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Article title matches
- Category:Ring1b (37 bytes)
1: List of pages with the keyword Ring1b - Image:Interaction 1 between Bmi1.Ring1b and UbcH5c.png (0 bytes)
- Image:Interaction 2 between Bmi1.Ring1b and UbcH5c.png (0 bytes)
- Image:Alignment of RING1a sequences and RING1b.png (0 bytes)
- Image:Interactions 2 between Ring1b (gray) and UbcH5c (green) along the N-terminal a-helix from UbcH5c.png (207 bytes)
1: Interactions between Ring1b, in gray, and UbcH5c, in green, along the N-termi... - Category:E3 ubiquitin ligase ring1b (57 bytes)
1: ...ist of pages with the keyword E3 ubiquitin ligase ring1b
Page text matches
- 2ckl (4,977 bytes)
2: ==Ring1b-Bmi1 E3 catalytic domain structure==
24: ...nterface shows that catalytic activity resides in Ring1b and not in Bmi1. These data provide a foundation ...
26: ...e Ring-Ring complex of polycomb proteins Bmi1 and Ring1b.,Buchwald G, van der Stoop P, Weichenrieder O, Pe... - 2h0d (3,082 bytes)
2: ==Structure of a Bmi-1-Ring1B Polycomb group ubiquitin ligase complex== - Category:Ring1b (37 bytes)
1: List of pages with the keyword Ring1b - 3gs2 (3,600 bytes)
2: ==Ring1B C-terminal domain/Cbx7 Cbox Complex== - 3h8h (3,907 bytes)
2: ...=Structure of the C-terminal domain of human RNF2/RING1B;== - 3ixs (3,650 bytes)
2: ==Ring1B C-terminal domain/RYBP C-terminal domain Complex=... - 3rpg (3,934 bytes)
2: ==Bmi1/Ring1b-UbcH5c complex structure== - 4af3 (5,650 bytes)
13: ...ive promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhanc... - Polycomb complex proteins 3D structures (3,593 bytes)
15: **[[6wi7]], [[8wi8]] – hBMI1 ring domain 1-108/Ring1B <br />
16: **[[7nd1]] – hBMI1 ring domain + Ring1B - NMR<br />
17: **[[3rpg]] – hBMI1 ring domain + Ring1B + Ubch5C<br />
18: **[[2ckl]] – mBMI1 ring domain + Ring1B - mouse<br />
19: **[[4r8p]] – BMI1 ring domain + Ring1B + Ubch5C + DNA - frog<br /> - 4r8p (4,088 bytes)
2: ==Crystal structure of the Ring1B/Bmi1/UbcH5c PRC1 ubiquitylation module bound to t...
14: ...ere we present the crystal structure of the human Ring1B-Bmi1-UbcH5c E3-E2 complex (the PRC1 ubiquitylatio... - 4s3o (5,395 bytes)
2: ==PCGF5-RING1B-UbcH5c complex==
14: ...sfer. The intrinsically low activity of the PCGF4-RING1B heterodimer is offset by a relatively favourable ...
16: BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase.,Tah... - Sandbox label (747 bytes)
1: ==RING1B-BMI1 fusion in closed conformation== - User:Ricardo Alberto Chiong Zevallos/Sandbox 1 (16,579 bytes)
12: ...lates the E3 ubiquitin-protein ligase activity of RING1b, which is also a protein component of the PcG PRC...
17: ...onical PRC1 complexes when in pair with RING1a or RING1b.
19: ...h0d/2'>RING1b</scene> form a heterodimer and only RING1b interacts with <scene name='78/787701/Ubiquitin-c...
23: ...scene name='78/787701/4r8p_ring_e2_highlighted/1'>RING1b attached to E2 in light-salmon</scene> and <scene...
25: ...talytically inactive RING1B mutant into Ring1A-/- Ring1B conditional knockout embryonic stem (ES) cells <r... - Polycomb complex protein (17,307 bytes)
16: ...lates the E3 ubiquitin-protein ligase activity of RING1b, which is also a protein component of the PcG PRC...
20: ...onical PRC1 complexes when in pair with RING1a or RING1b.
22: ...h0d/2'>RING1b</scene> form a heterodimer and only RING1b interacts with <scene name='78/787701/Ubiquitin-c...
26: ...scene name='78/787701/4r8p_ring_e2_highlighted/1'>RING1b attached to E2 in light-salmon</scene> and <scene...
28: ...talytically inactive RING1B mutant into Ring1A-/- Ring1B conditional knockout embryonic stem (ES) cells <r... - Image:Interactions 2 between Ring1b (gray) and UbcH5c (green) along the N-terminal a-helix from UbcH5c.png (207 bytes)
1: Interactions between Ring1b, in gray, and UbcH5c, in green, along the N-termi... - Histone 3D structures (31,408 bytes)
120: ...grm]] - hH3.1 + H4 + H2B in nucleosome + Commd3 + Ring1B + UbCH5B – Cryo EM<br /> - 6wi7 (5,324 bytes)
2: ==RING1B-BMI1 fusion in closed conformation==
14: ...studies demonstrate that these inhibitors bind to RING1B by inducing the formation of a hydrophobic pocket... - 6wi8 (5,219 bytes)
2: ...ibitor compound-induced confrontational change in Ring1b-Bmi1 domain structure==
14: ...studies demonstrate that these inhibitors bind to RING1B by inducing the formation of a hydrophobic pocket... - 8pp6 (2,818 bytes)
14: ...ding to H2Aub1-modified nucleosomes; this enables RING1B to monoubiquitinate H2A in neighboring unmodified... - 8pp7 (3,393 bytes)
14: ...ding to H2Aub1-modified nucleosomes; this enables RING1B to monoubiquitinate H2A in neighboring unmodified...
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