
Marie Curie EIF Research Fellow
Publications
The Folding Process of Acylphosphatase from Escherichia coli is Remarkably Accelerated by the Presence of a Disulfide Bond
– Journal of molecular biology
(2008)
379,
1107
(doi: 10.1016/j.jmb.2008.04.051)
The degree of structural protection at the edge beta-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
– Biophys J
(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 science : a publication of the Protein Society
(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 and crystallization communications
(2004)
61,
144
(doi: 10.1107/s1744309104032336)
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