On the public citation graph

Design, Synthesis and in Vitro Antitumor Activity Evaluation of a Novel Neddylation Inhibitor

https://doi.org/10.2139/ssrn.4633119
0 signed · 33 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1006/bbrc.1993.2056openalex-extracted
Cloning of a cDNA Which Encodes a Novel Ubiquitin-like Protein
inferredcites →https://doi.org/10.1016/j.cellsig.2018.01.009openalex-extracted
Protein neddylation and its alterations in human cancers for targeted therapy
inferredcites →https://doi.org/10.1016/j.ejmech.2017.03.076openalex-extracted
Discovery of benzothiazole derivatives as novel non-sulfamide NEDD8 activating enzyme inhibitors by target-based virtual screening
inferredcites →https://doi.org/10.1016/j.ejmech.2019.111848openalex-extracted
Discovery of candesartan cilexetic as a novel neddylation inhibitor for suppressing tumor growth
inferredcites →https://doi.org/10.1016/j.neo.2020.02.003openalex-extracted
Gossypol inhibits cullin neddylation by targeting SAG-CUL5 and RBX1-CUL1 complexes
inferredcites →https://doi.org/10.1016/j.sbi.2020.10.007openalex-extracted
NEDD8 and ubiquitin ligation by cullin-RING E3 ligases
inferredcites →https://doi.org/10.1016/s1097-2765(03)00452-0openalex-extracted
The Structure of the APPBP1-UBA3-NEDD8-ATP Complex Reveals the Basis for Selective Ubiquitin-like Protein Activation by an E1
inferredcites →https://doi.org/10.1021/acs.jmedchem.7b01277openalex-extracted
Piperidinyl Ureas Chemically Control Defective in Cullin Neddylation 1 (DCN1)-Mediated Cullin Neddylation
inferredcites →https://doi.org/10.1021/acs.jmedchem.7b01282openalex-extracted
Discovery of an Orally Bioavailable Inhibitor of Defective in Cullin Neddylation 1 (DCN1)-Mediated Cullin Neddylation
inferredcites →https://doi.org/10.1021/acs.jmedchem.7b01455openalex-extracted
High-Affinity Peptidomimetic Inhibitors of the DCN1-UBC12 Protein–Protein Interaction
inferredcites →https://doi.org/10.1021/acs.jmedchem.9b00410openalex-extracted
Discovery of Novel Pyrazolo-pyridone DCN1 Inhibitors Controlling Cullin Neddylation
inferredcites →https://doi.org/10.1021/ci5002058openalex-extracted
Effective Virtual Screening Strategy toward Covalent Ligands: Identification of Novel NEDD8-Activating Enzyme Inhibitors
inferredcites →https://doi.org/10.1038/cddis.2017.195openalex-extracted
Promoting tumorigenesis in nasopharyngeal carcinoma, NEDD8 serves as a potential theranostic target
inferredcites →https://doi.org/10.1038/nature05490openalex-extracted
Basis for a ubiquitin-like protein thioester switch toggling E1–E2 affinity
inferredcites →https://doi.org/10.1038/nchembio.2386openalex-extracted
Blocking an N-terminal acetylation–dependent protein interaction inhibits an E3 ligase
inferredcites →https://doi.org/10.1038/nm.4474openalex-extracted
A small-molecule inhibitor of the ubiquitin activating enzyme for cancer treatment
inferredcites →https://doi.org/10.1038/nrm1547openalex-extracted
Function and regulation of cullin–RING ubiquitin ligases
inferredcites →https://doi.org/10.1038/nrm3919openalex-extracted
Protein neddylation: beyond cullin–RING ligases
inferredcites →https://doi.org/10.1038/nsmb.2780openalex-extracted
New insights into ubiquitin E3 ligase mechanism
inferredcites →https://doi.org/10.1038/s41467-017-01243-7openalex-extracted
A potent small-molecule inhibitor of the DCN1-UBC12 interaction that selectively blocks cullin 3 neddylation
inferredcites →https://doi.org/10.1038/sj.onc.1207414openalex-extracted
Nedd8 on cullin: building an expressway to protein destruction
inferredcites →https://doi.org/10.1089/ars.2013.5795openalex-extracted
Targeting Neddylation Pathways to Inactivate Cullin-RING Ligases for Anticancer Therapy
inferredcites →https://doi.org/10.1093/jnci/dju083openalex-extracted
Overactivated Neddylation Pathway as a Therapeutic Target in Lung Cancer
inferredcites →https://doi.org/10.1101/cshperspect.a033951openalex-extracted
Functional Modules of the Proteostasis Network
inferredcites →https://doi.org/10.1146/annurev-biochem-013118-111552openalex-extracted
Chemical Biology Framework to Illuminate Proteostasis
inferredcites →https://doi.org/10.1152/physrev.00027.2001openalex-extracted
The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction
inferredcites →https://doi.org/10.1158/1078-0432.ccr-09-0343openalex-extracted
Targeting NEDD8-Activated Cullin-RING Ligases for the Treatment of Cancer
inferredcites →https://doi.org/10.1158/1078-0432.ccr-15-2254openalex-extracted
Neddylation Inhibition Activates the Extrinsic Apoptosis Pathway through ATF4–CHOP–DR5 Axis in Human Esophageal Cancer Cells
inferredcites →https://doi.org/10.1158/1535-7163.mct-18-0644openalex-extracted
TAS4464, A Highly Potent and Selective Inhibitor of NEDD8-Activating Enzyme, Suppresses Neddylation and Shows Antitumor Activity in Diverse Cancer Models
inferredcites →https://doi.org/10.18632/oncotarget.2309openalex-extracted
Neddylation pathway is up-regulated in human intrahepatic cholangiocarcinoma and serves as a potential therapeutic target
inferredcites →https://doi.org/10.18632/oncotarget.3191openalex-extracted
Stabilization of LKB1 and Akt by neddylation regulates energy metabolism in liver cancer
inferredcites →https://doi.org/10.2139/ssrn.3457385openalex-extracted
Discovery of Candesartan Cilexetic as a Novel Neddylation Inhibitor for Suppressing Tumor Growth
inferredcites →https://doi.org/10.3322/caac.21660openalex-extracted
Global Cancer Statistics 2020: GLOBOCAN Estimates of Incidence and Mortality Worldwide for 36 Cancers in 185 Countries
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.