scholarly journals Intrinsic Disorder Is a Common Feature of Hub Proteins from Four Eukaryotic Interactomes

2006 ◽  
Vol 2 (8) ◽  
pp. e100 ◽  
Author(s):  
Chad Haynes ◽  
Christopher J Oldfield ◽  
Fei Ji ◽  
Niels Klitgord ◽  
Michael E Cusick ◽  
...  
Keyword(s):  
Intrinsic Disorder ◽  
Hub Proteins

Role of intrinsic disorder in transient interactions of hub proteins

2006 ◽  
Vol 66 (4) ◽  
pp. 761-765 ◽  
Author(s):  
Gajinder Pal Singh ◽  
Mythily Ganapathi ◽  
Debasis Dash
Keyword(s):  
Intrinsic Disorder ◽  
Transient Interactions ◽  
Hub Proteins

scholarly journals Relationships between Subcellular Localization, Hub Proteins and Intrinsic Disorder

2017 ◽  
Vol 57 (2) ◽  
pp. 085-089
Author(s):  
Motonori OTA ◽  
Satoshi FUKUCHI ◽  
Ryotaro KOIKE
Keyword(s):  
Subcellular Localization ◽  
Intrinsic Disorder ◽  
Hub Proteins

Exploring the relationship between hub proteins and drug targets based on GO and intrinsic disorder

2015 ◽  
Vol 56 ◽  
pp. 41-48 ◽  
Author(s):  
Yuanyuan Fu ◽  
Yanzhi Guo ◽  
Yuelong Wang ◽  
Jiesi Luo ◽  
Xuemei Pu ◽  
...  
Keyword(s):  
Drug Targets ◽  
Intrinsic Disorder ◽  
The Relationship ◽  
Hub Proteins

scholarly journals Intrinsic Disorder is a Common Feature of Hub Proteins from Four Eukaryotic Interactomes

2005 ◽  
Vol preprint (2006) ◽  
pp. e100 ◽  
Author(s):  
Chad Haynes ◽  
Christopher J Oldfield ◽  
Fei Ji ◽  
Niels Klitgord ◽  
Michael E Cusick ◽  
...  
Keyword(s):  
Intrinsic Disorder ◽  
Hub Proteins

Hubsm: A Novel Amino Acid Substitution Matrix for Comparing Hub Proteins

2017 ◽  
Vol 7 (8) ◽  
pp. 212
Author(s):  
Renganayaki G. ◽  
Achuthsankar S. Nair
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Low Complexity ◽  
Database Search ◽  
Substitution Matrix ◽  
Compositional Bias ◽  
Sequence Alignments ◽  
Amino Acid Substitution Matrix ◽  
Alignment Algorithms ◽  
Hub Proteins

Sequence alignment algorithms and  database search methods use BLOSUM and PAM substitution matrices constructed from general proteins. These de facto matrices are not optimal to align sequences accurately, for the proteins with markedly different compositional bias in the amino acid.   In this work, a new amino acid substitution matrix is calculated for the disorder and low complexity rich region of Hub proteins, based on residue characteristics. Insights into the amino acid background frequencies and the substitution scores obtained from the Hubsm unveils the  residue substitution patterns which differs from commonly used scoring matrices .When comparing the Hub protein sequences for detecting homologs,  the use of this Hubsm matrix yields better results than PAM and BLOSUM matrices. Usage of Hubsm matrix can be optimal in database search and for the construction of more accurate sequence alignments of Hub proteins.

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