A thiol probe for measuring unfolded protein load and proteostasis in cells

10.1038/s41467-017-00203-5

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Main Authors: Chen, M.Z, Moily, N.S, Bridgford, J.L, Wood, R.J, Radwan, M, Smith, T.A, Song, Z, Tang, B.Z, Tilley, L, Xu, X, Reid, G.E, Pouladi, M.A, Hong, Y, Hatters, D.M
Other Authors: MEDICINE
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Published: Nature Publishing Group 2020
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dye
Online Access:https://scholarbank.nus.edu.sg/handle/10635/178580
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spelling sg-nus-scholar.10635-1785802024-11-10T18:39:36Z A thiol probe for measuring unfolded protein load and proteostasis in cells Chen, M.Z Moily, N.S Bridgford, J.L Wood, R.J Radwan, M Smith, T.A Song, Z Tang, B.Z Tilley, L Xu, X Reid, G.E Pouladi, M.A Hong, Y Hatters, D.M MEDICINE beta lactoglobulin cysteine dihydroartemisinin dye enolase globular protein glutathione huntingtin peroxiredoxin 3 protein proteome tetraphenylethene maleimide thiol ubiquitin unclassified drug artemisinin derivative epoxomicin fluorescent dye maleimide maleimide derivative mutant protein oligopeptide thiol derivative tunicamycin cells and cell components dye nervous system disorder parasite protein proteomics reaction kinetics thiol Article exon human Huntington chorea induced pluripotent stem cell nonhuman Plasmodium falciparum protein folding protein homeostasis protein unfolding animal cells chemistry drug effects HEK293 cell line HeLa cell line malaria metabolism molecular probe mouse parasite parasitology protein folding solubility Plasmodium falciparum Animals Artemisinins Cells Cysteine Fluorescent Dyes HEK293 Cells HeLa Cells Humans Huntingtin Protein Malaria Maleimides Mice Molecular Probes Mutant Proteins Oligopeptides Parasites Protein Folding Proteome Proteostasis Solubility Sulfhydryl Compounds Tunicamycin 10.1038/s41467-017-00203-5 Nature Communications 8 1 474 2020-10-20T10:24:32Z 2020-10-20T10:24:32Z 2017 Article Chen, M.Z, Moily, N.S, Bridgford, J.L, Wood, R.J, Radwan, M, Smith, T.A, Song, Z, Tang, B.Z, Tilley, L, Xu, X, Reid, G.E, Pouladi, M.A, Hong, Y, Hatters, D.M (2017). A thiol probe for measuring unfolded protein load and proteostasis in cells. Nature Communications 8 (1) : 474. ScholarBank@NUS Repository. https://doi.org/10.1038/s41467-017-00203-5 2041-1723 https://scholarbank.nus.edu.sg/handle/10635/178580 Attribution 4.0 International http://creativecommons.org/licenses/by/4.0/ Nature Publishing Group Unpaywall 20201031
institution National University of Singapore
building NUS Library
continent Asia
country Singapore
Singapore
content_provider NUS Library
collection ScholarBank@NUS
topic beta lactoglobulin
cysteine
dihydroartemisinin
dye
enolase
globular protein
glutathione
huntingtin
peroxiredoxin 3
protein
proteome
tetraphenylethene maleimide
thiol
ubiquitin
unclassified drug
artemisinin derivative
epoxomicin
fluorescent dye
maleimide
maleimide derivative
mutant protein
oligopeptide
thiol derivative
tunicamycin
cells and cell components
dye
nervous system disorder
parasite
protein
proteomics
reaction kinetics
thiol
Article
exon
human
Huntington chorea
induced pluripotent stem cell
nonhuman
Plasmodium falciparum
protein folding
protein homeostasis
protein unfolding
animal
cells
chemistry
drug effects
HEK293 cell line
HeLa cell line
malaria
metabolism
molecular probe
mouse
parasite
parasitology
protein folding
solubility
Plasmodium falciparum
Animals
Artemisinins
Cells
Cysteine
Fluorescent Dyes
HEK293 Cells
HeLa Cells
Humans
Huntingtin Protein
Malaria
Maleimides
Mice
Molecular Probes
Mutant Proteins
Oligopeptides
Parasites
Protein Folding
Proteome
Proteostasis
Solubility
Sulfhydryl Compounds
Tunicamycin
spellingShingle beta lactoglobulin
cysteine
dihydroartemisinin
dye
enolase
globular protein
glutathione
huntingtin
peroxiredoxin 3
protein
proteome
tetraphenylethene maleimide
thiol
ubiquitin
unclassified drug
artemisinin derivative
epoxomicin
fluorescent dye
maleimide
maleimide derivative
mutant protein
oligopeptide
thiol derivative
tunicamycin
cells and cell components
dye
nervous system disorder
parasite
protein
proteomics
reaction kinetics
thiol
Article
exon
human
Huntington chorea
induced pluripotent stem cell
nonhuman
Plasmodium falciparum
protein folding
protein homeostasis
protein unfolding
animal
cells
chemistry
drug effects
HEK293 cell line
HeLa cell line
malaria
metabolism
molecular probe
mouse
parasite
parasitology
protein folding
solubility
Plasmodium falciparum
Animals
Artemisinins
Cells
Cysteine
Fluorescent Dyes
HEK293 Cells
HeLa Cells
Humans
Huntingtin Protein
Malaria
Maleimides
Mice
Molecular Probes
Mutant Proteins
Oligopeptides
Parasites
Protein Folding
Proteome
Proteostasis
Solubility
Sulfhydryl Compounds
Tunicamycin
Chen, M.Z
Moily, N.S
Bridgford, J.L
Wood, R.J
Radwan, M
Smith, T.A
Song, Z
Tang, B.Z
Tilley, L
Xu, X
Reid, G.E
Pouladi, M.A
Hong, Y
Hatters, D.M
A thiol probe for measuring unfolded protein load and proteostasis in cells
description 10.1038/s41467-017-00203-5
author2 MEDICINE
author_facet MEDICINE
Chen, M.Z
Moily, N.S
Bridgford, J.L
Wood, R.J
Radwan, M
Smith, T.A
Song, Z
Tang, B.Z
Tilley, L
Xu, X
Reid, G.E
Pouladi, M.A
Hong, Y
Hatters, D.M
format Article
author Chen, M.Z
Moily, N.S
Bridgford, J.L
Wood, R.J
Radwan, M
Smith, T.A
Song, Z
Tang, B.Z
Tilley, L
Xu, X
Reid, G.E
Pouladi, M.A
Hong, Y
Hatters, D.M
author_sort Chen, M.Z
title A thiol probe for measuring unfolded protein load and proteostasis in cells
title_short A thiol probe for measuring unfolded protein load and proteostasis in cells
title_full A thiol probe for measuring unfolded protein load and proteostasis in cells
title_fullStr A thiol probe for measuring unfolded protein load and proteostasis in cells
title_full_unstemmed A thiol probe for measuring unfolded protein load and proteostasis in cells
title_sort thiol probe for measuring unfolded protein load and proteostasis in cells
publisher Nature Publishing Group
publishDate 2020
url https://scholarbank.nus.edu.sg/handle/10635/178580
_version_ 1821199726410727424