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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 UniProt accession Q9UJX6 corresponds to Homo sapiens ANAPC2 (synonyms: APC2, KIAA1406) annotated as anaphase‑promoting complex subunit 2, also called cyclosome subunit 2. The literature retrieved here consistently uses “APC2/Apc2” to denote the cullin-family catalytic scaffold subunit of the human anaphase‑promoting complex/cyclosome (APC/C) E3 ubiquitin ligase, which matches the UniProt description and the expected cullin-like domain architecture. (watson2019posingtheapcc pages 1-3, alfieri2017visualizingthecomplex pages 2-3)
ANAPC2 encodes APC2, a core subunit of the multi‑subunit E3 ubiquitin ligase APC/C (anaphase-promoting complex/cyclosome). APC2 is the cullin-like scaffold that pairs with the RING subunit APC11 to form the APC2–APC11 cullin–RING catalytic core (“CRL-like” module) responsible for recruiting and activating ubiquitin-loaded E2 enzymes for substrate ubiquitination. (watson2019posingtheapcc pages 1-3, alfieri2017visualizingthecomplex pages 2-3, bansal2019mechanismsforthe pages 1-2)
A central organizing principle is that APC/C function is achieved by:
- Catalytic module: APC2 (cullin-like) + APC11 (RING) that engages E2~Ub and catalyzes ubiquitin transfer. (watson2019posingtheapcc pages 1-3, alfieri2017visualizingthecomplex pages 2-3)
- Substrate recognition: coactivators CDC20 or CDH1 (FZR1), plus APC10/DOC1, which recognize substrate degrons (e.g., D‑box, KEN‑box, ABBA motifs) and position substrates for modification. (alfieri2017visualizingthecomplex pages 2-3, bansal2019mechanismsforthe pages 1-2, hofler2024cryoemstructuresof pages 1-3)
APC/C is a RING E3 ubiquitin ligase, meaning it does not form a covalent E3~Ub intermediate. Instead, APC2–APC11 recruits and activates an E2~Ub thioester and facilitates direct transfer of ubiquitin to lysine residues on substrates (or to ubiquitin to build chains). APC2 functions primarily as a structural/catalytic scaffold positioning the APC11 RING and providing key interaction surfaces (including the APC2 WHB region) needed for productive E2 engagement. (watson2019posingtheapcc pages 1-3, alfieri2017visualizingthecomplex pages 2-3, bodrug2023timeresolvedcryoem(trem) pages 2-3)
APC/C typically polyubiquitinates key cell‑cycle regulators (classically including securin and cyclins), using degron-guided substrate selection via CDC20/CDH1 and APC10. (curtis2020theanaphasepromoting pages 6-11, bansal2019mechanismsforthe pages 1-2)
A widely accepted model is a two‑E2 system:
- Initiation/priming E2s: especially UBE2C (UBCH10) (and sometimes UBE2D/UBCH5 family) to install initial ubiquitin(s) and short chains. (zhou2016insightsintoapcc pages 1-2, yamano2019apcccurrentunderstanding pages 3-5)
- Elongation E2: UBE2S to extend K11-linked chains, generating a proteasome-recognized degradation signal. (zhou2016insightsintoapcc pages 1-2, bodrug2023timeresolvedcryoem(trem) pages 1-2)
Structural work and reviews describe APC2 as the cullin within the APC/C catalytic module, with flexible tethering of the APC11 RING and the APC2 WHB region enabling catalytic conformational rearrangements. (alfieri2017visualizingthecomplex pages 2-3, alfieri2017visualizingthecomplex pages 4-4)
A major 2024 advance is the report of high‑resolution cryo‑EM structures of human apo‑APC/C and APC/C^CDH1:EMI1 (2.9–3.2 Å), which identified a previously unreported zinc-binding module in APC2; zinc ions were experimentally confirmed and proposed to stabilize APC2. (Nature Communications, publication date Nov 2024; https://doi.org/10.1038/s41467-024-54398-5) (hofler2024cryoemstructuresof pages 1-3)
Time-resolved cryo-EM (TR‑EM) of active human APC/C during substrate polyubiquitination revealed that the UBE2S C-terminal peptide (CTP) binds a groove formed by APC2–APC4, and that UBE2C is “clasped” by APC11 RING and the APC2 WHB region in active states. (Nature Structural & Molecular Biology, Sep 2023; https://doi.org/10.1038/s41594-023-01105-5) (bodrug2023timeresolvedcryoem(trem) pages 2-3)
Figure evidence: the CRL-up/CRL-down transitions and UBE2S CTP binding at the APC2–APC4 groove are shown in the cropped figure panels from Bodrug et al. 2023. (bodrug2023timeresolvedcryoem(trem) media b5724fab, bodrug2023timeresolvedcryoem(trem) media 4c971fd7, bodrug2023timeresolvedcryoem(trem) media 1866d704, bodrug2023timeresolvedcryoem(trem) media c7cbb8b1, bodrug2023timeresolvedcryoem(trem) media bafd06b8)
APC2 and APC11 comprise the minimal CRL-like catalytic module of APC/C. A classic biochemical reconstitution showed that an APC2–APC11 heterodimer can be sufficient to catalyze ubiquitination of at least some APC/C substrates in conjunction with appropriate E2s (e.g., UbcH10/UBE2C). (hoflerUnknownyeardriversofcell pages 44-47)
