A Fluorescent Probe with Improved Water Solubility Permits the Analysis of Protein S-Depalmitoylation Activity in Live Cells

Tian Qiu; Rahul S. Kathayat; Yang Cao; Michael William Beck; Bryan C. Dickinson

doi:10.1021/acs.biochem.7b00835

A Fluorescent Probe with Improved Water Solubility Permits the Analysis of Protein S-Depalmitoylation Activity in Live Cells

Tian Qiu, Rahul S. Kathayat, Yang Cao, Michael William Beck, Bryan C. Dickinson

Eastern Illinois University

Producción científica › revisión exhaustiva

Idioma original	American English
Publicación	Biochemistry
Volumen	57
DOI	https://doi.org/10.1021/acs.biochem.7b00835
Estado	Published - ene 16 2018

Disciplines

Biochemistry
Biology
Molecular Biology

Acceder al documento

10.1021/acs.biochem.7b00835Licencia: Unspecified

Otros archivos y enlaces

http://pubs.acs.org/doi/10.1021/acs.biochem.7b00835

Citar esto

@article{fbbb8ebf646f49d892a7cdf9fa1c441a,

title = "A Fluorescent Probe with Improved Water Solubility Permits the Analysis of Protein S-Depalmitoylation Activity in Live Cells",

author = "Tian Qiu and Kathayat, \{Rahul S.\} and Yang Cao and Beck, \{Michael William\} and Dickinson, \{Bryan C.\}",

note = "S-Palmitoylation is an abundant lipid post-translational modification that is dynamically installed on and removed from target proteins to regulate their activity and cellular localization. A dearth of tools for studying the activities and regulation of protein S-depalmitoylases, thioesterase {"}erasers{"} of protein cysteine S-palmitoylation, has contributed to an incomplete understanding of the role of dynamic S-palmitoylation in regulating proteome lipidation.",

year = "2018",

month = jan,

day = "16",

doi = "10.1021/acs.biochem.7b00835",

language = "American English",

volume = "57",

journal = "Biochemistry",

}

TY - JOUR

T1 - A Fluorescent Probe with Improved Water Solubility Permits the Analysis of Protein S-Depalmitoylation Activity in Live Cells

AU - Qiu, Tian

AU - Kathayat, Rahul S.

AU - Cao, Yang

AU - Beck, Michael William

AU - Dickinson, Bryan C.

N1 - S-Palmitoylation is an abundant lipid post-translational modification that is dynamically installed on and removed from target proteins to regulate their activity and cellular localization. A dearth of tools for studying the activities and regulation of protein S-depalmitoylases, thioesterase "erasers" of protein cysteine S-palmitoylation, has contributed to an incomplete understanding of the role of dynamic S-palmitoylation in regulating proteome lipidation.

PY - 2018/1/16

Y1 - 2018/1/16

UR - http://pubs.acs.org/doi/10.1021/acs.biochem.7b00835

U2 - 10.1021/acs.biochem.7b00835

DO - 10.1021/acs.biochem.7b00835

M3 - Article

VL - 57

JO - Biochemistry

JF - Biochemistry

ER -