Marie Curie EIF Research Fellow
Publications
The Degree of Structural Protection at the Edge β-Strands Determines the Pathway of Amyloid Formation in Globular Proteins
Journal of the American Chemical Society
(2008)
130
4295
(doi: 10.1021/ja076628s)
Sequence and structural determinants of amyloid fibril formation
Accounts of Chemical Research
(2006)
39
620
(doi: 10.1021/ar050067x)
Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus.
Structure
(2006)
14
993
(doi: 10.1016/j.str.2006.03.014)
Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus.
Proteins
(2005)
62
64
(doi: 10.1002/prot.20703)
Amyloid Formation of a Protein in the Absence of Initial Unfolding and Destabilization of the Native State
Biophysical journal
(2005)
89
4234
(doi: 10.1529/biophysj.105.067538)
Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates
J Mol Biol
(2005)
351
910
(doi: 10.1016/j.jmb.2005.06.043)
Self-assembly of a globular protein into native-like and enzymatically active aggregates that subsequently reorganize to form amyloid structures
FEBS JOURNAL
(2005)
272
493
Protein folding: Defining a “standard” set of experimental conditions and a preliminary kinetic data set of two‐state proteins
Protein Sci
(2005)
14
602
(doi: 10.1110/ps.041205405)
Preliminary characterization of two different crystal forms of acylphosphatase from the hyperthermophile archaeon Sulfolobus solfataricus
Acta Crystallographica Section F: Structural Biology Communications
(2004)
61
144
(doi: 10.1107/s1744309104032336)
Studying the Folding Process of the Acylphosphatase from Sulfolobus solfataricus. A Comparative Analysis with Other Proteins from the Same Superfamily
Biochemistry
(2004)
43
9116
(doi: 10.1021/bi030238a)
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