APC/C catalytic output depends on conformational transitions of the APC2–APC11 “CRL arm.” Coactivator binding (CDH1/CDC20) is linked to movement of the catalytic module from an autoinhibited “down” arrangement into an “up” state compatible with productive E2 engagement and ubiquitin transfer. (watson2019posingtheapcc pages 19-23)
The 2023 TR‑EM study quantified this landscape by cryoDRGN analysis, identifying dominant “CRL down” and “CRL up” states and measuring CRL movements (~15 Å and ~11 Å along principal components), supporting an energy landscape enabling thermally driven transitions. (bodrug2023timeresolvedcryoem(trem) pages 4-5)
A key recent concept is that UBE2S (elongating E2) can allosterically promote UBE2C (priming E2) engagement by stabilizing a catalytically competent APC/C conformation. Specifically, a UBE2S CTP interaction at an APC2–APC4 groove stabilized a “CRL up” state and increased recruitment of UBE2C~Ub to APC/C^CDH1 and substrate in dose-dependent assays. (bodrug2023timeresolvedcryoem(trem) pages 6-7)
During mitosis, the SAC restrains APC/C activation until proper kinetochore–microtubule attachment. Its key effector, the mitotic checkpoint complex (MCC) (CDC20, BUBR1, MAD2, BUB3), binds APC/C^CDC20 and inhibits substrate ubiquitination by blocking substrate engagement and/or E2 function. (curtis2020theanaphasepromoting pages 6-11, zhou2016insightsintoapcc pages 5-6)
EMI1 is a multi-domain inhibitor that acts as a pseudo-substrate and multivalent blocker. Structural analysis described EMI1 binding contacts including CDH1, APC10, APC11 RING, the APC2 WHB, and the APC2–APC4 groove, consistent with inhibition that directly targets APC2-centered catalytic and E2-binding interfaces. (watson2019posingtheapcc pages 19-23)
APC/C activation and coactivator exchange are regulated by phosphorylation: CDK1 and PLK1 promote CDC20 binding/early mitotic activation, while CDK1 phosphorylation of CDH1 restrains CDH1 binding in early mitosis; CDH1 becomes effective later as CDK activity falls. (hoflerUnknownyeardriversofcell pages 44-47, zhou2016insightsintoapcc pages 5-6)
The evidence gathered here supports mechanistic spatial context (e.g., SAC signaling from unattached kinetochores) rather than a detailed catalog of APC/C steady-state localization (nucleus vs cytoplasm vs spindle/kinetochores). SAC/MCC signaling is described as initiated at unattached kinetochores, producing a diffusible MCC that inhibits APC/C^CDC20. (liu2020theinteractionprofile pages 44-47, zhou2016insightsintoapcc pages 5-6)
Direct, specific localization statements for APC2/ANAPC2 itself (e.g., immunofluorescence localizing APC2 to spindle poles/kinetochores) were not recovered in the retrieved text corpus; therefore, this report does not assert such localization beyond checkpoint-associated spatial signaling.
Bodrug et al. (2023) provided multiple advances relevant to functional annotation of APC2:
- Visualized native active complexes of human APC/C^CDH1 with UBE2C and UBE2S without crosslinking, showing APC2’s role in E2 engagement via APC2 WHB and APC2–APC4 groove. (bodrug2023timeresolvedcryoem(trem) pages 2-3)
- Quantified conformational distributions and relationships to coactivator occupancy (e.g., in the CRL-down state, ~80% of particles lacked CDH1). (bodrug2023timeresolvedcryoem(trem) pages 6-7)
- Provided quantitative EM and biochemical metrics (e.g., final particle images ~661k and ~775k; map resolutions 3.5–4.0 Å). (bodrug2023timeresolvedcryoem(trem) pages 4-5)
- Reported quantitative recruitment/affinity proxies and bead-rolling (METRIS) statistics supporting ubiquitin-enhanced processivity, including RP values (Ub–CycBN 0.21 ± 0.007 vs CycBN 0.15 ± 0.004). (bodrug2023timeresolvedcryoem(trem) pages 10-11)
Höfler et al. (2024) achieved 2.9–3.2 Å structures that (i) clarified regulatory architecture in apo and inhibited states, and (ii) identified and experimentally confirmed a novel APC2 zinc-binding module, improving domain-level annotation for ANAPC2. (hofler2024cryoemstructuresof pages 1-3)
A 2023 JCI study established a mechanistic axis in Kras-driven lung tumorigenesis in which UBE2C cooperates with APC/C^CDH1 to ubiquitylate and degrade DEPTOR, activating mTORC signaling. Importantly, knockdown of APC2 (and CDH1) increased DEPTOR protein, consistent with APC2-containing APC/C being required for DEPTOR ubiquitination. (Journal of Clinical Investigation, Feb 2023; https://doi.org/10.1172/JCI162434) (zhang2023theube2ccdh1deptoraxis pages 5-6, zhang2023theube2ccdh1deptoraxis pages 9-11)
This supports practical uses of APC/C pathway components as mechanistic biomarkers or therapeutic nodes, even if APC2 itself is not directly drugged.
