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Home>Research>Subarea 4: Cell Dynamics and Molecular Damages in Aging
Research focus of Subarea 4.

Subarea 4: Cell Dynamics and Molecular Damages in Aging

The research focus of Subarea 4 is on studying damages of macromolecules (proteins, nucleic acids) and determining the structure-function relationship of biomolecules relevant to damage and damage repair processes and responses to molecular damage that might lead to aging and aging-associated pathologies.

The studies are focused on the following research areas: DNA replication, DNA damage responses (DDR), stress responses, metabolic stresses, protein trafficking and protein damages.

The research is defined by four focus areas:

  • DNA damage response in tissue homeostasis and neuropathies,
  • Quality control in the endoplasmic reticulum for secretory pathway in aging processes,
  • Intrinsic and extrinsic factors implicated in cellular decline during aging, and
  • DNA replication and genomic integrity preventing premature aging and diseases.

Research focus of Subarea 4.

The accumulation of damaged macromolecules or subcellular organelles is associated with dysfunction of a cell, which contributes to tissue & organ failure. DNA damage, genomic instability, protein misfolding or defects in toxic protein degradation can compromise cell functionality. Alterations of mitochondrial DNA and protein complexes affect cellular metabolism, which will have a general impact on cell integrity.

Publications

(since 2016)

2016

  • Heme interacts with histidine- and tyrosine-based protein motifs and inhibits enzymatic activity of chloramphenicol acetyltransferase from Escherichiacoli.
    Brewitz HH, Goradia N, Schubert E, Galler K, Kühl T, Syllwasschy B, Popp J, Neugebauer U, Hagelueken G, Schiemann O, Ohlenschläger** O, Imhof** D
    Bba-Gen Subjects 2016, 1860(6), 1343-53 ** co-corresponding authors
  • Identification of inhibitors of the transmembrane protease FlaK of Methanococcus maripaludis.
    Coburger I, Schaub Y, Roeser D, Hardes K, Maeder P, Klee N, Steinmetzer T, Imhof D, Diederich WE, Than ME
    Microbiologyopen 2016, 5(4), 637-46
  • The structure of a furin-antibody complex explains non-competitive inhibition by steric exclusion of substrate conformers.
    Dahms SO, Creemers JWM, Schaub Y, Bourenkov GP, Zögg T, Brandstetter H, Than ME
    Sci Rep 2016, 6, 34303.doi:10.1038/srep303
  • Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism.
    Dahms* SO, Arciniega* M, Steinmetzer T, Huber** R, Than** ME
    Proc Natl Acad Sci U S A 2016, 113(40), 11196-201 * equal contribution, ** co-corresponding authors
  • The role of hypothalamic NF-κB signaling in the response of the HPT-axis to acute inflammation in female mice.
    de Vries EM, Nagel S, Haenold R, Sundaram SM, Pfrieger FW, Fliers E, Heuer H, Boelen A
    Endocrinology 2016, 157(7), 2947-56
  • What a Difference an OH Makes: Conformational Dynamics as the Basis for the Ligand Specificity of the Neomycin-Sensing Riboswitch.
    Duchardt-Ferner E, Gottstein-Schmidtke SR, Weigand JE, Ohlenschläger O, Wurm JP, Hammann C, Suess B, Wöhnert J
    Angew Chem Int Ed Engl 2016, 55(4), 1527-30
  • DNA Damage as a Critical Factor of Stem Cell Aging and Organ Homeostasis
    Espada L, Ermolaeva MA
    Curr Stem Cell Rep 2016, 2, 290-8
  • The tumour suppressor CYLD regulates the p53 DNA damage response.
    Fernández-Majada V, Welz PS, Ermolaeva MA, Schell M, Adam A, Dietlein F, Komander D, Büttner R, Thomas RK, Schumacher B, Pasparakis M
    Nat Commun 2016, 7, 12508 published during change of institution
  • S100A11 plays a role in homologous recombination and genome maintenance by influencing the persistence of RAD51 in DNA repair foci.
    Foertsch F, Szambowska A, Weise A, Zielinski A, Schlott B, Kraft F, Mrasek K, Borgmann K, Pospiech** H, Grosse F, Melle** C
    Cell Cycle 2016, 15(20), 2766-79 ** co-corresponding authors
  • Structure determination of peptide-heme complexes
    Goradia N
    Dissertation 2016, Jena, Germany