Isolation and mass spectrometry of transcription factor complexes

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Standard

Isolation and mass spectrometry of transcription factor complexes. / Sebastiaan Winkler, G.; Lacomis, Lynne; Philip, John; Erdjument-Bromage, Hediye; Svejstrup, Jesper Q.; Tempst, Paul.

I: Methods, Bind 26, Nr. 3, 2002, s. 260-269.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Sebastiaan Winkler, G, Lacomis, L, Philip, J, Erdjument-Bromage, H, Svejstrup, JQ & Tempst, P 2002, 'Isolation and mass spectrometry of transcription factor complexes', Methods, bind 26, nr. 3, s. 260-269. https://doi.org/10.1016/S1046-2023(02)00030-0

APA

Sebastiaan Winkler, G., Lacomis, L., Philip, J., Erdjument-Bromage, H., Svejstrup, J. Q., & Tempst, P. (2002). Isolation and mass spectrometry of transcription factor complexes. Methods, 26(3), 260-269. https://doi.org/10.1016/S1046-2023(02)00030-0

Vancouver

Sebastiaan Winkler G, Lacomis L, Philip J, Erdjument-Bromage H, Svejstrup JQ, Tempst P. Isolation and mass spectrometry of transcription factor complexes. Methods. 2002;26(3):260-269. https://doi.org/10.1016/S1046-2023(02)00030-0

Author

Sebastiaan Winkler, G. ; Lacomis, Lynne ; Philip, John ; Erdjument-Bromage, Hediye ; Svejstrup, Jesper Q. ; Tempst, Paul. / Isolation and mass spectrometry of transcription factor complexes. I: Methods. 2002 ; Bind 26, Nr. 3. s. 260-269.

Bibtex

@article{498eb8d595b548e78608425ec415d426,
title = "Isolation and mass spectrometry of transcription factor complexes",
abstract = "Protocols are described that enable the isolation of novel proteins associated with a known protein and the subsequent identification of these proteins by mass spectrometry. We review the basics of nanosample handling and of two complementary approaches to mass analysis, and provide protocols for the entire process. The protein isolation procedure is rapid and based on two high-affinity chromatography steps. The method does not require previous knowledge of complex composition or activity and permits subsequent biochemical characterization of the isolated factor. As an example, we provide the procedures used to isolate and analyze yeast Elongator, a histone acetyltransferase complex important for transcript elongation, which led to the identification of three novel subunits.",
author = "{Sebastiaan Winkler}, G. and Lynne Lacomis and John Philip and Hediye Erdjument-Bromage and Svejstrup, {Jesper Q.} and Paul Tempst",
note = "Funding Information: Work in our laboratories was supported by grants from the Imperial Cancer Research Fund and the Human Frontier Science Program Project RG0193/97 (to J.Q.S.) and by NCI Core Grant P30 CA08748 (to P.T.). G.S.W. was supported by an EMBO Long Term Fellowship. ",
year = "2002",
doi = "10.1016/S1046-2023(02)00030-0",
language = "English",
volume = "26",
pages = "260--269",
journal = "Methods",
issn = "1046-2023",
publisher = "Academic Press",
number = "3",

}

RIS

TY - JOUR

T1 - Isolation and mass spectrometry of transcription factor complexes

AU - Sebastiaan Winkler, G.

AU - Lacomis, Lynne

AU - Philip, John

AU - Erdjument-Bromage, Hediye

AU - Svejstrup, Jesper Q.

AU - Tempst, Paul

N1 - Funding Information: Work in our laboratories was supported by grants from the Imperial Cancer Research Fund and the Human Frontier Science Program Project RG0193/97 (to J.Q.S.) and by NCI Core Grant P30 CA08748 (to P.T.). G.S.W. was supported by an EMBO Long Term Fellowship.

PY - 2002

Y1 - 2002

N2 - Protocols are described that enable the isolation of novel proteins associated with a known protein and the subsequent identification of these proteins by mass spectrometry. We review the basics of nanosample handling and of two complementary approaches to mass analysis, and provide protocols for the entire process. The protein isolation procedure is rapid and based on two high-affinity chromatography steps. The method does not require previous knowledge of complex composition or activity and permits subsequent biochemical characterization of the isolated factor. As an example, we provide the procedures used to isolate and analyze yeast Elongator, a histone acetyltransferase complex important for transcript elongation, which led to the identification of three novel subunits.

AB - Protocols are described that enable the isolation of novel proteins associated with a known protein and the subsequent identification of these proteins by mass spectrometry. We review the basics of nanosample handling and of two complementary approaches to mass analysis, and provide protocols for the entire process. The protein isolation procedure is rapid and based on two high-affinity chromatography steps. The method does not require previous knowledge of complex composition or activity and permits subsequent biochemical characterization of the isolated factor. As an example, we provide the procedures used to isolate and analyze yeast Elongator, a histone acetyltransferase complex important for transcript elongation, which led to the identification of three novel subunits.

UR - http://www.scopus.com/inward/record.url?scp=0036490552&partnerID=8YFLogxK

U2 - 10.1016/S1046-2023(02)00030-0

DO - 10.1016/S1046-2023(02)00030-0

M3 - Journal article

C2 - 12054882

AN - SCOPUS:0036490552

VL - 26

SP - 260

EP - 269

JO - Methods

JF - Methods

SN - 1046-2023

IS - 3

ER -

ID: 331042636