In the KrasG12D lung tumor model, Ube2c deletion produced quantitative disease modification: median survival increased from ~130 to ~150 days and delayed 100% mortality from day 175 to day 210 (P = 0.0241; n = 10/group). While this statistic is on the E2 component, the mechanism demonstrated requires APC/C function and includes APC2 dependence for DEPTOR regulation in vitro. (zhang2023theube2ccdh1deptoraxis pages 4-5, zhang2023theube2ccdh1deptoraxis pages 5-6)
OpenTargets reports disease associations for ANAPC2 (evidence size 4 in the retrieved snapshot) including colorectal carcinoma and neurodegenerative disease, among others; these should be treated as hypothesis-generating and require deeper primary-evidence evaluation for causal claims. (OpenTargets; accessed via tool context) (OpenTargets Search: -ANAPC2)
Authoritative reviews frame APC2 as part of a cullin–RING E3 whose core challenge is coordinating long-range substrate recruitment with catalysis via conformational mobility of the APC2–APC11 module; coactivators provide both substrate recruitment and catalytic activation by promoting an “up” catalytic state. (watson2019posingtheapcc pages 1-3, watson2019posingtheapcc pages 19-23)
The following table consolidates APC2/ANAPC2 functional annotation, emphasizing 2023–2024 advances and quantitative statistics.
| ANAPC2 (APC2) functional annotation: evidence summary | Key points | Recent (2023–2024) evidence | Foundational/consensus evidence | Practical implications/applications |
|---|---|---|---|---|
| Identity/domains | Human ANAPC2 encodes APC2, the cullin-family catalytic scaffold subunit of APC/C; literature matches UniProt Q9UJX6 and cullin-family/domain annotation. APC2 contains a cullin-like C-terminal region with a WHB subdomain; 2024 cryo-EM additionally identified a zinc-binding module stabilizing APC2. | High-resolution human APC/C structures identified a previously unreported APC2 zinc-binding module and confirmed APC2 as part of the catalytic module in 2.9–3.2 Å maps (hofler2024newstructuralfeatures pages 1-3, hofler2024cryoemstructuresof pages 1-3). | APC2 has long been defined as the cullin-like APC/C subunit, partnering APC11 in the catalytic core; structural reviews describe flexible APC2 CTD/WHB regions and cullin homology (alfieri2017visualizingthecomplex pages 2-3, alfieri2017visualizingthecomplex pages 4-4, curtis2020theanaphasepromoting pages 6-11). | Confirms the target is the human APC/C subunit rather than another APC2 symbol; domain knowledge supports functional annotation and variant interpretation in cell-cycle studies. |
| Catalytic role in APC/C | APC2 is the scaffold of the APC2–APC11 cullin–RING catalytic module, positioning APC11/RING and E2~Ub for ubiquitin transfer to APC/C substrates; APC2 itself is not the E2 or protease but a structural/catalytic organizer of the E3 ligase. | TR-EM directly visualized active APC/C with E2s and showed APC2 participates in E2/CTP engagement during substrate polyubiquitination (bodrug2023timeresolvedcryoem(trem) pages 2-3, bodrug2023timeresolvedcryoem(trem) pages 1-2). | Reconstitution showed APC2 plus APC11 is the minimal ubiquitin ligase module sufficient for ubiquitination with appropriate E2s; reviews consistently describe APC2 as the cullin scaffold of APC/C (hoflerUnknownyeardriversofcell pages 44-47, watson2019posingtheapcc pages 1-3, penas2012theapccubiquitin pages 1-2). | Central for interpreting APC/C-dependent proteolysis of cyclins, securin, and other cell-cycle substrates; useful when considering APC/C as a therapeutic vulnerability in proliferative disease. |
| E2/coactivator interactions | APC/C uses coactivators CDC20 or CDH1 for substrate recruitment and catalytic activation. APC2/APC11 engages initiating and elongating E2s, especially UBE2C/UBCH10 and UBE2S; APC10 and coactivators recognize degrons such as D-box/KEN/ABBA. | 2023 TR-EM showed UBE2C clasped by APC11 RING and APC2 WHB, while the UBE2S C-terminal peptide binds a groove formed by APC2–APC4; both E2s can be engaged in active complexes (bodrug2023timeresolvedcryoem(trem) pages 6-7, bodrug2023timeresolvedcryoem(trem) pages 2-3, bodrug2023timeresolvedcryoem(trem) pages 8-9). 2024 structures reaffirmed that coactivators stimulate a catalytic-module change permitting UBE2C binding (hofler2024newstructuralfeatures pages 1-3, hofler2024cryoemstructuresof pages 1-3). | Reviews define APC/C substrate selection through CDC20/CDH1 plus APC10 and distinguish initiating E2s (UBE2C/UBCH10, sometimes UBE2D/UBCH5) from elongating UBE2S (curtis2020theanaphasepromoting pages 6-11, bansal2019mechanismsforthe pages 1-2, zhou2016insightsintoapcc pages 1-2, yamano2019apcccurrentunderstanding pages 3-5). | Explains substrate specificity and timing of mitotic exit; relevant to experimental design, degron engineering, and efforts to modulate APC/C signaling indirectly via E2s or coactivators. |
