The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested identity is verified. In Schizosaccharomyces pombe, Apc11 is the product of ORF SPAC343.03, an approximately 11-kDa component of the 13-subunit anaphase-promoting complex/cyclosome (APC/C). This matches UniProt Q9UT86 and is not the similarly named budding-yeast gene. Its RING-H2/RING-box annotations are consistent with the conserved APC11 family. Direct S. pombe proteomics and structural studies establish complex membership, one-copy stoichiometry, and placement in the APC/C catalytic region; purified-protein studies in budding yeast and humans establish the detailed RING-E3 mechanism. (yoon2002proteomicsanalysisidentifies pages 1-2, yoon2002proteomicsanalysisidentifies pages 2-4, ohi2007structuralorganizationof pages 9-10, ohi2007structuralorganizationof pages 4-6)
The best-supported primary function is therefore:
Apc11 is the zinc-binding RING subunit of the APC/C E3 ubiquitin ligase. Together with the cullin-like Apc2 subunit, it recruits/activates ubiquitin-charged E2 enzymes and promotes transfer of ubiquitin to APC/C-bound cell-cycle substrates. It does not itself provide most physiological substrate specificity.
Its principal pathway consequences are polyubiquitylation and proteasomal destruction of Cut2/securin, permitting separase-dependent sister-chromatid separation, and Cdc13/B-type cyclin, lowering Cdk1 activity and enabling mitotic exit. (tang2001apc2cullinprotein pages 1-2, leverson2000theapc11ringh2 pages 1-2, ohi2007structuralorganizationof pages 1-2, yoon2002proteomicsanalysisidentifies pages 1-2)
| Topic | Conclusion | Evidence type/species | Confidence or limitation |
|---|---|---|---|
| Exact identity | Apc11 is the product of S. pombe ORF SPAC343.03, corresponding to UniProt Q9UT86, with a predicted mass of approximately 11 kDa. (yoon2002proteomicsanalysisidentifies pages 1-2, yoon2002proteomicsanalysisidentifies pages 2-4) | Comparative-genomics assignment and S. pombe proteomics | High. The sequence-based assignment is supported by recovery from APC/C preparations. |
| Domain architecture | Apc11 is the small zinc-binding RING-H2/RING-box subunit of APC/C. Conserved metal-chelating cysteine and histidine residues form its E2-binding RING fold. (leverson2000theapc11ringh2 pages 1-2, leverson2000theapc11ringh2 pages 2-3, leverson2000theapc11ringh2 pages 3-5) | Sequence comparison and mutagenesis, principally in S. cerevisiae, with the S. pombe sequence included in alignments | High conserved inference. Direct zinc stoichiometry and RING mutagenesis have not been reported for Q9UT86 itself. |
| APC/C membership | S. pombe APC/C contains 13 core subunits. Apc11/SPAC343.03 was recovered with 3 unique tryptic peptides in Lid1-TAP and 5 peptides in Apc13-TAP purifications. (yoon2002proteomicsanalysisidentifies pages 1-2, yoon2002proteomicsanalysisidentifies pages 2-4) | TAP purification and DALPC tandem mass spectrometry in S. pombe | High. This is direct, exact-organism evidence of complex membership, although not an isolated Apc11 activity assay. |
| Stoichiometry | Apc11 occurs at one copy per APC/C particle. Unlike Cut9, Cut23, and Nuc2, two differently tagged Apc11 variants did not co-immunoprecipitate. (ohi2007structuralorganizationof pages 4-6) | Double-tag co-immunoprecipitation and quantitative stoichiometry in S. pombe | High for the analyzed mitotic complex. Tagged strains grew normally, reducing concern that tagging disrupted assembly. |
| Structural role | Apc11 clusters with Apc2 and Apc10 along the right side of APC/C, forming its catalytic region and remaining spatially distinct from much of the TPR scaffold. (ohi2007structuralorganizationof pages 9-10) | Antibody labeling, mutant analysis, and cryo-EM of S. pombe APC/C–Slp1 | Moderate to high. Placement is direct, but the 27 Å map cannot resolve atomic contacts. |
