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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Identity is verified. The requested target is human CUL1/Cullin-1, UniProt Q13616, not a similarly named protein from another organism. Literature explicitly associates Q13616 with CUL1 and describes the same cullin-family architecture indicated by the supplied InterPro annotations: an elongated N-terminal region containing three cullin repeats and a globular C-terminal cullin-homology region. Papers concerning Leishmania, Plasmodium, plants, yeast, or other CUL1 homologs were not used as direct evidence for human Q13616. (petroski2005functionandregulation pages 1-2, petroski2005functionandregulation pages 12-14)
CUL1 is not a conventional enzyme, transporter, or substrate-binding receptor. Its primary function is to serve as the regulated molecular scaffold and catalytic organizer of SCF/CRL1 E3 ubiquitin ligases. CUL1 binds an SKP1–F-box substrate-receptor module at its N terminus and RBX1-associated ubiquitin-transfer machinery at its C terminus, positioning a receptor-bound substrate near an activated ubiquitin. The F-box protein—not CUL1 alone—provides most substrate specificity. (petroski2005functionandregulation pages 1-2, merlet2009regulationofcullinring pages 1-2, petroski2005functionandregulation pages 12-14)
| Aspect | Mechanistic conclusion | Strongest evidence/example | Interpretation/limitations |
|---|---|---|---|
| Verified identity and domains | The target is human CUL1 (Cullin-1; UniProt Q13616), a cullin-family protein with three N-terminal cullin repeats forming an elongated stalk and a C-terminal cullin-homology region that binds RBX1. This agrees with the supplied Cullin, Cullin-like_AB, Cullin_CS, and cullin-homology annotations. | Authoritative CRL literature explicitly associates CUL1 with Q13616 and describes the three-repeat N-terminal scaffold plus globular C-terminal domain. (petroski2005functionandregulation pages 1-2, petroski2005functionandregulation pages 12-14) | Identity, organism, family, and architecture are concordant. Studies of plant, parasite, or yeast CUL1 homologs are not direct evidence for Q13616. |
| Canonical SCF/CRL1 composition | CUL1 forms the central scaffold of SCF/CRL1 complexes: its N terminus binds SKP1, SKP1 recruits an interchangeable F-box protein, and its C terminus binds RBX1/ROC1, which recruits ubiquitin-charged catalytic machinery. | Structural and biochemical syntheses define the CUL1–SKP1–F-box–RBX1 organization and show that CUL1 positions substrate and E2 machinery across the complex. (petroski2005functionandregulation pages 1-2, merlet2009regulationofcullinring pages 1-2) | CUL1 is an architectural and catalytic-platform subunit, not the substrate receptor. “SCF” should identify the relevant F-box protein when substrate-level conclusions are made. |
| Ubiquitin-transfer mechanism and specificity | RBX1-bound ubiquitin-carrying enzymes transfer ubiquitin directly to substrate, without a CUL1–ubiquitin thioester intermediate. F-box receptors recognize degrons—frequently phosphorylation-dependent—and provide most substrate specificity. | The conserved cullin–RING core recruits E2 enzymes for direct transfer, whereas exchangeable F-box modules recruit distinct substrates. (petroski2005functionandregulation pages 9-10, petroski2005functionandregulation pages 12-14) | CUL1 has no intrinsic catalytic reaction or fixed substrate specificity comparable to an enzyme. Specificity also depends on degron state, localization, receptor abundance, and compatible ubiquitin-carrying enzymes. |
| NEDD8–CSN–CAND1 regulation | Covalent NEDD8 attachment activates CRL1 by promoting a productive catalytic architecture. The COP9 signalosome (CSN) removes NEDD8; CAND1 binds unneddylated CUL1 and promotes inhibition, disassembly, and exchange of SKP1–F-box modules. | Foundational and recent CRL models converge on cycles of neddylation, CSN-mediated deneddylation, and CAND1-dependent receptor exchange. (petroski2005functionandregulation pages 9-10, diaz2022rolesofcullinring pages 19-20, li2024cullinringligasesemploy pages 1-4) | Deneddylation is not simply permanent inactivation: together with CAND1, it remodels the cellular SCF repertoire. |
| Localization | CUL1 is not restricted to one organelle; localization is substantially determined by associated receptors and substrates. A clear human example is SCF–FBXL4 at the mitochondrial outer membrane in unstressed cells. | FBXL4 colocalized with outer-membrane marker TOM20 rather than inner-membrane TIM50; loss of CUL1 or FBXL4 stabilized mitochondrial NIX and BNIP3. (nguyen‐dien2023fbxl4suppressesmitophagy pages 1-2, nguyen‐dien2023fbxl4suppressesmitophagy pages 4-6) | Outer-mitochondrial localization is demonstrated for the FBXL4-containing SCF pool, not necessarily for all cellular CUL1. |
