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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 correctly identified as Pop2/Sud1 of Schizosaccharomyces pombe, encoded by pop2/sud1 (SPAC4D7.03). It is a Cdc4-like F-box/WD-repeat protein and substrate-recruiting component of SCF ubiquitin ligases, not an enzyme with an independently demonstrated catalytic reaction. Its best-supported primary function is to help recognize cell-cycle proteins—especially phosphorylated Cdc18 and Rum1—and present them to an SCF ubiquitin-ligase machinery for polyubiquitylation and subsequent 26S-proteasome degradation. This restrains replication licensing and CDK inhibition, thereby preventing DNA re-replication and inappropriate increases in ploidy. Later work implicates the same machinery in regulation of the translesion polymerase Rev1, while Cig2 is a reported SCF^Pop1/Pop2 target for which the Pop2-specific evidence recovered here is less complete. Pop2 is detected in both the nucleus and cytoplasm, although its established Cdc18/Rum1 cell-cycle function is principally nuclear. (seibert2002combinatorialdiversityof pages 5-7, seibert2002combinatorialdiversityof pages 2-4, uchiyama2015theproteinlevel pages 8-10, wolf1999fboxwdrepeatproteinspop1p pages 1-2)
The primary literature uses Pop2p, Sud1p, and Sud1p/Pop2p for the same fission-yeast F-box/WD-repeat protein. Pop2 was identified in the S. pombe genomic region represented by cosmid c4D7 through similarity to the Cdc4 class of F-box/WD-repeat proteins; target-specific knockout, immunoblotting, co-immunoprecipitation, and complementation experiments were subsequently performed in S. pombe. These properties agree with the supplied UniProt identity—O14170, SPAC4D7.03, organism strain 972/ATCC 24843—and with the listed F-box and WD40-domain annotations. (wolf1999fboxwdrepeatproteinspop1p pages 3-4, wolf1999fboxwdrepeatproteinspop1p pages 4-5)
The name POP2 is ambiguous across fungi. Much recent literature uses Pop2/Caf1 for the CCR4–NOT mRNA deadenylase, including work in budding yeast and metazoan CNOT7/CNOT8 systems. That nuclease is biologically and structurally different from O14170. Searches for 2023–2024 publications returned many such deadenylase papers, but these were excluded rather than transferred to the fission-yeast Pop2/Sud1 annotation. The defining identity checks for O14170 are: S. pombe organism, Sud1 alias, SPAC4D7.03 locus, F-box/WD-repeat architecture, and SCF-dependent protein proteolysis—not CCR4–NOT-mediated RNA deadenylation. (seibert2002combinatorialdiversityof pages 2-4, uchiyama2015theproteinlevel pages 8-10, seibert2002combinatorialdiversityof pages 11-13)
Pop2/Sud1 is an F-box/WD-repeat adaptor protein. In the canonical SCF arrangement, the cullin–RING core supplies the ubiquitin-ligase scaffold and catalytic geometry, while an F-box protein connects to the Skp1 module and contributes substrate recognition, commonly through additional WD repeats. Therefore, Pop2 should not be annotated as a protease or ubiquitin-transfer enzyme; its primary molecular role is protein binding and substrate recruitment within an E3 ubiquitin-ligase complex. (seibert2002combinatorialdiversityof pages 1-2, kipreos2000thefboxprotein pages 4-5)
Domain-swap experiments provide target-specific structure–function evidence. An amino-terminal Pop2 region mediates functional association with Pop1, while the carboxy-terminal region contains WD repeats implicated in substrate-facing interactions. A chimera comprising the first 241 residues of Pop2 fused to full-length Pop1 rescued both defective proteolysis and polyploidy in pop1Δ pop2Δ cells. This indicates that juxtaposition of the Pop1 and Pop2 amino termini is functionally important, although it does not establish an atomic structure or exact substrate-contact surface. (wolf1999fboxwdrepeatproteinspop1p pages 3-4)
The InterPro assignments supplied by the user—F-box domain/superfamily and WD40-repeat/PAC1-related annotations—are consequently well aligned with experimental literature. The precise biochemical division of labor is nevertheless unusual: in the Pop1–Pop2 heteromer, the Pop1 F-box is essential, whereas deletion of the Pop2 F-box can retain Rum1 degradation and ploidy control. Pop2 may therefore enter that heteromer primarily through Pop1, while its own F-box supports separate Pop2-containing assemblies. (seibert2002combinatorialdiversityof pages 11-13)
Endogenous co-immunoprecipitation identified a complex containing Pop1, Pop2, Pcu1/Cullin-1, Psh1/Skp1, and Pip1/Rbx1-like RING subunit. Gel filtration placed the assembly at approximately 500 kDa. The proteins form both a heterooligomeric SCF^Pop1–Pop2 complex and separately recoverable Pop1- or Pop2-containing SCF assemblies with ubiquitin-ligase activity. Pop1–Pop2 association remains relatively constant through the cell cycle, suggesting that periodic substrate destruction is controlled chiefly by substrate state—such as phosphorylation—rather than assembly and disassembly of the receptor complex. (seibert2002combinatorialdiversityof pages 2-4, seibert2002combinatorialdiversityof pages 11-13, seibert2002combinatorialdiversityof pages 1-2)
In reconstituted assays, phosphorylated Rum1 bound the Pop1–Pop2 complex and was polyubiquitylated in the presence of E1, UBC3 E2, ATP, and ubiquitin. Pip1 complexes isolated from pop2Δ cells failed to support Rum1 polyubiquitylation. These results support the following mechanism:
Thus there is no meaningful small-molecule “substrate specificity” or catalytic reaction to report for Pop2 itself. Its specificity is for protein degrons and associated protein complexes, particularly cell-cycle-regulated, phosphorylated substrates.