| Complex dimensions and mass | Mitotic S. pombe APC/C–Slp1 is an asymmetric tricorn-shaped particle measuring approximately 19 × 17 × 15 nm, with an 11.5 × 9.5 × 6.5 nm cavity. STEM measured 890 ± 133 kDa; stoichiometry predicted 986 kDa with Slp1 and 933 kDa without it. Cryo-EM resolution was 27 Å. (ohi2007structuralorganizationof pages 9-10, ohi2007structuralorganizationof pages 4-6, ohi2007structuralorganizationof pages 1-2) | STEM, quantitative immunochemistry, and single-particle cryo-EM in S. pombe | High for overall architecture and mass range. Measurements describe the complete APC/C rather than free Apc11. |
| Catalyzed reaction | Apc11 promotes transfer of ubiquitin from an E2–ubiquitin thioester to substrate lysines, forming isopeptide-linked ubiquitin conjugates. Apc2–Apc11 constitutes the conserved minimal ubiquitin-ligase module. (tang2001apc2cullinprotein pages 1-2, tang2001apc2cullinprotein pages 4-6, leverson2000theapc11ringh2 pages 1-2, gmachl2000theringh2finger pages 1-2) | Purified recombinant human and S. cerevisiae proteins; conserved inference for S. pombe | High mechanistic conservation. No purified-Q9UT86 kinetic assay was found; APC11 does not independently provide physiological substrate specificity. |
| E2 partners | S. pombe APC/C uses Ubc4 and Ubc11 in complementary ubiquitination functions. Depletion of either causes mitotic arrest and cyclin accumulation; Ubc11 can make short chains without Ubc4, whereas Ubc4 cannot modify APC/C substrates without Ubc11. (mclean2011stateofthe pages 12-14, ohi2007structuralorganizationof pages 1-2) | Genetic depletion and APC/C-pathway assays in S. pombe | Moderate to high at pathway level. Direct physical binding of Q9UT86 to each fission-yeast E2 remains unshown. |
| Substrates and specificity | Physiological APC/C targets include Cut2/securin and Cdc13/cyclin B. Slp1/Cdc20, Ste9/Cdh1, and coreceptor Apc10 recognize substrate degrons; Apc11 performs E2-dependent ubiquitin transfer rather than selecting substrates. (alfieri2017visualizingthecomplex pages 2-3, ohi2007structuralorganizationof pages 1-2, yoon2002proteomicsanalysisidentifies pages 1-2, yoon2002proteomicsanalysisidentifies pages 2-4) | Exact-species APC/C assays plus conserved structural and biochemical evidence | High for pathway substrates and division of labor. Direct Apc11–substrate recognition should not be inferred. |
| Cellular localization | Q9UT86 acts intracellularly as part of APC/C in the mitotic cell-cycle machinery. Its demonstrated structural position is within the catalytic side of isolated APC/C; no direct live-cell localization map for Apc11 itself was found. (ohi2007structuralorganizationof pages 9-10, ohi2007structuralorganizationof pages 1-2) | Purified S. pombe mitotic APC/C and structural localization | Moderate for cellular context. Specific enrichment at nuclei, spindle-pole bodies, kinetochores, or chromosomes should not be asserted without direct imaging. |
| 2024 structural update | Human APC/C cryo-EM structures reached 2.9 Å for APC/C–CDH1–EMI1 and 3.2 Å for apo-APC/C. A 2024 budding-yeast comparison found that apo-APC/C is already positioned for E2 binding, unlike human APC/C, revealing species-specific regulation despite conserved architecture. (vazquezfernandez2024acomparativestudy pages 1-2) | High-resolution human and S. cerevisiae cryo-EM | Authoritative but cross-species. These conformations cannot automatically be assigned to S. pombe Q9UT86. |
| 2024 S. pombe regulatory update | During spindle-checkpoint or environmental-stress responses, Pmk1 binds and phosphorylates Slp1/Cdc20, including Thr480, promoting Slp1 ubiquitylation and degradation and restraining APC/C activation. (sun2024negativeregulationof pages 8-9, sun2024negativeregulationof pages 1-2) | Binding assays, mutagenesis, phosphoproteomics, phospho-specific antibodies, and cellular experiments in S. pombe | High for upstream APC/C regulation. This does not show that Pmk1 directly modifies Apc11. |
Table: Compact evidence map for the identity, catalytic function, complex placement, localization, and regulation of S. pombe Apc11/Q9UT86. It distinguishes direct fission-yeast findings from conserved cross-species inference and highlights unresolved points.
