Met1-linked Ubiquitination in Immune Signalling

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Met1-linked Ubiquitination in Immune Signalling. / Fiil, Berthe Katrine; Gyrd-Hansen, Mads.

In: F E B S Journal, Vol. 81, No. 19, 10.2014, p. 4337-50.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Fiil, BK & Gyrd-Hansen, M 2014, 'Met1-linked Ubiquitination in Immune Signalling', F E B S Journal, vol. 81, no. 19, pp. 4337-50. https://doi.org/10.1111/febs.12944

APA

Fiil, B. K., & Gyrd-Hansen, M. (2014). Met1-linked Ubiquitination in Immune Signalling. F E B S Journal, 81(19), 4337-50. https://doi.org/10.1111/febs.12944

Vancouver

Fiil BK, Gyrd-Hansen M. Met1-linked Ubiquitination in Immune Signalling. F E B S Journal. 2014 Oct;81(19):4337-50. https://doi.org/10.1111/febs.12944

Author

Fiil, Berthe Katrine ; Gyrd-Hansen, Mads. / Met1-linked Ubiquitination in Immune Signalling. In: F E B S Journal. 2014 ; Vol. 81, No. 19. pp. 4337-50.

Bibtex

@article{251e505eaeb2477a93b752efa24ebc57,
title = "Met1-linked Ubiquitination in Immune Signalling",
abstract = "Methionine 1-linked ubiquitin chains (Met1-Ub), or linear ubiquitin, has emerged as a central post-translational modification in innate immune signalling. Molecular machinery that assembles, senses and, more recently, disassembles Met1-Ub has been identified, and technical advances have enabled identification of physiological substrates for Met1-Ub in response to activation of innate immune receptors. These discoveries have significantly advanced our understanding of how non-degradative ubiquitin modifications control pro-inflammatory responses mediated by nuclear factor κB and mitogen-activated protein kinases. In this review, we will discuss the current data on Met1-Ub function and regulation, and will point to some of the questions that still remain unanswered. This article is protected by copyright. All rights reserved.",
author = "Fiil, {Berthe Katrine} and Mads Gyrd-Hansen",
note = "This article is protected by copyright. All rights reserved.",
year = "2014",
month = oct,
doi = "10.1111/febs.12944",
language = "English",
volume = "81",
pages = "4337--50",
journal = "F E B S Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell",
number = "19",

}

RIS

TY - JOUR

T1 - Met1-linked Ubiquitination in Immune Signalling

AU - Fiil, Berthe Katrine

AU - Gyrd-Hansen, Mads

N1 - This article is protected by copyright. All rights reserved.

PY - 2014/10

Y1 - 2014/10

N2 - Methionine 1-linked ubiquitin chains (Met1-Ub), or linear ubiquitin, has emerged as a central post-translational modification in innate immune signalling. Molecular machinery that assembles, senses and, more recently, disassembles Met1-Ub has been identified, and technical advances have enabled identification of physiological substrates for Met1-Ub in response to activation of innate immune receptors. These discoveries have significantly advanced our understanding of how non-degradative ubiquitin modifications control pro-inflammatory responses mediated by nuclear factor κB and mitogen-activated protein kinases. In this review, we will discuss the current data on Met1-Ub function and regulation, and will point to some of the questions that still remain unanswered. This article is protected by copyright. All rights reserved.

AB - Methionine 1-linked ubiquitin chains (Met1-Ub), or linear ubiquitin, has emerged as a central post-translational modification in innate immune signalling. Molecular machinery that assembles, senses and, more recently, disassembles Met1-Ub has been identified, and technical advances have enabled identification of physiological substrates for Met1-Ub in response to activation of innate immune receptors. These discoveries have significantly advanced our understanding of how non-degradative ubiquitin modifications control pro-inflammatory responses mediated by nuclear factor κB and mitogen-activated protein kinases. In this review, we will discuss the current data on Met1-Ub function and regulation, and will point to some of the questions that still remain unanswered. This article is protected by copyright. All rights reserved.

U2 - 10.1111/febs.12944

DO - 10.1111/febs.12944

M3 - Review

C2 - 25060092

VL - 81

SP - 4337

EP - 4350

JO - F E B S Journal

JF - F E B S Journal

SN - 1742-464X

IS - 19

ER -

ID: 119770895