Dr Francesco Bemporad

Marie Curie EIF Research Fellow

Publications

The Folding Process of Acylphosphatase from Escherichia coli is Remarkably Accelerated by the Presence of a Disulfide Bond

C Parrini, F Bemporad, A Baroncelli, S Gianni, C Travaglini-Allocatelli, JE Kohn, M Ramazzotti, F Chiti, N Taddei

Journal of Molecular Biology

(2008)

379

1107

(doi: 10.1016/j.jmb.2008.04.051)

The Degree of Structural Protection at the Edge β-Strands Determines the Pathway of Amyloid Formation in Globular Proteins

G Soldi, F Bemporad, F Chiti

Journal of the American Chemical Society

(2008)

130

4295

(doi: 10.1021/ja076628s)

Sequence and structural determinants of amyloid fibril formation

F Bemporad, G Calloni, S Campioni, G Plakoutsi, N Taddei, F Chiti

Accounts of Chemical Research

(2006)

620

(doi: 10.1021/ar050067x)

Exploring the Mechanism of Formation of Native-like and Precursor Amyloid Oligomers for the Native Acylphosphatase from Sulfolobus solfataricus

G Plakoutsi, F Bemporad, M Monti, D Pagnozzi, P Pucci, F Chiti

Structure (London, England : 1993)

(2006)

993

(doi: 10.1016/j.str.2006.03.014)

Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus

A Corazza, C Rosano, K Pagano, V Alverdi, G Esposito, C Capanni, F Bemporad, G Plakoutsi, M Stefani, F Chiti, S Zuccotti, M Bolognesi, P Viglino

Proteins Structure Function and Bioinformatics

(2005)

(doi: 10.1002/prot.20703)

Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state.

G Soldi, F Bemporad, S Torrassa, A Relini, M Ramazzotti, N Taddei, F Chiti

Biophys J

(2005)

4234

(doi: 10.1529/biophysj.105.067538)

Evidence for a Mechanism of Amyloid Formation Involving Molecular Reorganisation within Native-like Precursor Aggregates

G Plakoutsi, F Bemporad, M Calamai, N Taddei, CM Dobson, F Chiti

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

G Plakoutsi, F Bemporad, N Taddei, CM Dobson, F Chiti

FEBS JOURNAL

(2005)

272

493

Protein folding:: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins

KL Maxwell, D Wildes, A Zarrine-Afsar, MA De Los Rios, AG Brown, CT Friel, L Hedberg, J-C Horng, D Bona, EJ Miller, A Vallée-Bélisle, ERG Main, F Bemporad, L Qiu, K Teilum, N-D Vu, AM Edwards, I Ruczinski, FM Poulsen, BB Kragelund, SW Michnick, F Chiti, Y Bai, SJ Hagen, L Serrano, M Oliveberg, DP Raleigh, P Wittung-Stafshede, SE Radford, SE Jackson, TR Sosnick, S Marqusee, AR Davidson, KW Plaxco

Protein Science

(2005)

602

(doi: 10.1110/ps.041205405)

Preliminary characterization of two different crystal forms of acylphosphatase from the hyperthermophile archaeon Sulfolobus solfataricus

S Zuccotti, C Rosano, F Bemporad, M Stefani, M Bolognesi

Acta crystallographica. Section F, Structural biology and crystallization communications

(2004)

144

(doi: 10.1107/S1744309104032336)

Dr Francesco Bemporad

Marie Curie EIF Research Fellow

Publications

Postdoctoral researcher

About the Department

Departmental Services

Study at Cambridge

About the University

Research at Cambridge