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Midline 1 RING Finger Protein

Known as: Midline 1, Midin, Putative Transcription Factor XPRF 
Midline-1 (667 aa, ~75 kDa) is encoded by the human MID1 gene. This protein is involved in microtubule formation.
National Institutes of Health

Related topics

Related topics

10 relations
Cell MovementCytokinesisCytoskeletal GeneCytoskeleton

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2019
2019
Novel mTORC1 Mechanism Suggests Therapeutic Targets for COMPopathies.
2017
2017
Fasting-induced hormonal regulation of lysosomal function
Lysosomes are centers for nutrient sensing and recycling that allow mammals to adapt to starvation. Regulation of lysosome… 
2017
2017
Two Novel Pathogenic MID1 Variants and Genotype-Phenotype Correlation Reanalysis in X-Linked Opitz G/BBB Syndrome
X-linked Opitz G/BBB syndrome (XLOS) is a multisystemic congenital condition, caused by mutations in the midline-1 gene (MID1… 
2015
2015
TNF-related apoptosis-inducing ligand (TRAIL) regulates midline-1, thymic stromal lymphopoietin, inflammation, and remodeling in experimental eosinophilic esophagitis.
2014
2014
Tumor necrosis factor-related apoptosis-inducing ligand regulates hallmark features of airways remodeling in allergic airways disease.
Allergic asthma is a complex disease characterized by acute inflammation of the airways that over time leads to the development… 
2013
2013
X-linked microtubule-associated protein, Mid1, regulates axon development
Significance The gene responsible for the X-linked form of Opitz syndrome (OS), Midline-1 (MID1), encodes an E3 ubiquitin ligase… 
Highly Cited
2012
Highly Cited
2012
TRIM16 Acts as an E3 Ubiquitin Ligase and Can Heterodimerize with Other TRIM Family Members
The TRIM family of proteins is distinguished by its tripartite motif (TRIM). Typically, TRIM proteins contain a RING finger… 
2011
2011
Detection and characterization of the in vitro e3 ligase activity of the human MID1 protein.
Highly Cited
2008
Highly Cited
2008
Structure of the MID1 tandem B-boxes reveals an interaction reminiscent of intermolecular ring heterodimers.
The tripartite motif (TRIM) protein family, defined by N-terminal RING, B-box, and coiled-coil (RBCC) domains, consists of either… 
Highly Cited
2006
Highly Cited
2006
The SPRY domain of SSB-2 adopts a novel fold that presents conserved Par-4–binding residues
The four mammalian SPRY domain–containing SOCS box proteins (SSB-1 to SSB-4) are characterized by a C-terminal SOCS box and a… 
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