@article{
 title = {Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS},
 type = {article},
 year = {2012},
 volume = {109},
 id = {b585d9ee-1807-3f19-9891-d5c72141f251},
 created = {2023-01-10T01:45:04.060Z},
 file_attached = {false},
 profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},
 group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},
 last_modified = {2023-01-10T01:45:04.060Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {false},
 hidden = {false},
 private_publication = {false},
 abstract = {The hydrophobin EAS from the fungus Neurospora crassa forms functional amyloid fibrils called rodlets that facilitate spore formation and dispersal. Self-assembly of EAS into fibrillar rodlets occurs spontaneously at hydrophobic:hydrophilic interfaces and the rodlets further associate laterally to form amphipathic monolayers. We have used site-directed mutagenesis and peptide experiments to identify the region of EAS that drives intermolecular association and formation of the cross-β rodlet structure. Transplanting this region into a nonamyloidogenic hydrophobin enables it to form rodlets. We have also determined the structure and dynamics of an EAS variant with reduced rodlet-forming ability. Taken together, these data allow us to pinpoint the conformational changes that take place when hydrophobins self-assemble at an interface and to propose a model for the amphipathic EAS rodlet structure.},
 bibtype = {article},
 author = {Macindoe, I. and Kwan, A.H. and Ren, Q. and Morris, V.K. and Yang, W. and Mackay, J.P. and Sunde, M.},
 doi = {10.1073/pnas.1114052109},
 journal = {Proceedings of the National Academy of Sciences of the United States of America},
 number = {14}
}

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Self-assembly of EAS into fibrillar rodlets occurs spontaneously at hydrophobic:hydrophilic interfaces and the rodlets further associate laterally to form amphipathic monolayers. We have used site-directed mutagenesis and peptide experiments to identify the region of EAS that drives intermolecular association and formation of the cross-β rodlet structure. Transplanting this region into a nonamyloidogenic hydrophobin enables it to form rodlets. We have also determined the structure and dynamics of an EAS variant with reduced rodlet-forming ability. Taken together, these data allow us to pinpoint the conformational changes that take place when hydrophobins self-assemble at an interface and to propose a model for the amphipathic EAS rodlet structure.","bibtype":"article","author":"Macindoe, I. and Kwan, A.H. and Ren, Q. and Morris, V.K. and Yang, W. and Mackay, J.P. and Sunde, M.","doi":"10.1073/pnas.1114052109","journal":"Proceedings of the National Academy of Sciences of the United States of America","number":"14","bibtex":"@article{\n title = {Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS},\n type = {article},\n year = {2012},\n volume = {109},\n id = {b585d9ee-1807-3f19-9891-d5c72141f251},\n created = {2023-01-10T01:45:04.060Z},\n file_attached = {false},\n profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},\n group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},\n last_modified = {2023-01-10T01:45:04.060Z},\n read = {false},\n starred = {false},\n authored = {false},\n confirmed = {false},\n hidden = {false},\n private_publication = {false},\n abstract = {The hydrophobin EAS from the fungus Neurospora crassa forms functional amyloid fibrils called rodlets that facilitate spore formation and dispersal. Self-assembly of EAS into fibrillar rodlets occurs spontaneously at hydrophobic:hydrophilic interfaces and the rodlets further associate laterally to form amphipathic monolayers. We have used site-directed mutagenesis and peptide experiments to identify the region of EAS that drives intermolecular association and formation of the cross-β rodlet structure. Transplanting this region into a nonamyloidogenic hydrophobin enables it to form rodlets. We have also determined the structure and dynamics of an EAS variant with reduced rodlet-forming ability. 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