| Cell-cycle pathway: p27 | SCF–SKP2 promotes ubiquitylation-dependent turnover of the CDK inhibitor p27/KIP1, supporting cell-cycle progression; CUL1 neddylation is required for efficient ligase activity. | In breast-cancer models, NNMT-derived 1-MNA increased CUL1 neddylation and p27 degradation; blocking neddylation with MLN4924 caused p27 accumulation and inhibited NNMT-driven proliferation. (ma2024nnmt1‐mnapromotecell‐cycle pages 6-7, ma2024nnmt1‐mnapromotecell‐cycle pages 1-2) | This is strong mechanistic evidence in cancer cells and xenografts, but the upstream NNMT/1-MNA axis may be context dependent. |
| Mitophagy pathway: NIX and BNIP3 | SCF–FBXL4 constitutively ubiquitylates and destabilizes the mitochondrial mitophagy receptors NIX/BNIP3L and BNIP3, suppressing basal mitophagy. | CUL1 or FBXL4 depletion stabilized NIX and BNIP3; FBXL4 knockout increased their mitochondrial abundance, whereas wild-type rescue restored turnover. Pathogenic FBXL4 variants assembled inefficiently with SKP1/CUL1. (nguyen‐dien2023fbxl4suppressesmitophagy pages 9-10, nguyen‐dien2023fbxl4suppressesmitophagy pages 1-2, nguyen‐dien2023fbxl4suppressesmitophagy pages 4-6) | This links SCF dysfunction to FBXL4-associated mtDNA-depletion syndrome, but disease variants affect the receptor FBXL4 rather than CUL1. The precise substrate degrons remain unresolved. |
| Mitotic pathway: AKAP2 | PLK1-dependent phosphorylation connects SCF–βTrCP to degradation of AKAP2 at G2/M, coordinating actin organization and mitotic-spindle integrity. | Quantitative proteomics and validation showed PLK1/βTrCP-dependent AKAP2 degradation; a nondegradable AKAP2 mutant produced actin and spindle abnormalities. (mouery2024proteomicanalysisreveals pages 1-3) | This is a receptor-specific CUL1 pathway, not evidence that AKAP2 is recognized intrinsically by CUL1. |
| Recent quantitative landscape | Human CRLs comprise approximately 300 modular complexes, and the CUL1/SCF system uses roughly 70 F-box substrate receptors, creating extensive receptor-dependent diversity. | A 2024 mechanistic study estimated approximately 300 human CRLs; a 2024 SCF study cited about 70 F-box receptors. (mouery2024proteomicanalysisreveals pages 1-3, li2024cullinringligasesemploy pages 1-4) | These are approximate family-level counts, not numbers of simultaneously active complexes or validated CUL1 substrates in one cell type. |
| 2024 metabolite-to-CRL mechanism | 1-MNA binds the NEDD8 E2 enzyme UBC12/UBE2M, reduces its lysosomal targeting, increases UBC12 abundance and CUL1 neddylation, and enhances SCF–SKP2-dependent p27 turnover. | Surface-plasmon resonance measured a 1-MNA–UBC12 dissociation constant of 168.3 nM; CETSA, immunoprecipitation–mass spectrometry, microscopy, inhibitor studies, and cycloheximide chases supported the pathway. (ma2024nnmt1‐mnapromotecell‐cycle pages 6-7, ma2024nnmt1‐mnapromotecell‐cycle pages 10-11) | Although the reported affinity is high, 1-MNA was often applied at millimolar concentrations in cell assays; physiological exposure and generalizability require further validation. |
| Translational implications | CUL1 pathways can be manipulated by inhibiting neddylation, altering individual F-box receptors, or recruiting CRLs to neo-substrates through targeted-protein-degradation technologies. | MLN4924 suppressed CUL1-dependent substrate turnover in cell models; recent work also shows that productive CRL–catalytic-enzyme geometry can determine degrader efficacy. (ma2024nnmt1‐mnapromotecell‐cycle pages 6-7, nguyen‐dien2023fbxl4suppressesmitophagy pages 1-2, li2024cullinringligasesemploy pages 1-4) | Global CUL1 or neddylation inhibition affects many essential SCFs and may produce broad toxicity. Recent catalytic-partner findings centered on CUL2 and should not automatically be assigned to CUL1. |
| Overall functional annotation | Primary function: CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. | Structural, biochemical, cell-biological, and disease-focused studies consistently support this model. (petroski2005functionandregulation pages 1-2, petroski2005functionandregulation pages 12-14, nguyen‐dien2023fbxl4suppressesmitophagy pages 1-2, mouery2024proteomicanalysisreveals pages 1-3) | Functional annotations should name the complete SCF complex whenever possible. Assigning a substrate directly to “CUL1” without identifying its F-box receptor, degron, and context overstates CUL1’s intrinsic specificity. |
Table: Compact evidence table summarizing the verified identity, molecular mechanism, regulation, localization, representative substrates, recent findings, and translational implications of human CUL1 (Q13616). It distinguishes CUL1’s scaffold role from the substrate specificity supplied by individual F-box receptors.
The gene symbol CUL1, protein name Cullin-1, human organism assignment, and accession Q13616 are mutually consistent. The protein belongs to the cullin family and is the defining scaffold of CUL1-RING ligases, commonly called CRL1 or SCF ligases. No ambiguity requiring termination of the analysis was detected. (petroski2005functionandregulation pages 1-2, petroski2005functionandregulation pages 12-14)
CUL1 has an elongated, curved N-terminal stalk comprising three five-helix cullin repeats, conventionally termed CR1–CR3, followed by a globular C-terminal cullin-homology domain. The N-terminal region binds SKP1, whereas the C-terminal region binds the RING protein RBX1/ROC1 and contains the regulatory cullin neddylation site. This architecture agrees with the supplied Cullin, Cullin-like_AB, Cullin_CS, Cullin_homology, and Cullin_homology_sf annotations. (petroski2005functionandregulation pages 1-2, merlet2009regulationofcullinring pages 1-2)
A canonical SCF complex contains four functional elements:
This modular construction separates substrate selection from catalysis. Human SCF complexes use approximately 70 F-box substrate receptors, while the broader human CRL system has been estimated to comprise approximately 300 modular ligases. These are approximate family-level counts, not the number of complexes active simultaneously in one cell. (mouery2024proteomicanalysisreveals pages 1-3, li2024cullinringligasesemploy pages 1-4)
CUL1 does not form a catalytic ubiquitin–CUL1 intermediate. Instead, RBX1-bound E2 or associated ubiquitin-carrying machinery transfers ubiquitin directly to lysine residues on a receptor-bound substrate. Repeated transfer can generate polyubiquitin chains, frequently producing a signal for 26S-proteasomal degradation, although ubiquitin can also alter localization, interactions, or activity. (merlet2009regulationofcullinring pages 1-2, petroski2005functionandregulation pages 12-14)
There is consequently no single intrinsic CUL1 substrate specificity. Specificity arises combinatorially from the F-box receptor, the substrate degron, degron phosphorylation or other modifications, compartmental colocalization, and compatible catalytic partners. For example, βTrCP recognizes a phosphorylated DSGxx(x)S-type degron, whereas Cyclin F uses its cyclin-homology domain to recognize Cy motifs. (mouery2024proteomicanalysisreveals pages 1-3)
The most accurate annotation is therefore: CUL1 scaffolds regulated SCF ubiquitin ligases that bring F-box-receptor-bound substrates into proximity with RBX1-associated ubiquitin-transfer machinery. Calling CUL1 itself the direct substrate receptor would be mechanistically incorrect.
Attachment of the ubiquitin-like protein NEDD8 to CUL1 stimulates CRL1 activity by promoting conformations that favor productive ubiquitin transfer. Neddylation is therefore a major activity switch rather than a substrate-selection mechanism. Foundational biochemical work showed that CUL1 neddylation enhances SCF activity, including SCF–SKP2 activity toward p27. (merlet2009regulationofcullinring pages 1-2, diaz2022rolesofcullinring pages 19-20)
The COP9 signalosome (CSN) removes NEDD8 from CUL1. Unneddylated CUL1 can bind CAND1, which inhibits and often dismantles inactive complexes and facilitates exchange of SKP1–F-box modules. Thus, deneddylation should not be interpreted merely as terminal inactivation: CSN and CAND1 help remodel the cellular repertoire of SCF ligases so that CUL1 can be redistributed among receptors. (petroski2005functionandregulation pages 9-10, diaz2022rolesofcullinring pages 19-20, li2024cullinringligasesemploy pages 1-4)
An expert synthesis is that CUL1 operates through a dynamic cycle: receptor/substrate engagement favors productive neddylated ligase assemblies; CSN-mediated deneddylation and CAND1-mediated exchange recycle the scaffold when substrates or receptor demand change. The exact sequence and kinetics can vary with cellular context. (petroski2005functionandregulation pages 9-10, li2024cullinringligasesemploy pages 1-4)
CUL1 should not be assigned to one exclusive organelle. Its functional location depends substantially on the associated F-box receptor and the substrate pool. SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. This context dependence explains why broad database labels such as “cytoplasm” or “nucleus” are less informative than localization of a defined SCF complex.
The strongest recent compartment-specific example is SCF–FBXL4 at the mitochondrial outer membrane. In human-cell experiments, FBXL4 colocalized with the outer-membrane marker TOM20 rather than inner-membrane TIM50. CUL1 or FBXL4 depletion stabilized NIX and BNIP3 and increased their mitochondrial abundance, showing that this organelle-associated SCF pool is functional. This localization applies to the FBXL4-containing fraction, not necessarily all CUL1 molecules. (nguyen‐dien2023fbxl4suppressesmitophagy pages 1-2, nguyen‐dien2023fbxl4suppressesmitophagy pages 4-6)
SCF–SKP2 targets the cyclin-dependent-kinase inhibitor p27/CDKN1B for ubiquitin-dependent turnover, promoting cell-cycle progression. This is one of the clearest examples of CUL1 acting as a pathway organizer: SKP2 supplies substrate recognition, CUL1 organizes the complex, and neddylation activates the ligase. (diaz2022rolesofcullinring pages 19-20, ma2024nnmt1‐mnapromotecell‐cycle pages 6-7)
A 2024 breast-cancer study connected metabolism to this mechanism. NNMT-derived 1-methylnicotinamide (1-MNA) increased the abundance of the NEDD8 E2 enzyme UBC12/UBE2M, enhanced CUL1 neddylation, shortened p27 protein persistence, and promoted proliferation. The neddylation inhibitor MLN4924 caused p27 accumulation and suppressed NNMT-driven cell-cycle progression, supporting causal involvement of the CUL1 pathway. (ma2024nnmt1‐mnapromotecell‐cycle pages 6-7, ma2024nnmt1‐mnapromotecell‐cycle pages 1-2)
The authors reported direct 1-MNA–UBC12 binding with an SPR-derived K_D of 168.3 nM. UBC12 contained a KFERQ-like motif at residues 158–162 and associated with HSC70; lysosomal inhibition, but not proteasome inhibition, increased UBC12, supporting chaperone-mediated lysosomal turnover. The proposed sequence is 1-MNA binding to UBC12 → reduced lysosomal localization → increased UBC12 stability → increased CUL1 neddylation → enhanced SCF–SKP2-dependent p27 degradation. (ma2024nnmt1‐mnapromotecell‐cycle pages 10-11)
Important limitations are that much of the cell work used millimolar 1-MNA exposure, and the mechanism was established in selected breast-cancer models and xenografts rather than normal tissues. The study therefore identifies a plausible disease-context regulatory axis, not a universal physiological regulator of CUL1.
A 2023 primary study identified NIX/BNIP3L and BNIP3 as substrates controlled by mitochondrial SCF–FBXL4. Under unstressed conditions, the complex constitutively ubiquitylates and destabilizes these mitophagy receptors, thereby restraining basal mitophagy. CUL1 or FBXL4 silencing stabilized both proteins; CRISPR disruption of FBXL4 increased their mitochondrial abundance; and wild-type FBXL4 rescue restored turnover. (nguyen‐dien2023fbxl4suppressesmitophagy pages 1-2, nguyen‐dien2023fbxl4suppressesmitophagy pages 4-6)
The disease relevance is mechanistically specific. Pathogenic FBXL4 variants causing mitochondrial-DNA depletion syndrome 13 assembled less efficiently with SKP1/CUL1 and were impaired in NIX/BNIP3 turnover and mitophagy suppression. In key imaging experiments, more than 100 cells per condition were analyzed, with three to five independent experiments depending on the condition. These findings implicate defective receptor-dependent SCF assembly—not mutation of CUL1 itself—as a contributor to excessive basal mitophagy. (nguyen‐dien2023fbxl4suppressesmitophagy pages 9-10)
The authors also noted unresolved questions: the precise NIX/BNIP3 degrons and FBXL4-binding interface remain unknown, and receptor stabilization alone does not make every mitochondrion undergo mitophagy. Additional local signals are therefore required. (nguyen‐dien2023fbxl4suppressesmitophagy pages 9-10)
Source: Nguyen-Dien et al., The EMBO Journal, published online 10 May 2023; DOI/URL: https://doi.org/10.15252/embj.2022112767. (nguyen‐dien2023fbxl4suppressesmitophagy pages 1-2)
A 2024 quantitative-proteomics study showed that PLK1 drives a broad G2/M degradation program through multiple E3 ligases, including SCF–βTrCP and SCF–Cyclin F. It identified AKAP2 as a PLK1/βTrCP-regulated substrate; expression of a nondegradable AKAP2 mutant produced actin defects and abnormal mitotic spindles, linking CUL1-dependent proteolysis to cytoskeletal coordination during mitosis. (mouery2024proteomicanalysisreveals pages 1-3)
This study also illustrates phosphodegron logic: an upstream kinase creates or exposes a receptor-recognition signal, and a specific F-box protein interprets that signal. The substrate should therefore be annotated to SCF–βTrCP, not to CUL1 alone.
Source: Mouery et al., Cell Reports, 27 August 2024; DOI/URL: https://doi.org/10.1016/j.celrep.2024.114510. (mouery2024proteomicanalysisreveals pages 1-3)
The most important recent developments for functional annotation are:
The last point refines expert understanding: substrate-receptor identity remains central, but productive ubiquitination additionally depends on three-dimensional geometry among the receptor, substrate lysines, cullin–RING core, and catalytic partner.
CUL1-dependent ligases can act in either tumor-promoting or tumor-suppressive directions depending on the receptor and substrate. Enhanced SCF–SKP2-mediated p27 destruction can support proliferation, whereas other SCF receptors remove oncogenic proteins. Consequently, total CUL1 abundance alone is generally less mechanistically informative than the active SCF receptor, substrate state, and neddylation status. The 2024 NNMT study provides direct evidence for a tumor-promoting UBC12–CUL1–p27 axis in breast-cancer models. (ma2024nnmt1‐mnapromotecell‐cycle pages 6-7, ma2024nnmt1‐mnapromotecell‐cycle pages 1-2)
SCF–FBXL4 dysfunction provides a mechanistic link between impaired CUL1-complex assembly and FBXL4-associated mitochondrial-DNA depletion syndrome. The causal genetic lesions reside in FBXL4, but their functional consequence includes deficient recruitment of the CUL1 core, NIX/BNIP3 accumulation, and excessive basal mitophagy. (nguyen‐dien2023fbxl4suppressesmitophagy pages 9-10, nguyen‐dien2023fbxl4suppressesmitophagy pages 1-2)
Neddylation inhibitors such as MLN4924/pevonedistat suppress CUL1 and other CRLs by blocking cullin activation. In experimental systems this causes accumulation of CRL substrates, including p27, NIX, and BNIP3. However, neddylation inhibition is not CUL1-specific and simultaneously affects many essential CRLs, creating a substantial therapeutic-window challenge. (ma2024nnmt1‐mnapromotecell‐cycle pages 6-7, nguyen‐dien2023fbxl4suppressesmitophagy pages 1-2)
SCF ligases can be redirected toward engineered or drug-induced neo-substrates through engineered F-box receptors, molecular glues, or PROTAC-like approaches. Their modularity makes them attractive degradation machinery, but efficacy depends on receptor expression, CAND1/CSN-controlled ligase availability, neddylation, subcellular colocalization, and productive catalytic geometry. Resistance can therefore arise without alteration of the intended target. (petroski2005functionandregulation pages 9-10, li2024cullinringligasesemploy pages 1-4)
No current evidence in the retrieved literature supports treating CUL1 itself as a routinely drugged, clinically selective target. Present applications predominantly manipulate the broader neddylation pathway or individual substrate receptors, or harness CRLs for induced proximity.
The core scaffold model is supported by structural and biochemical work and is high confidence. The NEDD8–CSN–CAND1 regulatory cycle is also well established, although individual steps are dynamic and context dependent. Recent substrate assignments are strongest when they combine perturbation of CUL1 and the F-box receptor, substrate-stability assays, rescue experiments, localization, and functional readouts—as in the FBXL4 study. (petroski2005functionandregulation pages 9-10, nguyen‐dien2023fbxl4suppressesmitophagy pages 9-10, nguyen‐dien2023fbxl4suppressesmitophagy pages 4-6)
Three annotation errors should be avoided:
Human CUL1/Q13616 is the central structural and regulatory scaffold of SCF/CRL1 ubiquitin ligases. It organizes SKP1–F-box substrate receptors and RBX1-associated ubiquitin-transfer machinery, while NEDD8, CSN, and CAND1 control catalytic activation and receptor exchange. Its cellular function is therefore best understood at the level of defined SCF complexes. Recent work has extended this framework from canonical cell-cycle regulation to mitochondrial quality control and metabolite-sensitive neddylation, identifying mechanistically precise roles for SCF–FBXL4 in NIX/BNIP3 turnover, SCF–SKP2 in p27 degradation, and SCF–βTrCP in mitotic AKAP2 destruction. These findings make CUL1 a central organizer of regulated proteostasis, but also show why therapeutic strategies must usually target a specific receptor, regulatory axis, or induced-proximity configuration rather than the ubiquitous CUL1 scaffold itself.
References
(petroski2005functionandregulation pages 1-2): Matthew D. Petroski and Raymond J. Deshaies. Function and regulation of cullin–ring ubiquitin ligases. Nature Reviews Molecular Cell Biology, 6:9-20, Jan 2005. URL: https://doi.org/10.1038/nrm1547, doi:10.1038/nrm1547. This article has 2772 citations and is from a domain leading peer-reviewed journal.
(petroski2005functionandregulation pages 12-14): Matthew D. Petroski and Raymond J. Deshaies. Function and regulation of cullin–ring ubiquitin ligases. Nature Reviews Molecular Cell Biology, 6:9-20, Jan 2005. URL: https://doi.org/10.1038/nrm1547, doi:10.1038/nrm1547. This article has 2772 citations and is from a domain leading peer-reviewed journal.
(merlet2009regulationofcullinring pages 1-2): Jorge Merlet, Julien Burger, J. Gomes, and L. Pintard. Regulation of cullin-ring e3 ubiquitin-ligases by neddylation and dimerization. Cellular and Molecular Life Sciences, 66:1924-1938, Feb 2009. URL: https://doi.org/10.1007/s00018-009-8712-7, doi:10.1007/s00018-009-8712-7. This article has 245 citations and is from a domain leading peer-reviewed journal.
(petroski2005functionandregulation pages 9-10): Matthew D. Petroski and Raymond J. Deshaies. Function and regulation of cullin–ring ubiquitin ligases. Nature Reviews Molecular Cell Biology, 6:9-20, Jan 2005. URL: https://doi.org/10.1038/nrm1547, doi:10.1038/nrm1547. This article has 2772 citations and is from a domain leading peer-reviewed journal.
(diaz2022rolesofcullinring pages 19-20): Stephanie Diaz, Kankan Wang, Benita Sjögren, and Xing Liu. Roles of cullin-ring ubiquitin ligases in cardiovascular diseases. Biomolecules, 12:416, Mar 2022. URL: https://doi.org/10.3390/biom12030416, doi:10.3390/biom12030416. This article has 26 citations.
(li2024cullinringligasesemploy pages 1-4): Jerry Li, Nicholas Purser, Joanna Liwocha, Daniel C. Scott, Holly A. Byers, Barbara Steigenberger, Spencer Hill, Ishita Tripathi-Giesgen, Trent Hinkle, Fynn M. Hansen, J. Rajan Prabu, Senthil K. Radhakrishnan, Donald S. Kirkpatrick, Kurt M. Reichermeier, Brenda A. Schulman, and Gary Kleiger. Cullin-ring ligases employ geometrically optimized catalytic partners for substrate targeting. Molecular Cell, 84:1304-1320.e16, Apr 2024. URL: https://doi.org/10.1016/j.molcel.2024.01.022, doi:10.1016/j.molcel.2024.01.022. This article has 51 citations and is from a highest quality peer-reviewed journal.
(nguyen‐dien2023fbxl4suppressesmitophagy pages 1-2): Giang Thanh Nguyen‐Dien, Keri‐Lyn Kozul, Yi Cui, Brendan Townsend, Prajakta Gosavi Kulkarni, Soo Siang Ooi, Antonio Marzio, Nissa Carrodus, Steven Zuryn, Michele Pagano, Robert G Parton, Michael Lazarou, S Sean Millard, Robert W Taylor, Brett M Collins, Mathew JK Jones, and Julia K Pagan.
(nguyen‐dien2023fbxl4suppressesmitophagy pages 4-6): Giang Thanh Nguyen‐Dien, Keri‐Lyn Kozul, Yi Cui, Brendan Townsend, Prajakta Gosavi Kulkarni, Soo Siang Ooi, Antonio Marzio, Nissa Carrodus, Steven Zuryn, Michele Pagano, Robert G Parton, Michael Lazarou, S Sean Millard, Robert W Taylor, Brett M Collins, Mathew JK Jones, and Julia K Pagan.
(ma2024nnmt1‐mnapromotecell‐cycle pages 6-7): Yilei Ma, Xucheng Huang, Yanzhong Wang, Yinjiao Lei, Jinwei Yu, Shaobo Yu, Yuzhen Gao, Jun Yang, Feng Zhao, Haitao Yu, Jin Zeng, Yadong Chu, Min Yang, Guoli Li, Xinyou Xie, and Jun Zhang. Nnmt/1‐mna promote cell‐cycle progression of breast cancer by targeting ubc12/cullin‐1‐mediated degradation of p27 proteins. Advanced Science, Dec 2024. URL: https://doi.org/10.1002/advs.202305907, doi:10.1002/advs.202305907. This article has 33 citations and is from a peer-reviewed journal.
(ma2024nnmt1‐mnapromotecell‐cycle pages 1-2): Yilei Ma, Xucheng Huang, Yanzhong Wang, Yinjiao Lei, Jinwei Yu, Shaobo Yu, Yuzhen Gao, Jun Yang, Feng Zhao, Haitao Yu, Jin Zeng, Yadong Chu, Min Yang, Guoli Li, Xinyou Xie, and Jun Zhang. Nnmt/1‐mna promote cell‐cycle progression of breast cancer by targeting ubc12/cullin‐1‐mediated degradation of p27 proteins. Advanced Science, Dec 2024. URL: https://doi.org/10.1002/advs.202305907, doi:10.1002/advs.202305907. This article has 33 citations and is from a peer-reviewed journal.
(nguyen‐dien2023fbxl4suppressesmitophagy pages 9-10): Giang Thanh Nguyen‐Dien, Keri‐Lyn Kozul, Yi Cui, Brendan Townsend, Prajakta Gosavi Kulkarni, Soo Siang Ooi, Antonio Marzio, Nissa Carrodus, Steven Zuryn, Michele Pagano, Robert G Parton, Michael Lazarou, S Sean Millard, Robert W Taylor, Brett M Collins, Mathew JK Jones, and Julia K Pagan.
(mouery2024proteomicanalysisreveals pages 1-3): Ryan D. Mouery, Kimberly Lukasik, Carolyn Hsu, Thomas Bonacci, Derek L. Bolhuis, Xianxi Wang, C. Allie Mills, E. Drew Toomer, Owen G. Canterbury, Kevin C. Robertson, Timothy B. Branigan, Nicholas G. Brown, Laura E. Herring, Stephanie L. Gupton, and Michael J. Emanuele. Proteomic analysis reveals a plk1-dependent g2/m degradation program and a role for akap2 in coordinating the mitotic cytoskeleton. Aug 2024. URL: https://doi.org/10.1016/j.celrep.2024.114510, doi:10.1016/j.celrep.2024.114510. This article has 16 citations and is from a highest quality peer-reviewed journal.
(ma2024nnmt1‐mnapromotecell‐cycle pages 10-11): Yilei Ma, Xucheng Huang, Yanzhong Wang, Yinjiao Lei, Jinwei Yu, Shaobo Yu, Yuzhen Gao, Jun Yang, Feng Zhao, Haitao Yu, Jin Zeng, Yadong Chu, Min Yang, Guoli Li, Xinyou Xie, and Jun Zhang. Nnmt/1‐mna promote cell‐cycle progression of breast cancer by targeting ubc12/cullin‐1‐mediated degradation of p27 proteins. Advanced Science, Dec 2024. URL: https://doi.org/10.1002/advs.202305907, doi:10.1002/advs.202305907. This article has 33 citations and is from a peer-reviewed journal.