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Article title matches
- Category:Tut4 (35 bytes)
1: List of pages with the keyword Tut4
Page text matches
- 2cqf (3,811 bytes)
11: ... Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal urid... - Sandbox Reserved 718 (9,261 bytes)
20: ...Cho, J., Yeom, K.H., Han, J., and Kim, V.N. In: ''TUT4 in concert with Lin28 suppresses microRNA biogene... - 3hiy (5,710 bytes)
24: ...acent to the UTP-binding site. Unlike the minimal TUT4 TUTase, MEAT1 shows no appreciable conformational... - 3hj4 (4,829 bytes)
22: ...acent to the UTP-binding site. Unlike the minimal TUT4 TUTase, MEAT1 shows no appreciable conformational... - Sandbox Reserved 329 (5,750 bytes)
6: ...t=2.0|Figure 1. Secondary structure succession of TUT4 with bound ATP. Secondary structure residues are ...
10: ... reference">PMID:11893335</ref> More specifically TUT4 catalyzes a reaction that adds a nucleotide, from...
16: ... β nucleotidyltransferase superfamily, including TUT4 is hG [G/S]X(9-13)Dh[D/E]h (where X is any a...
19: ...tidyltransferase superfamily, as shown (green) in TUT4 with bound ATP.]]
40: [[2q0d]] is TUT4 with bound ATP - 2li8 (2,930 bytes)
11: ... Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal urid... - 3trz (3,064 bytes)
11: ... Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal urid... - 3ts0 (3,067 bytes)
11: ... Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal urid... - 3ts2 (3,064 bytes)
11: ... Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal urid... - 4a4i (4,282 bytes)
13: ... Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal urid... - Terminal Uridylyl Transferase (5,882 bytes)
9: ...t=2.0|Figure 1. Secondary structure succession of TUT4 with bound ATP. Secondary structure residues are ...
13: ... reference">PMID:11893335</ref> More specifically TUT4 catalyzes a reaction that adds a nucleotide, from...
19: ... β nucleotidyltransferase superfamily, including TUT4 is hG [G/S]X(9-13)Dh[D/E]h (where X designat...
22: ...tidyltransferase superfamily, as shown (green) in TUT4 with bound ATP.]]
49: [[2q0d]] is TUT4 with bound ATP - 4pmw (4,340 bytes)
11: ...y a terminal uridylyltransferase, such as ZCCHC11/TUT4. Mediates degradation of cytoplasmic mRNAs that h...
14: ... molecular basis of Lin28-mediated recruitment of TUT4 and TUT7 to pre-let-7 and its subsequent degradat... - 8ost (4,176 bytes)
2: ...tructure of human terminal uridylyltransferase 4 (TUT4, ZCCHC11) in complex with pre-let7g miRNA and Lin...
11: ...ption once in the nucleus, whereas uridylation by TUT4 destabilizes mRNAs in cytoplasmic ribonucleoprote... - 5udz (4,516 bytes)
11: ... Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal urid...
14: ...mplex is crucial for the acquired processivity of TUT4. - 5w0o (4,169 bytes)
14: ...n pre-let-7 and the inactive LIM. Finally, ZK2 of TUT4(7) aids oligoU addition by engaging the growing o...
16: Multi-domain utilization by TUT4 and TUT7 in control of let-7 biogenesis.,Faehnle ... - 5w0m (4,259 bytes)
14: ...n pre-let-7 and the inactive LIM. Finally, ZK2 of TUT4(7) aids oligoU addition by engaging the growing o...
16: Multi-domain utilization by TUT4 and TUT7 in control of let-7 biogenesis.,Faehnle ... - 5w0n (4,603 bytes)
14: ...n pre-let-7 and the inactive LIM. Finally, ZK2 of TUT4(7) aids oligoU addition by engaging the growing o...
16: Multi-domain utilization by TUT4 and TUT7 in control of let-7 biogenesis.,Faehnle ... - 6i0s (3,931 bytes)
14: ...hat other eukaryotic TUTases, including mammalian TUT4 and TUT7, might exhibit similar, hitherto unknown... - 6i0t (3,705 bytes)
13: ...hat other eukaryotic TUTases, including mammalian TUT4 and TUT7, might exhibit similar, hitherto unknown... - 6i0u (3,880 bytes)
14: ...hat other eukaryotic TUTases, including mammalian TUT4 and TUT7, might exhibit similar, hitherto unknown...
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