Zobrazeno 1 - 10 of 10 pro vyhledávání: '"Abha Dangi"'
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Akademický článek
EGCG impedes human Tau aggregation and interacts with Tau
Autor: Shweta Kishor Sonawane, Hariharakrishnan Chidambaram, Debjyoti Boral, Nalini Vijay Gorantla, Abhishek Ankur Balmik, Abha Dangi, Sureshkumar Ramasamy, Udaya Kiran Marelli, Subashchandrabose Chinnathambi
Publikováno v: Scientific Reports, Vol 10, Iss 1, Pp 1-17 (2020)
Abstract Tau aggregation and accumulation is a key event in the pathogenesis of Alzheimer’s disease. Inhibition of Tau aggregation is therefore a potential therapeutic strategy to ameliorate the disease. Phytochemicals are being highlighted as pote
Externí odkaz: https://doaj.org/article/05e91abcad094074ac9bbd912436a094
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4
HDAC6 ZnF UBP as the Modifier of Tau Structure and Function
Autor: Hariharakrishnan Chidambaram, Abha Dangi, Udaya Kiran Marelli, Abhishek Ankur Balmik, Subashchandrabose Chinnathambi
Publikováno v: Biochemistry. 59:4546-4562
Histone deacetylase 6 is a class II histone deacetylase primarily present in the cytoplasm and involved in the regulation of various cellular functions. It consists of two catalytic deacetylase domains and a unique zinc finger ubiquitin binding prote
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ea0d9cbdc4ed62c8ac59a699a6f927a
https://doi.org/10.1021/acs.biochem.0c00585
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5
EGCG impedes human Tau aggregation and interacts with Tau
Autor: Hariharakrishnan Chidambaram, Nalini Vijay Gorantla, Abha Dangi, Debjyoti Boral, Subashchandrabose Chinnathambi, Abhishek Ankur Balmik, Sureshkumar Ramasamy, Udaya Kiran Marelli, Shweta Kishor Sonawane
Publikováno v: Scientific Reports, Vol 10, Iss 1, Pp 1-17 (2020)
Scientific Reports
Tau aggregation and accumulation is a key event in the pathogenesis of Alzheimer’s disease. Inhibition of Tau aggregation is therefore a potential therapeutic strategy to ameliorate the disease. Phytochemicals are being highlighted as potential agg
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9eb3297b1f7dc8917115a5f447cb46e
https://doi.org/10.1038/s41598-020-69429-6
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6
Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6* and AcPHF6
Autor: Abha Dangi, Abhishek Ankur Balmik, Nalini Vijay Gorantla, Subashchandrabose Chinnathambi, Udaya Kiran Marelli, Shweta Kishor Sonawane, Archana Kisan Ghorpade
Publikováno v: RSC advances. 10(46)
In Alzheimer's disease and related tauopathies, the aggregation of microtubule-associated protein, Tau, into fibrils occurs via the interaction of two hexapeptide motifs PHF* 275VQIINK280 and PHF 306VQIVYK311 as β-sheets. To understand the role of t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2dd498df3adad649b0de7888526bc9d3
https://pubmed.ncbi.nlm.nih.gov/35755580
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7
Correction: Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6* and AcPHF6
Autor: Abha Dangi, Abhishek Ankur Balmik, Archana Kisan Ghorpade, Nalini Vijay Gorantla, Shweta Kishor Sonawane, Subashchandrabose Chinnathambi, Udaya Kiran Marelli
Publikováno v: RSC Advances. 12:17049-17049
Correction for ‘Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6* and AcPHF6’ by Abha Dangi et al., RSC Adv., 2020, 10, 27331–27335, https://doi.org/10.1039/D0RA03809A.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e68b5d99dcfd4371bd5813ed14492496
https://doi.org/10.1039/d2ra90058k
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10
Melatonin interacts with repeat domain of Tau to mediate disaggregation of paired helical filaments
Autor: Abhishek Ankur Balmik, Abha Dangi, Nalini Vijay Gorantla, Rashmi Das, Subashchandrabose Chinnathambi, Udaya Kiran Marelli
Publikováno v: Biochimica et biophysica acta. General subjects. 1864(3)
Tau is the major neuronal protein involved in the stabilization of microtubule assembly. In Alzheimer's disease, Tau self-assembles to form intracellular protein aggregates which are toxic to cells. Various methods have been tried and tested to restr
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::861aad5e52187b276c5eed5f0d2f320f
https://pubmed.ncbi.nlm.nih.gov/31715192
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