Maleimide scavenging enhances determination of protein S-palmitoylation state in acyl-exchange methods

S-palmitoylation (S-acylation) is emerging as an important dynamic post-translational modification of cysteine residues within proteins. Current assays for protein S-palmitoylation involve either in vivo labeling or chemical cleavage of S-palmitoyl groups to reveal a free cysteine sulfhydryl that ca...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Charlotte H. Hurst [verfasserIn] Dionne Turnbull [verfasserIn] Fiona Plain [verfasserIn] William Fuller [verfasserIn] Piers A. Hemsley [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2017

Schlagwörter:	S-acylation palmitoylation S-palmitoylation acyl biotin exchange acyl-RAC biotin switch

Übergeordnetes Werk:	In: BioTechniques - Future Science Ltd, 2019, 62(2017), 2, Seite 69-75
Übergeordnetes Werk:	volume:62 ; year:2017 ; number:2 ; pages:69-75

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc Journal toc

DOI / URN:	10.2144/000114516

Katalog-ID:	DOAJ018158404

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520			\|a S-palmitoylation (S-acylation) is emerging as an important dynamic post-translational modification of cysteine residues within proteins. Current assays for protein S-palmitoylation involve either in vivo labeling or chemical cleavage of S-palmitoyl groups to reveal a free cysteine sulfhydryl that can be subsequently labeled with an affinity handle (acyl-exchange). Assays for protein S-palmitoylation using acyl-exchange chemistry therefore require blocking of non-S-palmitoylated cysteines, typically using N-ethylmaleimide (NEM), to prevent non-specific detection. This in turn necessitates multiple precipitation-based clean-up steps to remove reagents between stages, often leading to variable sample loss, reduced signal, or protein aggregation. These combine to reduce the sensitivity, reliability, and accuracy of these assays, which also require a substantial amount of time to perform. By substituting these precipitation steps with chemical scavenging of NEM by 2,3-dimethyl-1,3-butadiene in an aqueous Diels-Alder 4+2 cyclo-addition reaction, it is possible to greatly improve sensitivity and accuracy while reducing the hands-on time and overall time required for the assay.
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authorswithroles_txt_mv	Charlotte H. Hurst @@aut@@ Dionne Turnbull @@aut@@ Fiona Plain @@aut@@ William Fuller @@aut@@ Piers A. Hemsley @@aut@@
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callnumber-first	Q - Science
author	Charlotte H. Hurst
spellingShingle	Charlotte H. Hurst misc QH301-705.5 misc S-acylation misc palmitoylation misc S-palmitoylation misc acyl biotin exchange misc acyl-RAC misc biotin switch misc Biology (General) Maleimide scavenging enhances determination of protein S-palmitoylation state in acyl-exchange methods
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topic_title	QH301-705.5 Maleimide scavenging enhances determination of protein S-palmitoylation state in acyl-exchange methods S-acylation palmitoylation S-palmitoylation acyl biotin exchange acyl-RAC biotin switch
topic	misc QH301-705.5 misc S-acylation misc palmitoylation misc S-palmitoylation misc acyl biotin exchange misc acyl-RAC misc biotin switch misc Biology (General)
topic_unstemmed	misc QH301-705.5 misc S-acylation misc palmitoylation misc S-palmitoylation misc acyl biotin exchange misc acyl-RAC misc biotin switch misc Biology (General)
topic_browse	misc QH301-705.5 misc S-acylation misc palmitoylation misc S-palmitoylation misc acyl biotin exchange misc acyl-RAC misc biotin switch misc Biology (General)
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title	Maleimide scavenging enhances determination of protein S-palmitoylation state in acyl-exchange methods
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title_full	Maleimide scavenging enhances determination of protein S-palmitoylation state in acyl-exchange methods
author_sort	Charlotte H. Hurst
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author_browse	Charlotte H. Hurst Dionne Turnbull Fiona Plain William Fuller Piers A. Hemsley
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title_sort	maleimide scavenging enhances determination of protein s-palmitoylation state in acyl-exchange methods
callnumber	QH301-705.5