Cdc18, the fission-yeast Cdc6-family replication-initiation factor, is the strongest direct Pop2 target. Disruption of pop2 caused marked accumulation and slowed turnover of GFP-tagged and endogenous Cdc18 in cycloheximide-chase experiments. Cdc18 co-immunoprecipitated with Pop2 in wild-type cells, but this association was lost in pop1Δ cells, showing that Pop1 facilitates or is required for substrate engagement by Pop2 in the heteromeric receptor. (wolf1999fboxwdrepeatproteinspop1p pages 3-4, wolf1999fboxwdrepeatproteinspop1p pages 5-5, wolf1999fboxwdrepeatproteinspop1p pages 1-2)
Functionally, removing excess Cdc18 after origin licensing is essential because persistent licensing activity can permit repeated genome duplication without intervening mitosis. Pop2-dependent Cdc18 degradation therefore constitutes an anti-rereplication mechanism and explains much of the ploidy phenotype of pop2Δ cells. (wolf1999fboxwdrepeatproteinspop1p pages 4-5, wolf1999fboxwdrepeatproteinspop1p pages 1-2)
Rum1 is a cyclin-dependent-kinase inhibitor whose degradation promotes cell-cycle progression. Phosphorylated Rum1 bound purified Pop1–Pop2 complexes and was polyubiquitylated in vitro. The retrieved evidence identifies Ser58 and Thr62 as relevant CDK-phosphorylated residues. Loss of Pop2 compromises this pathway, although the phenotype is generally milder than loss of Pop1. (seibert2002combinatorialdiversityof pages 5-7, seibert2002combinatorialdiversityof pages 2-4, wolf1999fboxwdrepeatproteinspop1p pages 1-2)
Cdc18 and Rum1 connect the same molecular activity to two coordinated outcomes: elimination of a replication-licensing factor and removal of a CDK inhibitor. Their combined stabilization favors inappropriate S-phase entry or repetition and provides a mechanistic explanation for unwanted diploidization/polyploidization. (seibert2002combinatorialdiversityof pages 15-15, kipreos2000thefboxprotein pages 4-5)
A 2015 study extended the pathway to Rev1, a translesion-synthesis polymerase. Rev1 accumulated in proteasome-defective strains and in pop2Δ; Rev1 also co-immunoprecipitated with Pop2. A stabilized Rev1 variant lacking residues 761–818 failed to associate efficiently with Pop1, linking this region to SCF recognition. Pop1 loss produced the stronger effect, so Pop2 appears contributory rather than sufficient by itself. The pathway limits Rev1 around G1/S, plausibly reducing unnecessary access of a potentially mutagenic polymerase to undamaged DNA. (uchiyama2015theproteinlevel pages 8-10)
DNA damage also increases Rev1 abundance through a Rad3-dependent response described in that study, indicating that basal SCF/proteasome turnover and damage-induced regulation are integrated rather than constitutive. The exact Pop2-binding degron, requisite phosphorylation sites, and direct in-vitro ubiquitylation of Rev1 were not established in the retrieved evidence. (uchiyama2015theproteinlevel pages 8-10)
The S-phase cyclin Cig2 is reported to require SCF^Pop1/Pop2 for degradation, placing Pop2 in the network that sharpens the Cig2 pulse at the G1/S boundary. However, the full experimental text of the principal 2004 Cig2 paper was not retrieved, and one accessible earlier passage discussed a Pop1 effect on cig2 RNA abundance without resolving transcription versus RNA stability. Cig2 should therefore be retained as a supported literature target with moderate confidence for a Pop2-specific mechanistic annotation, below Cdc18, Rum1, and Rev1 in the evidence hierarchy. (seibert2002combinatorialdiversityof pages 11-13)
The most precise pathway annotation is SCF-dependent ubiquitin–proteasome regulation of the G1/S transition and replication licensing. Pop2 acts at the intersection of:
The broad phenotype—genome instability and altered ploidy—is consequently informative rather than merely pleiotropic: it follows directly from failure to eliminate proteins that license DNA replication or restrain CDKs.
Biochemical fractionation of endogenously Myc-tagged proteins, supported by GFP localization experiments, detected Pop2 in both nuclear and cytoplasmic fractions. Pop1 was predominantly or exclusively nuclear in the same study. The complete five-subunit Pop1–Pop2 SCF assembly can coexist in the nucleus, consistent with nuclear Cdc18 and Rum1 regulation. Pop2-only SCF assemblies may operate in the cytoplasm, but their physiological cytoplasmic substrates remain unidentified. (seibert2002combinatorialdiversityof pages 5-7, seibert2002combinatorialdiversityof pages 11-13, seibert2002combinatorialdiversityof pages 1-2)
Accordingly, the most defensible localization statement is: nuclear and cytoplasmic protein, with experimentally established cell-cycle substrate degradation centered on the nuclear compartment. It would be premature to assign Pop2 to a specific organelle or stable subnuclear body.
pop2Δ cells are viable but morphologically heterogeneous and prone to excess genome duplication. In one study, approximately 50% of cells accumulated DNA content above the normal 2C level after 16 hours in rich liquid medium. Red colonies on phloxin-B plates and flow-cytometric DNA-content measurements independently documented polyploid isolates. The phenotype was milder than pop1Δ, matching the biochemical finding that Pop1 supplies indispensable functions within the heteromer while Pop2 enhances substrate recognition and complex diversity. (wolf1999fboxwdrepeatproteinspop1p pages 4-5, wolf1999fboxwdrepeatproteinspop1p pages 1-2)
Cdc18 accumulated strongly in pop2Δ, while Rum1 accumulation and re-replication were less severe than in pop1Δ. This substrate-selective difference argues against Pop1 and Pop2 being simple redundant paralogues. Instead, they cooperate non-equivalently, and Pop2 may also form independent complexes with currently unknown substrates. (seibert2002combinatorialdiversityof pages 11-13, wolf1999fboxwdrepeatproteinspop1p pages 1-2)
The core evidence is summarized below.
| Claim/topic | Best experimental evidence | Conclusion | Confidence | Key source/date/DOI URL |
|---|---|---|---|---|
| Identity and architecture | Target-specific studies in Schizosaccharomyces pombe identify Sud1p/Pop2p as a Cdc4-like F-box/WD-repeat protein; domain-swap experiments distinguish an essential N-terminal oligomerization region from a replaceable C-terminal WD-repeat region. | O14170 Pop2/Sud1 is an F-box/WD-repeat SCF-associated protein, not a Pop2/Caf1 deadenylase. | High | Wolf et al., 29 Mar 1999, 10.1016/S0960-9822(99)80165-1 (wolf1999fboxwdrepeatproteinspop1p pages 3-4, wolf1999fboxwdrepeatproteinspop1p pages 4-5) |
| SCF composition and oligomerization | Endogenous co-immunoprecipitation and gel filtration detected Pop1, Pop2, Pcu1, Psh1 and Pip1 together in an approximately 500-kDa complex; separately active Pop1- and Pop2-containing assemblies were also recovered. | Pop2 participates in heterooligomeric SCF^Pop1–Pop2 and Pop2-containing homo-assemblies. | High | Seibert et al., Aug 2002, 10.1186/1471-2091-3-22 (seibert2002combinatorialdiversityof pages 2-4, seibert2002combinatorialdiversityof pages 11-13, seibert2002combinatorialdiversityof pages 1-2) |
| Nonenzymatic substrate-adaptor role | Pop-containing complexes bound phosphorylated substrate and supported polyubiquitylation in reactions containing E1, UBC3, ATP and ubiquitin; complexes isolated from pop2Δ cells failed to ubiquitylate Rum1. |
Pop2 is best classified as a substrate-recognition/adaptor component of an SCF ubiquitin ligase, rather than as the catalytic ubiquitin-transfer enzyme. | High | Seibert et al., Aug 2002, 10.1186/1471-2091-3-22 (seibert2002combinatorialdiversityof pages 5-7, seibert2002combinatorialdiversityof pages 2-4) |
| Cdc18 substrate | pop2 disruption stabilized GFP-tagged and endogenous Cdc18 in cycloheximide-turnover experiments; Cdc18 co-immunoprecipitated with Pop2 in a Pop1-dependent manner. |
