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@ARTICLE{Cable:163963,
author = {Cable, Jennifer and Weber-Ban, Eilika and Clausen, Tim and
Walters, Kylie J and Sharon, Michal and Finley, Daniel J and
Gu, Yangnan and Hanna, John and Feng, Yue and Martens,
Sascha and Simonsen, Anne and Hansen, Malene and Zhang, Hong
and Goodwin, Jonathan M and Reggio, Alessio and Chang,
Chunmei and Ge, Liang and Schulman, Brenda A and Deshaies,
Raymond J and Dikic, Ivan and Harper, J Wade and Wertz,
Ingrid E and Thomä, Nicolas H and Słabicki, Mikołaj and
Frydman, Judith and Jakob, Ursula and David, Della C and
Bennett, Eric J and Bertozzi, Carolyn R and Sardana, Richa
and Eapen, Vinay V and Carra, Serena},
title = {{T}argeted protein degradation: from small molecules to
complex organelles-a {K}eystone {S}ymposia report.},
journal = {Annals of the New York Academy of Sciences},
volume = {1510},
number = {1},
issn = {0077-8923},
address = {New York, NY},
publisher = {New York Acad. of Sciences},
reportid = {DZNE-2022-00632},
pages = {79 - 99},
year = {2022},
abstract = {Targeted protein degradation is critical for proper
cellular function and development. Protein degradation
pathways, such as the ubiquitin proteasomes system,
autophagy, and endosome-lysosome pathway, must be tightly
regulated to ensure proper elimination of misfolded and
aggregated proteins and regulate changing protein levels
during cellular differentiation, while ensuring that normal
proteins remain unscathed. Protein degradation pathways have
also garnered interest as a means to selectively eliminate
target proteins that may be difficult to inhibit via other
mechanisms. On June 7 and 8, 2021, several experts in
protein degradation pathways met virtually for the Keystone
eSymposium 'Targeting protein degradation: from small
molecules to complex organelles.' The event brought together
researchers working in different protein degradation
pathways in an effort to begin to develop a holistic,
integrated vision of protein degradation that incorporates
all the major pathways to understand how changes in them can
lead to disease pathology and, alternatively, how they can
be leveraged for novel therapeutics.},
keywords = {Autophagy: physiology / Humans / Organelles / Proteasome
Endopeptidase Complex: metabolism / Proteins: metabolism /
Proteolysis / Ubiquitin: metabolism / aggregation (Other) /
autophagy (Other) / lysophagy (Other) / proteasome (Other) /
protein degradation (Other) / ubiquitin (Other) / Proteins
(NLM Chemicals) / Ubiquitin (NLM Chemicals) / Proteasome
Endopeptidase Complex (NLM Chemicals)},
cin = {AG David},
ddc = {500},
cid = {I:(DE-2719)1210004},
pnm = {352 - Disease Mechanisms (POF4-352)},
pid = {G:(DE-HGF)POF4-352},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:35000205},
doi = {10.1111/nyas.14745},
url = {https://pub.dzne.de/record/163963},
}