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Neddylation of a breast cancer-associated protein recruits a class III histone deacetylase that represses NFκB-dependent transcription
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1006/bbrc.1999.0339openalex-snapshot
Identification of NEDD8-Conjugation Site in Human Cullin-2
inferredcites →https://doi.org/10.1016/j.bcp.2004.05.034openalex-snapshot
Histone deacetylase inhibitors open new doors in cancer therapy
inferredcites →https://doi.org/10.1016/j.cell.2004.06.016openalex-snapshot
Mdm2-Mediated NEDD8 Conjugation of p53 Inhibits Its Transcriptional Activity
inferredcites →https://doi.org/10.1016/s0092-8674(02)00654-2openalex-snapshot
Cooperation between Complexes that Regulate Chromatin Structure and Transcription
inferredcites →https://doi.org/10.1016/s0092-8674(04)00126-6openalex-snapshot
Mammalian SIRT1 Represses Forkhead Transcription Factors
inferredcites →https://doi.org/10.1016/s0167-4781(02)00562-6openalex-snapshot
Characterization of a novel human breast cancer associated gene (BCA3) encoding an alternatively spliced proline-rich protein
inferredcites →https://doi.org/10.1016/s0378-1119(00)00139-6openalex-snapshot
Ubiquitin-like proteins: new wines in new bottles
inferredcites →https://doi.org/10.1016/s0378-1119(01)00741-7openalex-snapshot
The molecular biology of the SIR proteins
inferredcites →https://doi.org/10.1016/s1097-2765(02)00783-9openalex-snapshot
NEDD8 Modification of CUL1 Dissociates p120CAND1, an Inhibitor of CUL1-SKP1 Binding and SCF Ligases
inferredcites →https://doi.org/10.1038/sj.emboj.7600244openalex-snapshot
Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase
inferredcites →https://doi.org/10.1042/bj20021321openalex-snapshot
Histone deacetylases (HDACs): characterization of the classical HDAC family
inferredcites →https://doi.org/10.1073/pnas.0408608102openalex-snapshot
A-kinase-interacting protein localizes protein kinase A in the nucleus
inferredcites →https://doi.org/10.1073/pnas.93.23.12861openalex-snapshot
Induction of cyclin D1 by simian virus 40 small tumor antigen
inferredcites →https://doi.org/10.1073/pnas.96.10.5510openalex-snapshot
Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel–Lindau tumor suppressor function
inferredcites →https://doi.org/10.1074/jbc.272.45.28557openalex-snapshot
Characterization of NEDD8, a Developmentally Down-regulated Ubiquitin-like Protein
inferredcites →https://doi.org/10.1074/jbc.275.5.3355openalex-snapshot
Differential Regulation of Sentrinized Proteins by a Novel Sentrin-specific Protease
inferredcites →https://doi.org/10.1074/jbc.m211051200openalex-snapshot
Basal Expression of IκBα Is Controlled by the Mammalian Transcriptional Repressor RBP-J (CBF1) and Its Activator Notch1
inferredcites →https://doi.org/10.1074/jbc.m212948200openalex-snapshot
NEDP1, a Highly Conserved Cysteine Protease That deNEDDylates Cullins
inferredcites →https://doi.org/10.1074/jbc.m302890200openalex-snapshot
Identification and Characterization of DEN1, a Deneddylase of the ULP Family
inferredcites →https://doi.org/10.1074/jbc.m408748200openalex-snapshot
SIRT1 Deacetylation and Repression of p300 Involves Lysine Residues 1020/1024 within the Cell Cycle Regulatory Domain 1
inferredcites →https://doi.org/10.1093/nar/gkh295openalex-snapshot
RING1 inhibits transactivation of RBP-J by Notch through interaction with LIM protein KyoT2
