ReviewFrontiers in microbiology2016
Candida albicans Agglutinin-Like Sequence (Als) Family Vignettes: A Review of Als Protein Structure and Function.
Review in Frontiers in microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
129 citing papers in PubMed.
- Antibiofilm and Anti-Hyphal Activities of Halogenated Benzophenones Against Azole-ResistantInternational journal of molecular sciences · 2026Article
- GcrR in Streptococcus mutans Inhibits the Morphological Transition of Candida albicans Through Ras1-cAMP/PKA Pathway in the Cross-Kingdom Biofilms.Molecular oral microbiology · 2026Article
- Targeting Als3 adhesin of clinically relevant Candida species using natural carotenoids: an in-silico study.Molecular diversity · 2026Article
- Cytokine signalling in vaginal epithelial cells: mechanistic insights into epithelial immunity and inflammatory milieu in vulvovaginal candidiasis.European cytokine network · 2026Review
- Effect of subsequent passages on biofilm formation intensity, ALS genes expression, and cell surface hydrophobicity variability in clinical Candida albicans isolates.Scientific reports · 2026Article
- Vulvovaginal candidiasis among Yemeni women: prevalence of Candida species, biofilm formation rates, antifungal susceptibility patterns, and biofilm-associated genes ALS1 and HWP1.BMC microbiology · 2026Article
- Insights on molecular drivers of phenotypic plasticity in Candidozyma auris.World journal of microbiology & biotechnology · 2026Review
- F2F-202, a Selective Histone Deacetylase 6 (HDAC6) Inhibitor, Behaves as an Arrow with Multiple Tips against Azole-ResistantACS infectious diseases · 2026Article
- A conserved Sas10/C1D domain protein, CaLrp1, is a critical regulator of hyphal development and pathogenicity in Candida albicans.BMC microbiology · 2026Article
- Candicidal Effect of a Nanoemulsion Based on the Essential Oil of the Medicinal PlantPharmaceuticals (Basel, Switzerland) · 2026Article
- Exploring the Mechanism of Tannic Acid AgainstPathogens (Basel, Switzerland) · 2026Article
- Protein-related hydrophobicity differences among strains belonging toMicrobiology spectrum · 2026Article
- The Four Critical Priority Fungi According to the World Health Organization and the Hope for New Therapies: A Focus on Cell Wall Antifungal Targets.Journal of fungi (Basel, Switzerland) · 2026Review
- EmergentMicroorganisms · 2026Review
- Integrated mechanistic and bioinformatics analysis of a traditional Chinese medicine compound MangHuang solution againstFrontiers in cellular and infection microbiology · 2026Article
- The V-ATPase VJournal of oral microbiology · 2026Article
- Context-dependent reprogramming ofFrontiers in microbiology · 2026Article
- Artemisinins inhibited the synergistic cariogenic effect betweenFrontiers in cellular and infection microbiology · 2026Article
- Amyloid fibrils of the Als5p-derived peptide NHVirulence · 2025Article
- The dual antifungal and antibiofilm activities of β-carotene against multidrug-resistant Candida albicans induce wound healing in a diabetic rat model: an in vitro and in vivo study.BMC microbiology · 2025Article
69 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Approximately two decades have passed since the description of the first gene in the Candida albicans ALS (agglutinin-like sequence) family. Since that time, much has been learned about the composition of the family and the function of its encoded cell-surface glycoproteins. Solution of the structure of the Als adhesive domain provides the opportunity to evaluate the molecular basis for protein function. This review article is formatted as a series of fundamental questions and explores the diversity of the Als proteins, as well as their role in ligand binding, aggregative effects, and attachment to abiotic surfaces. Interaction of Als proteins with each other, their functional equivalence, and the effects of protein abundance on phenotypic conclusions are also examined. Structural features of Als proteins that may facilitate invasive function are considered. Conclusions that are firmly supported by the literature are presented while highlighting areas that require additional investigation to reveal basic features of the Als proteins, their relatedness to each other, and their roles in C. albicans biology.
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