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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 target is correctly identified as fission-yeast mad3 (UniProt O59767; ORF aliases SPCC1795.01c/SPCC895.02), encoding mitotic spindle-checkpoint component Mad3. The direct literature describes a 933-bp chromosome III gene encoding an approximately 36-kDa protein. Its sequence and architecture are consistent with the supplied Bub1/Mad3, Mad3/Bub1_I and TPR-like domain annotations. It is a kinase-less Mad3/BubR1-family protein—not the kinase Bub1 and not an unrelated protein carrying a similar symbol. The original comparison found 31% identity to budding-yeast Mad3 and 28% identity to human BubR1. (millband2002fissionyeastmad3p pages 4-6)
Mad3 is not an enzyme or transporter. Its primary role is as a non-catalytic spindle assembly checkpoint (SAC) effector: it assembles with Mad2 and Slp1/Cdc20 in the mitotic checkpoint complex (MCC), enabling inhibition of Slp1-activated anaphase-promoting complex/cyclosome (APC/C). This delays anaphase and preserves sister-chromatid cohesion while kinetochores remain unattached or improperly attached to spindle microtubules. Mad3 acts both at unattached kinetochores, where checkpoint complexes are generated, and in soluble MCC/APC/C assemblies within the mitotic nucleus. (millband2002fissionyeastmad3p pages 10-12, sczaniecka2008thespindlecheckpoint pages 4-5)
The 2002 cloning study identified fission-yeast mad3 in chromosome III cosmid SPCC895 as a 933-bp open reading frame encoding an approximately 36-kDa checkpoint protein. This agrees with the supplied UniProt accession, organism and SPCC895 locus alias. A full-ORF deletion was viable under ordinary growth, while an endogenous C-terminal Mad3-GFP fusion was phenotypically indistinguishable from wild type, enabling functional localization experiments. (millband2002fissionyeastmad3p pages 4-6, millband2002fissionyeastmad3p pages 3-4)
The domain assignment is also coherent. Mad3 belongs to the Mad3/BubR1 branch of the broader Bub1/Mad3 checkpoint family but lacks the C-terminal protein-kinase domain found in Bub1. Its N-terminal region is a TPR-like helical domain, and functional sequence mapping identifies an N-terminal KEN1 motif plus a C-terminal region containing ABBA, KEN2 and D-box-mimicking elements. Thus, the UniProt/InterPro annotations Bub1/Mad3 (IPR015661), Mad3/Bub1_I (IPR013212), TPR-like helical domain (IPR011990) and PF08311 are consistent with the experimental literature. (millband2002fissionyeastmad3p pages 10-12, sewart2017differentfunctionalityof pages 3-3)
No evidence was used from an unrelated “mad3” gene. Results from budding yeast, animals or other fungi are treated only as comparative context, not as direct annotation evidence for O59767.
Mad3’s central biochemical function is to help convert the kinetochore-generated SAC signal into inhibition of APC/C–Slp1/Cdc20. Co-immunoprecipitation from S. pombe extracts demonstrated association of Mad3 with Mad2, Slp1/Cdc20 and Bub3. Functionally, Mad2 overexpression caused a short-spindle metaphase arrest in approximately 70% of wild-type, mad1Δ, bub1Δ and bub3Δ cells, but only 8% of mad3Δ cells, despite comparable Mad2 induction. Mad3 therefore acts with or downstream of Mad2 at the checkpoint-effector stage rather than merely controlling Mad2 abundance. (millband2002fissionyeastmad3p pages 6-8, millband2002fissionyeastmad3p pages 1-2)
Biochemical work subsequently placed Mad3–Mad2–Slp1 in an APC/C-associated MCC. Mad3, Mad2 and Slp1 co-fractionated with Lid1-tagged APC/C in the approximately 19S range. Quantitative depletion estimated that up to 8% of APC/C could be co-depleted with Mad2 and that at least 5% of core APC/C was Mad2-associated under the assay conditions. Stable checkpoint-protein association with mitotic APC/C required functional Slp1/Cdc20. (sczaniecka2008thespindlecheckpoint pages 4-5)
The N-terminal KEN1 motif is crucial for core MCC formation. Substitution of the KEN20 sequence with alanines eliminated detectable APC/C association of both Mad3 and Mad2. Mad3 association with APC/C was also Mad2-dependent, demonstrating reciprocal cooperation within the inhibitory complex. (sczaniecka2008thespindlecheckpoint pages 4-5, sczaniecka2008thespindlecheckpoint pages 1-1)
The C-terminal region provides a second layer of Cdc20 control. Endogenous motif mutagenesis showed that KEN2 and neighboring ABBA and D-box-mimicking elements are dispensable for formation of the core Mad3–Mad2–Slp1 MCC but are required for full checkpoint activity. Deleting residues 282–310 largely abolished checkpoint function; ABBA1 mutation produced a strong defect, ABBA2 mutation a weaker defect and mutation of the D-box mimic a partial defect. These observations support a model in which the Mad3 C terminus engages an additional Slp1/Cdc20 molecule and occupies substrate-recognition surfaces, allowing Mad3 to operate as a pseudosubstrate inhibitor of APC/C–Cdc20. (sewart2017differentfunctionalityof pages 3-3, sewart2017differentfunctionalityof pages 1-3)
The detailed two-Cdc20 arrangement is supported by S. pombe genetics and biochemistry integrated with structural information from other systems. It should therefore be considered a strong mechanistic model rather than a complete atomic structure determined for full-length O59767 itself. (sewart2017elucidatingthemolecular pages 105-110)
The best-supported pathway is:
unattached kinetochore → Mph1/Mps1 activity and Bub1–Bub3 scaffold → Mad1–Mad2 and Mad3 recruitment → MCC production → Slp1/Cdc20 inhibition → APC/C restraint → delayed securin/cyclin destruction and anaphase onset.
Bub1 has a direct structural role in Mad3 recruitment. Ectopic tethering showed that Mad3 colocalized with full-length Bub1 and a Bub1 fragment containing its N-terminal TPR domain, but not with Bub1 lacking that domain. With purified proteins, Bub1-TPR and Mad3-TPR eluted separately by size-exclusion chromatography at 15.2 and 14.3 mL, respectively, whereas their mixture eluted as a larger complex at 12.1 mL. The Bub1 TPR domain is therefore necessary and sufficient for recruitment and can bind Mad3 directly. (leontiou2019thebub1tprdomain pages 1-3, leontiou2019thebub1tprdomain pages 7-8)
This supports an expert scaffold model in which Bub1 simultaneously organizes checkpoint inputs: its CD1 region recruits Mad1–Mad2, whereas its TPR region recruits Mad3, increasing the local concentration of MCC components. The suggestion that this proximity directly promotes Mad3 phosphorylation or MCC incorporation remains plausible but was not itself demonstrated by the binding experiment. (leontiou2019thebub1tprdomain pages 1-3, leontiou2019thebub1tprdomain pages 7-8)
Functional Mad3-GFP appears as punctate nuclear foci at kinetochores early in mitosis, colocalizes with the centromeric histone Cnp1/CENP-A at unattached kinetochores and disappears during anaphase. During prolonged checkpoint activation, kinetochore accumulation becomes more prominent. Stable recruitment requires Bub1, Bub3 and the Mph1 kinase; in their absence, the bright focus is lost and Mad3 fluorescence becomes diffuse. Mad1 and Mad2 are not strictly required for kinetochore targeting. (millband2002fissionyeastmad3p pages 10-12, millband2002fissionyeastmad3p pages 1-2)
After hydroxyurea release, approximately 50% of wild-type cells displayed a bright Mad3-GFP focus at 165 minutes, compared with approximately 20% of mad1Δ or mad2Δ cells. The reduced frequency in these mutants likely reflects altered mitotic kinetics rather than an absolute recruitment requirement. (millband2002fissionyeastmad3p pages 10-12)
Accordingly, the biologically relevant locations are:
There is no evidence that Mad3 is secreted, membrane-integrated or associated with an extracellular compartment.
mad3 is dispensable for vegetative viability under favorable conditions but becomes critical when spindle assembly or kinetochore attachment is defective. A complete deletion produced benomyl hypersensitivity, elevated chromosome loss, failure to sustain mitotic arrest, premature sister-chromatid separation, DNA rereplication in a cut7-24 spindle-defective background and lethal “cut” phenotypes when cytokinesis occurred without proper chromosome segregation. (millband2002fissionyeastmad3p pages 6-8, millband2002fissionyeastmad3p pages 4-6, millband2002fissionyeastmad3p pages 3-4)
The quantitative effects are substantial:
These phenotypes define Mad3’s biological role narrowly and precisely: it is not a constitutive spindle structural component but a surveillance and inhibitory adaptor required to preserve chromosome-segregation fidelity when attachment is incomplete.
The literature search found no major 2023 study that redefined the primary molecular function of this exact S. pombe protein. The most relevant 2024 advance connects the canonical Mad3 checkpoint machinery to environmental-stress regulation of mitotic exit.
Iglesias-Romero and colleagues reported in March 2024 that the Pmk1 MAPK pathway helps sustain SAC signaling and promotes rapid degradation of mitotic Slp1/Cdc20 under stress through a mechanism requiring MAPK activity, the proteasome and Mad3. pmk1Δ cells showed as much as a twofold elevation of Slp1/Cdc20 during unperturbed growth, were hypersensitive to microtubule damage and were defective in maintaining metaphase arrest. Additivity between pmk1Δ and loss of Mad3 or Mad2 suggests overlapping but not simply linear contributions. The extracted source did not provide a Mad3-specific degradation percentage or complete kinetic series, so Mad3’s exact quantitative contribution remains unresolved. Published 18 March 2024: https://doi.org/10.1186/s12915-024-01865-6. (iglesiasromero2024mapkdependentcontrolof pages 1-2)
A separate September 2024 study independently showed that Pmk1/Sty1 signaling and phosphorylation-dependent attenuation of Slp1 restrain APC/C during osmotic or cell-wall stress. Experiments used 0.6 M KCl or 2 μg/mL caspofungin and monitored recovery for up to 50 minutes after release from a six-hour nda3-KM311 arrest. Fewer than 60% of pmk1Δ or sty1-T97A cells retained Cdc13-GFP-positive spindle-pole bodies, versus approximately 90% of wild type and spk1Δ. However, that study did not test a mad3 deletion in the relevant experiments; Mad3-GFP was used in MCC/APC/C association assays. It therefore strengthens the MAPK–Slp1 pathway but does not independently prove Mad3 dependence. Published September 2024: https://doi.org/10.7554/eLife.97896.2. (sun2024negativeregulationof pages 3-5, sun2024negativeregulationof pages 15-16)
Thus, the current view is that Mad3 retains its canonical MCC role while also contributing to integration of spindle status with environmental stress. The precise molecular connection between Mad3 and stress-induced Slp1 turnover remains less well resolved than its canonical checkpoint mechanism.
The following table organizes the principal claims, assays, numerical results and evidentiary caveats.
| Annotation topic | Best-supported conclusion | Evidence/assay | Key quantitative result | Primary source | Confidence / caveat |
|---|---|---|---|---|---|
| Identity and architecture | S. pombe mad3 is a 933-bp chromosome III gene encoding an ~36-kDa, kinase-less Mad3/BubR1-family spindle-checkpoint protein. Its N-terminal Bub1/Mad3 region has a TPR-like fold; conserved sequence features include KEN1, KEN2, ABBA motifs and a D-box-mimicking segment. This matches UniProt O59767 and the supplied SPCC895 locus designation. | Gene cloning and sequencing; comparative sequence/domain analysis; endogenous motif mapping. | 933-bp ORF; ~36-kDa product; 31% identity to budding-yeast Mad3 and 28% identity to human BubR1. | Millband & Hardwick (2002), DOI; Sewart & Hauf (2017), DOI (millband2002fissionyeastmad3p pages 4-6, sewart2017differentfunctionalityof pages 3-3) | High for identity and kinase-less family assignment. Exact modern InterPro/Pfam boundaries derive partly from database/comparative annotation rather than an atomic structure of full-length S. pombe Mad3. |
| Primary molecular function | Mad3 is not an enzyme. It is a non-catalytic mitotic checkpoint complex (MCC) component/adaptor and pseudosubstrate inhibitor that cooperates with Mad2 to restrain Slp1/Cdc20-activated APC/C, delaying anaphase until correct kinetochore–microtubule attachment. | Genetic epistasis, Mad2-overexpression arrest, co-immunoprecipitation, APC/C fractionation and motif mutagenesis. | Mad2 overexpression yielded short-spindle arrest in ~70% of wild-type and several upstream-mutant cells, but only 8% of mad3Δ cells. | Millband & Hardwick (2002), DOI; Sczaniecka et al. (2008), DOI (millband2002fissionyeastmad3p pages 6-8, sczaniecka2008thespindlecheckpoint pages 4-5) | High. “Pseudosubstrate” is a mechanistic interpretation supported by motif/function studies; Mad3 has no demonstrated catalytic activity. |
| Slp1/Cdc20 and APC/C association | Mad3 binds Mad2 and Slp1/Cdc20 in mitotic extracts and participates in an MCC–APC/C assembly. Stable Mad3/Mad2 association with APC/C requires functional Slp1 and Mad3 KEN1. | Endogenous tagged-protein co-IP; Mad2 depletion; Lid1-TAP APC/C pull-down; 19S sucrose-gradient co-fractionation; conditional slp1-362. | Up to 8% of APC/C was co-depleted with Mad2; at least 5% of core APC/C was estimated to be Mad2-associated. | Sczaniecka et al. (2008), DOI; Millband & Hardwick (2002), DOI (millband2002fissionyeastmad3p pages 1-2, sczaniecka2008thespindlecheckpoint pages 4-5) | High for association and functional dependency. Co-IP establishes complex membership, not necessarily every pairwise contact or binding affinity. |
| Bub1-TPR interaction | Bub1’s N-terminal TPR domain is necessary and sufficient to recruit Mad3 and forms a stable direct complex with the Mad3 TPR region. This supports a scaffold model in which Bub1 concentrates Mad3 near Mad1–Mad2 for efficient MCC production. | Ectopic tethering and fluorescence colocalization; domain deletion; purified-protein size-exclusion chromatography. | Bub1-TPR and Mad3-TPR eluted separately at 15.2 and 14.3 mL, but together as a larger complex at 12.1 mL. | Leontiou et al. (2019), DOI (leontiou2019thebub1tprdomain pages 1-3, leontiou2019thebub1tprdomain pages 7-8) | High for direct binding and recruitment. Promotion of Mad3 phosphorylation or MCC incorporation by this proximity remains a proposed mechanism rather than directly demonstrated. |
| Kinetochore localization | Functional Mad3-GFP forms punctate foci at unattached kinetochores during early mitosis, colocalizes with Cnp1/CENP-A, and disappears during anaphase. Robust recruitment requires Bub1, Bub3 and Mph1, but not Mad1 or Mad2. | Endogenous functional Mad3-GFP; live/fixed-cell fluorescence; Cnp1 colocalization; deletion backgrounds; hydroxyurea-release experiments. | At 165 min after HU release, bright Mad3-GFP foci occurred in ~50% of wild-type versus ~20% of mad1Δ or mad2Δ cells; foci were absent/diffuse in bub1Δ, bub3Δ and mph1Δ. | Millband & Hardwick (2002), DOI (millband2002fissionyeastmad3p pages 10-12) | High. Reduced signal in mad1Δ/mad2Δ likely reflects altered mitotic kinetics; these proteins were not required for the core recruitment mechanism. |
| Deletion phenotypes | mad3 is nonessential during unperturbed growth but is required for checkpoint arrest, sister-chromatid cohesion maintenance and survival when spindle assembly is compromised. Deletion causes microtubule-poison sensitivity, chromosome loss, premature chromatid separation, rereplication and “cut” phenotypes. | Full-ORF replacement; benomyl/CBZ treatment; nda3-KM311 and cut7-24 backgrounds; LacO/LacI-GFP chromatid assay; viability and chromosome-loss assays. | mad3Δ nda3-KM311 viability fell to ~45% after 6 h at 16°C versus >95% for either single mutant; mad3Δ chromatids separated ~45 min after G2 release; no colonies formed at 7.5 μg/mL benomyl. | Millband & Hardwick (2002), DOI (millband2002fissionyeastmad3p pages 6-8, millband2002fissionyeastmad3p pages 4-6, millband2002fissionyeastmad3p pages 3-4) | High. These are stress/checkpoint phenotypes rather than evidence that Mad3 is essential for ordinary vegetative proliferation. |