| Conformational regulation (CRL up/down) | APC2-containing catalytic module is mobile and switches between autoinhibited “CRL down” and active “CRL up” states; coactivators and UBE2S-linked interactions favor the active state and improve UBE2C recruitment/processivity. | CryoDRGN/TR-EM defined major CRL-down and CRL-up substates and showed UBE2S CTP allosterically stabilizes CRL-up, increasing UBE2C recruitment; APC2 CRL movements of ~15 Å and ~11 Å were quantified (bodrug2023timeresolvedcryoem(trem) pages 6-7, bodrug2023timeresolvedcryoem(trem) pages 4-5, bodrug2023timeresolvedcryoem(trem) media b5724fab). | Earlier structural work established that APC2 WHB and APC11 RING are flexibly tethered and undergo conformational changes required for catalysis (alfieri2017visualizingthecomplex pages 2-3, alfieri2017visualizingthecomplex pages 4-4, watson2019posingtheapcc pages 19-23). | Mechanistic basis for APC/C activity tuning; suggests allosteric control points for chemical probes or inhibitors and helps explain processive ubiquitin-chain assembly. |
| Inhibition/regulation (MCC, EMI1, phosphorylation) | APC/C is inhibited by the spindle assembly checkpoint via MCC (CDC20, BUBR1, MAD2, BUB3), which blocks substrate access and E2 function. EMI1 acts as a pseudosubstrate/multivalent inhibitor contacting CDH1, APC10, APC11, APC2 WHB, and the APC2–APC4 groove. Phosphorylation promotes CDC20 loading and regulates coactivator exchange, while CDK1 phosphorylation restrains CDH1 in early mitosis. | 2024 structural work further clarified APC/C–CDH1:EMI1 organization and regulatory architecture (hofler2024cryoemstructuresof pages 1-3). 2024 Cdc20 functional analysis reinforced SAC dependence on proper APC/C–MCC interactions (hoflerUnknownyeardriversofcell pages 44-47). | Reviews consistently describe MCC-mediated inhibition, EMI1 blockade, and mitotic phosphorylation as core APC/C regulatory layers (hoflerUnknownyeardriversofcell pages 44-47, watson2019posingtheapcc pages 19-23, curtis2020theanaphasepromoting pages 6-11, zhou2016insightsintoapcc pages 5-6, yamano2019apcccurrentunderstanding pages 3-5). | Relevant to anti-mitotic strategies, checkpoint biology, and explaining how APC/C remains inactive until chromosomes are properly attached. |
| Disease relevance (lung cancer DEPTOR axis; OpenTargets associations) | Direct ANAPC2 disease literature is limited, but APC2 function is implicated through APC/C-dependent oncogenic signaling. In lung cancer, APC/C^CDH1 with UBE2C requires APC2 for DEPTOR degradation, activating mTOR signaling. OpenTargets lists ANAPC2 associations with colorectal carcinoma, neurodegenerative disease, aplastic anemia, and skeletal phenotypes, though evidence depth is limited. | In Kras-driven lung cancer, knockdown of APC2 or CDH1 increased DEPTOR protein, supporting DEPTOR as an APC/C^CDH1 substrate; Ube2c deletion suppressed tumorigenesis and survival defects in vivo, placing APC/C catalytic function in a disease-relevant pathway (zhang2023theube2ccdh1deptoraxis pages 5-6, zhang2023theube2ccdh1deptoraxis pages 9-11, zhang2023theube2ccdh1deptoraxis pages 4-5). OpenTargets reports several ANAPC2 disease associations with modest evidence sizes (OpenTargets Search: -ANAPC2). | APC/C dysregulation is broadly linked to tumorigenesis and genome instability in consensus reviews (alfieri2017visualizingthecomplex pages 2-3, zhou2016insightsintoapcc pages 1-2, hofler2024cryoemstructuresof pages 1-3). | Supports using APC/C pathway readouts as cancer biomarkers or mechanistic stratifiers; suggests indirect therapeutic opportunities by targeting APC/C partners (e.g., UBE2C, checkpoint regulators) rather than APC2 directly. |
| Quantitative statistics highlighted | Recent studies provide structural and functional numbers that strengthen annotation: cryo-EM resolutions, particle counts, conformational fractions, biochemical recruitment windows, and cancer survival outcomes. | TR-EM used ~25,380 and 25,900 movies, yielding ~661,289 and 774,933 particle images and 3.5–4.0 Å maps; CRL-down particles were largely CDH1-lacking (~80%); timepoints included 0.5, 1.5, 5, 15 min; UBE2S CTP titrations 0–1.25 µM increased UBE2C recruitment; METRIS RP values included Ub–CycBN 0.21 ± 0.007 versus CycBN 0.15 ± 0.004 and UbV competition ~0.13 ± 0.003 (bodrug2023timeresolvedcryoem(trem) pages 6-7, bodrug2023timeresolvedcryoem(trem) pages 2-3, bodrug2023timeresolvedcryoem(trem) pages 4-5, bodrug2023timeresolvedcryoem(trem) pages 10-11, bodrug2023timeresolvedcryoem(trem) pages 1-2). 2024 structures reached 2.9 and 3.2 Å (hofler2024newstructuralfeatures pages 1-3, hofler2024cryoemstructuresof pages 1-3). In KrasG12D lung cancer, Ube2c deletion extended median survival from ~130 to ~150 days and delayed 100% mortality from day 175 to day 210 (P = 0.0241; n = 10/group) (zhang2023theube2ccdh1deptoraxis pages 4-5). | Quantitative biochemical and structural measurements are consistent with long-standing APC/C models of dynamic catalytic activation and processive ubiquitination (watson2019posingtheapcc pages 1-3, alfieri2017visualizingthecomplex pages 2-3, zhou2016insightsintoapcc pages 1-2). | Useful for benchmarking structural quality, prioritizing recent evidence, and conveying effect sizes in translational or grant/reporting contexts. |
Table: This table summarizes the strongest gathered evidence for human ANAPC2/APC2 function, mechanism, regulation, and disease relevance. It highlights both recent 2023–2024 structural advances and foundational consensus needed for functional annotation.
