Yeast cell adhesion molecules have functional amyloid-forming sequences. - Wikidata - awgldk - TriplyDB

Yeast cell adhesion molecules have functional amyloid-forming sequences.

Yeast cell adhesion molecules have functional amyloid-forming sequences.

http://www.wikidata.org/entity/Q39605902

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Candida albicans Agglutinin-Like Sequence (Als) Family Vignettes: A Review of Als Protein Structure and Function Diversity, biogenesis and function of microbial amyloids Systemic Staphylococcus aureus infection mediated by Candida albicans hyphal invasion of mucosal tissue.Structural basis of flocculin-mediated social behavior in yeast Structural basis for the broad specificity to host-cell ligands by the pathogenic fungus Candida albicans Flo11p, drug efflux pumps, and the extracellular matrix cooperate to form biofilm yeast colonies.The GPI anchor signal sequence dictates the folding and functionality of the Als5 adhesin from Candida albicans pH dependence of listeriolysin O aggregation and pore-forming ability Role of force-sensitive amyloid-like interactions in fungal catch bonding and biofilms.Strengthening relationships: amyloids create adhesion nanodomains in yeasts.Extensive Copy Number Variation in Fermentation-Related Genes Among Saccharomyces cerevisiae Wine Strains.A profile of differentially abundant proteins at the yeast cell periphery during pseudohyphal growth.A role for amyloid in cell aggregation and biofilm formation.Functional amyloid formation by Streptococcus mutans.Heterologous expression of Candida albicans cell wall-associated adhesins in Saccharomyces cerevisiae Reveals differential specificities in adherence and biofilm formation and in binding oral Streptococcus gordonii.Force-induced formation and propagation of adhesion nanodomains in living fungal cells.The Mnn2 mannosyltransferase family modulates mannoprotein fibril length, immune recognition and virulence of Candida albicans Structural insights into functional and pathological amyloid.Forces in yeast flocculation.Rbt1 protein domains analysis in Candida albicans brings insights into hyphal surface modifications and Rbt1 potential role during adhesion and biofilm formation.Effects of the strain background and autolysis process on the composition and biophysical properties of the cell wall from two different industrial yeasts.Quantitative Analyses of Force-Induced Amyloid Formation in Candida albicans Als5p: Activation by Standard Laboratory Procedures.Insight into the antiadhesive effect of yeast wall protein 1 of Candida albicans Unzipping a functional microbial amyloid.Architecture and biosynthesis of the Saccharomyces cerevisiae cell wall.The Human Disease-Associated Aβ Amyloid Core Sequence Forms Functional Amyloids in a Fungal Adhesin Nanoscale analysis of caspofungin-induced cell surface remodelling in Candida albicans.Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif.Adhesins in human fungal pathogens: glue with plenty of stick.Does Candida albicans Als5p amyloid play a role in commensalism in Caenorhabditis elegans?Candida albicans CUG mistranslation is a mechanism to create cell surface variation.Biofilm Exopolysaccharides of Pathogenic Fungi: Lessons from Bacteria.Choosing the right lifestyle: adhesion and development in Saccharomyces cerevisiae.A mass spectrometric view of the fungal wall proteome.Association of skin with the pathogenesis and treatment of neurodegenerative amyloidosis Recent developments in yeast cell surface display toward extended applications in biotechnology.Self-propagating amyloid as a critical regulator for diverse cellular functions.Structure and function of glycosylated tandem repeats from Candida albicans Als adhesins.Between Amyloids and Aggregation Lies a Connection with Strength and Adhesion.AMPK in Pathogens.

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P2860

Yeast cell adhesion molecules have functional amyloid-forming sequences.

http://www.wikidata.org/entity/Q39605902

description

2009 nî lūn-bûn

@nan

2009年の論文

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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

Yeast cell adhesion molecules have functional amyloid-forming sequences.

@en

Yeast cell adhesion molecules have functional amyloid-forming sequences.

@nl

type

label

Yeast cell adhesion molecules have functional amyloid-forming sequences.

@en

Yeast cell adhesion molecules have functional amyloid-forming sequences.

@nl

prefLabel

Yeast cell adhesion molecules have functional amyloid-forming sequences.

@en

Yeast cell adhesion molecules have functional amyloid-forming sequences.

@nl

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Eukaryotic Cell

P1476

Yeast cell adhesion molecules have functional amyloid-forming sequences.

@en

P2093

Anna Litewka

http://www.w3.org/2001/XMLSchema#string

Anne M Dranginis

http://www.w3.org/2001/XMLSchema#string

Caleen B Ramsook

http://www.w3.org/2001/XMLSchema#string

Cho Tan

http://www.w3.org/2001/XMLSchema#string

Chong K Jue

http://www.w3.org/2001/XMLSchema#string

Gregory Soybelman

http://www.w3.org/2001/XMLSchema#string

Henry N Otoo

http://www.w3.org/2001/XMLSchema#string

Jason M Rauceo

http://www.w3.org/2001/XMLSchema#string

Melissa C Garcia

http://www.w3.org/2001/XMLSchema#string

Nand K Gaur

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P2860

Functional amyloid formation within mammalian tissue.

FLO1 is a variable green beard gene that drives biofilm-like cooperation in budding yeast

A systematic survey identifies prions and illuminates sequence features of prionogenic proteins

Atomic structures of amyloid cross-beta spines reveal varied steric zippers

Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions

A Saccharomyces gene family involved in invasive growth, cell-cell adhesion, and mating

Region of FLO1 proteins responsible for sugar recognition

Prediction of the secondary structure of proteins from their amino acid sequence

Surface hydrophobin prevents immune recognition of airborne fungal spores

Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins

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393-404

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scholarly article

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10.1128/EC.00068-09

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3

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9

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2009-12-28T00:00:00Z

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20038605

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2837979

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