S
Sandra S. Haenni
Researcher at University of Zurich
Publications - 4
Citations - 1054
Sandra S. Haenni is an academic researcher from University of Zurich. The author has contributed to research in topics: Acetylation & Poly ADP ribose polymerase. The author has an hindex of 4, co-authored 4 publications receiving 993 citations.
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Journal ArticleDOI
Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?
TL;DR: A special focus is placed on the known roles of distinct mono- and poly-ADP-ribosylation reactions in physiological processes, such as mitosis, cellular differentiation and proliferation, telomere dynamics, and aging, as well as “programmed necrosis” and apoptosis.
Journal ArticleDOI
Acetylation of poly(ADP-ribose) polymerase-1 by p300/CREB-binding protein regulates coactivation of NF-kappaB-dependent transcription
Paul O. Hassa,Sandra S. Haenni,Christine Buerki,Nadja I. Meier,William S. Lane,Heather Owen,Monika Gersbach,Ralph Imhof,Michael O. Hottiger +8 more
TL;DR: It is shown that PARP-1 is acetylated in vivo at specific lysine residues by p300/CREB-binding protein upon stimulation and plays an important regulatory role in NF-κB-dependent gene activation by enhancing its functional interaction with p300 and the Mediator complex.
Journal ArticleDOI
Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation
TL;DR: Evidence is provided that acetylation of PARp-2 is a key post-translational modification that may regulate DNA binding and consequently also the enzymatic activity of PARP-2.
Journal ArticleDOI
Importin alpha binding and nuclear localization of PARP-2 is dependent on lysine 36, which is located within a predicted classical NLS
Sandra S. Haenni,Matthias Altmeyer,Paul O. Hassa,Paul O. Hassa,Taras Valovka,Taras Valovka,Monika Fey,Michael O. Hottiger +7 more
TL;DR: Results provide strong evidence that lysine 36 of PARP-2 is a critical residue for proper nuclear targeting of PARp-2 and consequently for the execution of its biological functions.