References
(watson2019posingtheapcc pages 1-3): Edmond R. Watson, Nicholas G. Brown, Jan-Michael Peters, Holger Stark, and Brenda A. Schulman. Posing the apc/c e3 ubiquitin ligase to orchestrate cell division. Trends in cell biology, 29 2:117-134, Feb 2019. URL: https://doi.org/10.1016/j.tcb.2018.09.007, doi:10.1016/j.tcb.2018.09.007. This article has 149 citations and is from a domain leading peer-reviewed journal.
(alfieri2017visualizingthecomplex pages 2-3): Claudio Alfieri, Suyang Zhang, and David Barford. Visualizing the complex functions and mechanisms of the anaphase promoting complex/cyclosome (apc/c). Open Biology, 7:170204, Nov 2017. URL: https://doi.org/10.1098/rsob.170204, doi:10.1098/rsob.170204. This article has 199 citations and is from a peer-reviewed journal.
(bansal2019mechanismsforthe pages 1-2): Shivangee Bansal and Swati Tiwari. Mechanisms for the temporal regulation of substrate ubiquitination by the anaphase-promoting complex/cyclosome. Cell Division, Dec 2019. URL: https://doi.org/10.1186/s13008-019-0057-5, doi:10.1186/s13008-019-0057-5. This article has 27 citations and is from a peer-reviewed journal.
(hofler2024cryoemstructuresof pages 1-3): Anna Höfler, Jun Yu, Jing Yang, Ziguo Zhang, Leifu Chang, Stephen H. McLaughlin, Geoffrey W. Grime, Elspeth F. Garman, Andreas Boland, and David Barford. Cryo-em structures of apo-apc/c and apc/ccdh1:emi1 complexes provide insights into apc/c regulation. Nature Communications, Nov 2024. URL: https://doi.org/10.1038/s41467-024-54398-5, doi:10.1038/s41467-024-54398-5. This article has 11 citations and is from a highest quality peer-reviewed journal.
(bodrug2023timeresolvedcryoem(trem) pages 2-3): Tatyana Bodrug, Kaeli A. Welsh, Derek L. Bolhuis, Ethan Paulаkonis, Raquel C. Martinez-Chacin, Bei Liu, Nicholas Pinkin, Thomas Bonacci, Liying Cui, Pengning Xu, Olivia Roscow, Sascha Josef Amann, Irina Grishkovskaya, Michael J. Emanuele, Joseph S. Harrison, Joshua P. Steimel, Klaus M. Hahn, Wei Zhang, Ellen D. Zhong, David Haselbach, and Nicholas G. Brown. Time-resolved cryo-em (tr-em) analysis of substrate polyubiquitination by the ring e3 anaphase-promoting complex/cyclosome (apc/c). Nature Structural & Molecular Biology, 30:1663-1674, Sep 2023. URL: https://doi.org/10.1038/s41594-023-01105-5, doi:10.1038/s41594-023-01105-5. This article has 21 citations and is from a highest quality peer-reviewed journal.
(curtis2020theanaphasepromoting pages 6-11): Natalie L. Curtis and V. Bolanos-Garcia. The anaphase promoting complex/cyclosome (apc/c): a versatile e3 ubiquitin ligase. Sub-cellular biochemistry, 93:539-623, 2020. URL: https://doi.org/10.1007/978-3-030-28151-9_18, doi:10.1007/978-3-030-28151-9_18. This article has 21 citations.
(zhou2016insightsintoapcc pages 1-2): Zhuan Zhou, Mingjing He, Anil A. Shah, and Yong Wan. Insights into apc/c: from cellular function to diseases and therapeutics. Cell Division, Mar 2016. URL: https://doi.org/10.1186/s13008-016-0021-6, doi:10.1186/s13008-016-0021-6. This article has 173 citations and is from a peer-reviewed journal.
