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
J Am Chem Soc
(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 (London, England : 1993)
(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 Structure Function and Bioinformatics
(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
Journal of Molecular Biology
(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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