Proteasome inhibition promotes Parkin-Ubc13 interaction and lysine 63-linked ubiquitination.

10.1371/journal.pone.0073235

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Main Authors:	Lim G.G., Neurodegeneration Research Laboratory National Neuroscience Institute, Chew K.C., Ng X.H., Henry-Basil A., Sim R.W., Tan J.M., Chai C.
Other Authors:	PHYSIOLOGY
Format:	Article
Published:	2019
Subjects:	carrier protein lysine nerve protein parkin proteasome proteasome inhibitor protein binding SNCAIP protein, human UBE2N protein, human ubiquitin conjugating enzyme ubiquitin protein ligase autophagy drug effects genetics HEK293 cell line homeostasis human metabolism mutation protein degradation protein transport ubiquitination Autophagy Carrier Proteins HEK293 Cells Homeostasis Humans Lysine Mutation Nerve Tissue Proteins Proteasome Endopeptidase Complex Proteasome Inhibitors Protein Binding Protein Transport Proteolysis Ubiquitin-Conjugating Enzymes Ubiquitin-Protein Ligases Ubiquitination
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/161353
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1613532024-04-04T01:09:48Z Proteasome inhibition promotes Parkin-Ubc13 interaction and lysine 63-linked ubiquitination. Lim G.G. Neurodegeneration Research Laboratory National Neuroscience Institute Chew K.C. Ng X.H. Henry-Basil A. Sim R.W. Tan J.M. Chai C. PHYSIOLOGY DUKE-NUS MEDICAL SCHOOL INSTITUTE OF MOLECULAR & CELL BIOLOGY DEAN'S OFFICE (DUKE-NUS MEDICAL SCHOOL) carrier protein lysine nerve protein parkin proteasome proteasome inhibitor protein binding SNCAIP protein, human UBE2N protein, human ubiquitin conjugating enzyme ubiquitin protein ligase autophagy drug effects genetics HEK293 cell line homeostasis human metabolism mutation protein degradation protein transport ubiquitination Autophagy Carrier Proteins HEK293 Cells Homeostasis Humans Lysine Mutation Nerve Tissue Proteins Proteasome Endopeptidase Complex Proteasome Inhibitors Protein Binding Protein Transport Proteolysis Ubiquitin-Conjugating Enzymes Ubiquitin-Protein Ligases Ubiquitination 10.1371/journal.pone.0073235 PloS one 8 9 e73235 2019-11-04T06:31:47Z 2019-11-04T06:31:47Z 2013 Article Lim G.G., Neurodegeneration Research Laboratory National Neuroscience Institute, Chew K.C., Ng X.H., Henry-Basil A., Sim R.W., Tan J.M., Chai C. (2013). Proteasome inhibition promotes Parkin-Ubc13 interaction and lysine 63-linked ubiquitination.. PloS one 8 (9) : e73235. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0073235 19326203 https://scholarbank.nus.edu.sg/handle/10635/161353 Attribution 4.0 International http://creativecommons.org/licenses/by/4.0/ Unpaywall 20191101
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	carrier protein lysine nerve protein parkin proteasome proteasome inhibitor protein binding SNCAIP protein, human UBE2N protein, human ubiquitin conjugating enzyme ubiquitin protein ligase autophagy drug effects genetics HEK293 cell line homeostasis human metabolism mutation protein degradation protein transport ubiquitination Autophagy Carrier Proteins HEK293 Cells Homeostasis Humans Lysine Mutation Nerve Tissue Proteins Proteasome Endopeptidase Complex Proteasome Inhibitors Protein Binding Protein Transport Proteolysis Ubiquitin-Conjugating Enzymes Ubiquitin-Protein Ligases Ubiquitination
spellingShingle	carrier protein lysine nerve protein parkin proteasome proteasome inhibitor protein binding SNCAIP protein, human UBE2N protein, human ubiquitin conjugating enzyme ubiquitin protein ligase autophagy drug effects genetics HEK293 cell line homeostasis human metabolism mutation protein degradation protein transport ubiquitination Autophagy Carrier Proteins HEK293 Cells Homeostasis Humans Lysine Mutation Nerve Tissue Proteins Proteasome Endopeptidase Complex Proteasome Inhibitors Protein Binding Protein Transport Proteolysis Ubiquitin-Conjugating Enzymes Ubiquitin-Protein Ligases Ubiquitination Lim G.G. Neurodegeneration Research Laboratory National Neuroscience Institute Chew K.C. Ng X.H. Henry-Basil A. Sim R.W. Tan J.M. Chai C. Proteasome inhibition promotes Parkin-Ubc13 interaction and lysine 63-linked ubiquitination.
description	10.1371/journal.pone.0073235
author2	PHYSIOLOGY
author_facet	PHYSIOLOGY Lim G.G. Neurodegeneration Research Laboratory National Neuroscience Institute Chew K.C. Ng X.H. Henry-Basil A. Sim R.W. Tan J.M. Chai C.
format	Article
author	Lim G.G. Neurodegeneration Research Laboratory National Neuroscience Institute Chew K.C. Ng X.H. Henry-Basil A. Sim R.W. Tan J.M. Chai C.
author_sort	Lim G.G.
title	Proteasome inhibition promotes Parkin-Ubc13 interaction and lysine 63-linked ubiquitination.
title_short	Proteasome inhibition promotes Parkin-Ubc13 interaction and lysine 63-linked ubiquitination.
title_full	Proteasome inhibition promotes Parkin-Ubc13 interaction and lysine 63-linked ubiquitination.
title_fullStr	Proteasome inhibition promotes Parkin-Ubc13 interaction and lysine 63-linked ubiquitination.
title_full_unstemmed	Proteasome inhibition promotes Parkin-Ubc13 interaction and lysine 63-linked ubiquitination.
title_sort	proteasome inhibition promotes parkin-ubc13 interaction and lysine 63-linked ubiquitination.
publishDate	2019
url	https://scholarbank.nus.edu.sg/handle/10635/161353
_version_	1795374098969264128

Proteasome inhibition promotes Parkin-Ubc13 interaction and lysine 63-linked ubiquitination.

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