ADAM17 cytoplasmic domain modulates Thioredoxin-1 conformation and activity

ADAM17 cytoplasmic domain modulates Thioredoxin-1 conformation and activity

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...

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Bibliographic Details
Main Authors: Rute A.P. e Costa, Daniela C. Granato, Luciana D. Trino, Sami Yokoo, Carolina M. Carnielli, Rebeca Kawahara, Romênia R. Domingues, Bianca Alves Pauletti, Leandro Xavier Neves, Aline G. Santana, Joao A. Paulo, Annelize Z.B. Aragão, Fernanda Aparecida Heleno Batista, Ana Carolina Migliorini Figueira, Francisco R.M. Laurindo, Denise Fernandes, Hinrich P. Hansen, Fabio Squina, Steven P. Gygi, Adriana F. Paes Leme
Format: Article
Language:English
Published: Elsevier 2020-10-01
Series:Redox Biology
Subjects:
ADAM17
Thioredoxin-1
Dimerization
Mass spectrometry
iodoTMT
Redox signaling
Online Access:http://www.sciencedirect.com/science/article/pii/S221323172030940X

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http://www.sciencedirect.com/science/article/pii/S221323172030940X

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