Associated Papers
Engineered Design of the E-Helix Structure on Ferritin Nanoparticles.
Qu Y et al.
Acs Applied Bio Materials, 2022
Structural and functional observations of the P151L MID1 mutation reveal alpha4 plays a significant role in X-linked Opitz Syndrome.
Wright KM et al.
The Febs Journal, 2017
Molecular dynamics simulation reveals insights into the mechanism of unfolding by the A130T/V mutations within the MID1 zinc-binding Bbox1 domain.
Zhao Y et al.
Plos One, 2015
MID1 catalyzes the ubiquitination of protein phosphatase 2A and mutations within its Bbox1 domain disrupt polyubiquitination of alpha4 but not of PP2Ac.
Du H et al.
Plos One, 2014
XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.
Wright KM et al.
Plos One, 2014
Protein phosphatase 2A (PP2A)-specific ubiquitin ligase MID1 is a sequence-dependent regulator of translation efficiency controlling 3-phosphoinositide-dependent protein kinase-1 (PDPK-1).
Aranda-Orgillés B et al.
The Journal of Biological Chemistry, 2011
Active transport of the ubiquitin ligase MID1 along the microtubules is regulated by protein phosphatase 2A.
Aranda-Orgillés B et al.
Plos One, 2008
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