{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Takahashi N"],"funding":["MEXT | Japan Society for the Promotion of Science (JSPS)","WPI-Nano Life Science Institute and World Premier International Research Center Initiative","Noda Institute for Scientific Research (NISR)"],"pagination":["e2523502123"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12912973"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["123(7)"],"pubmed_abstract":["Hydrophobins are functional amyloids conserved in filamentous fungi. They act as a protective coat in the fibrous form, called rodlet. Rodlets further assemble to form dense films where they are bundled and densely aligned, contributing to the hydrophobicity of the mycelium surface. The mechanism of this dense film formation is completely unknown. Here, we used high-speed atomic force microscopy to directly observe the structural dynamics of rodlet bundling and subsequent film formation by hydrophobin RolA from the industrial fungus <i><i>Aspergillus</i> oryzae</i> at a single-fibril level, and we revealed the film-formation mechanism. Rodlet elongation occurred at both ends and was discontinuous, alternating between periods when rodlets could elongate (growth state) and could not elongate"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["High-speed atomic force microscopy reveals a surface-catalyzed elongation mechanism of the fungal functional amyloid hydrophobin RolA."],"pmcid":["PMC12912973"],"funding_grant_id":["Bio-SPM Collaborative Research (K.A.)","23K26810 (K.A.)","(K.A.)","24KJ0419 (N.T.)"],"pubmed_authors":["Abe N","Watanabe-Nakayama T","Kimura T","Tanaka T","Yoshimi A","Takahashi N","Abe K","Terauchi Y"],"additional_accession":[]},"is_claimable":false,"name":"High-speed atomic force microscopy reveals a surface-catalyzed elongation mechanism of the fungal functional amyloid hydrophobin RolA.","description":"Hydrophobins are functional amyloids conserved in filamentous fungi. They act as a protective coat in the fibrous form, called rodlet. Rodlets further assemble to form dense films where they are bundled and densely aligned, contributing to the hydrophobicity of the mycelium surface. The mechanism of this dense film formation is completely unknown. Here, we used high-speed atomic force microscopy to directly observe the structural dynamics of rodlet bundling and subsequent film formation by hydrophobin RolA from the industrial fungus <i><i>Aspergillus</i> oryzae</i> at a single-fibril level, and we revealed the film-formation mechanism. Rodlet elongation occurred at both ends and was discontinuous, alternating between periods when rodlets could elongate (growth state) and could not elongate","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Feb","modification":"2026-07-16T06:54:37.525Z","creation":"2026-07-09T10:43:13.435Z"},"accession":"S-EPMC12912973","cross_references":{"pubmed":["41678311"],"doi":["10.1073/pnas.2523502123"]}}