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136 related items for PubMed ID: 21945526
1. Structural change in β-sheet A of Z α(1)-antitrypsin is responsible for accelerated polymerization and disease. Knaupp AS, Bottomley SP. J Mol Biol; 2011 Nov 04; 413(4):888-98. PubMed ID: 21945526 [Abstract] [Full Text] [Related]
2. Probing the equilibrium denaturation of the serpin alpha(1)-antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded state. Tew DJ, Bottomley SP. J Mol Biol; 2001 Nov 09; 313(5):1161-9. PubMed ID: 11700071 [Abstract] [Full Text] [Related]
3. The mechanism of Z alpha 1-antitrypsin accumulation in the liver. Lomas DA, Evans DL, Finch JT, Carrell RW. Nature; 1992 Jun 18; 357(6379):605-7. PubMed ID: 1608473 [Abstract] [Full Text] [Related]
4. The role of strand 1 of the C beta-sheet in the structure and function of alpha(1)-antitrypsin. Bottomley SP, Lawrenson ID, Tew D, Dai W, Whisstock JC, Pike RN. Protein Sci; 2001 Dec 18; 10(12):2518-24. PubMed ID: 11714919 [Abstract] [Full Text] [Related]
14. Alpha 1-antitrypsin polymerisation can occur by both loop A and C sheet mechanisms. Bottomley SP, Hopkins PC, Whisstock JC. Biochem Biophys Res Commun; 1998 Oct 09; 251(1):1-5. PubMed ID: 9790897 [Abstract] [Full Text] [Related]
15. Alpha 1-antitrypsin polymerization: a fluorescence correlation spectroscopic study. Purkayastha P, Klemke JW, Lavender S, Oyola R, Cooperman BS, Gai F. Biochemistry; 2005 Feb 22; 44(7):2642-9. PubMed ID: 15709777 [Abstract] [Full Text] [Related]