In this section
@article{Cota:2015:10.2217/fmb.15.79,
author = {Cota, E and Hoyer, LL},
doi = {10.2217/fmb.15.79},
journal = {Future Microbiology},
pages = {1635--1648},
title = {The Candida albicans agglutinin-like sequence family of adhesins: functional insights gained from structural analysis},
url = {http://dx.doi.org/10.2217/fmb.15.79},
volume = {10},
year = {2015}
}
TY - JOUR
AB - Candida albicans colonizes many host sites suggesting its interaction with diverse ligands.Candida albicans adhesion is mediated by a number of proteins including those in the Als(agglutinin-like sequence) family, which have been studied intensively. The recent solutionof the Als binding domain structure ended years of speculation regarding the molecularmechanism for Als adhesive function. Als adhesins bind flexible C termini from a broadcollection of proteins, providing the basis for adhesion to various cell types and perhaps forC. albicans broad tissue tropism. Understanding adhesive functions at the molecular level willreveal the sequence of events in C. albicans pathogenesis, from host recognition to complexinteractions such as development of polymicrobial biofilms or disseminated disease.
AU - Cota,E
AU - Hoyer,LL
DO - 10.2217/fmb.15.79
EP - 1648
PY - 2015///
SN - 1746-0921
SP - 1635
TI - The Candida albicans agglutinin-like sequence family of adhesins: functional insights gained from structural analysis
T2 - Future Microbiology
UR - http://dx.doi.org/10.2217/fmb.15.79
VL - 10
ER -
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