Prof. Massimo
Stefani answers a few questions about this month's new hot
paper in field of Multidisciplinary.
From
•>>July 2003
Field:
Multidisciplinary
Article Title:
"Inherent toxicity of aggregates implies a common
mechanism for protein misfolding diseases"
Authors: Bucciantini,
M;Giannoni, E;Chiti, F;Baroni, F;Formigli, L;Zurdo, JS;Taddei,
N;Ramponi, G;Dobson,
CM;Stefani,
M
Journal: NATURE
Volume: 416
Page: 507-511
Year: APR 4 2002
* Univ Florence, Dipartimento Sci Biochim, Viale Morgagni 50,
I-50134 Florence, Italy.
* Univ Florence, Dipartimento Sci Biochim, I-50134 Florence,
Italy.
* Univ Florence, Dipartimento Anat Istol & Med Legale,
I-50134 Florence, Italy.
* Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England.
|
 Why
do you think your paper is highly cited?
The paper is highly cited probably because it deals with
a theme of great interest at present, i.e. the molecular basis
of neurodegenerative and, most generally, degenerative diseases
of amyloid basis, comprising very important human pathologies,
either familial or sporadic, such as Alzheimer's and
Parkinson's diseases.
Does
it describe a new discovery or a new methodology that's useful to
others?
The new data we have reported are innovative in the sense
that they show for the first time that pre-fibrillar aggregates
of proteins that are not related to any amyloid disease display
cytotoxicity to cultured cells similarly to the corresponding
pre-fibrillar aggregates formed in the differing amyloidoses,
suggesting that most, possibly all proteins not only can
potentially aggregate into amyloid fibrils but that their early
aggregates are potentially cytotoxic. This suggests intriguing
considerations on the molecular basis of amyloid diseases,
particularly the sporadic forms linked to ageing, and on the
tools evolution has set up to avoid the general risk that
proteins can acquire toxic conformations and, when this happens,
to efficiently counteract the appearance of these toxic
materials .
What
were some of the circumstances that led you to do this research?
This
research is a consequence of my engagement in the field of
protein folding and misfolding using model proteins we found to
be able to aggregate into amyloid in vitro though not
being involved in any known amyloid disease in vivo. The
natural consequence was to investigate whether these aggregates
were toxic to living systems and, if so, at what level of
structural organization (i.e. pre-fibrillar aggregates,
protofilament of mature fibrils).
Could
you summarize the significance of your paper in layman's terms?
Showing
that most, perhaps all, proteins are endowed with the intrinsic
possibility to become toxic to cells, the paper provides new
information on the molecular basis of amyloid diseases and
suggests new clues on some aspects of protein and cell
evolution.
Massimo Stefani
Full Professor of Biochemistry
Dept. of Biochemical Sciences
University of Florence
Florence, Italy
 This
paper was most recently featured in Fast Breaking Papers
- February 2003.
Read comments by this new hot paper's co-author Professor Christopher M. Dobson.
|
ESI Special Topics,
July 2003
Citing URL - http://www.esi-topics.com/nhp/2003/july-03-MassimoStefani.html
|
|
