نتایج جستجو برای: aspartyl proteinase
تعداد نتایج: 13130 فیلتر نتایج به سال:
Proper morphology is essential for the ability of Candida albicans to switch between yeast and hyphae and thereby sustain its virulence. Here we identified, by differential screening, a novel C. albicans AAA ATPase encoding gene, CaYLL34 (RIX7), with enhanced expression in hyphae. Phylogenetic analysis suggests that CaYLL34 belongs to a "VCP-like" subgroup of AAA ATPases essential for yeast via...
Candida tropicalis infection is strongly associated with the presence of biofilms in urinary catheters. Thus, the aim of this work was to study the behaviour of C. tropicalis in biofilms of different ages (24-120 h) formed in artificial urine (AU) and their effect in human urinary bladder cells (TCC-SUP). Reference strain ATCC 750 and two isolates from patients with candiduria (U69 and U75) wer...
Candida dubliniensis is a recently identified species which is implicated in oral candidosis in HIV-infected and AIDS patients. The species shares many phenotypic characteristics with, and is phylogenetically closely related to, Candida albicans. In this study the phylogenetic relationship between these two species was investigated and a comparison of putative virulence factors was performed. F...
The ALS (agglutinin-like sequence) gene family of Candida albicans encodes cell-surface glycoproteins implicated in adhesion of the organism to host surfaces. Southern blot analysis with ALS-specific probes suggested the presence of ALS gene families in C. dubliniensis and C. tropicalis; three partial ALS genes were isolated from each organism. Northern blot analysis demonstrated that mechanism...
Chronic inflammation rather than invasion is characteristic of some forms of superficial candidiasis such as denture stomatitis. We hypothesized that Candida albicans may play a critical role in the pathogenesis of inflammatory lesions observed in chronic candidiasis by activating the proinflammatory cytokine interleukin-1beta (IL-1beta) from epithelial stores of the precursor. The aim of this ...
BACKGROUND AND OBJECTIVES Secreted Aspartyl Proteinase (SAP) is one of the main virulence factors in the pathogenesis of Candida. This enzyme is encoded by a family of at least ten genes. Among these genes, the role of SAP1-3 in mucosal infections is evident. This study aimed to investigate the expression of SAP1-3 genes of Candida albicans isolates after treatment with Echinophora platyloba ex...
The amino acid sequence of the major trypsin inhibitor, F, of ungerminated mung beans (Vigna radiata [L.] Wilczek) was determined by a combination of automatic solid phase and manual sequencing techniques. F is a typical Bowman-Birk-type proteinase inhibitor with 80 amino acid residues and exhibits a high degree of identity with the other sequenced members of the Bowman-Birk family of inhibitor...
No. Haka7191 Beamline(s): X4A, X12C Introduction: Aspartyl dipeptidase (peptidase E) and tripeptidase (peptidase T) from Salmonella typhimurium are intracellular peptidases with very different specificities and structures. Aspartyl dipeptidase is a serine hydrolase that cleaves dipeptides with an N-terminal aspartate, and tripeptidase is a metallopeptidase that releases the N-terminal, preferab...
N-terminal extension of sweet peptides in relation to the structural features of peptide sweeteners.
Sweet aspartyl di- and tripeptide esters were extended toward the N-terminus in relation to the structural features of sweet peptides. The sweet peptides were designed on the basis of the receptor site model. It was found that an extension of the sweet aspartyl dipeptide esters by adding a small D-amino acid residue mostly gave sweet compounds (e.g., D-Ala-L-Asp-D-Ala-OMe), although this signif...
Non-repair pathways for minimizing protein isoaspartyl damage in the yeast Saccharomyces cerevisiae.
The spontaneous degradation of asparaginyl and aspartyl residues to isoaspartyl residues is a common type of protein damage in aging organisms. Although the protein-l-isoaspartyl (d-aspartyl) O-methyltransferase (EC 2.1.1.77) can initiate the repair of l-isoaspartyl residues to l-aspartyl residues in most organisms, no gene homolog or enzymatic activity is present in the budding yeast Saccharom...
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