Zobrazeno 1 - 10 of 33 pro vyhledávání: '"Dibyendu Samanta"'
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Akademický článek
A Possible Role of the Full-Length Nascent Protein in Post-Translational Ribosome Recycling.
Autor: Debasis Das, Dibyendu Samanta, Arpita Bhattacharya, Arunima Basu, Anindita Das, Jaydip Ghosh, Abhijit Chakrabarti, Chanchal Das Gupta
Publikováno v: PLoS ONE, Vol 12, Iss 1, p e0170333 (2017)
Each cycle of translation initiation in bacterial cell requires free 50S and 30S ribosomal subunits originating from the post-translational dissociation of 70S ribosome from the previous cycle. Literature shows stable dissociation of 70S from model p
Externí odkaz: https://doaj.org/article/eec0cddde76d4b8fbf924f83e11082cb
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5
Structural Insights into N-terminal IgV Domain of BTNL2, a T Cell Inhibitory Molecule, Suggests a Non-canonical Binding Interface for Its Putative Receptors
Autor: Kheerthana Duraivelan, Dhrubajyoti Mahata, Soumya De, Snigdha Maiti, Gayatri Mukherjee, Woonghee Lee, Shankar V. Kundapura, Dibyendu Samanta, Anita Hansda, Aditya J. Basak
Publikováno v: J Mol Biol
T cell costimulation is mediated by the interaction of a number of receptors and ligands present on the surface of the T cell and antigen-presenting cell, respectively. Stimulatory or inhibitory signals from these receptor-ligand interactions work in
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::158cc237dc751a1298b0ad84ab58a8db
https://doi.org/10.1016/j.jmb.2020.09.013
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7
High-resolution crystal structure of LpqH, an immunomodulatory surface lipoprotein of Mycobacterium tuberculosis reveals a distinct fold and a conserved cleft on its surface
Autor: Shruti Chatterjee, Shankar V. Kundapura, Aditya J. Basak, Debangshu Mukherjee, Sagarika Dash, Namrata Ganguli, Amit K. Das, Gayatri Mukherjee, Dibyendu Samanta, Udupi A. Ramagopal
Publikováno v: International journal of biological macromolecules. 210
Tuberculosis, caused by Mycobacterium tuberculosis, is predominantly a disease of the lungs acquired by inhaling mycobacteria from infected individuals via airborne droplets. In order to facilitate their entry into the alveolar macrophages, mycobacte
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::743beea303e608ffff96f6727cdf079e
https://pubmed.ncbi.nlm.nih.gov/35504420
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8
Cryptic association of B7‐2 molecules and its implication for clustering
Autor: Deepak T. Nair, Swetha Lankipalli, Mahadeva Swamy H.S., Dibyendu Samanta, Deepak Selvam, Udupi A. Ramagopal
Publikováno v: Protein Sci
T-cell co-stimulation through CD28/CTLA4:B7-1/B7-2 axis is one of the extensively studied pathways that resulted in the discovery of several FDA-approved drugs for autoimmunity and cancer. However, many aspects of the signaling mechanism remain elusi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84934763963e3938f4c68b8bd10c07f4
https://europepmc.org/articles/PMC8376414/
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9
Cadherin-mediated host-pathogen interactions
Autor: Sagarika Dash, Kheerthana Duraivelan, Dibyendu Samanta
Publikováno v: Cellular microbiologyREFERENCES. 23(5)
Cell adhesion molecules mediate cell-to-cell and cell-to-matrix adhesions and play an immense role in a myriad of physiological processes during the growth and development of a multicellular organism. Cadherins belong to a major group of membrane-bou
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e51a52c2394c113f603f6afa2e7c4aac
https://pubmed.ncbi.nlm.nih.gov/33543826
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10
An evolutionarily conserved charged residue dictates the specificity of heterophilic interactions among nectins
Autor: Kheerthana Duraivelan, Sagarika Dash, Dibyendu Samanta
Publikováno v: Biochemical and biophysical research communications. 534
Nectins are a family of four cell surface glycoproteins belonging to the immunoglobulin superfamily that mediate cell-cell adhesion and associated signalling pathways, thereby regulating several physiological processes including morphogenesis, growth
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5113a4bbcde055d314df624c888b545c
https://pubmed.ncbi.nlm.nih.gov/33220924
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