inferredcites →https://doi.org/10.1093/nar/gki220openalex-snapshot
HIV-1 can escape from RNA interference by evolving an alternative structure in its RNA genome
inferredcites →https://doi.org/10.1101/gad.12.15.2263openalex-snapshot
A new NEDD8-ligating system for cullin-4A
inferredcites →https://doi.org/10.1101/gad.12.7.914openalex-snapshot
Modification of yeast Cdc53p by the ubiquitin-related protein Rub1p affects function of the SCFCdc4 complex
inferredcites →https://doi.org/10.1128/mcb.18.1.644openalex-snapshot
LIM Protein KyoT2 Negatively Regulates Transcription by Association with the RBP-J DNA-Binding Protein
inferredcites →https://doi.org/10.1128/mcb.19.8.5785openalex-snapshot
NF-κB Controls Cell Growth and Differentiation through Transcriptional Regulation of Cyclin D1
inferredcites →https://doi.org/10.1128/mcb.24.13.6021-6028.2004openalex-snapshot
SENP1 Enhances Androgen Receptor-Dependent Transcription through Desumoylation of Histone Deacetylase 1
inferredcites →https://doi.org/10.1128/mcb.24.8.3251-3261.2004openalex-snapshot
pVHL Modification by NEDD8 Is Required for Fibronectin Matrix Assembly and Suppression of Tumor Development
inferredcites →https://doi.org/10.1261/rna.2780503openalex-snapshot
Sequence requirements for micro RNA processing and function in human cells
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Trim4 Promotes Small-Molecule-Induced CORO1A Neddylated-Degradation for Triple Negative Breast Cancer Therapy
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NNMT/1‐MNA Promote Cell‐Cycle Progression of Breast Cancer by Targeting UBC12/Cullin‐1‐Mediated Degradation of P27 Proteins
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Isolation and the timing of mammary gland development, gonadarche, and ovarian senescence: Implications for mammary tumor burden
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Neddylation positively regulates the ubiquitin E3 ligase activity of parkin
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E2‐binding surface on Uba3 β‐grasp domain undergoes a conformational transition
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Ubiquitin, SUMO, and Nedd8 as Therapeutic Targets in Cancer
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Sirtuin Activation by Small Molecules
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Targeting Protein Neddylation for Cancer Therapy
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Targeting the neddylation pathway in cells as a potential therapeutic approach for diseases
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SIRT1 as a masterful reciprocal regulator of molecular mechanisms and signaling pathways involved in tumor growth and expansion
inferred← citeshttps://doi.org/10.1007/s13238-017-0455-xopenalex-snapshot
NEDDylation antagonizes ubiquitination of proliferating cell nuclear antigen and regulates the recruitment of polymerase η in response to oxidative DNA damage
inferred← citeshttps://doi.org/10.1007/s42764-021-00044-zopenalex-snapshot
Role of NEDD8 and neddylation dynamics in DNA damage response
inferred← citeshttps://doi.org/10.1016/b978-0-12-822467-0.00013-9openalex-snapshot
Sirtuins and the hallmarks of cancer
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A most versatile kinase: The catalytic subunit of PKA in T-cell biology
inferred← citeshttps://doi.org/10.1016/j.bbcan.2011.04.004openalex-snapshot
SIRT3 and cancer: Tumor promoter or suppressor?