(yamano2019apcccurrentunderstanding pages 3-5): Hiroyuki Yamano. Apc/c: current understanding and future perspectives. F1000Research, 8:725, May 2019. URL: https://doi.org/10.12688/f1000research.18582.1, doi:10.12688/f1000research.18582.1. This article has 137 citations and is from a peer-reviewed journal.
(bodrug2023timeresolvedcryoem(trem) pages 1-2): Tatyana Bodrug, Kaeli A. Welsh, Derek L. Bolhuis, Ethan Paulаkonis, Raquel C. Martinez-Chacin, Bei Liu, Nicholas Pinkin, Thomas Bonacci, Liying Cui, Pengning Xu, Olivia Roscow, Sascha Josef Amann, Irina Grishkovskaya, Michael J. Emanuele, Joseph S. Harrison, Joshua P. Steimel, Klaus M. Hahn, Wei Zhang, Ellen D. Zhong, David Haselbach, and Nicholas G. Brown. Time-resolved cryo-em (tr-em) analysis of substrate polyubiquitination by the ring e3 anaphase-promoting complex/cyclosome (apc/c). Nature Structural & Molecular Biology, 30:1663-1674, Sep 2023. URL: https://doi.org/10.1038/s41594-023-01105-5, doi:10.1038/s41594-023-01105-5. This article has 21 citations and is from a highest quality peer-reviewed journal.
(alfieri2017visualizingthecomplex pages 4-4): Claudio Alfieri, Suyang Zhang, and David Barford. Visualizing the complex functions and mechanisms of the anaphase promoting complex/cyclosome (apc/c). Open Biology, 7:170204, Nov 2017. URL: https://doi.org/10.1098/rsob.170204, doi:10.1098/rsob.170204. This article has 199 citations and is from a peer-reviewed journal.
(bodrug2023timeresolvedcryoem(trem) media b5724fab): Tatyana Bodrug, Kaeli A. Welsh, Derek L. Bolhuis, Ethan Paulаkonis, Raquel C. Martinez-Chacin, Bei Liu, Nicholas Pinkin, Thomas Bonacci, Liying Cui, Pengning Xu, Olivia Roscow, Sascha Josef Amann, Irina Grishkovskaya, Michael J. Emanuele, Joseph S. Harrison, Joshua P. Steimel, Klaus M. Hahn, Wei Zhang, Ellen D. Zhong, David Haselbach, and Nicholas G. Brown. Time-resolved cryo-em (tr-em) analysis of substrate polyubiquitination by the ring e3 anaphase-promoting complex/cyclosome (apc/c). Nature Structural & Molecular Biology, 30:1663-1674, Sep 2023. URL: https://doi.org/10.1038/s41594-023-01105-5, doi:10.1038/s41594-023-01105-5. This article has 21 citations and is from a highest quality peer-reviewed journal.
(bodrug2023timeresolvedcryoem(trem) media 4c971fd7): Tatyana Bodrug, Kaeli A. Welsh, Derek L. Bolhuis, Ethan Paulаkonis, Raquel C. Martinez-Chacin, Bei Liu, Nicholas Pinkin, Thomas Bonacci, Liying Cui, Pengning Xu, Olivia Roscow, Sascha Josef Amann, Irina Grishkovskaya, Michael J. Emanuele, Joseph S. Harrison, Joshua P. Steimel, Klaus M. Hahn, Wei Zhang, Ellen D. Zhong, David Haselbach, and Nicholas G. Brown. Time-resolved cryo-em (tr-em) analysis of substrate polyubiquitination by the ring e3 anaphase-promoting complex/cyclosome (apc/c). Nature Structural & Molecular Biology, 30:1663-1674, Sep 2023. URL: https://doi.org/10.1038/s41594-023-01105-5, doi:10.1038/s41594-023-01105-5. This article has 21 citations and is from a highest quality peer-reviewed journal.
(bodrug2023timeresolvedcryoem(trem) media 1866d704): Tatyana Bodrug, Kaeli A. Welsh, Derek L. Bolhuis, Ethan Paulаkonis, Raquel C. Martinez-Chacin, Bei Liu, Nicholas Pinkin, Thomas Bonacci, Liying Cui, Pengning Xu, Olivia Roscow, Sascha Josef Amann, Irina Grishkovskaya, Michael J. Emanuele, Joseph S. Harrison, Joshua P. Steimel, Klaus M. Hahn, Wei Zhang, Ellen D. Zhong, David Haselbach, and Nicholas G. Brown. Time-resolved cryo-em (tr-em) analysis of substrate polyubiquitination by the ring e3 anaphase-promoting complex/cyclosome (apc/c). Nature Structural & Molecular Biology, 30:1663-1674, Sep 2023. URL: https://doi.org/10.1038/s41594-023-01105-5, doi:10.1038/s41594-023-01105-5. This article has 21 citations and is from a highest quality peer-reviewed journal.
