Computational analysis of protein–protein interactions in motile T-cells

Analysis of protein–protein interactions is important for better understanding of molecular mechanisms involved in immune regulation and has potential for elaborating avenues for drug discovery targeting T-cell motility. Currently, only a small fraction of protein–protein interactions have been char...

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Published in:Methods in Molecular Biology
Main Author: Kumar S.; Fazil M.H.U.T.; Ahmad K.; Tripathy M.; Rajapakse J.C.; Verma N.K.
Format: Book chapter
Language:English
Published: Humana Press Inc. 2019
Online Access:https://www.scopus.com/inward/record.uri?eid=2-s2.0-85059493704&doi=10.1007%2f978-1-4939-9036-8_18&partnerID=40&md5=f520a32217aca7835fc5a346cc1a8486
id 2-s2.0-85059493704
spelling 2-s2.0-85059493704
Kumar S.; Fazil M.H.U.T.; Ahmad K.; Tripathy M.; Rajapakse J.C.; Verma N.K.
Computational analysis of protein–protein interactions in motile T-cells
2019
Methods in Molecular Biology
1930

10.1007/978-1-4939-9036-8_18
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85059493704&doi=10.1007%2f978-1-4939-9036-8_18&partnerID=40&md5=f520a32217aca7835fc5a346cc1a8486
Analysis of protein–protein interactions is important for better understanding of molecular mechanisms involved in immune regulation and has potential for elaborating avenues for drug discovery targeting T-cell motility. Currently, only a small fraction of protein–protein interactions have been characterized in T-lymphocytes although there are several detection methods available. In this regard, computational approaches garner importance, with the continued explosion of genomic and proteomic data, for handling protein modeling and protein–protein interactions in large scale. Here, we describe a computational method to identify protein–protein interactions based on in silico protein design. © 2019, Springer Science+Business Media, LLC, part of Springer Nature.
Humana Press Inc.
10643745
English
Book chapter

author Kumar S.; Fazil M.H.U.T.; Ahmad K.; Tripathy M.; Rajapakse J.C.; Verma N.K.
spellingShingle Kumar S.; Fazil M.H.U.T.; Ahmad K.; Tripathy M.; Rajapakse J.C.; Verma N.K.
Computational analysis of protein–protein interactions in motile T-cells
author_facet Kumar S.; Fazil M.H.U.T.; Ahmad K.; Tripathy M.; Rajapakse J.C.; Verma N.K.
author_sort Kumar S.; Fazil M.H.U.T.; Ahmad K.; Tripathy M.; Rajapakse J.C.; Verma N.K.
title Computational analysis of protein–protein interactions in motile T-cells
title_short Computational analysis of protein–protein interactions in motile T-cells
title_full Computational analysis of protein–protein interactions in motile T-cells
title_fullStr Computational analysis of protein–protein interactions in motile T-cells
title_full_unstemmed Computational analysis of protein–protein interactions in motile T-cells
title_sort Computational analysis of protein–protein interactions in motile T-cells
publishDate 2019
container_title Methods in Molecular Biology
container_volume 1930
container_issue
doi_str_mv 10.1007/978-1-4939-9036-8_18
url https://www.scopus.com/inward/record.uri?eid=2-s2.0-85059493704&doi=10.1007%2f978-1-4939-9036-8_18&partnerID=40&md5=f520a32217aca7835fc5a346cc1a8486
description Analysis of protein–protein interactions is important for better understanding of molecular mechanisms involved in immune regulation and has potential for elaborating avenues for drug discovery targeting T-cell motility. Currently, only a small fraction of protein–protein interactions have been characterized in T-lymphocytes although there are several detection methods available. In this regard, computational approaches garner importance, with the continued explosion of genomic and proteomic data, for handling protein modeling and protein–protein interactions in large scale. Here, we describe a computational method to identify protein–protein interactions based on in silico protein design. © 2019, Springer Science+Business Media, LLC, part of Springer Nature.
publisher Humana Press Inc.
issn 10643745
language English
format Book chapter
accesstype
record_format scopus
collection Scopus
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