The antimicrobial peptide histatin-5 causes a spatially restricted disruption on the Candida albicans surface, allowing rapid entry of the peptide into the cytoplasm
about
Two functional motifs define the interaction, internalization and toxicity of the cell-penetrating antifungal peptide PAF26 on fungal cellsAntifungal Activity and Action Mechanism of Histatin 5-Halocidin Hybrid Peptides against Candida ssppH Dependent Antimicrobial Peptides and Proteins, Their Mechanisms of Action and Potential as Therapeutic AgentsRevealing the sequence of interactions of PuroA peptide with Candida albicans cells by live-cell imagingA novel immune evasion strategy of candida albicans: proteolytic cleavage of a salivary antimicrobial peptide.Enhancement of antifungal activity by integrin-targeting of branched histidine rich peptides.Peptide-based Antifungal Therapies against Emerging Infections.Salivary histatin 5 internalization by translocation, but not endocytosis, is required for fungicidal activity in Candida albicans.The novel Candida albicans transporter Dur31 Is a multi-stage pathogenicity factor.Antibacterial activity and mechanism of a scorpion venom peptide derivative in vitro and in vivoHistatin 5 resistance of Candida glabrata can be reversed by insertion of Candida albicans polyamine transporter-encoding genes DUR3 and DUR31.Histatin 5 uptake by Candida albicans utilizes polyamine transporters Dur3 and Dur31 proteins.Membrane damage as first and DNA as the secondary target for anti-candidal activity of antimicrobial peptide P7 derived from cell-penetrating peptide ppTG20 against Candida albicans.Function and Regulation of Cph2 in Candida albicans.Antiproliferative effect and characterization of a novel antifungal peptide derived from human Chromogranin A.Anti-candidal activity of a novel peptide derived from human chromogranin A and its mechanism of action against Candida kruseiChemical genomic screening of a Saccharomyces cerevisiae genomewide mutant collection reveals genes required for defense against four antimicrobial peptides derived from proteins found in human saliva.Antifungal Properties of Cationic Phenylene Ethynylenes and Their Impact on β-Glucan Exposure.BAR domain proteins Rvs161 and Rvs167 contribute to Candida albicans endocytosis, morphogenesis, and virulence.The Mechanistic Targets of Antifungal Agents: An Overview.Multifunctional host defense peptides: intracellular-targeting antimicrobial peptides.Salivary peptidomics.Antimicrobial peptides: to membranes and beyond.Defensins: antifungal lessons from eukaryotesHow does it kill?: understanding the candidacidal mechanism of salivary histatin 5.Endocytosis-mediated vacuolar accumulation of the human ApoE apolipoprotein-derived ApoEdpL-W antimicrobial peptide contributes to its antifungal activity in Candida albicans.Exploiting new knowledge of Candidal infection for future antifungal combat.An unprecedented alteration in mode of action of IsCT resulting its translocation into bacterial cytoplasm and inhibition of macromolecular syntheses.Human Antimicrobial Peptides in Bodily Fluids: Current Knowledge and Therapeutic Perspectives in the Postantibiotic Era.Exploring the mechanisms of action of human secretory RNase 3 and RNase 7 against Candida albicansAntifungal activity in vitro and in vivo of a salmon protamine peptide and its derived cyclic peptide against Candida albicans.Msb2 shedding protects Candida albicans against antimicrobial peptidesImpaired Histatin-5 Levels and Salivary Antimicrobial Activity against C. albicans in HIV Infected Individuals.FLO11 Gene Is Involved in the Interaction of Flor Strains of Saccharomyces cerevisiae with a Biofilm-Promoting Synthetic Hexapeptide.Silver adducts of four-branched histidine rich peptides exhibit synergistic antifungal activityLive-cell imaging and analysis shed light on the complexity and dynamics of antimicrobial Peptide action.ZEBRA cell-penetrating peptide as an efficient delivery system in Candida albicans.Exploring the mode of action of antimicrobial peptide MUC7 12-mer by fitness profiling of Saccharomyces cerevisiae genomewide mutant collectionSpecific domains of plant defensins differentially disrupt colony initiation, cell fusion and calcium homeostasis in Neurospora crassa.Translocation of cell-penetrating peptides into Candida fungal pathogens.