Yoon and colleagues reported on 10 December 2002 that genome searches identified the S. pombe APC11 homolog as SPAC343.03. In two independent APC/C purifications, the predicted approximately 11-kDa protein was represented by 3 unique tryptic peptides in Lid1-TAP material and 5 in Apc13-TAP material. These data directly connect the exact fission-yeast ORF to the APC/C and support the supplied Q9UT86 annotation. [DOI/URL: https://doi.org/10.1016/S0960-9822(02)01331-3]. (yoon2002proteomicsanalysisidentifies pages 1-2, yoon2002proteomicsanalysisidentifies pages 2-4)
The supplied InterPro/Pfam assignments—RING-box E3 ubiquitin ligase, RING-H2 APC11, zinc-finger RING, and zf-ANAPC11—are mutually consistent. APC11 proteins contain a compact RING-H2 metal-binding fold with conserved cysteine and histidine ligands. In budding yeast, mutation of zinc-coordinating Apc11 residues disrupted complementation, showing that RING integrity is essential for function; the S. pombe sequence was included in the cross-species RING alignment. This is strong conserved-family evidence, although equivalent residue-by-residue mutagenesis has not been reported for Q9UT86 itself. [Published July 2000; DOI/URL: https://doi.org/10.1091/mbc.11.7.2315]. (leverson2000theapc11ringh2 pages 1-2, leverson2000theapc11ringh2 pages 2-3, leverson2000theapc11ringh2 pages 3-5)
Apc11 is a RING-type E3 ligase component, not a HECT-type ubiquitin carrier. It promotes the direct reaction:
E2–S~ubiquitin + substrate-Lys → E2-SH + substrate-Lys–NH–CO–ubiquitin, followed by additional cycles that build a proteasome-targeting ubiquitin chain.
Accordingly, no covalent Apc11–ubiquitin catalytic intermediate is expected. The RING domain binds and positions an E2~ubiquitin conjugate in a transfer-competent state, while APC/C-associated recognition machinery positions the substrate lysine.
Purified budding-yeast Apc11 bound Ubc4 directly and supported E1-, E2-, and ATP-dependent ubiquitination of Clb2 in vitro. RING integrity was required. [Published July 2000; https://doi.org/10.1091/mbc.11.7.2315]. (leverson2000theapc11ringh2 pages 1-2, leverson2000theapc11ringh2 pages 3-5)
Independent experiments with recombinant human APC11 showed formation of multiubiquitin chains with E1 and UBC4; about 60% of the chains remained in solution after APC11 removal, demonstrating that many were unanchored rather than merely APC11 autoubiquitylation products. The reaction required E1, UBC4, ATP, and ubiquitin and was not supported by every tested E2. [Published 1 August 2000; https://doi.org/10.1073/pnas.97.16.8973]. (gmachl2000theringh2finger pages 1-2, gmachl2000theringh2finger pages 3-4)
Human reconstitution demonstrated that APC2–APC11 is the minimal APC/C ubiquitin-ligase module. The heterodimer supported UbcH10- or Ubc4-dependent ubiquitylation of securin and cyclin B1. APC11 interacted strongly with APC2; Ubc4 bound APC11 directly, whereas UbcH10 primarily contacted the C-terminal cullin-homology region of APC2. [Published December 2001; https://doi.org/10.1091/mbc.12.12.3839]. (tang2001apc2cullinprotein pages 1-2, tang2001apc2cullinprotein pages 4-6)
This division of labor is the most defensible functional annotation for Q9UT86. The exact physical interface between S. pombe Apc11 and each endogenous E2 has not been purified and measured directly, but the relevant fold, catalytic-module organization, and pathway are conserved.
