Abstract
No public abstract is available from the verified source records.
Jingyu Luo, Shuya Song, Tingting Liu, Kun Cao, Fu Gao, Yanyong Yang
Abstract
Authors
Institutions
No ROR-resolved institution is linked to this work yet.
Provenance
crossref
Confidence 100%
unpaywall
Confidence 95%
datacite
Confidence 0%
No local reference links have been materialized yet.
No local citing links have been materialized yet.
Receptor-interacting protein kinase 1 (RIPK1) regulates cervical cancer cells via NF-κB-TNF-α pathway: an in vitro study
10.1016/j.tranon.2023.101748 · 2023
Kinase-independent functions of RIPK1 regulate hepatocyte survival and liver carcinogenesis
10.1172/jci92508 · 2017
Hepatocyte-specific TAK1 deficiency drives RIPK1 kinase-dependent inflammation to promote liver fibrosis and hepatocellular carcinoma
10.1073/pnas.2005353117 · 2020
Tumor-intrinsic and immune modulatory roles of receptor-interacting protein kinases
10.1016/j.tibs.2021.12.004 · 2022
Impaired RIPK1 ubiquitination sensitizes mice to TNF toxicity and inflammatory cell death
10.1038/s41418-020-00629-3 · 2021
Regulation of RIPK1 phosphorylation: implications for inflammation, cell death, and therapeutic interventions
10.3390/biomedicines12071525 · 2024
Palmitoylation licenses RIPK1 kinase activity and cytotoxicity in the TNF pathway
10.1016/j.molcel.2024.10.002 · 2024
Caspases in cell death, inflammation, and Pyroptosis
10.1146/annurev-immunol-073119-095439 · 2020
The RIP kinases: crucial integrators of cellular stress
10.1016/j.tibs.2005.01.003 · 2005
Comprehensive evolutionary analysis of lamprey TNFR-associated factors (TRAFs) and receptor-interacting protein kinase (RIPKs) and insights into the functional characterization of TRAF3/6 and RIPK1
10.3389/fimmu.2020.00663 · 2020
Mouse receptor interacting protein 3 does not contain a caspase-recruiting or a death domain but induces apoptosis and activates NF-κB
10.1128/mcb.19.10.6500 · 1999
Truncated RIP3 (tRIP3) acts upstream of FADD to induce apoptosis in the human hepatocellular carcinoma cell line QGY-7703
10.1016/j.bbrc.2006.06.118 · 2006
Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation
10.1016/j.cell.2009.05.037 · 2009
Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha
10.1016/j.cell.2009.05.021 · 2009
Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule
10.1038/82732 · 2000
RIPK1 in necroptosis and recent progress in related pharmaceutics
2025
Regulation of RIP1 kinase signalling at the crossroads of inflammation and cell death
10.1038/nrm3683 · 2013
RIPK1 in the inflammatory response and sepsis: recent advances, drug discovery and beyond
2023
RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death
10.1016/0092-8674(95)90072-1 · 1995
Death-domain dimerization-mediated activation of RIPK1 controls necroptosis and RIPK1-dependent apoptosis
10.1073/pnas.1722013115 · 2018
Autophosphorylation at serine 166 regulates RIP kinase 1-mediated cell death and inflammation
10.1038/s41467-020-15466-8 · 2020
Ubiquitin-mediated regulation of RIPK1 kinase activity independent of IKK and MK2
10.1016/j.molcel.2018.01.027 · 2018
Death by TNF: a road to inflammation
10.1038/s41577-022-00792-3 · 2023
Multitasking kinase RIPK1 regulates cell death and inflammation
10.1101/cshperspect.a036368 · 2020
The structure of mouse RIPK1 RHIM-containing domain as a homo-amyloid and in RIPK1/RIPK3 complex
10.1038/s41467-024-51303-y · 2024
The structure of the Necrosome RIPK1-RIPK3 core, a human hetero-amyloid signaling complex
10.1016/j.cell.2018.03.032 · 2018
10.7554/elife.102301.3
10.7554/elife.102301.3
The RIPK1 death domain restrains ZBP1- and TRIF-mediated cell death and inflammation
10.1016/j.immuni.2024.04.016 · 2024
Control of protein stability by post-translational modifications
10.1038/s41467-023-35795-8 · 2023
The role of post-translational modifications in necroptosis
10.3390/biom15040549 · 2025
Ubiquitination of RIPK1 regulates its activation mediated by TNFR1 and TLRs signaling in distinct manners
10.1038/s41467-020-19935-y · 2020
PPDPF suppresses the development of hepatocellular carcinoma through TRIM21-mediated ubiquitination of RIPK1
2023
Holding RIPK1 on the ubiquitin leash in TNFR1 signaling
10.1016/j.tcb.2016.01.006 · 2016
K63-linked ubiquitination regulates RIPK1 kinase activity to prevent cell death during embryogenesis and inflammation
10.1038/s41467-019-12033-8 · 2019
Opposing regulation of the K63-linked polyubiquitination of RIPK3 by SMURF1 and USP5 in necroptosis
10.1038/s41467-025-62723-9 · 2025
