http://www.cnr.it/ontology/cnr/individuo/prodotto/ID178826
Atomic force microscopy images suggest aggregation mechanism in cerato-platanin (Articolo in rivista)
- Type
- Label
- Atomic force microscopy images suggest aggregation mechanism in cerato-platanin (Articolo in rivista) (literal)
- Anno
- 2007-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1007/s00249-007-0159-x (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- F. Sbrana; L. Bongini; G. Cappugi; D. Fanelli; A. Guarino; L. Pazzagli; A. Scala; M. Vassalli; C. Zoppi; B. Tiribilli (literal)
- Pagina inizio
- Pagina fine
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- Rivista
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- C.S.D.C, Dip. Fisica, Universita` di Firenze, Via Sansone, 1, 50019 Sesto Fiorentino, Firenze, Italy
Dip. Fisica, Universita` di Firenze, Via Sansone, 1, 50019 Sesto Fiorentino, Firenze, Italy
Dip. di Scienze Biochimiche, Universita` di Firenze, Viale Morgagni, 50, 50134 Sesto Fiorentino, Firenze, Italy
Theoretical Physics, School of Physics and Astronomy, University of Manchester, Manchester, M13, 9PL Manchester, UK
Universite´ de la Polynesie Francaise, Tahiti, French Polynesia
Dip. di Biotecnologie Agrarie, Sezione di Patologia Vegetale, Universita` di Firenze, Via della Lastruccia 10, 50019 Sesto Fiorentino, Italy
ISC, CNR, Istituto Sistemi Complessi, Via Madonna del Piano, Sesto Fiorentino, Firenze 50019, Italy
I.N.F.N, Sezione di Firenze, Via Sansone, 1, 50019 Sesto Fiorentino, Firenze, Italy (literal)
- Titolo
- Atomic force microscopy images suggest aggregation mechanism in cerato-platanin (literal)
- Abstract
- Abstract Cerato-platanin (CP), the first member of the
''cerato-platanin family'', is a moderately hydrophobic
protein produced by Ceratocystis fimbriata, the causal
agent of a severe plant disease called ''canker stain''.
The protein is localized in the cell wall of the fungus
and it seems to be involved in the host-plane interaction
and induces both cell necrosis and phytoalexin synthesis
(one of the first plant defence-related events). Recently, it
has been determined that CP, like other fungal surface
protein, is able to self assemble in vitro. In this paper we
characterize the aggregates of CP by Atomic Force
Microscopy (AFM) images. We observe that CP tends
to form early annular-shaped oligomers that seem to
constitute the fundamental bricks of a hierarchical
aggregation process, eventually resulting in large macrofibrillar
assemblies. A simple model, based on the
hypothesis that the aggregation is energetically favourable
when the exposed surface is reduced, is compatible
with the measured aggregates' shape and size. The proposed
model can help to understand the mechanism by
which CP and many other fungal surface proteins exert
their effects. (literal)
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