skip to content
Home

Centre for Misfolding Diseases

Dr Benedetta Mannini

Publications

Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers.
B Mannini, R Cascella, M Zampagni, M van Waarde-Verhagen, S Meehan, C Roodveldt, S Campioni, M Boninsegna, A Penco, A Relini, HH Kampinga, CM Dobson, MR Wilson, C Cecchi, F Chiti
– Proceedings of the National Academy of Sciences
(2012)
109,
12479
(doi: 10.1073/pnas.1117799109)
Glycosaminoglycans (GAGs) suppress the toxicity of HypF-N prefibrillar aggregates
T Saridaki, M Zampagni, B Mannini, E Evangelisti, N Taddei, C Cecchi, F Chiti
– Journal of molecular biology
(2012)
421,
616
(doi: 10.1016/j.jmb.2012.02.007)
Chaperones suppress the toxicity of aberrant protein aggregates. Molecular insight into the mechanism of action
B Mannini, S Campioni, M Boninsegna, A Penco, R Cascella, M Zampagni, M Wilson, S Meehan, C Roodveldt, C Dobson, A Relini, C Cecchi, F Chiti
– FEBS JOURNAL
(2012)
279,
224
(link to publication)
A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells.
M Zampagni, R Cascella, F Casamenti, C Grossi, E Evangelisti, D Wright, M Becatti, G Liguri, B Mannini, S Campioni, F Chiti, C Cecchi
– Journal of Cellular and Molecular Medicine
(2011)
15,
2106
(doi: 10.1111/j.1582-4934.2010.01239.x)
Chaperones suppress protein oligomer toxicity: Insight into the molecular mechanism of action
B Mannini, S Campioni, M Boninsegna, E Palagano, R Cascella, M Zampagni, A Penco, M Wilson, S Meehan, C Roodveldt, A Relini, C Cecchi, F Chiti
– FEBS JOURNAL
(2011)
278,
117
(link to publication)
The induction of  -helical structure in partially unfolded HypF-N does not affect its aggregation propensity
B Ahmad, I Vigliotta, F Tatini, S Campioni, B Mannini, J Winkelmann, B Tiribilli, F Chiti
– Protein Engineering, Design and Selection
(2011)
24,
553
(doi: 10.1093/protein/gzr018)
Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils.
H Ramshini, C Parrini, A Relini, M Zampagni, B Mannini, A Pesce, AA Saboury, M Nemat-Gorgani, F Chiti
– PloS one
(2011)
6,
e16075
(doi: 10.1371/journal.pone.0016075)
Misfolded protein oligomers formed by a model protein mimic the effect of a-beta oligomers on synaptic plasticity involved in Alzheimer's disease
F Tatini, AM Pugliese, C Traini, S Niccoli, G Maraula, TE Dami, B Mannini, F Pedata, F Casamenti, F Chiti
– FEBS JOURNAL
(2011)
278,
481
(link to publication)
Low-Level Expression of a Folding-Incompetent Protein in Escherichia coli: Search for the Molecular Determinants of Protein Aggregation In Vivo
J Winkelmann, G Calloni, S Campioni, B Mannini, N Taddei, F Chiti
– Journal of molecular biology
(2010)
398,
600
(doi: 10.1016/j.jmb.2010.03.030)
A causative link between the structure of aberrant protein oligomers and their toxicity.
S Campioni, B Mannini, M Zampagni, A Pensalfini, C Parrini, E Evangelisti, A Relini, M Stefani, CM Dobson, C Cecchi, F Chiti
– Nature chemical biology
(2010)
6,
140
(doi: 10.1038/NCHEMBIO.283)
  • <
  • 3 of 4
  • >

Visitor

Telephone number

01223 766544

Email address

    Study at Cambridge

    About the University

    Research at Cambridge