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Biochemical and Biophysical Research Communications|October 29, 1998
Alpha 1-antitrypsin polymerisation can occur by both loop A and C sheet mechanismsS P Bottomley, P C Hopkins, J C WhisstockBiophysical Journal|February 13, 2001
Structure of a serpin-enzyme complex probed by cysteine substitutions and fluorescence spectroscopyJ P Ludeman, J C Whisstock, P C Hopkins, et al.The Journal of Biological Chemistry|March 27, 1999
Probing the unfolding pathway of alpha1-antitrypsinE L James, J C Whisstock, M G Gore, et al.Proteins|June 18, 1999
Serpins in the Caenorhabditis elegans genomeJ C Whisstock, J A Irving, S P Bottomley, et al.Protein Science : a Publication of the Protein Society|November 21, 2001
The role of strand 1 of the C beta-sheet in the structure and function of alpha(1)-antitrypsinS P Bottomley, I D Lawrenson, D Tew, et al.The Journal of Biological Chemistry|August 30, 2000
The inositol polyphosphate 5-phosphatases and the apurinic/apyrimidinic base excision repair endonucleases share a common mechanism for catalysisJ C Whisstock, S Romero, R Gurung, et al.Protein Science : a Publication of the Protein Society|March 15, 2000
Cleaved antitrypsin polymers at atomic resolutionM A Dunstone, W Dai, J C Whisstock, et al.Journal of Molecular Biology|November 9, 2001
Probing the equilibrium denaturation of the serpin alpha(1)-antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded stateD J Tew, S P BottomleyBiochemical and Biophysical Research Communications|January 13, 1998
The effects of reactive centre loop length upon serpin polymerisationS P Bottomley, W S ChangProtein Engineering|February 4, 1999
Protein engineering of chimeric Serpins: an investigation into effects of the serpin scaffold and reactive centre loop lengthS P Bottomley, S R StonePageof 7