(bodrug2023timeresolvedcryoem(trem) media c7cbb8b1): Tatyana Bodrug, Kaeli A. Welsh, Derek L. Bolhuis, Ethan Paulаkonis, Raquel C. Martinez-Chacin, Bei Liu, Nicholas Pinkin, Thomas Bonacci, Liying Cui, Pengning Xu, Olivia Roscow, Sascha Josef Amann, Irina Grishkovskaya, Michael J. Emanuele, Joseph S. Harrison, Joshua P. Steimel, Klaus M. Hahn, Wei Zhang, Ellen D. Zhong, David Haselbach, and Nicholas G. Brown. Time-resolved cryo-em (tr-em) analysis of substrate polyubiquitination by the ring e3 anaphase-promoting complex/cyclosome (apc/c). Nature Structural & Molecular Biology, 30:1663-1674, Sep 2023. URL: https://doi.org/10.1038/s41594-023-01105-5, doi:10.1038/s41594-023-01105-5. This article has 21 citations and is from a highest quality peer-reviewed journal.
(bodrug2023timeresolvedcryoem(trem) media bafd06b8): Tatyana Bodrug, Kaeli A. Welsh, Derek L. Bolhuis, Ethan Paulаkonis, Raquel C. Martinez-Chacin, Bei Liu, Nicholas Pinkin, Thomas Bonacci, Liying Cui, Pengning Xu, Olivia Roscow, Sascha Josef Amann, Irina Grishkovskaya, Michael J. Emanuele, Joseph S. Harrison, Joshua P. Steimel, Klaus M. Hahn, Wei Zhang, Ellen D. Zhong, David Haselbach, and Nicholas G. Brown. Time-resolved cryo-em (tr-em) analysis of substrate polyubiquitination by the ring e3 anaphase-promoting complex/cyclosome (apc/c). Nature Structural & Molecular Biology, 30:1663-1674, Sep 2023. URL: https://doi.org/10.1038/s41594-023-01105-5, doi:10.1038/s41594-023-01105-5. This article has 21 citations and is from a highest quality peer-reviewed journal.
(hoflerUnknownyeardriversofcell pages 44-47): AK Höfler. Drivers of cell cycle progression: structures and functions of the e3 ubiquitin ligases trip12 and apc/c. Unknown journal, Unknown year.
(watson2019posingtheapcc pages 19-23): Edmond R. Watson, Nicholas G. Brown, Jan-Michael Peters, Holger Stark, and Brenda A. Schulman. Posing the apc/c e3 ubiquitin ligase to orchestrate cell division. Trends in cell biology, 29 2:117-134, Feb 2019. URL: https://doi.org/10.1016/j.tcb.2018.09.007, doi:10.1016/j.tcb.2018.09.007. This article has 149 citations and is from a domain leading peer-reviewed journal.
(bodrug2023timeresolvedcryoem(trem) pages 4-5): Tatyana Bodrug, Kaeli A. Welsh, Derek L. Bolhuis, Ethan Paulаkonis, Raquel C. Martinez-Chacin, Bei Liu, Nicholas Pinkin, Thomas Bonacci, Liying Cui, Pengning Xu, Olivia Roscow, Sascha Josef Amann, Irina Grishkovskaya, Michael J. Emanuele, Joseph S. Harrison, Joshua P. Steimel, Klaus M. Hahn, Wei Zhang, Ellen D. Zhong, David Haselbach, and Nicholas G. Brown. Time-resolved cryo-em (tr-em) analysis of substrate polyubiquitination by the ring e3 anaphase-promoting complex/cyclosome (apc/c). Nature Structural & Molecular Biology, 30:1663-1674, Sep 2023. URL: https://doi.org/10.1038/s41594-023-01105-5, doi:10.1038/s41594-023-01105-5. This article has 21 citations and is from a highest quality peer-reviewed journal.
(bodrug2023timeresolvedcryoem(trem) pages 6-7): Tatyana Bodrug, Kaeli A. Welsh, Derek L. Bolhuis, Ethan Paulаkonis, Raquel C. Martinez-Chacin, Bei Liu, Nicholas Pinkin, Thomas Bonacci, Liying Cui, Pengning Xu, Olivia Roscow, Sascha Josef Amann, Irina Grishkovskaya, Michael J. Emanuele, Joseph S. Harrison, Joshua P. Steimel, Klaus M. Hahn, Wei Zhang, Ellen D. Zhong, David Haselbach, and Nicholas G. Brown. Time-resolved cryo-em (tr-em) analysis of substrate polyubiquitination by the ring e3 anaphase-promoting complex/cyclosome (apc/c). Nature Structural & Molecular Biology, 30:1663-1674, Sep 2023. URL: https://doi.org/10.1038/s41594-023-01105-5, doi:10.1038/s41594-023-01105-5. This article has 21 citations and is from a highest quality peer-reviewed journal.
(zhou2016insightsintoapcc pages 5-6): Zhuan Zhou, Mingjing He, Anil A. Shah, and Yong Wan. Insights into apc/c: from cellular function to diseases and therapeutics. Cell Division, Mar 2016. URL: https://doi.org/10.1186/s13008-016-0021-6, doi:10.1186/s13008-016-0021-6. This article has 173 citations and is from a peer-reviewed journal.
(liu2020theinteractionprofile pages 44-47): Y Liu. The interaction profile between cdc20 and the components of the anaphase promoting complex or cyclosome (apc/c) in human hela cells. Unknown journal, 2020.
