Associated Papers
A scalable approach to resolving variants of uncertain significance.
Tejura M et al.
Biorxiv : the Preprint Server for Biology, 2026
41727046 (PubMed )
Supplement: media-7.xlsx › VarChAMP_data_supp_mat_PP
TRIM E3 Ubiquitin Ligases in Rare Genetic Disorders.
Meroni G
Advances in Experimental Medicine and Biology, 2020
A Comprehensive Atlas of E3 Ubiquitin Ligase Mutations in Neurological Disorders.
George AJ et al.
Frontiers in Genetics, 2018
29491882 (PubMed )
Supplement: Table2.xlsx › Sheet1
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
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
X-linked Opitz syndrome: novel mutations in the MID1 gene and redefinition of the clinical spectrum.
De Falco F et al.
American Journal of Medical Genetics. Part A, 2003
New mutations in MID1 provide support for loss of function as the cause of X-linked Opitz syndrome.
Cox TC et al.
Human Molecular Genetics, 2000
Functional characterization of the Opitz syndrome gene product (midin): evidence for homodimerization and association with microtubules throughout the cell cycle.
Cainarca S et al.
Human Molecular Genetics, 1999
Opitz G/BBB syndrome in Xp22: mutations in the MID1 gene cluster in the carboxy-terminal domain.
Gaudenz K et al.
American Journal of Human Genetics, 1998
Select a paper to view details