsprofessor Dr. med. J. Dötsch ; aus dem Zentrum für Kinder- und Jugendmedizin der Universität zu Köln, Klinik und Poliklinik für Kinder- und Jugendmedizin
    Subject code 610
    Language German
    Size 87 S. : graph. Darst.
    Publishing country Germany
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Köln, Univ., Diss., 2011
    HBZ-ID HT017181766
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    2012 D 247 order for loan Magazin

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  3. Book ; Online ; Thesis: Sozioökonomischer Hintergrund chronisch nierenkranker Kinder im Vergleich mit gleichaltriger Gesamtbevölkerung und anderen Gruppen chronisch kranker Kinder

    Kuder, Martin / Hoppe, Bernd / Dötsch, Jörg

    2011  

    Institution Klinik und Poliklinik für Kinder- und Jugendmedizin
    Author's details vorgelegt von Martin Kuder ; 1. Berichterstatter: Professor Dr. med. B. Hoppe, 2. Berichterstatter: Universitätsprofessor Dr. med. J. Dötsch ; aus dem Zentrum für Kinder- und Jugendmedizin der Universität zu Köln, Klinik und Poliklinik für Kinder- und Jugendmedizin
    Subject code 610
    Language German
    Size 87 S. : graph. Darst.
    Publishing country Germany
    Document type Book ; Online ; Thesis
    Thesis / German Habilitation thesis Köln, Univ., Diss., 2011
    HBZ-ID HT017110257
    DOI 10.4126/38m-000000513
    Database Repository for Life Sciences

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  4. Book ; Thesis: Stellenwert der präoperativen Nadellokalisation suspekter mammographischer Befunde

    Dötsch, Martin

    1998  

    Author's details vorgelegt von Martin Dötsch
    Language German
    Size III, 98 Bl. : Ill., graph. Darst.
    Edition [Mikrofiche-Ausg.]
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Mainz, Univ., Diss., 1998
    Note Mikrofiche-Ausg.: 2 Mikrofiches : 24x
    HBZ-ID HT011148403
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    1999 MB 1542 order for loan Magazin

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  5. Book ; Online ; Thesis: Tuning an elevator

    Kuhn, Benedikt [Verfasser] / Pos, Klaas Martinus Gutachter] / [Dötsch, Volker [Gutachter]

    conformational space of the SLC23 transporter UraA and its rational modulation by off-site mutations and conformational-selective binders

    2022  

    Author's details Benedikt Thomas Kuhn ; Gutachter: Klaas Martinus Pos, Volker Dötsch
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Universitätsbibliothek Johann Christian Senckenberg
    Publishing place Frankfurt am Main
    Document type Book ; Online ; Thesis
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  6. Article ; Online: Bi-allelic mutations in uncoordinated mutant number-45 myosin chaperone B are a cause for congenital myopathy.

    Dafsari, Hormos Salimi / Kocaturk, Nur Mehpare / Daimagüler, Hülya-Sevcan / Brunn, Anna / Dötsch, Jörg / Weis, Joachim / Deckert, Martina / Cirak, Sebahattin

    Acta neuropathologica communications

    2019  Volume 7, Issue 1, Page(s) 211

    Abstract: Congenital myopathies (CM) form a genetically heterogeneous group of disorders characterized by perinatal muscle weakness. Here, we report an 11-year old male offspring of consanguineous parents of Lebanese origin. He presented with proximal weakness ... ...

    Abstract Congenital myopathies (CM) form a genetically heterogeneous group of disorders characterized by perinatal muscle weakness. Here, we report an 11-year old male offspring of consanguineous parents of Lebanese origin. He presented with proximal weakness including Gower's sign, and skeletal muscle biopsy revealed myopathic changes with core-like structures. Whole exome sequencing of this index patient lead to the discovery of a novel genetically defined CM subtype based on bi-allelic mutations in the uncoordinated mutant number-45 myosin chaperone B (UNC45B) NM_173167:c.2261G > A, p.Arg754Gln. The mutation is conserved in evolution and co-segregates within the pedigree with the phenotype, and located in the myosin binding armadillo repeat domain 3 (ARM3), and has a CADD Score of 35. On a multimeric level, UNC45B aggregates to a chain which serves as an assembly line and functions as a "template" defining the geometry, regularity, and periodicity of myosin arranged into muscle thick filaments. Our discovery is in line with the previously described myopathological phenotypes in C. elegans and in vertebrate mutants and knockdown-models. In conclusion, we here report for the first time a patient with an UNC45B mutation causing a novel genetically defined congenital myopathy disease entity.
    MeSH term(s) Alleles ; Amino Acid Sequence ; Child ; Humans ; Male ; Molecular Chaperones/genetics ; Muscular Diseases/diagnosis ; Muscular Diseases/genetics ; Mutation/genetics ; Pedigree
    Chemical Substances Molecular Chaperones ; UNC45B protein, human
    Language English
    Publishing date 2019-12-18
    Publishing country England
    Document type Case Reports ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2715589-4
    ISSN 2051-5960 ; 2051-5960
    ISSN (online) 2051-5960
    ISSN 2051-5960
    DOI 10.1186/s40478-019-0869-1
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  7. Article ; Online: In vitro

    Mezhyrova, Julija / Martin, Janosch / Börnsen, Clara / Dötsch, Volker / Frangakis, Achilleas Stefanos / Morgner, Nina / Bernhard, Frank

    Microbiome research reports

    2023  Volume 2, Issue 4, Page(s) 28

    Abstract: Background: ...

