about
Production of extracellular traps against Aspergillus fumigatus in vitro and in infected lung tissue is dependent on invading neutrophils and influenced by hydrophobin RodADevelopment in AspergillusAspergillus fumigatus: principles of pathogenesis and host defenseVirulence factors of medically important fungiInteractions of Aspergillus fumigatus Conidia with Airway Epithelial Cells: A Critical ReviewHyphal growth of phagocytosed Fusarium oxysporum causes cell lysis and death of murine macrophagesTranscriptional Control of Drug Resistance, Virulence and Immune System Evasion in Pathogenic Fungi: A Cross-Species ComparisonIsolate-dependent growth, virulence, and cell wall composition in the human pathogen Aspergillus fumigatusAspergillus terreus accessory conidia are unique in surface architecture, cell wall composition and germination kineticsThe spectrum of fungi that infects humansAspergillus fumigatus and aspergillosisDisruption of the gene which encodes a serodiagnostic antigen and chitinase of the human fungal pathogen Coccidioides immitis.Rodent Models of Invasive Aspergillosis due to Aspergillus fumigatus: Still a Long Path toward Standardization.The developmentally regulated alb1 gene of Aspergillus fumigatus: its role in modulation of conidial morphology and virulence.Hydrophobins from Aspergillus species cannot be clearly divided into two classesLack of evidence for a role of hydrophobins in conferring surface hydrophobicity to conidia and hyphae of Botrytis cinereaThe Aspergillus fumigatus cspA gene encoding a repeat-rich cell wall protein is important for normal conidial cell wall architecture and interaction with host cellsCalcineurin controls growth, morphology, and pathogenicity in Aspergillus fumigatusHost cell invasion by medically important fungiNikA/TcsC histidine kinase is involved in conidiation, hyphal morphology, and responses to osmotic stress and antifungal chemicals in Aspergillus fumigatus.Fungal virulence genes as targets for antifungal chemotherapy.Six hydrophobins are involved in hydrophobin rodlet formation in Aspergillus nidulans and contribute to hydrophobicity of the spore surface.Targeted disruption of nonribosomal peptide synthetase pes3 augments the virulence of Aspergillus fumigatusThe proteomic signature of Aspergillus fumigatus during early development.Global transcriptome changes underlying colony growth in the opportunistic human pathogen Aspergillus fumigatus.Transcription Factor SomA Is Required for Adhesion, Development and Virulence of the Human Pathogen Aspergillus fumigatus.Coding tandem repeats generate diversity in Aspergillus fumigatus genes.Molecular mechanism of Aspergillus fumigatus adherence to host constituents.High-resolution cell surface dynamics of germinating Aspergillus fumigatus conidia.Chitin synthases with a myosin motor-like domain control the resistance of Aspergillus fumigatus to echinocandins.Adhesins in human fungal pathogens: glue with plenty of stick.Regulation of Development in Aspergillus nidulans and Aspergillus fumigatus.Pharmacokinetics of posaconazole within epithelial cells and fungi: insights into potential mechanisms of action during treatment and prophylaxis.Aspergillosis and stem cell transplantation: An overview of experimental pathogenesis studies.Co-recognition of β-glucan and chitin and programming of adaptive immunity to Aspergillus fumigatus.Fungal Biofilms: Inside Out.Purification and partial characterization of a 32-kilodalton sialic acid-specific lectin from Aspergillus fumigatus.Conidial hydrophobins of Aspergillus fumigatus.Binding of human fibronectin to Aspergillus fumigatus conidia.Binding of extracellular matrix proteins to Aspergillus fumigatus conidia.
P2860
Q21559410-397648AC-EDAF-442E-909A-FA4545812EB0Q24627669-5CC56E52-28AB-4550-92F5-B2CB4452967BQ24681995-D4316698-E0A0-4E4C-AC43-14A6B5EFB3BDQ24683790-6F7ED9C1-D94E-44F9-ACEA-3A3D026B68C1Q26863572-11294FA9-08B8-4826-BCB3-95E5AF3F22AEQ27320017-FF15DF9D-19F9-4A62-B1B3-0742DFF8B4C0Q28079641-B65F82C5-EB4A-45C4-A4CD-D9397754B923Q28388263-BC02F98E-3829-4DF2-B065-E30F46D11809Q28471716-AF3C30B4-7154-411F-BF29-D3708E95C7E8Q28652321-E9474CD6-C3E3-485A-8572-E116C3F4BC95Q29617908-815C88CD-D2A2-4C7A-8697-664D305ABAA7Q33592423-DD1E3611-6A19-4D39-9B4A-9654A22577F7Q33689767-DF9E3DD6-51AD-4D75-ACA0-475734BA4435Q33745136-F404852F-0252-4A2B-94EA-FEF25C1222C4Q33779561-2F7DC3B5-7696-45AB-81A5-7B2374C8F6DCQ33792668-2DA09754-48AA-413F-88ED-70F336662D72Q34118934-6AF2CC1D-0F75-4E58-90AC-501804B82330Q34718619-1C3E2D31-6B0A-416D-9110-33F06B480677Q34930227-FB1E609E-596B-4D7D-9E32-54EE00985B5FQ35061130-3089907B-2038-4A8B-9E77-30D3796BA63CQ35125420-A61028F7-A58E-4D19-BBCE-AC6CE561E5A0Q35145425-2D041C82-D52F-4A06-A021-D17F997DBF69Q35272907-F7EE1B52-41AF-46A3-AADE-3E34EFB15C28Q35579624-AEE47D87-74E2-40C6-98C4-79E6423F1BD7Q35666165-59B31ACE-99E0-419D-94AB-355496F53D2FQ35830582-2762A4A9-EEDC-4DA9-B19F-B4394FB6DAD7Q35947161-BCA59892-B915-4617-B52F-383658BACEBAQ36018382-8E653BA4-040F-42F2-916D-EA808C4D5777Q36303163-C38DB3FF-BAF1-438D-8EFD-38D22CD8BBEEQ36396188-17BBC23F-99F2-4E77-B4B9-1CC0687B8919Q36757905-510870E7-4F07-4052-8104-2F383C39203CQ37090153-BB10236E-D36B-49C3-9F1F-A85B873980D6Q37247452-4D3AA812-885C-4018-8F50-1CAF838E4FFDQ38968506-8C742F18-83B0-45A5-9D69-F968178E2806Q39009509-F61D5AF7-A3B8-406A-AED3-1454AE4FD56CQ39226110-8BEAC3FD-550D-4657-A931-3827941DC437Q39672337-233DF477-242D-42E0-A1AC-C65AF9F28796Q39734734-9922551D-750C-4DFC-B678-1D69F37C5C2DQ39824574-7F709D40-2F1A-4395-95C6-6E56DE58A6AAQ39826901-108C7144-5588-490F-B52C-D02F8C27099C
P2860
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
rodletless mutants of Aspergillus fumigatus.
@en
type
label
rodletless mutants of Aspergillus fumigatus.
@en
prefLabel
rodletless mutants of Aspergillus fumigatus.
@en
P2093
P2860
P921
P1476
rodletless mutants of Aspergillus fumigatus.
@en
P2093
Crestani B
Tronchin G
P2860
P304
P407
P577
1994-10-01T00:00:00Z