1H, 13C and 15N resonance assignments of human muscle acylphosphatase-Reference-Cited by-同舟云学术

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1H, 13C and 15N resonance assignments of human muscle acylphosphatase

Published:2011-06-05 Issue:1 Volume:6 Page:27-29
ISSN:1874-2718
Container-title:Biomolecular NMR Assignments
language:en
Short-container-title:Biomol NMR Assign

Author:

Fusco Giuliana,De Simone Alfonso,Hsu Shang-Te Danny,Bemporad Francesco,Vendruscolo Michele,Chiti Fabrizio,Dobson Christopher M.

Publisher

Springer Science and Business Media LLC

Subject

Biochemistry,Structural Biology

Link

http://link.springer.com/content/pdf/10.1007/s12104-011-9318-1.pdf

Reference10 articles.

1. Berjanskii MV, Wishart DS (2007) The RCI server: rapid and accurate calculation of protein flexibility using chemical shifts. Nucleic Acids Res 35:W531–W537

2. Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333–366

3. Chiti F, Taddei N, White PM, Bucciantini M, Magherini F, Stefani M, Dobson CM (1999) Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat Struct Biol 6:1005–1009

4. Chiti F, Taddei N, Bucciantini M, White P, Ramponi G, Dobson CM (2000) Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J 19:1441–1449

5. Chiti F, Stefani M, Taddei N, Ramponi G, Dobson CM (2003) Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424:805–808

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