SCF complexes containing Pop2 promote proteolysis of the DNA-replication licensing factor Cdc18. | High | Wolf et al., 29 Mar 1999, 10.1016/S0960-9822(99)80165-1 (wolf1999fboxwdrepeatproteinspop1p pages 3-4, wolf1999fboxwdrepeatproteinspop1p pages 5-5, wolf1999fboxwdrepeatproteinspop1p pages 1-2) |
| Rum1 and phosphorylation | Phosphorylated Rum1 bound Pop1–Pop2 complexes and was polyubiquitylated in vitro; the relevant CDK-phosphorylated residues reported were Ser58 and Thr62. | Pop2-containing SCF recognizes phosphorylated Rum1 and promotes its polyubiquitylation and degradation. | High | Seibert et al., Aug 2002, 10.1186/1471-2091-3-22 (seibert2002combinatorialdiversityof pages 5-7, seibert2002combinatorialdiversityof pages 2-4) |
| Rev1 substrate | pop2Δ increased Rev1 abundance; Rev1 co-immunoprecipitated with Pop2, while proteasome-defective strains stabilized Rev1. Deleting Rev1 residues 761–818 impaired Pop1 interaction and stabilized Rev1 in S phase. |
Pop2 contributes to SCF-dependent control of Rev1 abundance around G1/S, helping restrict translesion-synthesis polymerase availability. | High | Uchiyama et al., 6 Jul 2015, 10.1371/journal.pone.0130000 (uchiyama2015theproteinlevel pages 8-10) |
| Cig2 substrate | Retrieved literature identifies SCF^Pop1/Pop2 as required for Cig2 degradation, but the directly retrieved full experimental passages were limited; one retrieved study discussed Pop1 effects on cig2 RNA without establishing a Pop2-specific mechanism. |
Cig2 is a reported Pop1/Pop2 SCF target, but Pop2-specific mechanistic support is weaker in the evidence retrieved here than for Cdc18, Rum1 or Rev1. | Moderate | Yamano et al., Apr 2004, 10.1074/jbc.M311060200; Seibert et al., Aug 2002, 10.1186/1471-2091-3-22 (seibert2002combinatorialdiversityof pages 11-13) |
| Cellular localization | Endogenously Myc-tagged and mildly overexpressed GFP-tagged proteins were examined by fractionation/localization assays: Pop2 occurred in nuclear and cytoplasmic fractions, whereas Pop1 was predominantly nuclear. | Pop2 can function in both nucleus and cytoplasm; the established Pop1–Pop2 substrate pathway is strongly associated with the nucleus. | High | Seibert et al., Aug 2002, 10.1186/1471-2091-3-22 (seibert2002combinatorialdiversityof pages 5-7, seibert2002combinatorialdiversityof pages 11-13) |
| Deletion and ploidy phenotype | After 16 h in rich liquid medium, approximately 50% of pop2Δ cells accumulated DNA content above the normal 2C level; phloxin-B colony scoring and flow cytometry documented polyploid isolates. |
Loss of Pop2 permits inappropriate DNA re-replication/diploidization, consistent with failure to eliminate replication and cell-cycle regulators. | High | Wolf et al., 29 Mar 1999, 10.1016/S0960-9822(99)80165-1 (wolf1999fboxwdrepeatproteinspop1p pages 4-5, wolf1999fboxwdrepeatproteinspop1p pages 1-2) |
| 2023–2024 evidence gap and symbol ambiguity | Targeted searches retrieved no 2023–2024 study directly examining S. pombe O14170 Pop2/Sud1. Recent “POP2” literature largely concerned the unrelated Caf1/CNOT7-type CCR4–NOT deadenylase or proteins in other organisms. | Current annotation remains based mainly on 1998–2004 studies plus the 2015 Rev1 work; Caf1/POP2 deadenylase findings must not be transferred to O14170. | High | Evidence search through 2024; latest retrieved target-specific study: Uchiyama et al., 6 Jul 2015, 10.1371/journal.pone.0130000 (uchiyama2015theproteinlevel pages 8-10, seibert2002combinatorialdiversityof pages 11-13, wolf1999fboxwdrepeatproteinspop1p pages 4-5) |
Table: Evidence-graded functional annotation of fission-yeast Pop2/Sud1 (O14170), separating direct biochemical and genetic findings from lower-confidence claims and same-symbol Caf1/POP2 literature.
