Acid Denaturation of α₁-Antitrypsin: Characterization of a Novel Mechanism of Serpin Polymerization

Author： Devlin G.L. Chow M.K.M. Howlett G.J. Bottomley S.P.

ISSN： 0022-2836

Source： Journal of Molecular Biology, Vol.324, Iss.4, 2002-12, pp. : 859-870

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

Probing the Equilibrium Denaturation of the serpin ₁-Antitrypsin with Single Tryptophan Mutants; Evidence for Structure in the Urea Unfolded State

By Tew D.J. Bottomley S.P.

Journal of Molecular Biology, Vol. 313, Iss. 5, 2001-11 ,pp. : 1161-1169

Academic Press

Access to resources Recommend Favorite

The Mechanism of ₁-Antitrypsin Polymerization Probed by Fluorescence Spectroscopy

By James E.L. Bottomley S.P.

Archives of Biochemistry and Biophysics, Vol. 356, Iss. 2, 1998-08 ,pp. : 296-300

Elsevier

Access to resources Recommend Favorite

The effects of Tubulin denaturation on the characterization of its polymerization behavior

By Hall D.

Biophysical Chemistry, Vol. 104, Iss. 3, 2003-07 ,pp. : 655-682

Elsevier

Access to resources Recommend Favorite

Genetic Variants of  1-Antitrypsin

Current Protein and Peptide Science, Vol. 11, Iss. 2, 2010-03 ,pp. : 101-117

Bentham Science Publishers

Access to resources Recommend Favorite

The in Vitro Effect of Lithocholic Acid on the Polymerization Properties of PiZ Alpha-1-Antitrypsin

By Gerbod M.C. Janciauskiene S. Jeppsson J.O. Eriksson S.

Archives of Biochemistry and Biophysics, Vol. 351, Iss. 2, 1998-03 ,pp. : 167-174

Elsevier

Access to resources Recommend Favorite