(bodrug2023timeresolvedcryoem(trem) pages 10-11): Tatyana Bodrug, Kaeli A. Welsh, Derek L. Bolhuis, Ethan Paulаkonis, Raquel C. Martinez-Chacin, Bei Liu, Nicholas Pinkin, Thomas Bonacci, Liying Cui, Pengning Xu, Olivia Roscow, Sascha Josef Amann, Irina Grishkovskaya, Michael J. Emanuele, Joseph S. Harrison, Joshua P. Steimel, Klaus M. Hahn, Wei Zhang, Ellen D. Zhong, David Haselbach, and Nicholas G. Brown. Time-resolved cryo-em (tr-em) analysis of substrate polyubiquitination by the ring e3 anaphase-promoting complex/cyclosome (apc/c). Nature Structural & Molecular Biology, 30:1663-1674, Sep 2023. URL: https://doi.org/10.1038/s41594-023-01105-5, doi:10.1038/s41594-023-01105-5. This article has 21 citations and is from a highest quality peer-reviewed journal.
(zhang2023theube2ccdh1deptoraxis pages 5-6): Shizhen Zhang, Xiahong You, Yawen Zheng, Yanwen Shen, Xiufang Xiong, and Yi Sun. The ube2c/cdh1/deptor axis is an oncogene and tumor suppressor cascade in lung cancer cells. Journal of Clinical Investigation, Feb 2023. URL: https://doi.org/10.1172/jci162434, doi:10.1172/jci162434. This article has 79 citations and is from a highest quality peer-reviewed journal.
(zhang2023theube2ccdh1deptoraxis pages 9-11): Shizhen Zhang, Xiahong You, Yawen Zheng, Yanwen Shen, Xiufang Xiong, and Yi Sun. The ube2c/cdh1/deptor axis is an oncogene and tumor suppressor cascade in lung cancer cells. Journal of Clinical Investigation, Feb 2023. URL: https://doi.org/10.1172/jci162434, doi:10.1172/jci162434. This article has 79 citations and is from a highest quality peer-reviewed journal.
(zhang2023theube2ccdh1deptoraxis pages 4-5): Shizhen Zhang, Xiahong You, Yawen Zheng, Yanwen Shen, Xiufang Xiong, and Yi Sun. The ube2c/cdh1/deptor axis is an oncogene and tumor suppressor cascade in lung cancer cells. Journal of Clinical Investigation, Feb 2023. URL: https://doi.org/10.1172/jci162434, doi:10.1172/jci162434. This article has 79 citations and is from a highest quality peer-reviewed journal.
(OpenTargets Search: -ANAPC2): Open Targets Query (-ANAPC2, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
(hofler2024newstructuralfeatures pages 1-3): Anna Höfler, Jun Yu, Jing Yang, Ziguo Zhang, Leifu Chang, Stephen H. McLaughlin, Geoffrey W. Grime, Elspeth F. Garman, Andreas Boland, and David Barford. New structural features of the apc/c from high-resolution cryo-em structures of apo-apc/c and apc/ccdh1:emi1 complexes. bioRxiv, Nov 2024. URL: https://doi.org/10.1101/2023.08.31.555674, doi:10.1101/2023.08.31.555674. This article has 2 citations.
(penas2012theapccubiquitin pages 1-2): Clara Penas, Vimal Ramachandran, and Nagi George Ayad. The apc/c ubiquitin ligase: from cell biology to tumorigenesis. Frontiers in Oncology, Jan 2012. URL: https://doi.org/10.3389/fonc.2011.00060, doi:10.3389/fonc.2011.00060. This article has 66 citations.
(bodrug2023timeresolvedcryoem(trem) pages 8-9): Tatyana Bodrug, Kaeli A. Welsh, Derek L. Bolhuis, Ethan Paulаkonis, Raquel C. Martinez-Chacin, Bei Liu, Nicholas Pinkin, Thomas Bonacci, Liying Cui, Pengning Xu, Olivia Roscow, Sascha Josef Amann, Irina Grishkovskaya, Michael J. Emanuele, Joseph S. Harrison, Joshua P. Steimel, Klaus M. Hahn, Wei Zhang, Ellen D. Zhong, David Haselbach, and Nicholas G. Brown. Time-resolved cryo-em (tr-em) analysis of substrate polyubiquitination by the ring e3 anaphase-promoting complex/cyclosome (apc/c). Nature Structural & Molecular Biology, 30:1663-1674, Sep 2023. URL: https://doi.org/10.1038/s41594-023-01105-5, doi:10.1038/s41594-023-01105-5. This article has 21 citations and is from a highest quality peer-reviewed journal.
(zhang2023theube2ccdh1deptoraxis pages 1-2): Shizhen Zhang, Xiahong You, Yawen Zheng, Yanwen Shen, Xiufang Xiong, and Yi Sun. The ube2c/cdh1/deptor axis is an oncogene and tumor suppressor cascade in lung cancer cells. Journal of Clinical Investigation, Feb 2023. URL: https://doi.org/10.1172/jci162434, doi:10.1172/jci162434. This article has 79 citations and is from a highest quality peer-reviewed journal.