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The Journal of Biological Chemistry|August 2, 2001
Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphataseN Taddei, C Capanni, F Chiti, et al.International Journal of Peptide and Protein Research|July 1, 1986
Purification and characterization of rabbit muscle acylphosphatase in the thiol (-SH) formA Berti, M Stefani, G Camici, et al.FEBS Letters|April 15, 1996
C-terminal region contributes to muscle acylphosphatase three-dimensional structure stabilisationN Taddei, F Magherini, F Chiti, et al.European Journal of Biochemistry|November 1, 1994
Equilibrium unfolding studies of horse muscle acylphosphataseN Taddei, M Buck, R W Broadhurst, et al.The Italian Journal of Biochemistry|January 1, 1984
Turkey muscle acylphosphatase: purification and comparative studiesG Camici, G Manao, M Stefani, et al.European Journal of Biochemistry|December 1, 1983
The primary structure of turkey muscle acylphosphataseG Camici, G Manao, G Cappugi, et al.The Italian Journal of Biochemistry|November 1, 1979
Horse muscle acylphosphatase: a more rapid purification procedure and crystallizationG Ramponi, G Camici, G Cappugi, et al.Journal of Molecular Biology|May 20, 1989
Identification and description of beta-structure in horse muscle acylphosphatase by nuclear magnetic resonance spectroscopyV Saudek, M R Wormald, R J Williams, et al.Journal of Protein Chemistry|August 1, 1988
Guinea pig acylphosphatase: the amino acid sequenceG Manao, G Cappugi, A Modesti, et al.Biochemical Medicine|October 1, 1985
Acylphosphatase from human skeletal muscle: purification, some properties and levels in normal and myopathic musclesP Nassi, G Liguri, N Landi, et al.Pageof 27