The cleavable N-terminal domain of plant endopolygalacturonases from clade B may be involved in a regulated secretion mechanism

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

Standard

The cleavable N-terminal domain of plant endopolygalacturonases from clade B may be involved in a regulated secretion mechanism. / Degan, F. D.; Child, R.; Svendsen, I.; Ulvskov, P.

In: Journal of Biological Chemistry, Vol. 276, No. 38, 2001, p. 35297-35304.

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

Harvard

Degan, FD, Child, R, Svendsen, I & Ulvskov, P 2001, 'The cleavable N-terminal domain of plant endopolygalacturonases from clade B may be involved in a regulated secretion mechanism', Journal of Biological Chemistry, vol. 276, no. 38, pp. 35297-35304. https://doi.org/10.1074/jbc.M102136200

APA

Degan, F. D., Child, R., Svendsen, I., & Ulvskov, P. (2001). The cleavable N-terminal domain of plant endopolygalacturonases from clade B may be involved in a regulated secretion mechanism. Journal of Biological Chemistry, 276(38), 35297-35304. https://doi.org/10.1074/jbc.M102136200

Vancouver

Degan FD, Child R, Svendsen I, Ulvskov P. The cleavable N-terminal domain of plant endopolygalacturonases from clade B may be involved in a regulated secretion mechanism. Journal of Biological Chemistry. 2001;276(38):35297-35304. https://doi.org/10.1074/jbc.M102136200

Author

Degan, F. D. ; Child, R. ; Svendsen, I. ; Ulvskov, P. / The cleavable N-terminal domain of plant endopolygalacturonases from clade B may be involved in a regulated secretion mechanism. In: Journal of Biological Chemistry. 2001 ; Vol. 276, No. 38. pp. 35297-35304.

Bibtex

@article{7bdf4910a1bb11ddb6ae000ea68e967b,
title = "The cleavable N-terminal domain of plant endopolygalacturonases from clade B may be involved in a regulated secretion mechanism",
author = "Degan, {F. D.} and R. Child and I. Svendsen and P. Ulvskov",
year = "2001",
doi = "10.1074/jbc.M102136200",
language = "English",
volume = "276",
pages = "35297--35304",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "38",

}

RIS

TY - JOUR

T1 - The cleavable N-terminal domain of plant endopolygalacturonases from clade B may be involved in a regulated secretion mechanism

AU - Degan, F. D.

AU - Child, R.

AU - Svendsen, I.

AU - Ulvskov, P.

PY - 2001

Y1 - 2001

U2 - 10.1074/jbc.M102136200

DO - 10.1074/jbc.M102136200

M3 - Journal article

VL - 276

SP - 35297

EP - 35304

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 38

ER -

ID: 7804202