inferred← citeshttps://doi.org/10.1016/j.bbrc.2007.12.066openalex-snapshot
Inhibition of APP intracellular domain (AICD) transcriptional activity via covalent conjugation with Nedd8
inferred← citeshttps://doi.org/10.1016/j.bbrc.2008.07.019openalex-snapshot
TRIP12 functions as an E3 ubiquitin ligase of APP-BP1
inferred← citeshttps://doi.org/10.1016/j.bbrc.2016.11.084openalex-snapshot
MyD88 NEDDylation negatively regulates MyD88-dependent NF-κB signaling through antagonizing its ubiquitination
inferred← citeshttps://doi.org/10.1016/j.bbrep.2024.101650openalex-snapshot
Etoposide-induced SENP8 confers a feed-back drug resistance on acute lymphoblastic leukemia cells
inferred← citeshttps://doi.org/10.1016/j.bmc.2020.115875openalex-snapshot
Review of NEDDylation inhibition activity detection methods
inferred← citeshttps://doi.org/10.1016/j.ccr.2011.01.002openalex-snapshot
NEDD8 Pathways in Cancer, Sine Quibus Non
inferred← citeshttps://doi.org/10.1016/j.cellsig.2016.05.016openalex-snapshot
Itch promotes the neddylation of JunB and regulates JunB-dependent transcription
inferred← citeshttps://doi.org/10.1016/j.cellsig.2018.01.009openalex-snapshot
Protein neddylation and its alterations in human cancers for targeted therapy
inferred← citeshttps://doi.org/10.1016/j.celrep.2021.109854openalex-snapshot
RNF8-mediated regulation of Akt promotes lung cancer cell survival and resistance to DNA damage
inferred← citeshttps://doi.org/10.1016/j.compbiolchem.2025.108395openalex-snapshot
2-(Diarylalkyl)aminobenzothiazole derivatives induce autophagy and apoptotic death through SIRT inhibition and P53 activation In MCF7 breast cancer cells
inferred← citeshttps://doi.org/10.1016/j.drup.2023.101014openalex-snapshot
Cisplatin-activated ERβ/DCAF8 positive feedback loop induces chemoresistance in non-small cell lung cancer via PTEN/Akt axis
inferred← citeshttps://doi.org/10.1016/j.ejmech.2018.05.027openalex-snapshot
A novel NAE/UAE dual inhibitor LP0040 blocks neddylation and ubiquitination leading to growth inhibition and apoptosis of cancer cells
inferred← citeshttps://doi.org/10.1016/j.ejmech.2020.112676openalex-snapshot
Identification of the subtype-selective Sirt5 inhibitor balsalazide through systematic SAR analysis and rationalization via theoretical investigations
inferred← citeshttps://doi.org/10.1016/j.febslet.2012.04.056openalex-snapshot
X‐linked inhibitor of apoptosis protein mediates neddylation by itself but does not function as a NEDD8–E3 ligase for caspase‐7
inferred← citeshttps://doi.org/10.1016/j.jare.2025.11.010openalex-snapshot
Neddylation: from regulatory mechanisms to clinical implications in cancer
inferred← citeshttps://doi.org/10.1016/j.jpha.2024.101140openalex-snapshot
Inhibiting neddylation: A new strategy for tumor therapy
inferred← citeshttps://doi.org/10.1016/j.molcel.2007.12.012openalex-snapshot
Dcn1 Functions as a Scaffold-Type E3 Ligase for Cullin Neddylation
inferred← citeshttps://doi.org/10.1016/j.molcel.2009.01.011openalex-snapshot
E2-RING Expansion of the NEDD8 Cascade Confers Specificity to Cullin Modification
inferred← citeshttps://doi.org/10.1016/j.molcel.2010.11.011openalex-snapshot
Systematic In Vivo RNAi Analysis Identifies IAPs as NEDD8-E3 Ligases
inferred← citeshttps://doi.org/10.1016/j.molonc.2012.01.003openalex-snapshot
Inhibition of NEDD8‐conjugation pathway by novel molecules: Potential approaches to anticancer therapy
inferred← citeshttps://doi.org/10.1016/j.mrfmmm.2017.07.001openalex-snapshot
Ubiquitin-like modifications in the DNA damage response
inferred← citeshttps://doi.org/10.1016/j.pan.2015.03.006openalex-snapshot