    Abstract Background:
    Language English
    Publishing date 2023-07-20
    Publishing country United States
    Document type Journal Article
    ISSN 2771-5965
    ISSN (online) 2771-5965
    DOI 10.20517/mrr.2023.28
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  8. Article ; Online: Fuzzy interactions between the auto-phosphorylated C-terminus and the kinase domain of CK1δ inhibits activation of TAp63α.

    Lambert, Mahil / Gebel, Jakob / Trejtnar, Charlotte / Wesch, Nicole / Bozkurt, Süleyman / Adrian-Allgood, Martin / Löhr, Frank / Münch, Christian / Dötsch, Volker

    Scientific reports

    2023  Volume 13, Issue 1, Page(s) 16423

    Abstract: The p53 family member TAp63α plays an important role in maintaining the genetic integrity in oocytes. DNA damage, in particular DNA double strand breaks, lead to the transformation of the inhibited, only dimeric conformation into the active tetrameric ... ...

    Abstract The p53 family member TAp63α plays an important role in maintaining the genetic integrity in oocytes. DNA damage, in particular DNA double strand breaks, lead to the transformation of the inhibited, only dimeric conformation into the active tetrameric one that results in the initiation of an apoptotic program. Activation requires phosphorylation by the kinase CK1 which phosphorylates TAp63α at four positions. The third phosphorylation event is the decisive step that transforms TAp63α into the active state. This third phosphorylation, however, is ~ 20 times slower than the first two phosphorylation events. This difference in the phosphorylation kinetics constitutes a safety mechanism that allows oocytes with a low degree of DNA damage to survive. So far these kinetic investigations of the phosphorylation steps have been performed with the isolated CK1 kinase domain. However, all CK1 enzymes contain C-terminal extensions that become auto-phosphorylated and inhibit the activity of the kinase. Here we have investigated the effect of auto-phosphorylation of the C-terminus in the kinase CK1δ and show that it slows down phosphorylation of the first two sites in TAp63α but basically inhibits the phosphorylation of the third site. We have identified up to ten auto-phosphorylation sites in the CK1δ C-terminal domain and show that all of them interact with the kinase domain in a "fuzzy" way in which not a single site is particularly important. Through mutation analysis we further show that hydrophobic amino acids following the phosphorylation site are important for a substrate to be able to successfully compete with the auto-inhibitory effect of the C-terminal domain. This auto-phosphorylation adds a new layer to the regulation of apoptosis in oocytes.
    MeSH term(s) Phosphorylation ; DNA Damage ; Apoptosis ; Oocytes/metabolism ; DNA Breaks, Double-Stranded
    Language English
    Publishing date 2023-09-30
    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/s41598-023-43515-x
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  9. Book ; Online ; Thesis: Adaptations of autophagy and lysosomal systems upon membrane damage and pathogenic invasion

    Bhattacharya, Anshu [Verfasser] / Grininger, Martin [Akademischer Betreuer] / Windbergs, Maike Akademischer Betreuer] / [Đikić, Ivan [Gutachter] / Dötsch, Volker [Gutachter]

    2023  

    Author's details Anshu Bhattacharya ; Gutachter: Ivan Đikić, Volker Dötsch ; Martin Grininger, Maike Windbergs
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Universitätsbibliothek Johann Christian Senckenberg
    Publishing place Frankfurt am Main
    Document type Book ; Online ; Thesis
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  10. Article ; Online: Transient RNA-protein interactions in RNA folding.

    Doetsch, Martina / Schroeder, Renée / Fürtig, Boris

    The FEBS journal

    2011  Volume 278, Issue 10, Page(s) 1634–1642

    Abstract: The RNA folding trajectory features numerous off-pathway folding traps, which represent conformations that are often equally as stable as the native functional ones. Therefore, the conversion between these off-pathway structures and the native correctly ... ...

    Abstract The RNA folding trajectory features numerous off-pathway folding traps, which represent conformations that are often equally as stable as the native functional ones. Therefore, the conversion between these off-pathway structures and the native correctly folded ones is the critical step in RNA folding. This process, referred to as RNA refolding, is slow, and is represented by a transition state that has a characteristic high free energy. Because this kinetically limiting process occurs in vivo, proteins (called RNA chaperones) have evolved that facilitate the (re)folding of RNA molecules. Here, we present an overview of how proteins interact with RNA molecules in order to achieve properly folded states. In this respect, the discrimination between static and transient interactions is crucial, as different proteins have evolved a multitude of mechanisms for RNA remodeling. For RNA chaperones that act in a sequence-unspecific manner and without the use of external sources of energy, such as ATP, transient RNA-protein interactions represent the basis of the mode of action. By presenting stretches of positively charged amino acids that are positioned in defined spatial configurations, RNA chaperones enable the RNA backbone, via transient electrostatic interactions, to sample a wider conformational space that opens the route for efficient refolding reactions.
    MeSH term(s) DEAD-box RNA Helicases/chemistry ; DNA-Binding Proteins/chemistry ; Escherichia coli Proteins/chemistry ; Gene Products, tat/chemistry ; Kinetics ; Models, Chemical ; Molecular Chaperones/chemistry ; Nucleic Acid Conformation ; Proteins/chemistry ; RNA/chemistry ; RNA-Binding Proteins/chemistry ; Thermodynamics
    Chemical Substances DNA-Binding Proteins ; Escherichia coli Proteins ; Gene Products, tat ; Molecular Chaperones ; Proteins ; RNA-Binding Proteins ; StpA protein, E coli ; RNA (63231-63-0) ; DEAD-box RNA Helicases (EC 3.6.4.13)
    Language English
    Publishing date 2011-04-13
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/j.1742-4658.2011.08094.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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