Apc11 should not be annotated as independently recognizing Cut2, Cdc13, or a particular degron. The APC2–APC11 minimal module also ubiquitylated destruction-box-deleted substrates in vitro, showing that isolated catalytic activity lacks normal substrate discrimination. Physiological specificity is generated principally by the coactivators Slp1/Cdc20 and Ste9/Cdh1, together with Apc10, which recognize D-box, KEN-box, and related degrons and orient substrates toward the catalytic module. (tang2001apc2cullinprotein pages 1-2, alfieri2017visualizingthecomplex pages 2-3, ohi2007structuralorganizationof pages 1-2)
In S. pombe, the major well-established APC/C outputs are:
Purified mitotic S. pombe APC/C ubiquitylated a Cdc2–Cdc13 substrate in an E1-, E2-, and ATP-dependent assay, while cellular APC/C activity generated ubiquitylated Cut2. (yoon2002proteomicsanalysisidentifies pages 1-2, yoon2002proteomicsanalysisidentifies pages 2-4)
The fission-yeast APC/C has 13 core subunits. Quantitative double-tag co-immunoprecipitation indicated that Apc11 is present at one copy per particle, whereas Cut9, Cut23, and Nuc2 occur at approximately two copies. Apc11, Apc2, and Apc10 occupy the catalytic side of the assembly, spatially separated from much of the TPR scaffold. (ohi2007structuralorganizationof pages 4-6, ohi2007structuralorganizationof pages 9-10)
The mitotic S. pombe APC/C–Slp1 complex was reconstructed at 27 Å resolution and measured approximately 19 × 17 × 15 nm. It contains a central cavity of approximately 11.5 × 9.5 × 6.5 nm. STEM yielded a mass of 890 ± 133 kDa, while subunit stoichiometry predicted approximately 986 kDa with Slp1 and 933 kDa without Slp1. These are measurements of the intact assembly, not free Apc11. [Published 14 December 2007; https://doi.org/10.1016/j.molcel.2007.10.003]. (ohi2007structuralorganizationof pages 9-10, ohi2007structuralorganizationof pages 4-6, ohi2007structuralorganizationof pages 1-2)
Functionally, Apc11 is therefore both catalytic and structural: it supplies the RING platform for E2-dependent transfer while remaining anchored to the complex through the Apc2-centered catalytic module. It is not the principal scaffold for the whole APC/C and is not the degron receptor.
The defensible localization is intracellular, within the APC/C mitotic cell-cycle machinery. Structural labeling places Apc11 on the catalytic side of purified mitotic APC/C. APC/C activity acts on soluble/nuclear mitotic regulators associated with chromosome segregation and mitotic exit. (ohi2007structuralorganizationof pages 9-10, ohi2007structuralorganizationof pages 1-2)
However, the retrieved literature did not provide an Apc11-specific live-cell localization series establishing enrichment at nuclei, spindle-pole bodies, kinetochores, spindles, or chromosomes. Therefore, such finer localization should not be assigned to Q9UT86 without additional imaging evidence. Localization reported for Slp1, checkpoint proteins, or other APC/C subunits is not automatically equivalent to Apc11 localization.
In fission yeast, APC/C activity uses Ubc4 and Ubc11 in complementary roles. Depletion of either causes mitotic arrest and cyclin accumulation. Ubc11 can generate short ubiquitin chains in the absence of Ubc4, whereas Ubc4 cannot ubiquitylate APC/C substrates without Ubc11, supporting a model in which Ubc11 participates in initial substrate modification and Ubc4 supports chain extension. (mclean2011stateofthe pages 12-14)
Chain topology should be annotated cautiously. Budding-yeast APC/C has been associated predominantly with K48-linked chains, whereas human APC/C prominently uses K11-linked chain assembly machinery. The exact linkage distribution generated by the Q9UT86-containing S. pombe complex was not established in the retrieved evidence. (mclean2011stateofthe pages 12-14)
Apc11 functions in the ubiquitin–proteasome system, specifically the APC/C arm controlling metaphase-to-anaphase transition and mitotic exit. The sequence is:
Sun and colleagues reported in the 16 October 2024 version of record that the Pmk1 MAP kinase binds the APC/C coactivator Slp1/Cdc20 and phosphorylates it, including at Thr480. This promotes Slp1 ubiquitylation and degradation, restrains APC/C activation, and helps sustain the spindle checkpoint under environmental stress. Their evidence included recombinant binding/pull-down assays, mutagenesis, phosphoproteomics, phospho-specific antibodies, and cellular checkpoint assays with at least 300 cells per time point and three experimental repeats. [https://doi.org/10.7554/eLife.97896]. (sun2024negativeregulationof pages 8-9, sun2024negativeregulationof pages 1-2)
This is important current context for Q9UT86 because it regulates activity of the Apc11-containing holoenzyme. It is not evidence that Pmk1 directly phosphorylates Apc11.
