The glycosylphosphatidylinositol-anchored protease Sap9 modulates the interaction of Candida albicans with human neutrophils.
about
Candida albicans possesses Sap7 as a pepstatin A-insensitive secreted aspartic proteaseThe Extracellular Matrix of Candida albicans Biofilms Impairs Formation of Neutrophil Extracellular TrapsProteolytic cleavage of covalently linked cell wall proteins by Candida albicans Sap9 and Sap10Glycosylation of Candida albicans cell wall proteins is critical for induction of innate immune responses and apoptosis of epithelial cells.Defining the transcriptomic landscape of Candida glabrata by RNA-Seq.A virtual infection model quantifies innate effector mechanisms and Candida albicans immune escape in human blood.In vivo induction of neutrophil chemotaxis by secretory aspartyl proteinases of Candida albicans.Secretory aspartyl proteinases induce neutrophil chemotaxis in vivoSap6, a secreted aspartyl proteinase, participates in maintenance the cell surface integrity of Candida albicans.Innate antifungal immunity: the key role of phagocytes.Aspartic proteinases of Candida spp.: role in pathogenicity and antifungal resistance.Expression of Secreted Aspartyl Proteinases in an Experimental Model of Candida albicans-Associated Denture Stomatitis.Description of the interaction between Candida albicans and macrophages by mixed and quantitative proteome analysis without isolation.Aspartic Proteases and Major Cell Wall Components in Candida albicans Trigger the Release of Neutrophil Extracellular Traps.The Inflammatory response induced by aspartic proteases of Candida albicans is independent of proteolytic activity.Carbon source-induced reprogramming of the cell wall proteome and secretome modulates the adherence and drug resistance of the fungal pathogen Candida albicans.NLRP3 inflammasome is a key player in human vulvovaginal disease caused by Candida albicans.
P2860
Q28481265-C1EDD718-1748-43AF-B64E-7E7E221570BFQ28554057-62B4AE09-80D7-49C4-8974-2DEEC2AB8C54Q34484177-53FF119E-1E5A-4A84-837F-A32101421071Q34505465-6A2AD97E-6356-4C84-8C9B-ED9AB817B363Q35088957-CE39CDA4-4E0E-459D-933F-BA8446B7DEFDQ35105573-3A80CE4F-AF2C-4327-A046-FF4F84ACBDFBQ37268449-5877D703-6DDA-43AE-8EC8-514E86CB0272Q37268454-759C85FE-63AA-4506-9766-962F733875E0Q37473868-12FEF85F-A39B-4CF7-913E-BD4970057876Q37799378-D10DDE02-3B40-404C-84FA-FAB935D47FD5Q38111859-BFCDB697-B709-4F27-B1BC-48D77293299AQ41096656-BD66BB50-D03B-4F9E-AD01-9F0ACD399F81Q41690473-C0B22D3E-CA6B-4D52-A723-0FFBB182CB18Q42098852-E14BE1D7-6B5E-4960-8F81-153AE142DBE7Q42220965-FD316C67-1E36-4C47-B3C2-AD027B74F9B9Q42944837-87D1F8E0-B8F3-4AAD-86CA-7685B18AC6BEQ47138065-818F3866-BE45-4F92-A6D9-784FE869CA28
P2860
The glycosylphosphatidylinositol-anchored protease Sap9 modulates the interaction of Candida albicans with human neutrophils.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
The glycosylphosphatidylinosit ...... bicans with human neutrophils.
@en
The glycosylphosphatidylinosit ...... bicans with human neutrophils.
@nl
type
label
The glycosylphosphatidylinosit ...... bicans with human neutrophils.
@en
The glycosylphosphatidylinosit ...... bicans with human neutrophils.
@nl
prefLabel
The glycosylphosphatidylinosit ...... bicans with human neutrophils.
@en
The glycosylphosphatidylinosit ...... bicans with human neutrophils.
@nl
P2093
P2860
P356
P1476
The glycosylphosphatidylinosit ...... bicans with human neutrophils.
@en
P2093
Anke Hornbach
Antje Heyken
Jürgen Löffler
Lydia Schild
P2860
P304
P356
10.1128/IAI.00723-09
P407
P577
2009-10-05T00:00:00Z