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Basant K. Patel
Researcher at Indian Institute of Technology, Hyderabad
Publications - 26
Citations - 1125
Basant K. Patel is an academic researcher from Indian Institute of Technology, Hyderabad. The author has contributed to research in topics: Amyloid & Amyloidosis. The author has an hindex of 12, co-authored 24 publications receiving 827 citations. Previous affiliations of Basant K. Patel include University of Illinois at Chicago & University of Nevada, Reno.
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Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis.
TL;DR: The roles of TDP-43's mutations, its cytoplasmic mis-localization and aberrant post-translational modifications in ALS, its amyloid-like in vitro aggregation, its physiological vs. pathological oligomerization in vivo, liquid-liquid phase separation (LLPS), and potential prion-like propagation propensity of the TDP -43 inclusions are discussed.
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The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion
TL;DR: The finding that Cyc8 can propagate as a prions, together with a recent report that Swi1 of the Swi–Snf global transcriptional regulatory complex also has a prion form, shows that prionization can lead to mass activation or repression of yeast genes and is suggestive of a link between the epigenetic phenomena of chromatin remodelling and prion formation.
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"Prion-proof" for [PIN+]: infection with in vitro-made amyloid aggregates of Rnq1p-(132-405) induces [PIN+].
Basant K. Patel,Susan W. Liebman +1 more
TL;DR: This work proves that [PIN(+)] is a prion mediated by amyloid-like aggregates of Rnq1p, and supports the hypothesis that heterologous prions affect each other's appearance and propagation through interaction of their amyloids-like regions.
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Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis.
Sei Kyoung Park,Joo Y. Hong,Fatih Arslan,Fatih Arslan,Vydehi Kanneganti,Basant K. Patel,Alex Tietsort,Elizabeth M. H. Tank,Xingli Li,Sami J. Barmada,Susan W. Liebman +10 more
TL;DR: It is shown that TDP-43 overexpression dramatically alters cell shape and reduces ubiquitin dependent proteolysis of a reporter construct, and overexposure of the mammalian Sis1 homologue, DNAJB1, relieves T DP-43 mediated toxicity in primary rodent cortical neurons, suggesting that Sis 1 and its homologues may have neuroprotective effects in ALS.
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An acridine derivative, [4,5-bis{(N-carboxy methyl imidazolium)methyl}acridine] dibromide, shows anti-TDP-43 aggregation effect in ALS disease models
Archana Prasad,Gembali Raju,Vishwanath Sivalingam,Amandeep Girdhar,Meenakshi Verma,Abhishek Vats,Vibha Taneja,Ganesan Prabusankar,Basant K. Patel +8 more
TL;DR: Among several acridine derivatives examined, AIM4, which contains polar carboxyl groups in the side arms, significantly reduces TDP-43-YFP aggregation in the powerful yeast model cell and also abolishes in vitro amyloid-like aggregation of car boxyl terminal domain of TDP -43, as observed by AFM imaging.