Imperial College London
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Dr Ernesto Cota

Faculty of Natural Sciences, Department of Life Sciences

Senior Lecturer
 
 
 
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Contact

 

+44 (0)20 7594 3689e.cota Website

 
 
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Location

 

601Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Hoyer:2016:10.3389/fmicb.2016.00280,
author = {Hoyer, LL and Cota, E},
doi = {10.3389/fmicb.2016.00280},
journal = {Frontiers in Microbiology},
title = {Candida albicans agglutinin-like sequence (aIs) family vignettes: a review of aIs protein structure and function},
url = {http://dx.doi.org/10.3389/fmicb.2016.00280},
volume = {7},
year = {2016}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Approximately two decades have passed since the description of the first gene inthe Candida albicans ALS (agglutinin-like sequence) family. Since that time, much hasbeen learned about the composition of the family and the function of its encoded cellsurfaceglycoproteins. Solution of the structure of the Als adhesive domain providesthe opportunity to evaluate the molecular basis for protein function. This review articleis formatted as a series of fundamental questions and explores the diversity of the Alsproteins, as well as their role in ligand binding, aggregative effects, and attachment toabiotic 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 highlightingareas that require additional investigation to reveal basic features of the Als proteins,their relatedness to each other, and their roles in C. albicans biology.
AU  - Hoyer,LL
AU  - Cota,E
DO  - 10.3389/fmicb.2016.00280
PY  - 2016///
SN  - 1664-302X
TI  - Candida albicans agglutinin-like sequence (aIs) family vignettes: a review of aIs protein structure and function
T2  - Frontiers in Microbiology
UR  - http://dx.doi.org/10.3389/fmicb.2016.00280
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000372116100002&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - http://hdl.handle.net/10044/1/31000
VL  - 7
ER  -
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