z-logo
open-access-imgOpen Access
Dscam1 web server: online prediction of Dscam1 self- and hetero-affinity
Author(s) -
Simone Marini,
N. Nazzicari,
Filippo Biscarini,
Guang-Zhong Wang
Publication year - 2017
Publication title -
bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.599
H-Index - 390
eISSN - 1367-4811
pISSN - 1367-4803
DOI - 10.1093/bioinformatics/btx039
Subject(s) - web server , computer science , clickstream , key (lock) , binding site , computational biology , world wide web , the internet , biology , web api , biochemistry , operating system
Formation of homodimers by identical Dscam1 protein isomers on cell surface is the key factor for the self-avoidance of growing neurites. Dscam1 immense diversity has a critical role in the formation of arthropod neuronal circuit, showing unique evolutionary properties when compared to other cell surface proteins. Experimental measures are available for 89 self-binding and 1722 hetero-binding protein samples, out of more than 19 thousands (self-binding) and 350 millions (hetero-binding) possible isomer combinations.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom