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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 protein is unambiguously the budding-yeast anaphase-promoting complex subunit 2, encoded by APC2, formerly RSI1, at locus YLR127C in Saccharomyces cerevisiae S288c. The original gene-specific study identified an 853-residue, approximately 99-kDa essential protein, demonstrated its association with the known APC/C subunit Cdc23, and renamed RSI1 as APC2. These observations match the supplied UniProt identity and exclude same-symbol genes from other organisms. Early sequence comparisons and modern yeast APC/C structures both support its assignment to the cullin family. (kramer1998buddingyeastrsi1apc2 pages 2-3, kramer1998buddingyeastrsi1apc2 pages 6-7, vazquezfernandez2024acomparativestudy pages 5-8)
Apc2 is best described as the cullin-like structural organizer of the APC/C catalytic module. It binds and positions the RING-domain protein Apc11 and thereby helps present E2-conjugated ubiquitin to APC/C-bound substrates. Apc2 is not a conventional metabolic enzyme with an independently defined reaction, is not itself the RING active component, and is not the principal degron receptor. Rather, its biological function emerges within the intact APC/C E3 ubiquitin ligase. In budding yeast, APC/C-dependent ubiquitination drives destruction of Pds1/securin to permit sister-chromatid separation and destruction of Clb mitotic cyclins—especially Clb2—to lower mitotic CDK activity and permit mitotic exit. (kramer1998buddingyeastrsi1apc2 pages 6-7, kramer1998buddingyeastrsi1apc2 pages 1-2, alfieri2017visualizingthecomplex pages 2-3, vazquezfernandez2024acomparativestudy pages 1-2)
| Annotation question | Best-supported conclusion | Direct evidence | Caveat |
|---|---|---|---|
| Identity, aliases, and size | The target is budding-yeast Apc2, encoded by APC2/RSI1/YLR127C, matching UniProt Q12440; it is an 853-aa, approximately 99-kDa protein. | The original gene study mapped RSI1 to YLR127C, reported an 853-residue product of approximately 99 kDa, and renamed it APC2 after demonstrating association with APC/C (kramer1998buddingyeastrsi1apc2 pages 2-3, kramer1998buddingyeastrsi1apc2 pages 6-7). | These data verify the yeast target and should not be conflated with unrelated same-symbol genes or APC2 orthologs in other organisms. |
| Cullin family and domains | Apc2 is the APC/C's cullin-family subunit; its cullin-like architecture includes a C-terminal cullin/WHB region and agrees with the supplied ANAPC2 and cullin-homology annotations. | Early sequence comparisons found 23–28% identity and 49–55% similarity to animal cullins; structural work places yeast Apc2 in the conserved Apc2:Apc11 module (kramer1998buddingyeastrsi1apc2 pages 2-3, alfieri2017visualizingthecomplex pages 2-3, vazquezfernandez2024acomparativestudy pages 5-8). | The 1998 sequence evidence was weak by itself; the family assignment is substantially strengthened by later comparative structural evidence. Exact InterPro boundaries are database annotations rather than boundaries established in the cited experiments. |
| Molecular role | Apc2 is chiefly an elongated catalytic-module scaffold that binds and positions the RING protein Apc11. It is neither the principal substrate receptor nor a standalone ubiquitin-transfer enzyme. | Apc2 and Apc11 form the cullin–RING module; Apc11 supplies the RING domain, whereas coactivators Cdc20/Cdh1 together with Apc10 recognize D-box, KEN-box, and ABBA degrons (alfieri2017visualizingthecomplex pages 2-3, vazquezfernandez2024acomparativestudy pages 5-8). | “Catalytic subunit” or “catalytic module” does not mean Apc2 alone catalyzes ubiquitin transfer. APC/C ligase activity emerges from Apc2-organized Apc11–E2 machinery integrated with the substrate-receptor module. |
| Yeast E2 enzymes | Budding-yeast APC/C uses Ubc4 as the priming E2 and Ubc1 as the processive chain-extending E2. | The 2024 yeast structural analysis identifies Ubc4 as directly ubiquitylating substrates and Ubc1 as extending substrate-attached ubiquitin (vazquezfernandez2024acomparativestudy pages 1-2). | These are APC/C-level assignments; they do not demonstrate an independent catalytic reaction by isolated Apc2. |
| Principal biological outputs | Apc2 enables APC/C-dependent turnover of Pds1/securin, permitting sister-chromatid separation and anaphase onset, and Clb2/B-type cyclin, lowering mitotic CDK activity and promoting mitotic exit. | apc2/rsi1 mutants stabilize Clb2 and arrest before anaphase; deleting PDS1 bypasses the initial metaphase block but cells subsequently arrest in telophase, showing separable requirements for Pds1 and Clb2 turnover (kramer1998buddingyeastrsi1apc2 pages 6-7, kramer1998buddingyeastrsi1apc2 pages 1-2). | Substrate selection is mediated principally by APC/C coactivators and degrons, not by direct substrate specificity intrinsic to Apc2. |
| Essentiality and arrest phenotypes | APC2 is essential. Severe loss of function causes large-budded metaphase arrest and defective initiation of anaphase; bypass of the Pds1-dependent block reveals a later telophase/mitotic-exit defect. | Heterozygous gene disruption produced 2 viable:2 dead tetrads; temperature-sensitive rsi1-8 cells arrested in metaphase, while rsi1-8 pds1Δ cells initiated anaphase but arrested in telophase. Compromised alleles were synthetically lethal with sic1Δ (kramer1998buddingyeastrsi1apc2 pages 2-3, kramer1998buddingyeastrsi1apc2 pages 6-7, kramer1998buddingyeastrsi1apc2 pages 7-8). | Phenotypes reflect failure of the complete APC/C pathway and do not imply that Apc2 directly binds every affected substrate. |
| Cellular localization | APC/C activity is best placed primarily in the nucleus, with discrete kinetochore/microtubule-end-associated foci and transient anaphase-spindle localization. | Endogenous Cdc23-GFP was nuclear with one or two foci and appeared on the anaphase spindle; Apc9-GFP showed a similar, weaker pattern. Cdc23-YFP spindle-like signal overlapped CFP-Tub1 in 90% of cells in which that signal was detectable (melloy2004changesinthe pages 1-2, melloy2004changesinthe pages 5-6). | This is indirect for Apc2: the reporters were Cdc23 and Apc9, not Apc2. The foci were not spindle-pole bodies and could not be distinguished conclusively as kinetochores versus microtubule ends; localization of every intact APC/C particle cannot be assumed (melloy2004changesinthe pages 12-13, melloy2004changesinthe pages 1-2). |
| 2024 yeast cryo-EM update | Yeast apo-APC/C already holds the Apc2:Apc11 module in an E2-compatible position. Reported phosphorylated and unphosphorylated apo maps were 4.5 Å and 4.9 Å, respectively; in the active arrangement Apc11's RING domain is approximately 30 Å from substrate. | Comparative cryo-EM directly analyzed unphosphorylated apo yeast APC/C, phosphorylated apo APC/C, and APC/C–Cdh1–substrate, demonstrating conserved architecture but species-specific activation mechanisms (vazquezfernandez2024acomparativestudy pages 5-8, vazquezfernandez2024acomparativestudy pages 1-2). | At these medium resolutions, mechanistic interpretation integrates fitted structural models; the approximately 30-Å separation concerns Apc11-to-substrate geometry, not an Apc2 active-site distance. |
| Human zinc-binding insert comparison | The recently defined 45-residue, four-cysteine APC2 zinc-binding module is a human feature and is absent from budding-yeast Apc2. | Human APC2's zinc-binding insert was resolved in a 2.9-Å map and linked to thermal stability; sequence/structure comparison found that the corresponding module is absent from yeast (vazquezfernandez2024acomparativestudy pages 5-8). | Human zinc-binding results must not be transferred to Q12440; their value here is to define a species-specific architectural difference. |
Table: Compact evidence matrix distinguishing direct budding-yeast findings from APC/C-level inference and human-specific structural features. It summarizes identity, molecular role, pathway outputs, phenotypes, localization, and the principal 2024 cryo-EM results.
The foundational study by Kramer and colleagues, published 19 January 1998 in The EMBO Journal, mapped RSI1 to YLR127C, described an 853-amino-acid, approximately 99-kDa protein, and established that it is an APC/C component. The correspondence among APC2, RSI1, YLR127C, the expected protein size, and APC/C membership verifies that the literature concerns the requested S. cerevisiae protein rather than an unrelated APC2 symbol. URL: https://doi.org/10.1093/emboj/17.2.498. (kramer1998buddingyeastrsi1apc2 pages 2-3, kramer1998buddingyeastrsi1apc2 pages 6-7)
The 1998 study found 23–28% sequence identity and 49–55% similarity to selected animal cullins. Although modest sequence similarity alone was initially suggestive rather than definitive, later structural work places yeast Apc2 in the conserved cullin–RING architecture of APC/C. This agrees with the supplied InterPro annotations ANAPC2, ANAPC2_C, Cullin-like_AB, and Cullin homology. Precise InterPro boundaries, however, are database-derived annotations rather than boundaries established in the original yeast genetic experiments. (kramer1998buddingyeastrsi1apc2 pages 2-3, alfieri2017visualizingthecomplex pages 2-3, vazquezfernandez2024acomparativestudy pages 5-8)
“APC2” is used for orthologs in many eukaryotes and can occur in literature unrelated to budding yeast. Conclusions below are therefore separated into: (1) direct S. cerevisiae Apc2 evidence; (2) yeast APC/C-level inference; and (3) comparative evidence from other species. In particular, a recently characterized zinc-binding insert in human APC2 should not be annotated onto Q12440 because the corresponding 45-residue, four-cysteine module is absent from budding-yeast Apc2. (vazquezfernandez2024acomparativestudy pages 5-8)
APC/C is a multisubunit cullin–RING E3 ubiquitin ligase. Its catalytic module contains cullin-like Apc2 and RING-domain Apc11. Apc2 provides an elongated structural platform and a flexible C-terminal/WHB region that organizes Apc11; Apc11 supplies the RING domain that recruits and activates an E2~ubiquitin conjugate. Thus, descriptions of Apc2 as a “catalytic subunit” mean that it belongs to the catalytic module—not that isolated Apc2 contains an enzyme active site or transfers ubiquitin by itself. (alfieri2017visualizingthecomplex pages 2-3, vazquezfernandez2024acomparativestudy pages 5-8)
Substrate recognition is also not principally an intrinsic property of Apc2. APC/C coactivators—Cdc20 or Cdh1/Hct1 in mitotic cycles and Ama1 in yeast meiosis—cooperate with Apc10 to recognize substrate degrons such as D boxes and KEN boxes. Apc2 instead positions the Apc11–E2 machinery relative to substrates captured elsewhere on the complex. This division of labor explains how Apc2 can be indispensable to ubiquitination without possessing narrow substrate specificity of its own. (alfieri2017visualizingthecomplex pages 2-3, vazquezfernandez2024acomparativestudy pages 1-2)
At the complex level, APC/C catalyzes transfer of ubiquitin from an E2–ubiquitin thioester to lysine residues on protein substrates, followed by polyubiquitin-chain construction and proteasomal degradation. The 2024 yeast structural analysis assigns Ubc4 as the priming E2 that directly modifies substrates and Ubc1 as the processive E2 that extends substrate-attached ubiquitin. Apc2's contribution is architectural: it organizes Apc11 and the E2-binding geometry rather than independently catalyzing a small-molecule reaction. (harris2026increasingcellularlongevity pages 30-35, vazquezfernandez2024acomparativestudy pages 1-2)
Accordingly, no substrate should be described as an “Apc2 substrate” in the enzyme–substrate sense. Pds1, Clb2, and other cell-cycle proteins are substrates of the assembled APC/C under the control of coactivators, degrons, phosphorylation, and checkpoint state.
The clearest direct function is APC/C-dependent destruction of Pds1, the budding-yeast securin. Pds1 degradation releases the separase pathway and permits sister-chromatid separation. Temperature-sensitive rsi1/apc2 mutants arrested in metaphase, while deletion of PDS1 allowed mutant cells to initiate anaphase. This genetic bypass places Apc2-dependent APC/C function upstream of Pds1 destruction and anaphase onset. (kramer1998buddingyeastrsi1apc2 pages 6-7, kramer1998buddingyeastrsi1apc2 pages 1-2)
Apc2 is also required for degradation of mitotic B-type cyclins, especially Clb2. Clb2 was stabilized in rsi1-8 cells. Importantly, rsi1-8 pds1Δ cells escaped the initial metaphase block but subsequently arrested in telophase, demonstrating that bypassing securin does not restore the later APC/C requirement for cyclin destruction and mitotic exit. Synthetic lethality between compromised APC2 and sic1Δ further supports this interpretation: when APC/C-mediated Clb2 turnover is impaired, the CDK inhibitor Sic1 becomes critical for suppressing residual mitotic CDK activity. (kramer1998buddingyeastrsi1apc2 pages 6-7, kramer1998buddingyeastrsi1apc2 pages 7-8)
Ase1, a spindle-associated protein involved in spindle organization/disassembly, was also recognized in the early literature as an APC/C substrate. Nevertheless, Pds1 and Clb2 provide the most direct gene-specific explanation for the characteristic apc2 metaphase and telophase phenotypes. (kramer1998buddingyeastrsi1apc2 pages 1-2)
The spindle-assembly checkpoint prevents premature APC/C activation until chromosome–spindle attachments are satisfactory. Apc2 is not itself established as the checkpoint sensor; rather, its Apc2:Apc11 module executes ubiquitination after checkpoint and coactivator inputs license APC/C activity. This distinction avoids attributing upstream sensing functions to a catalytic-module scaffold. The APC/C's localization also changes under microtubule and checkpoint perturbations, consistent with spatial regulation of the assembled ligase. (melloy2004changesinthe pages 13-14, melloy2004changesinthe pages 1-2)
A heterozygous APC2/RSI1 disruption yielded tetrads with two viable and two dead spores, and the viable spores lacked the disruption, establishing that the gene is essential under the tested growth conditions. Even a promoter deletion ending approximately 300 bp upstream of the start codon was lethal, whereas the recovered rsi1-1 promoter insertion produced a partial-loss-of-function state. (kramer1998buddingyeastrsi1apc2 pages 2-3, kramer1998buddingyeastrsi1apc2 pages 7-8)
Physical association was shown by in-vivo interaction/co-immunoprecipitation with Cdc23, an established APC/C subunit. Combined with the approximately 100-kDa size, genetic interactions, metaphase arrest, and defective Pds1/Clb2 turnover, this supplied convergent genetic, cytological, physiological, and biochemical evidence that Rsi1 is Apc2 rather than merely an upstream regulator of APC/C. (kramer1998buddingyeastrsi1apc2 pages 2-3, kramer1998buddingyeastrsi1apc2 pages 6-7, kramer1998buddingyeastrsi1apc2 pages 1-2)
The strongest phenotype logic is:
Direct localization evidence for Apc2 itself is limited in the retrieved primary literature. The most informative yeast experiments tagged other APC/C subunits at their endogenous loci, especially Cdc23-GFP/YFP and Apc9-GFP. Cdc23 signal was predominantly nuclear throughout the cell cycle, with one or two nuclear foci; Apc9 showed a similar but weaker pattern. During anaphase, tagged Cdc23 also appeared along the mitotic spindle. Among cells with a detectable spindle-like Cdc23-YFP signal, 90% overlapped CFP-Tub1, supporting genuine spindle association. (melloy2004changesinthe pages 1-2, melloy2004changesinthe pages 5-6, melloy2004changesinthe pages 3-5)
The nuclear foci colocalized with kinetochore-associated markers but not with the spindle-pole-body marker Spc42. The authors therefore excluded a simple spindle-pole-body assignment but cautioned that the foci could represent kinetochores, microtubule ends, or their interface. Microtubule depolymerization and checkpoint-related mutations altered the foci without necessarily removing general nuclear APC/C signal. In cdc20-1, cells displaying a Cdc23 nuclear spot decreased approximately ninefold. (melloy2004changesinthe pages 12-13, melloy2004changesinthe pages 10-12, melloy2004changesinthe pages 1-2)
The defensible functional annotation is therefore that the yeast APC/C acts predominantly in the nucleus and can associate dynamically with kinetochore/microtubule-end regions and the anaphase spindle. Because these studies visualized Cdc23 or Apc9 rather than Apc2, this is complex-level localization evidence and should not be overinterpreted as a directly measured Apc2 distribution. The localization study was published in Genetics in July 2004. URL: https://doi.org/10.1534/genetics.103.025478. (melloy2004changesinthe pages 13-14, melloy2004changesinthe pages 1-2, melloy2004changesinthe pages 5-6)
The most important recent Apc2-relevant advance is the comparative cryo-EM study by Vazquez-Fernandez and colleagues, published in eLife in October 2024. It examined three S. cerevisiae assemblies: unphosphorylated apo-APC/C, phosphorylated apo-APC/C, and APC/C–Cdh1–substrate. URL: https://doi.org/10.7554/eLife.100821. The phosphorylated and unphosphorylated apo structures were reported at approximately 4.5 Å and 4.9 Å, respectively. (vazquezfernandez2024acomparativestudy pages 5-8, vazquezfernandez2024acomparativestudy pages 1-2)
The work confirmed conserved overall APC/C architecture but identified a notable species difference: in budding-yeast apo-APC/C, the Apc2:Apc11 module is already positioned compatibly with E2 binding, whereas human APC/C relies more strongly on coactivator-induced repositioning of this module. In the active yeast arrangement, the Apc11 RING domain lies approximately 30 Å from the substrate, providing a structural explanation for how the Apc2 scaffold positions ubiquitin-transfer machinery near a receptor-bound target. (vazquezfernandez2024acomparativestudy pages 5-8, vazquezfernandez2024acomparativestudy pages 1-2)
This result refines, rather than overturns, the established annotation. Apc2 remains the conserved cullin scaffold, but activation mechanisms inferred from human APC/C should not automatically be transferred to budding yeast. The 2024 structures also show why current annotation should treat APC/C as a conformational machine: Apc2's significance lies not merely in static complex assembly but in the spatial organization of Apc11, E2, and substrate.
For Q12440 itself, current “applications” are primarily experimental rather than clinical or industrial:
No evidence in the retrieved literature supports a direct clinical implementation of budding-yeast Apc2, nor would it be appropriate to transfer human APC/C therapeutic claims to Q12440. Its practical value is as a genetically tractable model for irreversible cell-cycle transitions and cullin–RING E3-ligase mechanism.
Recommended functional description:
Apc2 is the essential cullin-family scaffold of the S. cerevisiae anaphase-promoting complex/cyclosome catalytic module. It binds and positions the Apc11 RING subunit and thereby organizes Ubc4/Ubc1-dependent ubiquitination of coactivator-bound APC/C substrates. APC/C activity supported by Apc2 promotes Pds1/securin destruction for sister-chromatid separation and Clb2 destruction for mitotic exit. The complex functions mainly in the nucleus, with regulated association at kinetochore/microtubule-end regions and the anaphase spindle; direct Apc2-specific localization remains insufficiently established. (kramer1998buddingyeastrsi1apc2 pages 6-7, alfieri2017visualizingthecomplex pages 2-3, vazquezfernandez2024acomparativestudy pages 1-2, melloy2004changesinthe pages 1-2)
References
(kramer1998buddingyeastrsi1apc2 pages 2-3): Kate M. Kramer, D. Fesquet, A. Johnson, and L. Johnston. Budding yeast rsi1/apc2, a novel gene necessary for initiation of anaphase, encodes an apc subunit. The EMBO Journal, 17:498-506, Jan 1998. URL: https://doi.org/10.1093/emboj/17.2.498, doi:10.1093/emboj/17.2.498. This article has 70 citations.
(kramer1998buddingyeastrsi1apc2 pages 6-7): Kate M. Kramer, D. Fesquet, A. Johnson, and L. Johnston. Budding yeast rsi1/apc2, a novel gene necessary for initiation of anaphase, encodes an apc subunit. The EMBO Journal, 17:498-506, Jan 1998. URL: https://doi.org/10.1093/emboj/17.2.498, doi:10.1093/emboj/17.2.498. This article has 70 citations.
(vazquezfernandez2024acomparativestudy pages 5-8): 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.
(kramer1998buddingyeastrsi1apc2 pages 1-2): Kate M. Kramer, D. Fesquet, A. Johnson, and L. Johnston. Budding yeast rsi1/apc2, a novel gene necessary for initiation of anaphase, encodes an apc subunit. The EMBO Journal, 17:498-506, Jan 1998. URL: https://doi.org/10.1093/emboj/17.2.498, doi:10.1093/emboj/17.2.498. This article has 70 citations.
(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 208 citations and is from a peer-reviewed journal.
(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.
(kramer1998buddingyeastrsi1apc2 pages 7-8): Kate M. Kramer, D. Fesquet, A. Johnson, and L. Johnston. Budding yeast rsi1/apc2, a novel gene necessary for initiation of anaphase, encodes an apc subunit. The EMBO Journal, 17:498-506, Jan 1998. URL: https://doi.org/10.1093/emboj/17.2.498, doi:10.1093/emboj/17.2.498. This article has 70 citations.
(melloy2004changesinthe pages 1-2): Patricia G Melloy and Sandra L Holloway. Changes in the localization of the saccharomyces cerevisiae anaphase-promoting complex upon microtubule depolymerization and spindle checkpoint activation. Genetics, 167:1079-1094, Jul 2004. URL: https://doi.org/10.1534/genetics.103.025478, doi:10.1534/genetics.103.025478. This article has 22 citations and is from a domain leading peer-reviewed journal.
(melloy2004changesinthe pages 5-6): Patricia G Melloy and Sandra L Holloway. Changes in the localization of the saccharomyces cerevisiae anaphase-promoting complex upon microtubule depolymerization and spindle checkpoint activation. Genetics, 167:1079-1094, Jul 2004. URL: https://doi.org/10.1534/genetics.103.025478, doi:10.1534/genetics.103.025478. This article has 22 citations and is from a domain leading peer-reviewed journal.
(melloy2004changesinthe pages 12-13): Patricia G Melloy and Sandra L Holloway. Changes in the localization of the saccharomyces cerevisiae anaphase-promoting complex upon microtubule depolymerization and spindle checkpoint activation. Genetics, 167:1079-1094, Jul 2004. URL: https://doi.org/10.1534/genetics.103.025478, doi:10.1534/genetics.103.025478. This article has 22 citations and is from a domain leading peer-reviewed journal.
(harris2026increasingcellularlongevity pages 30-35): R Harris. Increasing cellular longevity in saccharomyces cerevisiae by activating the anaphase promoting complex. Unknown journal, 2026.
(melloy2004changesinthe pages 13-14): Patricia G Melloy and Sandra L Holloway. Changes in the localization of the saccharomyces cerevisiae anaphase-promoting complex upon microtubule depolymerization and spindle checkpoint activation. Genetics, 167:1079-1094, Jul 2004. URL: https://doi.org/10.1534/genetics.103.025478, doi:10.1534/genetics.103.025478. This article has 22 citations and is from a domain leading peer-reviewed journal.
(melloy2004changesinthe pages 3-5): Patricia G Melloy and Sandra L Holloway. Changes in the localization of the saccharomyces cerevisiae anaphase-promoting complex upon microtubule depolymerization and spindle checkpoint activation. Genetics, 167:1079-1094, Jul 2004. URL: https://doi.org/10.1534/genetics.103.025478, doi:10.1534/genetics.103.025478. This article has 22 citations and is from a domain leading peer-reviewed journal.
(melloy2004changesinthe pages 10-12): Patricia G Melloy and Sandra L Holloway. Changes in the localization of the saccharomyces cerevisiae anaphase-promoting complex upon microtubule depolymerization and spindle checkpoint activation. Genetics, 167:1079-1094, Jul 2004. URL: https://doi.org/10.1534/genetics.103.025478, doi:10.1534/genetics.103.025478. This article has 22 citations and is from a domain leading peer-reviewed journal.