NEDDylation in liver cancer: The regulation of the RNA binding protein Hu antigen R
inferred← citeshttps://doi.org/10.1016/j.phrs.2024.107532openalex-snapshot
A novel approach to explore metabolic diseases: Neddylation
inferred← citeshttps://doi.org/10.1016/j.semcdb.2020.03.008openalex-snapshot
SUMOylation, a multifaceted regulatory mechanism in the pancreatic beta cells
inferred← citeshttps://doi.org/10.1016/j.yexcr.2008.07.011openalex-snapshot
sirt1-null mice develop an autoimmune-like condition
inferred← citeshttps://doi.org/10.1016/j.yexcr.2017.06.019openalex-snapshot
Inhibition of Mcl-1 enhances Pevonedistat-triggered apoptosis in osteosarcoma cells
inferred← citeshttps://doi.org/10.1016/j.yexcr.2017.11.011openalex-snapshot
BCA3 contributes to the malignant progression of hepatocellular carcinoma through AKT activation and NF-κB translocation
inferred← citeshttps://doi.org/10.1021/ml2000615openalex-snapshot
Identification of NAE Inhibitors Exhibiting Potent Activity in Leukemia Cells: Exploring the Structural Determinants of NAE Specificity
inferred← citeshttps://doi.org/10.1021/pr700749vopenalex-snapshot
A Targeted Proteomic Analysis of the Ubiquitin-Like Modifier Nedd8 and Associated Proteins
inferred← citeshttps://doi.org/10.1038/embor.2008.10openalex-snapshot
Ribosomal proteins are targets for the NEDD8 pathway
inferred← citeshttps://doi.org/10.1038/embor.2008.183openalex-snapshot
Function and regulation of protein neddylation
inferred← citeshttps://doi.org/10.1038/embor.2008.19openalex-snapshot
NEDD8 acts as a ‘molecular switch’ defining the functional selectivity of VHL
inferred← citeshttps://doi.org/10.1038/embor.2012.113openalex-snapshot
NEDDylation regulates E2F‐1‐dependent transcription
inferred← citeshttps://doi.org/10.1038/nrm3919openalex-snapshot
Protein neddylation: beyond cullin–RING ligases
inferred← citeshttps://doi.org/10.1038/onc.2012.428openalex-snapshot
NEDDylation controls the target specificity of E2F1 and apoptosis induction
inferred← citeshttps://doi.org/10.1038/s41374-018-0175-8openalex-snapshot
TRAF6 neddylation drives inflammatory arthritis by increasing NF-κB activation
inferred← citeshttps://doi.org/10.1038/s41388-023-02796-2openalex-snapshot
AKIP1 accelerates glioblastoma progression through stabilizing EGFR expression
inferred← citeshttps://doi.org/10.1038/s41392-024-01800-9openalex-snapshot
Protein neddylation and its role in health and diseases
inferred← citeshttps://doi.org/10.1038/s41598-020-75286-0openalex-snapshot
Neddylation blockade induces HIF-1α driven cancer cell migration via upregulation of ZEB1
inferred← citeshttps://doi.org/10.1038/s41598-020-77001-5openalex-snapshot
Characterization of Plasmodium falciparum NEDD8 and identification of cullins as its substrates
inferred← citeshttps://doi.org/10.1038/s41598-025-04153-7openalex-snapshot
Neddylation status determines the therapeutic sensitivity of tyrosine kinase inhibitors in chronic myeloid leukemia
inferred← citeshttps://doi.org/10.1038/s44355-025-00032-0openalex-snapshot
Rearrangement of the liver ubiquitome and NEDDylome in metabolic dysfunction-associated steatotic liver disease
inferred← citeshttps://doi.org/10.1039/c5sc01351hopenalex-snapshot
An inhibitor of ubiquitin conjugation and aggresome formation
inferred← citeshttps://doi.org/10.1042/bj20070140openalex-snapshot
Sirtuins in mammals: insights into their biological function
inferred← citeshttps://doi.org/10.1042/bj20070817openalex-snapshot
Sirt1 interacts with transducin-like enhancer of split-1 to inhibit nuclear factor κB-mediated transcription
inferred← citeshttps://doi.org/10.1042/bj20111671openalex-snapshot
Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes
inferred← citeshttps://doi.org/10.1042/bst0360802openalex-snapshot
Novel substrates and functions for the ubiquitin-like molecule NEDD8
inferred← citeshttps://doi.org/10.1073/pnas.0802917105openalex-snapshot
Sirt1 protects against high-fat diet-induced metabolic damage
inferred← citeshttps://doi.org/10.1073/pnas.0812528106openalex-snapshot
The human Dcn1-like protein DCNL3 promotes Cul3 neddylation at membranes
inferred← citeshttps://doi.org/10.1073/pnas.1221670110openalex-snapshot
A kinase interacting protein (AKIP1) is a key regulator of cardiac stress
inferred← citeshttps://doi.org/10.1074/jbc.m110.164384openalex-snapshot
SLUG-induced Elevation of D1 Cyclin in Breast Cancer Cells through the Inhibition of Its Ubiquitination
inferred← citeshttps://doi.org/10.1074/jbc.m112.384511openalex-snapshot
The Bicyclic Intermediate Structure Provides Insights into the Desuccinylation Mechanism of Human Sirtuin 5 (SIRT5)
inferred← citeshttps://doi.org/10.1074/jbc.m710285200openalex-snapshot
AKIP1 Enhances NF-κB-dependent Gene Expression by Promoting the Nuclear Retention and Phosphorylation of p65
inferred← citeshttps://doi.org/10.1089/ars.2013.5795openalex-snapshot
Targeting Neddylation Pathways to Inactivate Cullin-RING Ligases for Anticancer Therapy
inferred← citeshttps://doi.org/10.1093/carcin/bgr068openalex-snapshot
TRIM40 promotes neddylation of IKK and is downregulated in gastrointestinal cancers
inferred← citeshttps://doi.org/10.1093/cvr/cvw161openalex-snapshot
Overexpression of A kinase interacting protein 1 attenuates myocardial ischaemia/reperfusion injury but does not influence heart failure development
inferred← citeshttps://doi.org/10.1093/hmg/dds070openalex-snapshot
Regulation of parkin and PINK1 by neddylation
inferred← citeshttps://doi.org/10.1093/nar/gkp1039openalex-snapshot
SIRT1 deacetylates APE1 and regulates cellular base excision repair
inferred← citeshttps://doi.org/10.1096/fj.06-7615revopenalex-snapshot
Beyond IκBs: alternative regulation of NF‐KB activity
inferred← citeshttps://doi.org/10.1099/vir.0.064345-0openalex-snapshot
Breast cancer-associated protein – a novel binding partner of Mason-Pfizer monkey virus protease
inferred← citeshttps://doi.org/10.1104/pp.111.176677openalex-snapshot
MLN4924 Is an Efficient Inhibitor of NEDD8 Conjugation in Plants
inferred← citeshttps://doi.org/10.1111/cbdd.13457openalex-snapshot
Identifying de‐NEDDylation inhibitors: Virtual high‐throughput screens targeting SENP8
inferred← citeshttps://doi.org/10.1111/febs.15584openalex-snapshot
Diverse and pivotal roles of neddylation in metabolism and immunity
inferred← citeshttps://doi.org/10.1111/j.1349-7006.2011.01904.xopenalex-snapshot
Histone deacetylase inhibitors block nuclear factor‐κB‐dependent transcription by interfering with RNA polymerase II recruitment
inferred← citeshttps://doi.org/10.1111/j.1462-5822.2009.01375.xopenalex-snapshot
Secretory protein with RING finger domain (SPRING) specific toTrypanosoma cruziis directed, as a ubiquitin ligase related protein, to the nucleus of host cells
inferred← citeshttps://doi.org/10.1111/j.1751-2980.2009.00416.xopenalex-snapshot
SIRT3 reduces lipid accumulation via AMPK activation in human hepatic cells
inferred← citeshttps://doi.org/10.1128/mbio.00289-10openalex-snapshot
Functional Analysis of VopF Activity Required for Colonization in Vibrio cholerae
inferred← citeshttps://doi.org/10.1128/mcb.00775-14openalex-snapshot
Nedd8 Regulates Inflammasome-Dependent Caspase-1 Activation
inferred← citeshttps://doi.org/10.1155/2019/7283639openalex-snapshot