High-resolution human APC/C structures published in November 2024 resolved apo-APC/C at 3.2 Å and APC/C–CDH1–EMI1 at 2.9 Å, strengthening atomic models of APC2–APC11 organization and regulated catalytic access. [https://doi.org/10.1038/s41467-024-54398-5]. These data support the conserved catalytic interpretation but do not directly determine the conformation of fission-yeast Q9UT86. (vazquezfernandez2024acomparativestudy pages 1-2)
A comparative cryo-EM study published in October 2024 found broad architectural conservation between budding-yeast and human APC/C but significant regulatory differences: budding-yeast apo-APC/C already positioned its APC2–APC11 module for E2 binding, whereas human APC/C undergoes a coactivator-linked catalytic-module rearrangement. The study also found no budding-yeast equivalent of the human APC1 phosphoregulatory autoinhibitory segment. [https://doi.org/10.7554/eLife.100821]. (vazquezfernandez2024acomparativestudy pages 1-2)
The expert interpretation is therefore conservative: APC11’s core RING-E3 chemistry is deeply conserved, but detailed conformational regulation cannot simply be transferred from humans or budding yeast to S. pombe. Direct fission-yeast structural work remains at substantially lower resolution.
Direct loss-of-function phenotyping specifically for S. pombe apc11/SPAC343.03 was limited in the retrieved primary literature. Therefore, essentiality and exact null phenotype should not be claimed solely by transferring results from other organisms.
Nevertheless, conserved evidence strongly predicts an essential mitotic function. Budding-yeast APC11 RING mutants arrested with predominantly 2N DNA; after 3 hours at restrictive temperature, more than 70% of cells had large buds, short spindles, and DNA at the bud neck. Zinc-ligand mutations failed to complement the temperature-sensitive allele. These observations demonstrate what disruption of APC11 catalysis does in a close fungal homolog, not a directly measured Q9UT86 phenotype. (leverson2000theapc11ringh2 pages 2-3, leverson2000theapc11ringh2 pages 3-5)
At the exact-species pathway level, defective APC/C or depletion of its E2 machinery causes mitotic arrest, cyclin accumulation, failed chromosome segregation, and characteristic cut phenotypes. These support the expected consequences of disabling Apc11-containing APC/C but are not substitutes for an apc11-specific deletion experiment. (mclean2011stateofthe pages 12-14, yoon2002proteomicsanalysisidentifies pages 2-4)
Apc11/Q9UT86 currently has greatest practical value as a mechanistic research component, not as a clinical or industrial target:
No direct therapeutic, diagnostic, agricultural, or biotechnological implementation specifically using S. pombe Q9UT86 was identified. Human APC/C is relevant to proliferative disease and targeted-proteolysis research, but that does not make the fission-yeast protein itself a validated drug target.
Molecular function: RING-type E3 ubiquitin-ligase catalytic subunit of APC/C; binds/activates ubiquitin-conjugating E2 machinery as part of the Apc2–Apc11 catalytic module and promotes ubiquitin transfer to APC/C-recruited substrates.
Biological process: APC/C-dependent proteasomal turnover during the metaphase–anaphase transition and mitotic exit; regulation of sister-chromatid separation, cyclin-dependent kinase inactivation, and chromosome segregation.
Complex: One-copy core component of the 13-subunit S. pombe APC/C/20S cyclosome; catalytic region associated with Apc2 and Apc10.
Principal substrates of the holoenzyme: Cut2/securin and Cdc13/B-type cyclin. Substrate specificity is conferred mainly by Slp1/Cdc20 or Ste9/Cdh1 with Apc10, not by Apc11 alone.
Localization: Intracellular APC/C-associated protein acting in mitotic cell-cycle control; finer Apc11-specific live-cell localization remains insufficiently resolved.
Confidence: High for identity, APC/C membership, RING-family assignment, complex stoichiometry, and conserved catalytic role; moderate for exact endogenous E2 contacts and subcellular distribution; presently insufficient for Q9UT86-specific catalytic kinetics, ubiquitin-chain linkage preference, detailed mutant phenotype, or direct post-translational regulation.