| KEN1 motif | The N-terminal KEN1/KEN20 motif is essential for core MCC formation and stable Mad3/Mad2 association with Slp1–APC/C. | Endogenous KEN-to-AAA mutagenesis; Mad2 IP; Lid1-TAP APC/C pull-down; checkpoint assays. | KEN20AAA eliminated detectable APC/C association of both Mad3 and Mad2. | Sczaniecka et al. (2008), DOI (sczaniecka2008thespindlecheckpoint pages 4-5, sczaniecka2008thespindlecheckpoint pages 1-1) | High. Strong direct S. pombe genetic and biochemical evidence. |
| KEN2, ABBA motifs and D-box mimic | The C-terminal ABBA–KEN2–ABBA region engages an additional Slp1/Cdc20 molecule and enables full checkpoint inhibition beyond core MCC assembly. KEN2 and ABBA1 are especially important; ABBA2 is weaker, while the D-box mimic makes a partial contribution. | Endogenous motif mutations and C-terminal truncation; nda3-KM311 arrest; Plo1-mCherry mitotic timing; Mad3-GFP/Slp1 IP. | Deletion of residues 282–310 largely abolished checkpoint activity; ABBA1 mutation caused a strong defect, ABBA2 a weaker defect and D-box-mimic mutation a partial defect. | Sewart & Hauf (2017), DOI (sewart2017differentfunctionalityof pages 3-3, sewart2017differentfunctionalityof pages 1-3) | Moderate–high. Functional separation is direct, but the detailed two-Cdc20/pseudosubstrate model integrates S. pombe experiments with structural knowledge from other systems. |
| 2024 MAPK/stress integration | One 2024 study directly reports that mitotic stress-induced Slp1/Cdc20 degradation requires Mad3, MAPK activity and the proteasome, extending Mad3’s role into environmental-stress control of mitotic exit. Pmk1 loss is additive with mad3Δ, suggesting partially distinct contributions to SAC maintenance. | Stress treatments, genetics/epistasis, Slp1 abundance and degradation assays, mitotic-arrest measurements. | pmk1Δ cells showed up to a twofold increase in Slp1/Cdc20 during unperturbed growth; the available excerpt gives no Mad3-specific degradation percentage or time course. | Iglesias-Romero et al. (2024; published March 2024), DOI (iglesiasromero2024mapkdependentcontrolof pages 1-2) | Moderate–high for the reported Mad3 requirement, but exact mad3Δ kinetics were unavailable in the extracted text; additivity cautions against placing Pmk1 and Mad3 in one simple linear pathway. |
| Independent 2024 MAPK study | A separate 2024 study shows that Pmk1/Sty1 signaling and Slp1 phosphorylation restrain APC/C and sustain SAC signaling under KCl or caspofungin stress, but it does not test mad3 deletion; Mad3-GFP is used in APC/C–MCC association assays only. It therefore cannot independently establish Mad3 dependence. | nda3-KM311 arrest/release; 0.6 M KCl or 2 μg/mL caspofungin for 1 h; MAPK and Slp1-site mutants; Lid1-TAP/Mad2-GFP/Mad3-GFP co-IP. | After a 6-h arrest and release, <60% of pmk1Δ or sty1-T97A cells retained Cdc13-GFP-positive spindle-pole bodies versus ~90% of wild type and spk1Δ. | Sun et al. (2024; published September 2024), DOI (sun2024negativeregulationof pages 3-5, sun2024negativeregulationof pages 15-16) | High for MAPK–Slp1 regulation; no direct Mad3-dependency evidence. Any Mad3-specific interpretation from this paper alone would be inference from established MCC biology. |
Table: Direct evidence supporting the functional annotation of Schizosaccharomyces pombe Mad3 (UniProt O59767), with quantitative results and explicit evidentiary caveats. The table separates established Mad3-specific findings from broader or inferred checkpoint mechanisms.
