Zobrazeno 1 - 10
of 10
pro vyhledávání: '"S Binny Priya"'
Publikováno v:
PLoS ONE, Vol 14, Iss 1, p e0210475 (2019)
Human variant databases could be better exploited if the variant data available in multiple resources is integrated in a single comprehensive resource along with sequence and structural features. Such integration would improve the analyses of variant
Externí odkaz:
https://doaj.org/article/32ea9fd909954160badda5d33ab5d603
Autor:
S. Binny Priya, M. Michael Gromiha
Publikováno v:
Journal of Cellular Biochemistry. 120:10519-10529
Huntington disease is a neurodegenerative disorder caused by the expansion of polyglutamine (polyQ) at the N-terminal of the huntingtin exon 1 protein. The detailed structure and the mechanism behind this aggregation remain unclear and it is assumed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32877d61b73ca73f9653268da3cd087e
https://doi.org/10.1002/jcb.28338
https://doi.org/10.1002/jcb.28338
Autor:
S. Binny Priya, M. Michael Gromiha, Pradeep Kumar, R. Nagarajan, A. Kulandaisamy, Ambuj Srivastava
Publikováno v:
IEEE/ACM Transactions on Computational Biology and Bioinformatics. 15:1436-1444
Protein-RNA complexes play important roles in various biological processes. The functions of protein-RNA complexes are dictated by their interactions, binding, stability, and affinity. In this work, we have identified the key residues (KRs), which ar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::471bd8af7fc24472b2c13b2bfb463fc0
https://doi.org/10.1109/tcbb.2018.2834387
https://doi.org/10.1109/tcbb.2018.2834387
Publikováno v:
PLoS ONE
PLoS ONE, Vol 14, Iss 1, p e0210475 (2019)
PLoS ONE, Vol 14, Iss 1, p e0210475 (2019)
Human variant databases could be better exploited if the variant data available in multiple resources is integrated in a single comprehensive resource along with sequence and structural features. Such integration would improve the analyses of variant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11d5286d507fb2c6979a165a573001ee
https://pubmed.ncbi.nlm.nih.gov/30703169
https://pubmed.ncbi.nlm.nih.gov/30703169
Publikováno v:
Proteins. 87(6)
Mutations in transmembrane proteins (TMPs) have diverse effects on their structure and functions, which may lead to various diseases. In this present study, we have investigated variations in human membrane proteins and found that negatively charged
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4a32308d06f79206e6f90037f02add7
https://pubmed.ncbi.nlm.nih.gov/30714211
https://pubmed.ncbi.nlm.nih.gov/30714211
Autor:
M. Michael Gromiha, Ramasamy Sakthivel, Ilya V. Bizin, A. Kulandaisamy, Dmitrij Frishman, S. Binny Priya, S. I. Tarnovskaya, Peter Hönigschmid
Publikováno v:
Bioinformatics. 34:2325-2326
Motivation Existing sources of experimental mutation data do not consider the structural environment of amino acid substitutions and distinguish between soluble and membrane proteins. They also suffer from a number of further limitations, including d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0bbd886323a7ee47214513ab8fd69a11
https://doi.org/10.1093/bioinformatics/bty054
https://doi.org/10.1093/bioinformatics/bty054
A matrix based algorithm for Protein-Protein Interaction prediction using Domain-Domain Associations
Publikováno v:
Journal of theoretical biology. 326
Protein–Protein Interactions (PPI) are vital to many cellular processes. The availability of high-throughput protein interaction data has provided us with an opportunity to assess domain associations in interacting proteins using computational appr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2de0c34a4c3dbd1b10425408eae4675
https://pubmed.ncbi.nlm.nih.gov/23473859
https://pubmed.ncbi.nlm.nih.gov/23473859
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