References
(yoon2002proteomicsanalysisidentifies pages 1-2): Hyun-Joo Yoon, Anna Feoktistova, Benjamin A. Wolfe, Jennifer L. Jennings, Andrew J. Link, and Kathleen L. Gould. Proteomics analysis identifies new components of the fission and budding yeast anaphase-promoting complexes. Current Biology, 12:2048-2054, Dec 2002. URL: https://doi.org/10.1016/s0960-9822(02)01331-3, doi:10.1016/s0960-9822(02)01331-3. This article has 137 citations and is from a highest quality peer-reviewed journal.
(yoon2002proteomicsanalysisidentifies pages 2-4): Hyun-Joo Yoon, Anna Feoktistova, Benjamin A. Wolfe, Jennifer L. Jennings, Andrew J. Link, and Kathleen L. Gould. Proteomics analysis identifies new components of the fission and budding yeast anaphase-promoting complexes. Current Biology, 12:2048-2054, Dec 2002. URL: https://doi.org/10.1016/s0960-9822(02)01331-3, doi:10.1016/s0960-9822(02)01331-3. This article has 137 citations and is from a highest quality peer-reviewed journal.
(ohi2007structuralorganizationof pages 9-10): Melanie D. Ohi, Anna Feoktistova, Liping Ren, Calvin Yip, Yifan Cheng, Jun-Song Chen, Hyun-Joo Yoon, Joseph S. Wall, Zhong Huang, Pawel A. Penczek, Kathleen L. Gould, and Thomas Walz. Structural organization of the anaphase-promoting complex bound to the mitotic activator slp1. Molecular cell, 28 5:871-85, Dec 2007. URL: https://doi.org/10.1016/j.molcel.2007.10.003, doi:10.1016/j.molcel.2007.10.003. This article has 64 citations and is from a highest quality peer-reviewed journal.
(ohi2007structuralorganizationof pages 4-6): Melanie D. Ohi, Anna Feoktistova, Liping Ren, Calvin Yip, Yifan Cheng, Jun-Song Chen, Hyun-Joo Yoon, Joseph S. Wall, Zhong Huang, Pawel A. Penczek, Kathleen L. Gould, and Thomas Walz. Structural organization of the anaphase-promoting complex bound to the mitotic activator slp1. Molecular cell, 28 5:871-85, Dec 2007. URL: https://doi.org/10.1016/j.molcel.2007.10.003, doi:10.1016/j.molcel.2007.10.003. This article has 64 citations and is from a highest quality peer-reviewed journal.
(tang2001apc2cullinprotein pages 1-2): Zhanyun Tang, Bing Li, Rajnish Bharadwaj, Haizhen Zhu, Engin Özkan, Kevin Hakala, Johann Deisenhofer, and Hongtao Yu. Apc2 cullin protein and apc11 ring protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex. Molecular biology of the cell, 12 12:3839-51, Dec 2001. URL: https://doi.org/10.1091/mbc.12.12.3839, doi:10.1091/mbc.12.12.3839. This article has 253 citations and is from a domain leading peer-reviewed journal.
(leverson2000theapc11ringh2 pages 1-2): Joel D. Leverson, Claudio A.P. Joazeiro, Andrew M. Page, Han-kuei Huang, Philip Hieter, and Tony Hunter. The apc11 ring-h2 finger mediates e2-dependent ubiquitination. Molecular biology of the cell, 11 7:2315-25, Jul 2000. URL: https://doi.org/10.1091/mbc.11.7.2315, doi:10.1091/mbc.11.7.2315. This article has 231 citations and is from a domain leading peer-reviewed journal.
(ohi2007structuralorganizationof pages 1-2): Melanie D. Ohi, Anna Feoktistova, Liping Ren, Calvin Yip, Yifan Cheng, Jun-Song Chen, Hyun-Joo Yoon, Joseph S. Wall, Zhong Huang, Pawel A. Penczek, Kathleen L. Gould, and Thomas Walz. Structural organization of the anaphase-promoting complex bound to the mitotic activator slp1. Molecular cell, 28 5:871-85, Dec 2007. URL: https://doi.org/10.1016/j.molcel.2007.10.003, doi:10.1016/j.molcel.2007.10.003. This article has 64 citations and is from a highest quality peer-reviewed journal.
