Rapid identification of DNA-binding proteins by mass spectrometry.

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Rapid identification of DNA-binding proteins by mass spectrometry. / Nordhoff, E; Krogsdam, A M; Jorgensen, H F; Kallipolitis, B H; Clark, B F; Roepstorff, P; Kristiansen, K.

In: Nature Biotechnology, Vol. 17, No. 9, 1999, p. 884-8.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Nordhoff, E, Krogsdam, AM, Jorgensen, HF, Kallipolitis, BH, Clark, BF, Roepstorff, P & Kristiansen, K 1999, 'Rapid identification of DNA-binding proteins by mass spectrometry.', Nature Biotechnology, vol. 17, no. 9, pp. 884-8. https://doi.org/10.1038/12873

APA

Nordhoff, E., Krogsdam, A. M., Jorgensen, H. F., Kallipolitis, B. H., Clark, B. F., Roepstorff, P., & Kristiansen, K. (1999). Rapid identification of DNA-binding proteins by mass spectrometry. Nature Biotechnology, 17(9), 884-8. https://doi.org/10.1038/12873

Vancouver

Nordhoff E, Krogsdam AM, Jorgensen HF, Kallipolitis BH, Clark BF, Roepstorff P et al. Rapid identification of DNA-binding proteins by mass spectrometry. Nature Biotechnology. 1999;17(9):884-8. https://doi.org/10.1038/12873

Author

Nordhoff, E ; Krogsdam, A M ; Jorgensen, H F ; Kallipolitis, B H ; Clark, B F ; Roepstorff, P ; Kristiansen, K. / Rapid identification of DNA-binding proteins by mass spectrometry. In: Nature Biotechnology. 1999 ; Vol. 17, No. 9. pp. 884-8.

Bibtex

@article{0ee44f60f75411ddbf70000ea68e967b,
title = "Rapid identification of DNA-binding proteins by mass spectrometry.",
abstract = "We report a protocol for the rapid identification of DNA-binding proteins. Immobilized DNA probes harboring a specific sequence motif are incubated with cell or nuclear extract. Proteins are analyzed directly off the solid support by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The determined molecular masses are often sufficient for identification. If not, the proteins are subjected to mass spectrometric peptide mapping followed by database searches. Apart from protein identification, the protocol also yields information on posttranslational modifications. The protocol was validated by the identification of known prokaryotic and eukaryotic DNA-binding proteins, and its use provided evidence that poly(ADP-ribose) polymerase exhibits DNA sequence-specific binding to DNA.",
author = "E Nordhoff and Krogsdam, {A M} and Jorgensen, {H F} and Kallipolitis, {B H} and Clark, {B F} and P Roepstorff and K Kristiansen",
year = "1999",
doi = "10.1038/12873",
language = "English",
volume = "17",
pages = "884--8",
journal = "Nature Biotechnology",
issn = "1087-0156",
publisher = "nature publishing group",
number = "9",

}

RIS

TY - JOUR

T1 - Rapid identification of DNA-binding proteins by mass spectrometry.

AU - Nordhoff, E

AU - Krogsdam, A M

AU - Jorgensen, H F

AU - Kallipolitis, B H

AU - Clark, B F

AU - Roepstorff, P

AU - Kristiansen, K

PY - 1999

Y1 - 1999

N2 - We report a protocol for the rapid identification of DNA-binding proteins. Immobilized DNA probes harboring a specific sequence motif are incubated with cell or nuclear extract. Proteins are analyzed directly off the solid support by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The determined molecular masses are often sufficient for identification. If not, the proteins are subjected to mass spectrometric peptide mapping followed by database searches. Apart from protein identification, the protocol also yields information on posttranslational modifications. The protocol was validated by the identification of known prokaryotic and eukaryotic DNA-binding proteins, and its use provided evidence that poly(ADP-ribose) polymerase exhibits DNA sequence-specific binding to DNA.

AB - We report a protocol for the rapid identification of DNA-binding proteins. Immobilized DNA probes harboring a specific sequence motif are incubated with cell or nuclear extract. Proteins are analyzed directly off the solid support by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The determined molecular masses are often sufficient for identification. If not, the proteins are subjected to mass spectrometric peptide mapping followed by database searches. Apart from protein identification, the protocol also yields information on posttranslational modifications. The protocol was validated by the identification of known prokaryotic and eukaryotic DNA-binding proteins, and its use provided evidence that poly(ADP-ribose) polymerase exhibits DNA sequence-specific binding to DNA.

U2 - 10.1038/12873

DO - 10.1038/12873

M3 - Journal article

C2 - 10471930

VL - 17

SP - 884

EP - 888

JO - Nature Biotechnology

JF - Nature Biotechnology

SN - 1087-0156

IS - 9

ER -

ID: 10243184