Recommended primary annotation: Mad3 is a non-enzymatic, kinase-less spindle assembly checkpoint adaptor and MCC component. At unattached kinetochores, Mph1- and Bub1/Bub3-dependent recruitment positions Mad3 near Mad1–Mad2. Mad3 then binds Mad2 and Slp1/Cdc20, using KEN, ABBA and D-box-like motifs to assemble inhibitory MCC species and block APC/C–Slp1 recognition or processing of anaphase-promoting substrates. The resulting delay in anaphase maintains sister-chromatid cohesion and protects chromosome-segregation fidelity.
Localization annotation: Mitotic nucleus; transiently enriched at unattached kinetochores during prometaphase/metaphase; subsequently present in soluble MCC and APC/C-associated checkpoint complexes; kinetochore signal disappears during anaphase.
Pathway annotation: Spindle assembly checkpoint/mitotic checkpoint → MCC formation → negative regulation of APC/C–Slp1/Cdc20 → control of metaphase-to-anaphase transition and chromosome segregation. A newer, incompletely resolved branch links Mad3-dependent Slp1 regulation to Pmk1-mediated environmental-stress responses.
Evidence confidence: High for protein identity, non-catalytic checkpoint function, Mad2/Slp1/APC/C association, Bub1-TPR binding, kinetochore localization and spindle-stress phenotypes. Moderate-to-high for the detailed second-Cdc20 pseudosubstrate model and Mad3’s 2024 stress-regulatory extension, because parts of those interpretations rely on integrated structural models or incompletely quantified Mad3-specific experiments.
References
(millband2002fissionyeastmad3p pages 4-6): David N. Millband and Kevin G. Hardwick. Fission yeast mad3p is required for mad2p to inhibit the anaphase-promoting complex and localizes to kinetochores in a bub1p-, bub3p-, and mph1p-dependent manner. Molecular and Cellular Biology, 22:2728-2742, Apr 2002. URL: https://doi.org/10.1128/mcb.22.8.2728-2742.2002, doi:10.1128/mcb.22.8.2728-2742.2002. This article has 187 citations and is from a domain leading peer-reviewed journal.
(millband2002fissionyeastmad3p pages 10-12): David N. Millband and Kevin G. Hardwick. Fission yeast mad3p is required for mad2p to inhibit the anaphase-promoting complex and localizes to kinetochores in a bub1p-, bub3p-, and mph1p-dependent manner. Molecular and Cellular Biology, 22:2728-2742, Apr 2002. URL: https://doi.org/10.1128/mcb.22.8.2728-2742.2002, doi:10.1128/mcb.22.8.2728-2742.2002. This article has 187 citations and is from a domain leading peer-reviewed journal.
(sczaniecka2008thespindlecheckpoint pages 4-5): Matylda Sczaniecka, Anna Feoktistova, Karen M. May, Jun-Song Chen, Julie Blyth, Kathleen L. Gould, and Kevin G. Hardwick. The spindle checkpoint functions of mad3 and mad2 depend on a mad3 ken box-mediated interaction with cdc20-anaphase-promoting complex (apc/c). The Journal of Biological Chemistry, 283:23039-23047, Aug 2008. URL: https://doi.org/10.1074/jbc.m803594200, doi:10.1074/jbc.m803594200. This article has 126 citations.
(millband2002fissionyeastmad3p pages 3-4): David N. Millband and Kevin G. Hardwick. Fission yeast mad3p is required for mad2p to inhibit the anaphase-promoting complex and localizes to kinetochores in a bub1p-, bub3p-, and mph1p-dependent manner. Molecular and Cellular Biology, 22:2728-2742, Apr 2002. URL: https://doi.org/10.1128/mcb.22.8.2728-2742.2002, doi:10.1128/mcb.22.8.2728-2742.2002. This article has 187 citations and is from a domain leading peer-reviewed journal.
(sewart2017differentfunctionalityof pages 3-3): Katharina Sewart and Silke Hauf. Different functionality of cdc20 binding sites within the mitotic checkpoint complex. Current Biology, 27:1213-1220, Apr 2017. URL: https://doi.org/10.1016/j.cub.2017.03.007, doi:10.1016/j.cub.2017.03.007. This article has 31 citations and is from a highest quality peer-reviewed journal.
