about
Environmentally induced reversible conformational switching in the yeast cell adhesion protein alpha-agglutinin.A spheroplast rate assay for determination of cell wall integrity in yeast.Role of force-sensitive amyloid-like interactions in fungal catch bonding and biofilms.Systematic analysis of oxidative degradation of polysaccharides using PAGE and HPLC--MS.Strengthening relationships: amyloids create adhesion nanodomains in yeasts.A role for amyloid in cell aggregation and biofilm formation.Functional amyloid formation by Streptococcus mutans.Unfolding individual als5p adhesion proteins on live cells.A screen for deficiencies in GPI-anchorage of wall glycoproteins in yeast.Postmortem candidaemia: marker of disseminated disease.Forces in yeast flocculation.Accelerated and adaptive evolution of yeast sexual adhesinsQuantitative Analyses of Force-Induced Amyloid Formation in Candida albicans Als5p: Activation by Standard Laboratory Procedures.Garcinia xanthochymus Benzophenones Promote Hyphal Apoptosis and Potentiate Activity of Fluconazole against Candida albicans BiofilmsGlycosyl phosphatidylinositol-dependent cross-linking of alpha-agglutinin and beta 1,6-glucan in the Saccharomyces cerevisiae cell wall.Identification of six complementation classes involved in the biosynthesis of glycosylphosphatidylinositol anchors in Saccharomyces cerevisiae.Atomic force microscopy - looking at mechanosensors on the cell surface.Single-molecule imaging and functional analysis of Als adhesins and mannans during Candida albicans morphogenesisThe Human Disease-Associated Aβ Amyloid Core Sequence Forms Functional Amyloids in a Fungal AdhesinNanoscale analysis of caspofungin-induced cell surface remodelling in Candida albicans.Does Candida albicans Als5p amyloid play a role in commensalism in Caenorhabditis elegans?Polymicrobial bloodstream infections involving Candida species: analysis of patients and review of the literature.Single-cell force spectroscopy of the medically important Staphylococcus epidermidis-Candida albicans interaction.Quantifying the forces driving cell-cell adhesion in a fungal pathogen.Identification of a ligand-binding site in an immunoglobulin fold domain of the Saccharomyces cerevisiae adhesion protein alpha-agglutinin.Global cell surface conformational shift mediated by a Candida albicans adhesin.On the evolution of fungal and yeast cell walls.Structure of Saccharomyces cerevisiae alpha-agglutinin. Evidence for a yeast cell wall protein with multiple immunoglobulin-like domains with atypical disulfides.Glycomics for Microbes and Microbiologists.Structure and function of glycosylated tandem repeats from Candida albicans Als adhesins.Threonine-rich repeats increase fibronectin binding in the Candida albicans adhesin Als5p.Between Amyloids and Aggregation Lies a Connection with Strength and Adhesion.Candida albicans Als adhesins have conserved amyloid-forming sequences.Molecular Basis for Strain Variation in the Saccharomyces cerevisiae Adhesin Flo11pSerum Amyloid P Component and Systemic Fungal Infection: Does It Protect the Host or Is It a Trojan Horse?A unique biofilm in human deep mycoses: fungal amyloid is bound by host serum amyloid P component.Delineation of functional regions within the subunits of the Saccharomyces cerevisiae cell adhesion molecule a-agglutinin.Force Sensitivity in Saccharomyces cerevisiae Flocculins.Peptide detection of fungal functional amyloids in infected tissue.New features of invasive candidiasis in humans: amyloid formation by fungi and deposition of serum amyloid P component by the host.
P50
Q27931020-51077A72-A866-421C-91E3-D7FE7E44798FQ27932276-674B59BF-9CF1-4BA5-B311-E1AD752F9316Q30589576-2F846602-4E50-4969-A657-56DA7B552D53Q32058849-173471FA-BFE9-423F-ADF6-C6D59B36A87EQ33352559-9C0FA22A-2B17-4D44-AC7A-A6ACFF42AA97Q33847424-1D184477-EE71-49AF-9F4B-0E9A2EC80C84Q33852480-F46F75D4-506D-46AD-92DB-E6B773F56C13Q33925394-BF483F4E-A380-485F-A67B-B80DF9395F42Q34631992-4E067E6C-A29B-40EE-B206-739A4D717890Q34907626-9A3B23CD-108A-409E-849C-EA044C4C254AQ35007513-AEDFD8C6-EF11-4FA3-9FAC-9D57D56C41FBQ35639194-3105CB64-6A37-4084-A644-5675D6D2F63DQ35654457-F2C95E32-84C5-4BB5-B504-5916A0B91FD8Q36075771-C3E36205-4732-4B2D-A0DF-4E6048FE22F3Q36235200-45DEA901-B398-4BBE-B20B-4104F270671AQ36235994-CF0A80F2-3D4E-478A-93B9-6B4C3D9E039EQ36451179-150D7756-0950-43CD-8541-066746320594Q36484574-44B2F800-682E-4C16-B79E-1DCECFEF22FAQ36496535-C58FB6CD-86B5-4DA6-B525-8A9EB94B8F3FQ36587196-C2352673-BB53-407C-9397-248D980E0B4DQ36826438-AB09A1D7-B4E7-48B4-8AF9-4D03266CD896Q36948816-4E15506A-F745-49A2-9991-7452325923BDQ37300922-7F56F951-0C3C-4263-80FD-F4B664A49E92Q37382369-6FC0BF7A-19AE-4B61-9165-F43DD7B38E8DQ37450130-15F5CD32-2E89-49E3-A3A7-882105E79F8FQ37521454-E30EF530-97FF-410F-AD5D-472358B84DC8Q37773858-926A3667-7FFD-432D-A404-3AC02FEA02CFQ38289500-7011D843-A6E0-418A-BD4B-CFC97C25D227Q38291319-7F8B2727-0A84-45C8-AC84-A33D4205B5AEQ38349717-6E9D2D65-4019-409E-A2E3-A2C79B22F789Q38499396-78756F57-CD89-4601-A4CA-AB6BFFB42269Q38563842-4FD5685D-38A6-499D-8A46-43B35E65E742Q38608303-254E71CE-3787-4A33-B41C-0CA61B95EFDCQ39467488-F87A4B75-61FB-44C6-97A7-3E487C128956Q40516613-B7807E34-6CB3-41DA-BDDE-9225DA4E313AQ41002244-414AC394-93AA-4B63-A9A4-76A028996786Q41355863-1736A154-CC1A-4E60-A6EB-58E9042DFA06Q41690477-3BC662E9-46EE-437A-9157-A2226817A8FEQ41808969-C911ADC0-58B1-4B27-89AB-D237CD29D724Q42057069-AAAE9A4D-D0C4-4243-BDAE-6386DED6A578
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Peter N Lipke
@ast
Peter N Lipke
@en
Peter N Lipke
@es
Peter N Lipke
@nl
type
label
Peter N Lipke
@ast
Peter N Lipke
@en
Peter N Lipke
@es
Peter N Lipke
@nl
prefLabel
Peter N Lipke
@ast
Peter N Lipke
@en
Peter N Lipke
@es
Peter N Lipke
@nl
P106
P1153
7005706089
P31
P496
0000-0003-1733-0690