MLN4924 Exerts a Neuroprotective Effect against Oxidative Stress via Sirt1 in Spinal Cord Ischemia-Reperfusion Injury
inferred← citeshttps://doi.org/10.1158/0008-5472.can-10-0688openalex-snapshot
Interaction of TAp73 and Breast Cancer–Associated Gene 3 Enhances the Sensitivity of Cervical Cancer Cells in Response to Irradiation-Induced Apoptosis
inferred← citeshttps://doi.org/10.1177/1947601912475079openalex-snapshot
The Roles of SIRT1 in Cancer
inferred← citeshttps://doi.org/10.1186/1742-4690-11-37openalex-snapshot
HIV-1 protease-induced apoptosis
inferred← citeshttps://doi.org/10.1186/s11658-024-00624-3openalex-snapshot
Crosstalk between SUMOylation and other post-translational modifications in breast cancer
inferred← citeshttps://doi.org/10.1201/9781420045802.ch9openalex-snapshot
Role of Sirtuins in Aging and Tumorigenesis
inferred← citeshttps://doi.org/10.1242/jcs.030445openalex-snapshot
DEN1 deneddylates non-cullin proteins in vivo
inferred← citeshttps://doi.org/10.1242/jcs.150706openalex-snapshot
Proteomic analysis unveils a FANCA-modulated neddylation pathway involved in CXCR5 membrane targeting and cell mobility
inferred← citeshttps://doi.org/10.1359/jbmr.070105openalex-snapshot
Breast Cancer–Associated Gene 3 (BCA3) Is a Novel Rac1-Interacting Protein
inferred← citeshttps://doi.org/10.1371/journal.pone.0018713openalex-snapshot
The Rate of NF-κB Nuclear Translocation Is Regulated by PKA and A Kinase Interacting Protein 1
inferred← citeshttps://doi.org/10.1371/journal.pone.0050637openalex-snapshot
SUMOylation Regulates the Transcriptional Repression Activity of FOG-2 and Its Association with GATA-4
inferred← citeshttps://doi.org/10.1371/journal.pone.0080815openalex-snapshot
AKIP1 Expression Modulates Mitochondrial Function in Rat Neonatal Cardiomyocytes
inferred← citeshttps://doi.org/10.1517/14728222.2011.550877openalex-snapshot
Targeting protein neddylation: a novel therapeutic strategy for the treatment of cancer
inferred← citeshttps://doi.org/10.1530/erc-14-0315openalex-snapshot
Regulation of cancer-related pathways by protein NEDDylation and strategies for the use of NEDD8 inhibitors in the clinic
inferred← citeshttps://doi.org/10.18632/oncotarget.9543openalex-snapshot
Inhibition of neddylation regulates dendritic cell functions via Deptor accumulation driven mTOR inactivation
inferred← citeshttps://doi.org/10.2147/ott.s151952openalex-snapshot
Upregulation of AKIP1 contributes to metastasis and progression and predicts poor prognosis of patients with colorectal cancer
inferred← citeshttps://doi.org/10.2174/1381612811319220014openalex-snapshot
Targeting the Ubiquitin Proteasome System: Beyond Proteasome Inhibition
inferred← citeshttps://doi.org/10.2174/1566524019666190112132103openalex-snapshot
Differential Expression of Seven De-sumoylation Enzymes (SENPs) in Major Ocular Tissues of Mouse Eye
inferred← citeshttps://doi.org/10.2174/1568026619666190311110646openalex-snapshot
Pharmaceutical Inhibition of Neddylation as Promising Treatments for Various Cancers
inferred← citeshttps://doi.org/10.2174/187153009787582441openalex-snapshot
Targeting Histone Deacetylases for the Treatment of Immune, Endocrine & Metabolic Disorders
inferred← citeshttps://doi.org/10.33549/physiolres.933961openalex-snapshot
Various AKIP1 Expression Levels Affect Its Subcellular Localization but Have no Effect on NF-κB Activation
inferred← citeshttps://doi.org/10.3389/fcell.2021.653882openalex-snapshot
Advances in Cancer Treatment by Targeting the Neddylation Pathway
inferred← citeshttps://doi.org/10.3389/fcell.2022.890121openalex-snapshot
