A bifunctional enzyme of Legionella that distinctly regulates phosphoribosyl ubiquitination of the SidE family effectors
Research output: Contribution to journal › Editorial › Research › peer-review
Standard
A bifunctional enzyme of Legionella that distinctly regulates phosphoribosyl ubiquitination of the SidE family effectors. / Jiao, Jun; Ouyang, Xuan; Xu, You; Xiong, Xiaolu.
In: Journal of Translational Internal Medicine, Vol. 10, No. 2, 2022, p. 86-88.Research output: Contribution to journal › Editorial › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - A bifunctional enzyme of Legionella that distinctly regulates phosphoribosyl ubiquitination of the SidE family effectors
AU - Jiao, Jun
AU - Ouyang, Xuan
AU - Xu, You
AU - Xiong, Xiaolu
PY - 2022
Y1 - 2022
N2 - Legionella pneumophila encodes a family of phosphoribosyl ubiquitination ligases (SidEs) to co-opt the host ubiquitin network to promote its intracellular replication. A recent paper in mBio showed that a bifunctional enzyme of Legionella, named SdjA, distinctly regulates phosphoribosyl ubiquitination of the members of SidEs.
AB - Legionella pneumophila encodes a family of phosphoribosyl ubiquitination ligases (SidEs) to co-opt the host ubiquitin network to promote its intracellular replication. A recent paper in mBio showed that a bifunctional enzyme of Legionella, named SdjA, distinctly regulates phosphoribosyl ubiquitination of the members of SidEs.
U2 - 10.2478/jtim-2022-0014
DO - 10.2478/jtim-2022-0014
M3 - Editorial
C2 - 35959449
VL - 10
SP - 86
EP - 88
JO - Journal of Translational Internal Medicine
JF - Journal of Translational Internal Medicine
SN - 2450-131X
IS - 2
ER -
ID: 315267732