(millband2002fissionyeastmad3p pages 6-8): David N. Millband and Kevin G. Hardwick. Fission yeast mad3p is required for mad2p to inhibit the anaphase-promoting complex and localizes to kinetochores in a bub1p-, bub3p-, and mph1p-dependent manner. Molecular and Cellular Biology, 22:2728-2742, Apr 2002. URL: https://doi.org/10.1128/mcb.22.8.2728-2742.2002, doi:10.1128/mcb.22.8.2728-2742.2002. This article has 187 citations and is from a domain leading peer-reviewed journal.
(millband2002fissionyeastmad3p pages 1-2): David N. Millband and Kevin G. Hardwick. Fission yeast mad3p is required for mad2p to inhibit the anaphase-promoting complex and localizes to kinetochores in a bub1p-, bub3p-, and mph1p-dependent manner. Molecular and Cellular Biology, 22:2728-2742, Apr 2002. URL: https://doi.org/10.1128/mcb.22.8.2728-2742.2002, doi:10.1128/mcb.22.8.2728-2742.2002. This article has 187 citations and is from a domain leading peer-reviewed journal.
(sczaniecka2008thespindlecheckpoint pages 1-1): Matylda Sczaniecka, Anna Feoktistova, Karen M. May, Jun-Song Chen, Julie Blyth, Kathleen L. Gould, and Kevin G. Hardwick. The spindle checkpoint functions of mad3 and mad2 depend on a mad3 ken box-mediated interaction with cdc20-anaphase-promoting complex (apc/c). The Journal of Biological Chemistry, 283:23039-23047, Aug 2008. URL: https://doi.org/10.1074/jbc.m803594200, doi:10.1074/jbc.m803594200. This article has 126 citations.
(sewart2017differentfunctionalityof pages 1-3): Katharina Sewart and Silke Hauf. Different functionality of cdc20 binding sites within the mitotic checkpoint complex. Current Biology, 27:1213-1220, Apr 2017. URL: https://doi.org/10.1016/j.cub.2017.03.007, doi:10.1016/j.cub.2017.03.007. This article has 31 citations and is from a highest quality peer-reviewed journal.
(sewart2017elucidatingthemolecular pages 105-110): Katharina Sewart. Elucidating the molecular basis of spindle assembly checkpoint signaling. ArXiv, Jan 2017. URL: https://doi.org/10.15496/publikation-16331, doi:10.15496/publikation-16331. This article has 0 citations.
(leontiou2019thebub1tprdomain pages 1-3): Ioanna Leontiou, Nitobe London, Karen M. May, Yingrui Ma, Lucile Grzesiak, Bethan Medina-Pritchard, Priya Amin, A. Arockia Jeyaprakash, Sue Biggins, and Kevin G. Hardwick. The bub1-tpr domain interacts directly with mad3 to generate robust spindle checkpoint arrest. Current Biology, 29:2407-2414.e7, Jul 2019. URL: https://doi.org/10.1016/j.cub.2019.06.011, doi:10.1016/j.cub.2019.06.011. This article has 39 citations and is from a highest quality peer-reviewed journal.
(leontiou2019thebub1tprdomain pages 7-8): Ioanna Leontiou, Nitobe London, Karen M. May, Yingrui Ma, Lucile Grzesiak, Bethan Medina-Pritchard, Priya Amin, A. Arockia Jeyaprakash, Sue Biggins, and Kevin G. Hardwick. The bub1-tpr domain interacts directly with mad3 to generate robust spindle checkpoint arrest. Current Biology, 29:2407-2414.e7, Jul 2019. URL: https://doi.org/10.1016/j.cub.2019.06.011, doi:10.1016/j.cub.2019.06.011. This article has 39 citations and is from a highest quality peer-reviewed journal.
(iglesiasromero2024mapkdependentcontrolof pages 1-2): Ana Belén Iglesias-Romero, Terersa Soto, Ignacio Flor-Parra, Silvia Salas-Pino, Gabriel Ruiz-Romero, Kathleen L. Gould, José Cansado, and Rafael R. Daga. Mapk-dependent control of mitotic progression in s. pombe. BMC Biology, Mar 2024. URL: https://doi.org/10.1186/s12915-024-01865-6, doi:10.1186/s12915-024-01865-6. This article has 3 citations and is from a domain leading peer-reviewed journal.
(sun2024negativeregulationof pages 3-5): 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 15-16): 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.