Association Between Neddylation and Immune Response
inferred← citeshttps://doi.org/10.3389/fimmu.2019.01432openalex-snapshot
Neddylation Facilitates the Antiviral Response in Zebrafish
inferred← citeshttps://doi.org/10.3389/fmed.2020.586881openalex-snapshot
Neddylation: A Versatile Pathway Takes on Chronic Liver Diseases
inferred← citeshttps://doi.org/10.3389/fnins.2024.1467562openalex-snapshot
Neddylation of protein, a new strategy of protein post-translational modification for targeted treatment of central nervous system diseases
inferred← citeshttps://doi.org/10.3389/fpls.2014.00103openalex-snapshot
The NEDD8 modification pathway in plants
inferred← citeshttps://doi.org/10.3390/ijms130911804openalex-snapshot
Modification by Ubiquitin-Like Proteins: Significance in Apoptosis and Autophagy Pathways
inferred← citeshttps://doi.org/10.3390/ijms141121378openalex-snapshot
AKIP1, a Cardiac Hypertrophy Induced Protein that Stimulates Cardiomyocyte Growth via the Akt Pathway
inferred← citeshttps://doi.org/10.3390/ijms22041716openalex-snapshot
The Effect of Neddylation Inhibition on Inflammation-Induced MMP9 Gene Expression in Esophageal Squamous Cell Carcinoma
inferred← citeshttps://doi.org/10.3390/ijms23073480openalex-snapshot
The Next Frontier: Translational Development of Ubiquitination, SUMOylation, and NEDDylation in Cancer
inferred← citeshttps://doi.org/10.3390/ijms23158298openalex-snapshot
UBE2G1 Is a Critical Component of Immune Response to the Infection of Pseudomonas Plecoglossicida in Large Yellow Croaker (Larimichthys crocea)
inferred← citeshttps://doi.org/10.3390/v10040212openalex-snapshot
Does BCA3 Play a Role in the HIV-1 Replication Cycle?
inferred← citeshttps://doi.org/10.3724/sp.j.1206.2009.00077openalex-snapshot
Progress in Function and Regulation of Protein Neddylation*
inferred← citeshttps://doi.org/10.3892/ijmm.2017.3091openalex-snapshot
Breast cancer-associated gene 3 interacts with Rac1 and augments NF-κB signaling in vitro, but has no effect on RANKL-induced bone resorption in vivo
inferred← citeshttps://doi.org/10.3892/ol.2018.8333openalex-snapshot
MLN4924 suppresses lipopolysaccharide‑induced proinflammatory cytokine production in neutrophils in a dose‑dependent manner
inferred← citeshttps://doi.org/10.4049/jimmunol.1202041openalex-snapshot
Central Role for Endothelial Human Deneddylase-1/SENP8 in Fine-Tuning the Vascular Inflammatory Response
inferred← citeshttps://doi.org/10.4049/jimmunol.1501752openalex-snapshot
MLN4924, a First-in-Class NEDD8-Activating Enzyme Inhibitor, Attenuates IFN-β Production
inferred← citeshttps://doi.org/10.4161/cc.11.6.19559openalex-snapshot
The ubiquitin E1 enzyme Ube1 mediates NEDD8 activation under diverse stress conditions
inferred← citeshttps://doi.org/10.4238/2014.december.18.7openalex-snapshot
Cloning and functional identification of a novel BCA3 splice
inferred← citeshttps://doi.org/10.5772/26409openalex-snapshot
Anticancer Target Molecules Against the SCF Ubiquitin E3 Ligase in RCC: Potential Approaches to the NEDD8 Pathway
inferred← citeshttps://doi.org/10.5772/intechopen.83426openalex-snapshot
New Insights into the Mechanisms Underlying NEDD8 Structural and Functional Specificities
inferred← citeshttps://doi.org/10.70675/a9a79207z0857z4ed5zb207z749cdceb9430openalex-snapshot
The role of NEDD8 pathway in cell invasion and strategies for the use of NEDD8 inhibitors in the clinic
inferred← citeshttps://doi.org/10.70675/f67a0612z3cccz46b5zb058zebfbc60f1ac4openalex-snapshot
Regulation of proteotoxicity through atypical NEDDylation
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