(leverson2000theapc11ringh2 pages 2-3): Joel D. Leverson, Claudio A.P. Joazeiro, Andrew M. Page, Han-kuei Huang, Philip Hieter, and Tony Hunter. The apc11 ring-h2 finger mediates e2-dependent ubiquitination. Molecular biology of the cell, 11 7:2315-25, Jul 2000. URL: https://doi.org/10.1091/mbc.11.7.2315, doi:10.1091/mbc.11.7.2315. This article has 231 citations and is from a domain leading peer-reviewed journal.
(leverson2000theapc11ringh2 pages 3-5): Joel D. Leverson, Claudio A.P. Joazeiro, Andrew M. Page, Han-kuei Huang, Philip Hieter, and Tony Hunter. The apc11 ring-h2 finger mediates e2-dependent ubiquitination. Molecular biology of the cell, 11 7:2315-25, Jul 2000. URL: https://doi.org/10.1091/mbc.11.7.2315, doi:10.1091/mbc.11.7.2315. This article has 231 citations and is from a domain leading peer-reviewed journal.
(tang2001apc2cullinprotein pages 4-6): Zhanyun Tang, Bing Li, Rajnish Bharadwaj, Haizhen Zhu, Engin Özkan, Kevin Hakala, Johann Deisenhofer, and Hongtao Yu. Apc2 cullin protein and apc11 ring protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex. Molecular biology of the cell, 12 12:3839-51, Dec 2001. URL: https://doi.org/10.1091/mbc.12.12.3839, doi:10.1091/mbc.12.12.3839. This article has 253 citations and is from a domain leading peer-reviewed journal.
(gmachl2000theringh2finger pages 1-2): Michael Gmachl, Christian Gieffers, Alexandre V. Podtelejnikov, Matthias Mann, and Jan-Michael Peters. The ring-h2 finger protein apc11 and the e2 enzyme ubc4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex. Proceedings of the National Academy of Sciences of the United States of America, 97 16:8973-8, Aug 2000. URL: https://doi.org/10.1073/pnas.97.16.8973, doi:10.1073/pnas.97.16.8973. This article has 242 citations and is from a highest quality peer-reviewed journal.
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(vazquezfernandez2024acomparativestudy pages 1-2): Ester Vazquez-Fernandez, Jing Yang, Ziguo Zhang, Antonina E Andreeva, Paul Emsley, and David Barford. A comparative study of the cryo-em structures of saccharomyces cerevisiae and human anaphase-promoting complex/cyclosome (apc/c). eLife, Oct 2024. URL: https://doi.org/10.7554/elife.100821, doi:10.7554/elife.100821. This article has 7 citations and is from a domain leading peer-reviewed journal.
(sun2024negativeregulationof pages 8-9): Li Sun, Xuejin Chen, Chunlin Song, Wen-Jing Shi, Libo Liu, Shuang Bai, Xi Wang, Jiali Chen, Chengyu Jiang, Shuang-min Wang, Zhou-Qing Luo, Ruiwen Wang, Yamei Wang, and Quan-Wen Jin. Negative regulation of apc/c activation by mapk-mediated attenuation of cdc20slp1 under stress. Sep 2024. URL: https://doi.org/10.7554/elife.97896.2, doi:10.7554/elife.97896.2. This article has 4 citations and is from a domain leading peer-reviewed journal.
(sun2024negativeregulationof pages 1-2): Li Sun, Xuejin Chen, Chunlin Song, Wen-Jing Shi, Libo Liu, Shuang Bai, Xi Wang, Jiali Chen, Chengyu Jiang, Shuang-min Wang, Zhou-Qing Luo, Ruiwen Wang, Yamei Wang, and Quan-Wen Jin. Negative regulation of apc/c activation by mapk-mediated attenuation of cdc20slp1 under stress. Sep 2024. URL: https://doi.org/10.7554/elife.97896.2, doi:10.7554/elife.97896.2. This article has 4 citations and is from a domain leading peer-reviewed journal.
(gmachl2000theringh2finger pages 3-4): Michael Gmachl, Christian Gieffers, Alexandre V. Podtelejnikov, Matthias Mann, and Jan-Michael Peters. The ring-h2 finger protein apc11 and the e2 enzyme ubc4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex. Proceedings of the National Academy of Sciences of the United States of America, 97 16:8973-8, Aug 2000. URL: https://doi.org/10.1073/pnas.97.16.8973, doi:10.1073/pnas.97.16.8973. This article has 242 citations and is from a highest quality peer-reviewed journal.