Hydrophobins: multipurpose proteins
HAB Wösten - Annual Reviews in Microbiology, 2001 - annualreviews.org
▪ Abstract Class I and class II hydrophobins are small secreted fungal proteins that play a
role in a broad range of processes in the growth and development of filamentous fungi. For …
role in a broad range of processes in the growth and development of filamentous fungi. For …
Hydrophobins: the protein-amphiphiles of filamentous fungi
MB Linder, GR Szilvay, T Nakari-Setälä… - FEMS microbiology …, 2005 - academic.oup.com
Hydrophobins are surface active proteins produced by filamentous fungi. They have a role in
fungal growth as structural components and in the interaction of fungi with their environment …
fungal growth as structural components and in the interaction of fungi with their environment …
Surface attachment and pre-penetration stage development by plant pathogenic fungi
SL Tucker, NJ Talbot - Annual review of phytopathology, 2001 - annualreviews.org
▪ Abstract Fungal pathogens cause many of the most serious crop diseases. One of the
principal reasons for the success of this group is their ability to locate and perceive …
principal reasons for the success of this group is their ability to locate and perceive …
MHP1, a Magnaporthe grisea hydrophobin gene, is required for fungal development and plant colonization
Fungal hydrophobins are implicated in cell morphogenesis and pathogenicity in several
plant pathogenic fungi including the rice blast fungus Magnaporthe grisea. A cDNA clone …
plant pathogenic fungi including the rice blast fungus Magnaporthe grisea. A cDNA clone …
The role of pathogen-secreted proteins in fungal vascular wilt diseases
M De Sain, M Rep - International journal of molecular sciences, 2015 - mdpi.com
A limited number of fungi can cause wilting disease in plants through colonization of the
vascular system, the most well-known being Verticillium dahliae and Fusarium oxysporum …
vascular system, the most well-known being Verticillium dahliae and Fusarium oxysporum …
TasHyd1, a new hydrophobin gene from the biocontrol agent Trichoderma asperellum, is involved in plant root colonization
ADA Viterbo, I Chet - Molecular plant pathology, 2006 - Wiley Online Library
SUMMARY A hydrophobin‐like clone (TasHyd1) was isolated during a PCR differential
mRNA display analysis conducted on Trichoderma asperellum mycelia interacting with plant …
mRNA display analysis conducted on Trichoderma asperellum mycelia interacting with plant …
Hydrophobins: proteins with potential
HJ Hektor, K Scholtmeijer - Current opinion in biotechnology, 2005 - Elsevier
Hydrophobins are self-assembling proteins of fungal origin. Their ability to self-assemble
into an amphipathic membrane is of interest for many different applications, ranging from …
into an amphipathic membrane is of interest for many different applications, ranging from …
Breeding and scientific advances in the fight against Dutch elm disease: Will they allow the use of elms in forest restoration?
Elms (Ulmus spp.) were once dominant trees in mixed broadleaf forests of many European
territories, mainly distributed near rivers and streams or on floodplains. Since ancient times …
territories, mainly distributed near rivers and streams or on floodplains. Since ancient times …
Interaction and Comparison of a Class I Hydrophobin from Schizophyllum commune and Class II Hydrophobins from Trichoderma reesei
S Askolin, M Linder, K Scholtmeijer… - …, 2006 - ACS Publications
Hydrophobins fulfill a wide spectrum of functions in fungal growth and development. These
proteins self-assemble at hydrophilic− hydrophobic interfaces into amphipathic membranes …
proteins self-assemble at hydrophilic− hydrophobic interfaces into amphipathic membranes …
Hydrophobins, from molecular structure to multiple functions in fungal development
HAB Wösten, JGH Wessels - Mycoscience, 1997 - Springer
Mycelial fungi secrete small, cysteine-rich, proteins, called hydrophobins, that self-assemble
at hydrophilic-hydrophobic interfaces into amphipathic membranes, highly insoluble in case …
at hydrophilic-hydrophobic interfaces into amphipathic membranes, highly insoluble in case …