P2860
Q27318277-9EF798C3-10D4-4F72-B4D4-F277555FA2D5Q27320076-39AD1880-51BC-4B07-A876-B35C3286EFEBQ28070241-1DEBE14C-AB52-42DD-A788-D7C482D99810Q30840368-349447AA-2499-423D-9FF2-B76B0BDDD988Q33427799-5E819A22-927A-4F7D-861B-AA9A2C2CD92CQ33811522-DFA1C88E-0505-4875-8FA8-ECE2DF79F6B3Q33862289-C49D9E77-57B1-418E-BF85-37EB52BF487BQ34017572-370DAB6F-7670-4B02-A76A-9A41EA269203Q34205894-C486F95F-663B-45C0-B2A1-22ECBFAC39A6Q34335954-032D0506-B4B8-4880-AD34-9184F3AE3600Q34684434-9CD4DA96-2254-443D-A0C9-FCB630C0EAD9Q35626181-01942764-4ACC-41B7-9917-C5E3221A77ECQ36023033-FFB15A57-B690-4F3C-99C6-1BFCAB6746DEQ36208858-55CCE7AE-A0C2-4643-8F78-36A62080D8A6Q36334389-7F4A16AC-40A4-4EF2-A1FE-72E32F34E2AFQ36335705-CD127644-2B20-4FD7-8C2D-7A6F0B4396B6Q36558457-57436024-8E4E-4527-B748-75B67AAD53D1Q37120200-98D4CA8E-1AE5-419A-A230-326EA08B3F5DQ37333447-5D8A0E7E-5A01-4045-9CBB-0DBB59196810Q37562147-C3E7D5A6-5945-4A78-95AC-FA97E04D781FQ37611973-CAB780CB-877A-4B5A-B430-73271711C7BDQ37802873-99DCE7CD-F239-4B62-BB9E-EF7475ACA6E3Q38089201-FC5AA14F-BA33-4A40-92A9-69768B239119Q38201011-FE514C57-42F8-459C-833F-254460A7D95BQ38222086-FB5E2AB8-BE7B-4B09-ABD0-E4ADF27C513AQ38626954-7DEDC329-340A-4F65-898F-6338354EE50CQ38839324-AD0F2EDD-8952-4387-951C-09222B51A85EQ38899655-201A543B-E0F9-4411-92E5-1555DD911757Q39091774-F93E8463-A64A-4609-BF22-32B778A07B1DQ39699474-7B2D845C-AE0F-4A75-ACA7-CEC8B8E0D048Q40424835-64B5C82F-8053-4CFF-90EF-C4F38B241209Q40812978-ABB2B333-BB11-458A-A38D-669449645D5BQ41125894-0223ABE7-8E4E-48EF-A172-3E9811F9463AQ42012886-5AAE6235-A7D1-487E-9994-9EDA2922A753Q42014331-89B88048-E7F4-4145-BE97-2C082C398166Q42115303-9B2C49BC-CF73-4069-9E03-6E715E89830DQ42241969-72EBF67C-86DF-4842-8211-79E01F12E11BQ42545794-1D93E791-2092-4059-8D9D-B4CAF5977111Q44285864-0116E5D4-B064-4056-BAF3-CC969AE0ACB2Q46359263-B895DD9F-B4F5-4E30-A3A5-A0BA8F5A0258
P2860
The antimicrobial peptide histatin-5 causes a spatially restricted disruption on the Candida albicans surface, allowing rapid entry of the peptide into the cytoplasm
description
2008 nî lūn-bûn
@nan
2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
The antimicrobial peptide hist ...... the peptide into the cytoplasm
@ast
The antimicrobial peptide hist ...... the peptide into the cytoplasm
@en
The antimicrobial peptide hist ...... the peptide into the cytoplasm
@nl
type
label
The antimicrobial peptide hist ...... the peptide into the cytoplasm
@ast
The antimicrobial peptide hist ...... the peptide into the cytoplasm
@en
The antimicrobial peptide hist ...... the peptide into the cytoplasm
@nl
prefLabel
The antimicrobial peptide hist ...... the peptide into the cytoplasm
@ast
The antimicrobial peptide hist ...... the peptide into the cytoplasm
@en
The antimicrobial peptide hist ...... the peptide into the cytoplasm
@nl
P2860
P3181
P1433
P1476
The antimicrobial peptide hist ...... the peptide into the cytoplasm
@en
P2093
A Brian Mochon
Haoping Liu
P2860
P304
P3181
P356
10.1371/JOURNAL.PPAT.1000190
P407
P577
2008-10-01T00:00:00Z