Il n’y a pas de produits dans votre liste de comparaison.
Votre panier est vide.
Afficher tous les synonymes
Sélectionnez vos espèces d'intérêt
Findings suggest that MLN64 overexpression induces an increase in mitochondrial cholesterol content and consequently a decrease in mitochondrial GSH content leading to mitochondrial dysfunction. In addition, MLN64 expression is increased in Niemann-Pick C1 deficient cells and plays a key role in cholesterol transport into the mitochondria.
Study present a rare case of a 46,XY patient with CHD associated with ambiguous genitalia consisting of a clitoris-like phallus and a bifid scrotum. Exome sequencing revealed novel homozygous mutations in the FGFR1 and STARD3 genes that may be associated with the phenotype.
Structure of the lutein-binding domain of human StARD3 at 1.74 A resolution and model of a complex with lutein has been presented.
Thus, STARD3 is a cholesterol transporter scaffolding endoplasmic reticulum-endosome contacts and modulating cellular cholesterol repartition by delivering cholesterol to endosomes.
STARD3 or STARD3NL-mediated ER-endosome contacts, which affect endosome dynamics, are believed to be involved in cholesterol transport
Elevated StARD3 expression may contribute to breast cancer aggressiveness by increasing membrane cholesterol and enhancing oncogenic signaling.
Data indicate that mitochondrial proteolytic activation of START domain-containing protein 3 (STARD3) enhances steroidogenesis.
Findings show that PPP1R1B-STARD3 fusion transcript has a key role in subsets of gastric cancers through the activation of PI3K/AKT signaling.
STARD3 or STARD3NL and VAP form a novel molecular tether between late endosomes and the endoplasmic reticulum.
Haplotype analysis indicated that combined effect of STARD3 variants (rs9972882, rs881844, rs11869286 and rs1877031) might affect the risk of GC.
With saturating MLN64, steroidogenesis by placental mitochondria proceeds at near-maximal rate.
data indicate that StARD3 is the primary lutein-binding protein in macula lutea; recombinant StARD3 selectively binds lutein with high affinity
a transport pathway for endosomal cholesterol to mitochondria that requires MLN64, but not NPC1
FAK contributed to the increased adhesion in MDA-MB-231DeltaMLN64 cells.
role of MLN64 in cholesterol transport from lysosomes to steroidogenic mitochondria
NPC2, NPC1 and MLN64 may act in an ordered sequence to sense cholesterol, effect sterol movement, and consequently, influence the process of vesicular trafficking.
The MENTAL (MLN64 amino-terminal shared with MENTHO) domain might serve to maintain cholesterol at the membrane of late endosomes prior to its shuttle to cytoplasmic acceptor(s).
local sterol enrichment by MLN64 in the late endosomal membranes facilitates their association with actin, thereby governing actin-dependent fusion and degradative activity of late endocytic organelles
In this review, MLN64 defines discrete cholesterol-containing subdomains within the membrane of late endosomes where they may function in cholesterol transport.
three-dimensional atomic models of the StART domains of metastatic lymph node 64 (MLN64) and steroidogenic acute regulatory protein (StAR) proteins in complex with cholesterol
The results suggested that MLN64 played a critical role in the meditation of osteoclastic differentiation, and its suppression alleviated diabetic osteoporosis in streptozotocin-induced mice.
Stard3 is an essential factor for the 3T3-L1 cells' differentiation
The role of endosomal cholesterol trafficking protein, StAR-related lipid transfer domain 3 (StarD3/MLN64), in BRIN-BD11 insulinoma cells.
mice homozygous for the Mln64 mutant were viable, neurologically intact,and fertile. No significant changes in plasma lipids, liver lipids, or expression of genes involved in sterol metabolism were observed, except for an increase in sterol ester storage
Hepatic MLN64 over-expression induced damage and apoptosis in murine livers and altered cholesterol metabolism.
This gene encodes a member of a subfamily of lipid trafficking proteins that are characterized by a C-terminal steroidogenic acute regulatory domain and an N-terminal metastatic lymph node 64 domain. The encoded protein localizes to the membranes of late endosomes and may be involved in exporting cholesterol. Alternative splicing results in multiple transcript variants.
StAR-related lipid transfer (START) domain containing 3
, stAR-related lipid transfer protein 3
, START domain containing 3
, MLN 64
, START domain-containing protein 3
, metastatic lymph node gene 64 protein
, metastatic lymph node protein 64
, steroidogenic acute regulatory protein related
, protein ES 64
, protein MLN 64
, mln64-like protein