Marie Curie EIF Research Fellow
Publications
Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships.
– Chemistry & biology
(2012)
19,
315
Characterizing the amyloidogenic state of the acylphosphatase from Sulfolobus solfataricus
– EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2011)
40,
87
1H, 13C and 15N resonance assignments of human muscle acylphosphatase
– Biomolecular NMR Assignments
(2011)
6,
1
(doi: 10.1007/s12104-011-9318-1)
Characterization of the aggregation competent state of the acylphosphatase from Sulfolobus solfataricus
– FEBS JOURNAL
(2010)
277,
258
Structural and dynamics characteristics of acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates.
– J Biol Chem
(2010)
285,
14689
(doi: 10.1074/jbc.m109.082156)
Enzymatic activity outside the folded states of proteins
– Chimica Oggi
(2009)
27,
38
"Native-like aggregation" of the acylphosphatase from Sulfolobus solfataricus and its biological implications
– FEBS letters
(2009)
583,
2630
Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase
– Protein science : a publication of the Protein Society
(2009)
15,
862
(doi: 10.1110/ps.051915806)
A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state
– Biochimica et Biophysica Acta
(2008)
1784,
1986
(doi: 10.1016/j.bbapap.2008.08.021)
Biological function in a non-native partially folded state of a protein.
– EMBO Journal
(2008)
27,
1525
(doi: 10.1038/emboj.2008.82)
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