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Susanne Kostka
Researcher at Max Delbrück Center for Molecular Medicine
Publications - 36
Citations - 4468
Susanne Kostka is an academic researcher from Max Delbrück Center for Molecular Medicine. The author has contributed to research in topics: Protein subunit & Importin. The author has an hindex of 27, co-authored 36 publications receiving 4340 citations.
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Journal ArticleDOI
Export of Importin α from the Nucleus Is Mediated by a Specific Nuclear Transport Factor
TL;DR: It is reported that the previously identified CAS protein mediates importin α re-export and binds preferentially to NLS-free Importin α, explaining why import substrates stay in the nucleus.
Journal ArticleDOI
Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope.
Dirk Görlich,Susanne Kostka,Regine Kraft,Colin Dingwall,Ronald A. Laskey,Enno Hartmann,Siegfried Prehn +6 more
TL;DR: Importin 90 potentiates the effects of importin 60 on nuclear protein import, indicating that the importin complex is the physiological unit responsible for import.
Journal ArticleDOI
Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p
TL;DR: It is hypothesize that distinct membrane protein complexes function in co- and posttranslational translocation pathways.
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Importin 13: a novel mediator of nuclear import and export.
TL;DR: A novel family member from higher eukaryotes that functions primarily, but not exclusively, in import is identified and is referred to as importin 13 (Imp13), a case where a single importin β‐like receptor transports different substrates in opposite directions.
Journal ArticleDOI
Analysis of mammalian 20S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis.
Gunter Schmidtke,Regine Kraft,Susanne Kostka,Peter Henklein,Cornelius Frömmel,Jan Löwe,Robert Huber,Peter M. Kloetzel,Marion Schmidt +8 more
TL;DR: A model for self‐activation of proteasomal beta‐subunits is proposed in which residue Thr1 serves as nucleophile and Lys33 as proton donor/acceptor and evidence that subunit processing of mammalian beta‐ subunits proceeds via a novel ordered two‐step mechanism involving autocatalysis is provided.