A focused search for 2023–2024 studies using pop2, sud1, SPAC4D7.03, O14170, and S. pombe did not identify a recent paper directly investigating this protein. The latest target-specific experimental study recovered was the Rev1 paper published 6 July 2015. Most mechanistic foundations date from 1998–2004. This is itself an important annotation result: apparent newer “POP2” advances predominantly concern the unrelated Caf1/CNOT7 deadenylase and cannot update O14170’s function. (uchiyama2015theproteinlevel pages 8-10, seibert2002combinatorialdiversityof pages 11-13, wolf1999fboxwdrepeatproteinspop1p pages 4-5)
Consequently, there are no defensible 2023–2024 target-specific structural, interactomic, inhibitor, or in-vivo application claims to report. Current understanding remains robust for the core SCF/cell-cycle role but incomplete for Pop2-only substrates, degron recognition, structural organization, and regulation of nuclear–cytoplasmic partitioning.
No clinical, agricultural, or industrial implementation specific to O14170 was found. Its applications are presently basic and translationally informative model-system uses:
pop2Δ provides a genetically tractable system for studying how failed proteolysis produces re-replication and polyploidization.These applications illuminate general eukaryotic principles, but direct extrapolation to human F-box proteins or therapeutic targets requires orthology and mechanism-specific validation.
High-confidence annotation: Pop2/Sud1 is a nonenzymatic F-box/WD-repeat substrate adaptor in S. pombe SCF ubiquitin ligases. It cooperates with Pop1 and the Pcu1–Psh1–Pip1 core to polyubiquitylate cell-cycle substrates, particularly Cdc18 and phosphorylated Rum1, causing proteasomal degradation and preventing re-replication. It is present in nucleus and cytoplasm. (seibert2002combinatorialdiversityof pages 5-7, seibert2002combinatorialdiversityof pages 2-4, seibert2002combinatorialdiversityof pages 11-13, wolf1999fboxwdrepeatproteinspop1p pages 1-2)
Moderate-confidence extensions: Pop2 contributes to Rev1 turnover around G1/S, supported by deletion and interaction data, but direct reconstituted Rev1 ubiquitylation remains to be shown. Cig2 is a published Pop1/Pop2 SCF target, but Pop2-specific molecular evidence was incompletely accessible in this search. (uchiyama2015theproteinlevel pages 8-10, seibert2002combinatorialdiversityof pages 11-13)
Key unresolved questions:
References
(seibert2002combinatorialdiversityof pages 5-7): Volker Seibert, Corinna Prohl, Ida Schoultz, Edward Rhee, Rebecca Lopez, Kareem Abderazzaq, Chunshui Zhou, and Dieter A Wolf. Combinatorial diversity of fission yeast scf ubiquitin ligases by homo- and heterooligomeric assemblies of the f-box proteins pop1p and pop2p. BMC Biochemistry, 3:22-22, Aug 2002. URL: https://doi.org/10.1186/1471-2091-3-22, doi:10.1186/1471-2091-3-22. This article has 46 citations and is from a peer-reviewed journal.
(seibert2002combinatorialdiversityof pages 2-4): Volker Seibert, Corinna Prohl, Ida Schoultz, Edward Rhee, Rebecca Lopez, Kareem Abderazzaq, Chunshui Zhou, and Dieter A Wolf. Combinatorial diversity of fission yeast scf ubiquitin ligases by homo- and heterooligomeric assemblies of the f-box proteins pop1p and pop2p. BMC Biochemistry, 3:22-22, Aug 2002. URL: https://doi.org/10.1186/1471-2091-3-22, doi:10.1186/1471-2091-3-22. This article has 46 citations and is from a peer-reviewed journal.
(uchiyama2015theproteinlevel pages 8-10): Masashi Uchiyama, Junko Terunuma, and Fumio Hanaoka. The protein level of rev1, a tls polymerase in fission yeast, is strictly regulated during the cell cycle and after dna damage. PLoS ONE, 10:e0130000, Jul 2015. URL: https://doi.org/10.1371/journal.pone.0130000, doi:10.1371/journal.pone.0130000. This article has 20 citations and is from a peer-reviewed journal.
(wolf1999fboxwdrepeatproteinspop1p pages 1-2): Dieter A. Wolf, Frank McKeon, and Peter K. Jackson. F-box/wd-repeat proteins pop1p and sud1p/pop2p form complexes that bind and direct the proteolysis of cdc18p. Current Biology, 9:373-377, Apr 1999. URL: https://doi.org/10.1016/s0960-9822(99)80165-1, doi:10.1016/s0960-9822(99)80165-1. This article has 85 citations and is from a highest quality peer-reviewed journal.
(wolf1999fboxwdrepeatproteinspop1p pages 3-4): Dieter A. Wolf, Frank McKeon, and Peter K. Jackson. F-box/wd-repeat proteins pop1p and sud1p/pop2p form complexes that bind and direct the proteolysis of cdc18p. Current Biology, 9:373-377, Apr 1999. URL: https://doi.org/10.1016/s0960-9822(99)80165-1, doi:10.1016/s0960-9822(99)80165-1. This article has 85 citations and is from a highest quality peer-reviewed journal.
(wolf1999fboxwdrepeatproteinspop1p pages 4-5): Dieter A. Wolf, Frank McKeon, and Peter K. Jackson. F-box/wd-repeat proteins pop1p and sud1p/pop2p form complexes that bind and direct the proteolysis of cdc18p. Current Biology, 9:373-377, Apr 1999. URL: https://doi.org/10.1016/s0960-9822(99)80165-1, doi:10.1016/s0960-9822(99)80165-1. This article has 85 citations and is from a highest quality peer-reviewed journal.
(seibert2002combinatorialdiversityof pages 11-13): Volker Seibert, Corinna Prohl, Ida Schoultz, Edward Rhee, Rebecca Lopez, Kareem Abderazzaq, Chunshui Zhou, and Dieter A Wolf. Combinatorial diversity of fission yeast scf ubiquitin ligases by homo- and heterooligomeric assemblies of the f-box proteins pop1p and pop2p. BMC Biochemistry, 3:22-22, Aug 2002. URL: https://doi.org/10.1186/1471-2091-3-22, doi:10.1186/1471-2091-3-22. This article has 46 citations and is from a peer-reviewed journal.
(seibert2002combinatorialdiversityof pages 1-2): Volker Seibert, Corinna Prohl, Ida Schoultz, Edward Rhee, Rebecca Lopez, Kareem Abderazzaq, Chunshui Zhou, and Dieter A Wolf. Combinatorial diversity of fission yeast scf ubiquitin ligases by homo- and heterooligomeric assemblies of the f-box proteins pop1p and pop2p. BMC Biochemistry, 3:22-22, Aug 2002. URL: https://doi.org/10.1186/1471-2091-3-22, doi:10.1186/1471-2091-3-22. This article has 46 citations and is from a peer-reviewed journal.
(kipreos2000thefboxprotein pages 4-5): Edward T Kipreos and Michele Pagano. The f-box protein family. Genome Biology, 1:reviews3002.1-reviews3002.7, Nov 2000. URL: https://doi.org/10.1186/gb-2000-1-5-reviews3002, doi:10.1186/gb-2000-1-5-reviews3002. This article has 1024 citations and is from a highest quality peer-reviewed journal.
(wolf1999fboxwdrepeatproteinspop1p pages 5-5): Dieter A. Wolf, Frank McKeon, and Peter K. Jackson. F-box/wd-repeat proteins pop1p and sud1p/pop2p form complexes that bind and direct the proteolysis of cdc18p. Current Biology, 9:373-377, Apr 1999. URL: https://doi.org/10.1016/s0960-9822(99)80165-1, doi:10.1016/s0960-9822(99)80165-1. This article has 85 citations and is from a highest quality peer-reviewed journal.
(seibert2002combinatorialdiversityof pages 15-15): Volker Seibert, Corinna Prohl, Ida Schoultz, Edward Rhee, Rebecca Lopez, Kareem Abderazzaq, Chunshui Zhou, and Dieter A Wolf. Combinatorial diversity of fission yeast scf ubiquitin ligases by homo- and heterooligomeric assemblies of the f-box proteins pop1p and pop2p. BMC Biochemistry, 3:22-22, Aug 2002. URL: https://doi.org/10.1186/1471-2091-3-22, doi:10.1186/1471-2091-3-22. This article has 46 citations and is from a peer-reviewed journal.