title_auth	Maleimide scavenging enhances determination of protein S-palmitoylation state in acyl-exchange methods
abstract	S-palmitoylation (S-acylation) is emerging as an important dynamic post-translational modification of cysteine residues within proteins. Current assays for protein S-palmitoylation involve either in vivo labeling or chemical cleavage of S-palmitoyl groups to reveal a free cysteine sulfhydryl that can be subsequently labeled with an affinity handle (acyl-exchange). Assays for protein S-palmitoylation using acyl-exchange chemistry therefore require blocking of non-S-palmitoylated cysteines, typically using N-ethylmaleimide (NEM), to prevent non-specific detection. This in turn necessitates multiple precipitation-based clean-up steps to remove reagents between stages, often leading to variable sample loss, reduced signal, or protein aggregation. These combine to reduce the sensitivity, reliability, and accuracy of these assays, which also require a substantial amount of time to perform. By substituting these precipitation steps with chemical scavenging of NEM by 2,3-dimethyl-1,3-butadiene in an aqueous Diels-Alder 4+2 cyclo-addition reaction, it is possible to greatly improve sensitivity and accuracy while reducing the hands-on time and overall time required for the assay.
abstractGer	S-palmitoylation (S-acylation) is emerging as an important dynamic post-translational modification of cysteine residues within proteins. Current assays for protein S-palmitoylation involve either in vivo labeling or chemical cleavage of S-palmitoyl groups to reveal a free cysteine sulfhydryl that can be subsequently labeled with an affinity handle (acyl-exchange). Assays for protein S-palmitoylation using acyl-exchange chemistry therefore require blocking of non-S-palmitoylated cysteines, typically using N-ethylmaleimide (NEM), to prevent non-specific detection. This in turn necessitates multiple precipitation-based clean-up steps to remove reagents between stages, often leading to variable sample loss, reduced signal, or protein aggregation. These combine to reduce the sensitivity, reliability, and accuracy of these assays, which also require a substantial amount of time to perform. By substituting these precipitation steps with chemical scavenging of NEM by 2,3-dimethyl-1,3-butadiene in an aqueous Diels-Alder 4+2 cyclo-addition reaction, it is possible to greatly improve sensitivity and accuracy while reducing the hands-on time and overall time required for the assay.
abstract_unstemmed	S-palmitoylation (S-acylation) is emerging as an important dynamic post-translational modification of cysteine residues within proteins. Current assays for protein S-palmitoylation involve either in vivo labeling or chemical cleavage of S-palmitoyl groups to reveal a free cysteine sulfhydryl that can be subsequently labeled with an affinity handle (acyl-exchange). Assays for protein S-palmitoylation using acyl-exchange chemistry therefore require blocking of non-S-palmitoylated cysteines, typically using N-ethylmaleimide (NEM), to prevent non-specific detection. This in turn necessitates multiple precipitation-based clean-up steps to remove reagents between stages, often leading to variable sample loss, reduced signal, or protein aggregation. These combine to reduce the sensitivity, reliability, and accuracy of these assays, which also require a substantial amount of time to perform. By substituting these precipitation steps with chemical scavenging of NEM by 2,3-dimethyl-1,3-butadiene in an aqueous Diels-Alder 4+2 cyclo-addition reaction, it is possible to greatly improve sensitivity and accuracy while reducing the hands-on time and overall time required for the assay.
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700
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title_short	Maleimide scavenging enhances determination of protein S-palmitoylation state in acyl-exchange methods
url	https://doi.org/10.2144/000114516 https://doaj.org/article/314315093c43443bbafe979ff037d8cc https://www.future-science.com/doi/10.2144/000114516 https://doaj.org/toc/0736-6205 https://doaj.org/toc/1940-9818
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up_date	2024-07-03T16:16:38.275Z
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Maleimide scavenging enhances determination of protein S-palmitoylation state in acyl-exchange methods

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