Revisiting AMPylation through the lens of Fic enzymes

Burak Gulen; Aymelt Itzen

doi:10.1016/j.tim.2021.08.003

Revisiting AMPylation through the lens of Fic enzymes

Standard

Revisiting AMPylation through the lens of Fic enzymes. / Gulen, Burak; Itzen, Aymelt.

in: TRENDS MICROBIOL, Jahrgang 30, Nr. 4, 04.2022, S. 350-363.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Review › Forschung

Harvard

Gulen, B & Itzen, A 2022, 'Revisiting AMPylation through the lens of Fic enzymes', TRENDS MICROBIOL, Jg. 30, Nr. 4, S. 350-363. https://doi.org/10.1016/j.tim.2021.08.003

APA

Gulen, B., & Itzen, A. (2022). Revisiting AMPylation through the lens of Fic enzymes. TRENDS MICROBIOL, 30(4), 350-363. https://doi.org/10.1016/j.tim.2021.08.003

Vancouver

Gulen B, Itzen A. Revisiting AMPylation through the lens of Fic enzymes. TRENDS MICROBIOL. 2022 Apr;30(4):350-363. https://doi.org/10.1016/j.tim.2021.08.003

Bibtex

@article{7076bf2bbc03445db80611ccfbd1a7e4,

title = "Revisiting AMPylation through the lens of Fic enzymes",

abstract = "AMPylation, a post-translational modification (PTM) first discovered in the late 1960s, is catalyzed by adenosine monophosphate (AMP)-transferring enzymes. The observation that filamentation-induced-by-cyclic-AMP (fic) enzymes are associated with this unique PTM revealed that AMPylation plays a major role in hijacking of host signaling by pathogenic bacteria during infection. Studies over the past decade showed that AMPylation is conserved across all kingdoms of life and, outside their role in infection, also modulates cellular functions. Many aspects of AMPylation are yet to be uncovered. In this review we present the advancement in research on AMPylation and Fic enzymes as well as other distinct classes of enzymes that catalyze AMPylation.",

author = "Burak Gulen and Aymelt Itzen",

year = "2022",

month = apr,

doi = "10.1016/j.tim.2021.08.003",

language = "English",

volume = "30",

pages = "350--363",

journal = "TRENDS MICROBIOL",

issn = "0966-842X",

publisher = "Elsevier Limited",

number = "4",

}

RIS

TY - JOUR

T1 - Revisiting AMPylation through the lens of Fic enzymes

AU - Gulen, Burak

AU - Itzen, Aymelt

PY - 2022/4

Y1 - 2022/4

N2 - AMPylation, a post-translational modification (PTM) first discovered in the late 1960s, is catalyzed by adenosine monophosphate (AMP)-transferring enzymes. The observation that filamentation-induced-by-cyclic-AMP (fic) enzymes are associated with this unique PTM revealed that AMPylation plays a major role in hijacking of host signaling by pathogenic bacteria during infection. Studies over the past decade showed that AMPylation is conserved across all kingdoms of life and, outside their role in infection, also modulates cellular functions. Many aspects of AMPylation are yet to be uncovered. In this review we present the advancement in research on AMPylation and Fic enzymes as well as other distinct classes of enzymes that catalyze AMPylation.

AB - AMPylation, a post-translational modification (PTM) first discovered in the late 1960s, is catalyzed by adenosine monophosphate (AMP)-transferring enzymes. The observation that filamentation-induced-by-cyclic-AMP (fic) enzymes are associated with this unique PTM revealed that AMPylation plays a major role in hijacking of host signaling by pathogenic bacteria during infection. Studies over the past decade showed that AMPylation is conserved across all kingdoms of life and, outside their role in infection, also modulates cellular functions. Many aspects of AMPylation are yet to be uncovered. In this review we present the advancement in research on AMPylation and Fic enzymes as well as other distinct classes of enzymes that catalyze AMPylation.

U2 - 10.1016/j.tim.2021.08.003

DO - 10.1016/j.tim.2021.08.003

M3 - SCORING: Review article

C2 - 34531089

VL - 30

SP - 350

EP - 363

JO - TRENDS MICROBIOL

JF - TRENDS MICROBIOL

SN - 0966-842X

IS - 4

ER -