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The protein encoded by MID1 is a member of the tripartite motif (TRIM) family, also known as the 'RING-B box-coiled coil' (RBCC) subgroup of RING finger proteins. Zusätzlich bieten wir Ihnen MID1 Proteine (9) und MID1 Kits (8) und viele weitere Produktgruppen zu diesem Protein an.
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Human Polyclonal MID1 Primary Antibody für WB - ABIN439762
Bell, Malyukova, Holien, Koach, Parker, Kavallaris, Marshall, Cheung: TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members. in PLoS ONE 2012
Human Monoclonal MID1 Primary Antibody für ELISA, WB - ABIN517934
Liu, Knutzen, Krauss, Schweiger, Chiang: Control of mTORC1 signaling by the Opitz syndrome protein MID1. in Proceedings of the National Academy of Sciences of the United States of America 2011
P151L MID1 mutation is associated with X-linked Opitz Syndrome.
the coiled-coil and COS domain (CC-COS) bind to microtubules, demonstrating for the first time that MID1 can directly associate with the microtubules
Osx is upregulated in patients with Ossification of the posterior longitudinal ligament.
A130T/V mutations within the MID1 zinc-binding Bbox1 (zeige BBOX1 Antikörper) domain affects protein folding.
MID1 catalyzes the ubiquitination of protein phosphatase 2A and mutations within its Bbox1 (zeige BBOX1 Antikörper) domain disrupt polyubiquitination of alpha4 but not of PP2Ac (zeige PPP2CA Antikörper) in X-linked Opitz syndrome.
TRAIL regulates MID1 and TSLP (zeige TSLP Antikörper), inflammation, fibrosis, smooth muscle hypertrophy, and expression of inflammatory effector chemokines and cytokines in experimental eosinophilic esophagitis.
These studies provide insight into the mechanism by which mutations observed in X-linked Opitz G syndrome affect the structure and function of the MID1 Bbox1 (zeige BBOX1 Antikörper) domain
A familial c.1102C>T (p.R368X) mutation in the MID1 gene, is reported.
Results revealed S422 as a novel phosphorylation site of Osx and GSK-3b played an important role in regulating the protein stability and transactivational activity of Osx.
Fu ubiquitination and cleavage is one of the key elements connecting the MID1-PP2A (zeige PPP2R4 Antikörper) protein complex with GLI3 (zeige GLI3 Antikörper) activity control
we show that MID1 controls exocytosis of lytic granules and cytotoxicity in murine cytotoxic lymphocytes
X-linked microtubule-associated protein (zeige SPAG5 Antikörper), Mid1, regulates axon development.
MID1 inhibition also limited rhinovirus-induced exacerbation of allergic airway disease
Thus, lack of Mid1 causes a misspecification of the midbrain/cerebellar boundary that results in an abnormal development of the most anterior cerebellar lobes.
Analysis of Mid1, Hccs (zeige HCCS Antikörper), Arhgap6 (zeige ARHGAP6 Antikörper), and Msl3l1 (zeige MSL3 Antikörper) in X-linked polydactyly (Xpl) and Patchy-fur (Paf (zeige KIAA0101 Antikörper)) mutant mice
The protein encoded by this gene is a member of the tripartite motif (TRIM) family, also known as the 'RING-B box-coiled coil' (RBCC) subgroup of RING finger proteins. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein forms homodimers which associate with microtubules in the cytoplasm. The protein is likely involved in the formation of multiprotein structures acting as anchor points to microtubules. Mutations in this gene have been associated with the X-linked form of Opitz syndrome, which is characterized by midline abnormalities such as cleft lip, laryngeal cleft, heart defects, hypospadias, and agenesis of the corpus callosum. This gene was also the first example of a gene subject to X inactivation in human while escaping it in mouse. Multiple different transcript variants are generated by alternate splicing\; however, the full-length nature of some of the variants has not been determined.
RING finger protein 59
, midline 1 RING finger protein
, putative transcription factor XPRF
, tripartite motif protein TRIM18
, tripartite motif-containing protein 18
, zinc finger on X and Y, mouse, homolog of
, Finger on X and Y (in rat only on X)
, E3 ubiquitin-protein ligase Midline-1
, midline 1 (Opitz/BBB syndrome)