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• W4297383237 abstract "Before the discovery of the proteasome complex, the lysosomes with acidic proteases and caspases in apoptotic pathways were thought to be the only pathways for the degradation of damaged, unfolded, and aged proteins. However, the discovery of 26S and 20S proteasome complexes in eukaryotes and microbes, respectively, established that the degradation of most proteins is a highly regulated ATP-dependent pathway that is significantly conserved across each domain of life. The proteasome is part of the ubiquitin-proteasome system (UPS), where the covalent tagging of a small molecule called ubiquitin (Ub) on the proteins marks its proteasomal degradation. The type and chain length of ubiquitination further determine whether a protein is designated for further roles in multi-cellular processes like DNA repair, trafficking, signal transduction, etc., or whether it will be degraded by the proteasome to recycle the peptides and amino acids. Deubiquitination, on the contrary, is the removal of ubiquitin from its substrate molecule or the conversion of polyubiquitin chains into monoubiquitin as a precursor to ubiquitin. Therefore, deubiquitylating enzymes (DUBs) can maintain the dynamic state of cellular ubiquitination by releasing conjugated ubiquitin from proteins and controlling many cellular pathways that are essential for their survival. Many DUBs are well characterized in the human system with potential drug targets in different cancers. Although, proteasome complex and UPS of parasites, like plasmodium and leishmania, were recently coined as multi-stage drug targets the role of DUBs is completely unexplored even though structural domains and functions of many of these parasite DUBs are conserved having high similarity even with its eukaryotic counterpart. This review summarizes the identification &amp; characterization of different parasite DUBs based on in silico and a few functional studies among different phylogenetic classes of parasites including Metazoan ( Schistosoma , Trichinella ), Apicomplexan protozoans ( Plasmodium , Toxoplasma , Eimeria , Cryptosporidium ), Kinetoplastidie ( Leishmania , Trypanosoma ) and Microsporidia ( Nosema ). The identification of different homologs of parasite DUBs with structurally similar domains with eukaryotes, and the role of these DUBs alone or in combination with the 20S proteosome complex in regulating the parasite survival/death is further elaborated. We propose that small molecules/inhibitors of human DUBs can be potential antiparasitic agents due to their significant structural conservation." @default.
• W4297383237 created "2022-09-28" @default.
• W4297383237 creator A5007807726 @default.
• W4297383237 creator A5032831718 @default.
• W4297383237 creator A5050031621 @default.
• W4297383237 creator A5060803163 @default.
• W4297383237 date "2022-09-27" @default.
• W4297383237 modified "2023-10-18" @default.
• W4297383237 title "The emerging role of Deubiquitinases (DUBs) in parasites: A foresight review" @default.
• W4297383237 cites W114138574 @default.
• W4297383237 cites W1421935743 @default.
• W4297383237 cites W1680652826 @default.
• W4297383237 cites W1689860552 @default.
• W4297383237 cites W1864563621 @default.
• W4297383237 cites W1925142678 @default.
• W4297383237 cites W1953012310 @default.
• W4297383237 cites W1954801073 @default.
• W4297383237 cites W1973665633 @default.
• W4297383237 cites W1974115460 @default.
• W4297383237 cites W1975462016 @default.
• W4297383237 cites W1981237612 @default.
• W4297383237 cites W1982791431 @default.
• W4297383237 cites W1986865371 @default.
• W4297383237 cites W1999290683 @default.
• W4297383237 cites W2003399160 @default.
• W4297383237 cites W2005415117 @default.
• W4297383237 cites W2007588515 @default.
• W4297383237 cites W2015063536 @default.
• W4297383237 cites W2018284639 @default.
• W4297383237 cites W2019223168 @default.
• W4297383237 cites W2026934409 @default.
• W4297383237 cites W2029688045 @default.
• W4297383237 cites W2031663826 @default.
• W4297383237 cites W2033205044 @default.
• W4297383237 cites W2038147049 @default.
• W4297383237 cites W2038852478 @default.
• W4297383237 cites W2040391028 @default.
• W4297383237 cites W2041618720 @default.
• W4297383237 cites W2042990622 @default.
• W4297383237 cites W2048504106 @default.
• W4297383237 cites W2054221206 @default.
• W4297383237 cites W2055722788 @default.
• W4297383237 cites W2055929418 @default.
• W4297383237 cites W2064110684 @default.
• W4297383237 cites W2065362756 @default.
• W4297383237 cites W2070008395 @default.
• W4297383237 cites W2072310367 @default.
• W4297383237 cites W2073435376 @default.
• W4297383237 cites W2074122828 @default.
• W4297383237 cites W2075939050 @default.
• W4297383237 cites W2076978342 @default.
• W4297383237 cites W2082560252 @default.
• W4297383237 cites W2088504425 @default.
• W4297383237 cites W2094362595 @default.
• W4297383237 cites W2094941696 @default.
• W4297383237 cites W2096080350 @default.
• W4297383237 cites W2101090646 @default.
• W4297383237 cites W2101594125 @default.
• W4297383237 cites W2107915297 @default.
• W4297383237 cites W2109609912 @default.
• W4297383237 cites W2113019206 @default.
• W4297383237 cites W2117641259 @default.
• W4297383237 cites W2118225942 @default.
• W4297383237 cites W2119803499 @default.
• W4297383237 cites W2123281631 @default.
• W4297383237 cites W2132485651 @default.
• W4297383237 cites W2134350784 @default.
• W4297383237 cites W2135072453 @default.
• W4297383237 cites W2135743054 @default.
• W4297383237 cites W2136903689 @default.
• W4297383237 cites W2139364069 @default.
• W4297383237 cites W2139592339 @default.
• W4297383237 cites W2140151996 @default.
• W4297383237 cites W2147917253 @default.
• W4297383237 cites W2150925238 @default.
• W4297383237 cites W2160260545 @default.
• W4297383237 cites W2161549147 @default.
• W4297383237 cites W2165688553 @default.
• W4297383237 cites W2178354439 @default.
• W4297383237 cites W2205130032 @default.
• W4297383237 cites W2256548132 @default.
• W4297383237 cites W2310322011 @default.
• W4297383237 cites W2316880913 @default.
• W4297383237 cites W2318390251 @default.
• W4297383237 cites W2322132111 @default.
• W4297383237 cites W2379073606 @default.
• W4297383237 cites W2409179396 @default.
• W4297383237 cites W2467062547 @default.
• W4297383237 cites W2515462226 @default.
• W4297383237 cites W2560317077 @default.
• W4297383237 cites W2577226088 @default.
• W4297383237 cites W2597145668 @default.
• W4297383237 cites W2602929512 @default.
• W4297383237 cites W2616310256 @default.
• W4297383237 cites W2741889880 @default.
• W4297383237 cites W2769534618 @default.
• W4297383237 cites W2772653075 @default.
• W4297383237 cites W2783469772 @default.
• W4297383237 cites W2789304108 @default.
• W4297383237 cites W2790295680 @default.

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