Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap Velos
ORGANISM(S): Homo Sapiens (human)
TISSUE(S): Epithelial Cell
SUBMITTER: Adriana Franco Paes Leme
LAB HEAD: Adriana Franco Paes Leme
PROVIDER: PXD015431 | Pride | 2020-10-19
REPOSITORIES: Pride
Action | DRS | |||
---|---|---|---|---|
09jun_Trx_D_DG_1.mgf | Mgf | |||
09jun_Trx_D_DG_1.msf | Msf | |||
09jun_Trx_D_DG_1.raw | Raw | |||
09jun_Trx_D_DG_2.mgf | Mgf | |||
09jun_Trx_D_DG_2.msf | Msf |
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Redox biology 20200924
The activity of Thioredoxin-1 (Trx-1) is adjusted by the balance of its monomeric, active and its dimeric, inactive state. The regulation of this balance is not completely understood. We have previously shown that the cytoplasmic domain of the transmembrane protein A Disintegrin And Metalloprotease 17 (ADAM17cyto) binds to Thioredoxin-1 (Trx-1) and the destabilization of this interaction favors the dimeric state of Trx-1. Here, we investigate whether ADAM17 plays a role in the conformation and a ...[more]