Reversible S-glutathionylation of Cys 374 regulates actin filament formation by inducing structural changes in the actin molecule

Author： Dalle-Donne I. Giustarini D. Rossi R. Colombo R. Milzani A.

Publisher： Elsevier

ISSN： 0891-5849

Source： Free Radical Biology and Medicine, Vol.34, Iss.1, 2003-01, pp. : 23-32

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

Previous Menu Next

Abstract

Related content

Actin S-glutathionylation: evidence against a thiol-disulphide exchange mechanism

By Dalle-Donne I. Rossi R. Giustarini D. Colombo R. Milzani A.

Free Radical Biology and Medicine, Vol. 35, Iss. 10, 2003-11 ,pp. : 1185-1193

Elsevier

Access to resources Recommend Favorite

Smoke decreases reversible oxidations S-glutathionylation and S-nitrosylation in mice

By Kuipers Ine Bracke Ken R Brusselle Guy G Wouters Emiel Fm Reynaert Niki L

Free Radical Research, Vol. 46, Iss. 2, 2012-02 ,pp. : 164-173

Informa Healthcare

Access to resources Recommend Favorite

Structural Dynamics of F-actin I. Changes in the C terminus

By Orlova A. Egelman E.H.

Journal of Molecular Biology, Vol. 245, Iss. 5, 1995-02 ,pp. : 582-597

Academic Press

Access to resources Recommend Favorite

ADF/Cofilin Weakens Lateral Contacts in the Actin Filament

By McGough A. Chiu W.

Journal of Molecular Biology, Vol. 291, Iss. 3, 1999-08 ,pp. : 513-519

Academic Press

Access to resources Recommend Favorite

Effects of Chlorpromazine on Actin Polymerization: Slackening of Filament Elongation and Filament Annealing

By Milzani A. Dalledonne I.

Archives of Biochemistry and Biophysics, Vol. 369, Iss. 1, 1999-09 ,pp. : 59-67

Elsevier

Access to resources Recommend Favorite