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000163963 041__ $$aEnglish
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000163963 1001_ $$aCable, Jennifer$$b0
000163963 245__ $$aTargeted protein degradation: from small molecules to complex organelles-a Keystone Symposia report.
000163963 260__ $$aNew York, NY$$bNew York Acad. of Sciences$$c2022
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000163963 520__ $$aTargeted 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.
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000163963 650_7 $$2Other$$aaggregation
000163963 650_7 $$2Other$$aautophagy
000163963 650_7 $$2Other$$alysophagy
000163963 650_7 $$2Other$$aproteasome
000163963 650_7 $$2Other$$aprotein degradation
000163963 650_7 $$2Other$$aubiquitin
000163963 650_7 $$2NLM Chemicals$$aProteins
000163963 650_7 $$2NLM Chemicals$$aUbiquitin
000163963 650_7 $$0EC 3.4.25.1$$2NLM Chemicals$$aProteasome Endopeptidase Complex
000163963 650_2 $$2MeSH$$aAutophagy: physiology
000163963 650_2 $$2MeSH$$aHumans
000163963 650_2 $$2MeSH$$aOrganelles
000163963 650_2 $$2MeSH$$aProteasome Endopeptidase Complex: metabolism
000163963 650_2 $$2MeSH$$aProteins: metabolism
000163963 650_2 $$2MeSH$$aProteolysis
000163963 650_2 $$2MeSH$$aUbiquitin: metabolism
000163963 7001_ $$aWeber-Ban, Eilika$$b1
000163963 7001_ $$aClausen, Tim$$b2
000163963 7001_ $$aWalters, Kylie J$$b3
000163963 7001_ $$aSharon, Michal$$b4
000163963 7001_ $$aFinley, Daniel J$$b5
000163963 7001_ $$aGu, Yangnan$$b6
000163963 7001_ $$aHanna, John$$b7
000163963 7001_ $$aFeng, Yue$$b8
000163963 7001_ $$aMartens, Sascha$$b9
000163963 7001_ $$aSimonsen, Anne$$b10
000163963 7001_ $$aHansen, Malene$$b11
000163963 7001_ $$aZhang, Hong$$b12
000163963 7001_ $$aGoodwin, Jonathan M$$b13
000163963 7001_ $$aReggio, Alessio$$b14
000163963 7001_ $$aChang, Chunmei$$b15
000163963 7001_ $$aGe, Liang$$b16
000163963 7001_ $$aSchulman, Brenda A$$b17
000163963 7001_ $$aDeshaies, Raymond J$$b18
000163963 7001_ $$aDikic, Ivan$$b19
000163963 7001_ $$aHarper, J Wade$$b20
000163963 7001_ $$aWertz, Ingrid E$$b21
000163963 7001_ $$aThomä, Nicolas H$$b22
000163963 7001_ $$aSłabicki, Mikołaj$$b23
000163963 7001_ $$aFrydman, Judith$$b24
000163963 7001_ $$aJakob, Ursula$$b25
000163963 7001_ $$0P:(DE-2719)2810353$$aDavid, Della C$$b26$$udzne
000163963 7001_ $$aBennett, Eric J$$b27
000163963 7001_ $$aBertozzi, Carolyn R$$b28
000163963 7001_ $$aSardana, Richa$$b29
000163963 7001_ $$aEapen, Vinay V$$b30
000163963 7001_ $$aCarra, Serena$$b31
000163963 773__ $$0PERI:(DE-600)2071584-5$$a10.1111/nyas.14745$$gVol. 1510, no. 1, p. 79 - 99$$n1$$p79 - 99$$tAnnals of the New York Academy of Sciences$$v1510$$x0077-8923$$y2022
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