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TMX1 selectively intervenes in clearance of membrane-tethered Endoplasmic Reticulum-Associated Degradation substrates. TMX1 preferentially acts on membrane-tethered folding-defective polypeptides essentially ignoring the same misfolded ectodomains, when not associated to the Endoplasmic Reticulum membrane.
TMX1 increases mitochondrial ATP production and apoptosis progression.
Here we show that TMX1, one of the few transmembrane members of the family, forms functional complexes with the ER lectin calnexin and preferentially intervenes during maturation of cysteine-containing, membrane-associated proteins
We conclude that TMX plays a major role in host defense under the type of inflammatory conditions associated with oxidative stress.
the silencing of TMX in the prostatic cell line DU145 reduced the sensitivity of the cells to ricin intoxication further confirming a role for this enzyme in intracellular ricin activation.
TMX1 is enriched on the mitochondria-associated membrane. Targeting TMX to the MAM requires palmitoylation of two membrane-proximal cytosolic cysteines.
These results suggest a specific role for transmembrane thioredoxin-related protein TMX and its mechanism of action in redox-based ER quality control.
TXNDC1 is a thioredoxin (TXN\; see MIM 187700)-related protein with disulfide reductase activity (Matsuo et al., 2001
protein disulfide isomerase family A, member 11
, thioredoxin domain containing 1
, thioredoxin domain-containing protein 1
, transmembrane Trx-related protein
, Trx-like protein