Home > Publications Database > Targeted protein degradation: from small molecules to complex organelles-a Keystone Symposia report. > print

001     163963
005     20230915090540.0
024 7 _ |a 10.1111/nyas.14745
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024 7 _ |a 0077-8923
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024 7 _ |a 1749-6632
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037 _ _ |a DZNE-2022-00632
041 _ _ |a English
082 _ _ |a 500
100 1 _ |a Cable, Jennifer
|b 0
245 _ _ |a Targeted protein degradation: from small molecules to complex organelles-a Keystone Symposia report.
260 _ _ |a New York, NY
|c 2022
|b New York Acad. of Sciences
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520 _ _ |a 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.
536 _ _ |a 352 - Disease Mechanisms (POF4-352)
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588 _ _ |a Dataset connected to CrossRef, PubMed, , Journals: pub.dzne.de
650 _ 7 |a aggregation
|2 Other
650 _ 7 |a autophagy
|2 Other
650 _ 7 |a lysophagy
|2 Other
650 _ 7 |a proteasome
|2 Other
650 _ 7 |a protein degradation
|2 Other
650 _ 7 |a ubiquitin
|2 Other
650 _ 7 |a Proteins
|2 NLM Chemicals
650 _ 7 |a Ubiquitin
|2 NLM Chemicals
650 _ 7 |a Proteasome Endopeptidase Complex
|0 EC 3.4.25.1
|2 NLM Chemicals
650 _ 2 |a Autophagy: physiology
|2 MeSH
650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a Organelles
|2 MeSH
650 _ 2 |a Proteasome Endopeptidase Complex: metabolism
|2 MeSH
650 _ 2 |a Proteins: metabolism
|2 MeSH
650 _ 2 |a Proteolysis
|2 MeSH
650 _ 2 |a Ubiquitin: metabolism
|2 MeSH
700 1 _ |a Weber-Ban, Eilika
|b 1
700 1 _ |a Clausen, Tim
|b 2
700 1 _ |a Walters, Kylie J
|b 3
700 1 _ |a Sharon, Michal
|b 4
700 1 _ |a Finley, Daniel J
|b 5
700 1 _ |a Gu, Yangnan
|b 6
700 1 _ |a Hanna, John
|b 7
700 1 _ |a Feng, Yue
|b 8
700 1 _ |a Martens, Sascha
|b 9
700 1 _ |a Simonsen, Anne
|b 10
700 1 _ |a Hansen, Malene
|b 11
700 1 _ |a Zhang, Hong
|b 12
700 1 _ |a Goodwin, Jonathan M
|b 13
700 1 _ |a Reggio, Alessio
|b 14
700 1 _ |a Chang, Chunmei
|b 15
700 1 _ |a Ge, Liang
|b 16
700 1 _ |a Schulman, Brenda A
|b 17
700 1 _ |a Deshaies, Raymond J
|b 18
700 1 _ |a Dikic, Ivan
|b 19
700 1 _ |a Harper, J Wade
|b 20
700 1 _ |a Wertz, Ingrid E
|b 21
700 1 _ |a Thomä, Nicolas H
|b 22
700 1 _ |a Słabicki, Mikołaj
|b 23
700 1 _ |a Frydman, Judith
|b 24
700 1 _ |a Jakob, Ursula
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700 1 _ |a David, Della C
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700 1 _ |a Bennett, Eric J
|b 27
700 1 _ |a Bertozzi, Carolyn R
|b 28
700 1 _ |a Sardana, Richa
|b 29
700 1 _ |a Eapen, Vinay V
|b 30
700 1 _ |a Carra, Serena
|b 31
773 _ _ |a 10.1111/nyas.14745
|g Vol. 1510, no. 1, p. 79 - 99
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|t Annals of the New York Academy of Sciences
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