Phosphorylation of RIPK1 serine 25 mediates IKK dependent control of extrinsic cell death in T cells
10.3389/fimmu.2022.1067164 · 2022
p38(MAPK)/MK2-dependent phosphorylation controls cytotoxic RIPK1 signalling in inflammation and infection
10.1038/ncb3614 · 2017
Metabolic orchestration of cell death by AMPK-mediated phosphorylation of RIPK1
10.1126/science.abn1725 · 2023
Tyrosine phosphorylation regulates RIPK1 activity to limit cell death and inflammation
10.1038/s41467-022-34080-4 · 2022
ATR-mediated phosphorylation of RIPK1 inhibits DNA damage-induced necroptosis
10.1016/j.bcp.2025.117069 · 2025
RIPK1-mediated immunogenic cell death promotes anti-tumour immunity against soft-tissue sarcoma
10.15252/emmm.201910979 · doi-reference
Necroptosis regulates tumor repopulation after radiotherapy via RIP1/RIP3/MLKL/JNK/IL8 pathway
10.1186/s13046-019-1423-5 · doi-reference
Stem cell factor SOX9 interacts with a cell death regulator RIPK1 and results in escape of Cancer stem cell death
10.3390/cells11030363 · doi-reference
The interaction between RIPK1 and FADD controls perinatal lethality and inflammation
10.1016/j.celrep.2024.114335 · doi-reference
The interferon-stimulated gene RIPK1 regulates cancer cell intrinsic and extrinsic resistance to immune checkpoint blockade
10.1016/j.immuni.2022.03.007 · doi-reference
Necroptosis-driving genes RIPK1, RIPK3 and MLKL-p are associated with intratumoral CD3+ and CD8+ T cell density and predict prognosis in hepatocellular carcinoma
10.1136/jitc-2021-004031 · doi-reference
Design, synthesis, and biological evaluation of RIPK1-targeting PROTACs
10.1007/s11030-025-11166-x · doi-reference
Targeted degradation of receptor-interacting protein kinase 1 to modulate the necroptosis pathway
10.1021/acsptsci.4c00421 · doi-reference
A RIPK1-specific PROTAC degrader achieves potent antitumor activity by enhancing immunogenic cell death
10.1016/j.immuni.2024.04.025 · doi-reference
Proteolysis-targeting chimera (PROTAC) for targeted protein degradation and cancer therapy
10.1186/s13045-020-00885-3 · doi-reference
Development of a RIPK1 degrader to enhance antitumor immunity
10.1038/s41467-024-55006-2 · doi-reference
Synthesis and evaluation of hybrid molecules as RIPK1 and HDACs dual inhibitors
10.1016/j.molstruc.2024.139238 · doi-reference
A phase I randomized study to evaluate safety, pharmacokinetics, and pharmacodynamics of SIR2446M, a selective RIPK1 inhibitor, in healthy participants
10.1111/cts.13857 · doi-reference
A phase I randomized, double-blinded, placebo-controlled study assessing the safety and pharmacokinetics of RIPK1 inhibitor GFH312 in healthy subjects
10.1111/cts.13580 · doi-reference
Safety, pharmacokinetics, and target engagement of a brain penetrant RIPK1 inhibitor, SAR443820 (DNL788), in healthy adult participants
10.1111/cts.13690 · doi-reference
DNL104, a centrally penetrant RIPK1 inhibitor, inhibits RIP1 kinase phosphorylation in a randomized phase I ascending dose study in healthy volunteers
10.1002/cpt.1615 · doi-reference
Safety, pharmacokinetics and target engagement of a novel brain penetrant RIPK1 inhibitor (SIR9900) in healthy adults and elderly participants
10.1111/cts.70151 · doi-reference
A randomized phase I trial evaluating safety and pharmacokinetics of single and multiple ascending doses of Eclitasertib, a RIPK1 inhibitor, in healthy participants
10.1007/s12325-025-03255-y · doi-reference
Immunomodulatory and clinical effects of receptor-interacting protein kinase 1 (RIPK1) inhibitor eclitasertib (SAR443122) in patients with severe COVID-19: a phase 1b, randomized, double-blinded, placebo-controlled study
10.1186/s12931-024-02670-z · doi-reference
Safety and efficacy of selective RIPK1 inhibitor SIR1-365 in hospitalized patients with severe COVID-19: a multicenter, randomized, double-blind, phase 1b trial
10.1016/j.jointm.2024.07.003 · doi-reference
Discovery of a highly potent, selective, and metabolically stable inhibitor of receptor-interacting protein 1 (RIP1) for the treatment of systemic inflammatory response syndrome
10.1021/acs.jmedchem.6b01196 · doi-reference
Repurposing crizotinib to target RIPK1-dependent cell death
10.1093/intimm/dxac061 · doi-reference
Discovery of potent necroptosis inhibitors targeting RIPK1 kinase activity for the treatment of inflammatory disorder and cancer metastasis
10.1038/s41419-019-1735-6 · doi-reference
Discovery of 7-Oxo-2,4,5,7-tetrahydro-6 H-pyrazolo[3,4- c]pyridine derivatives as potent, orally available, and brain-penetrating receptor interacting protein 1 (RIP1) kinase inhibitors: analysis of structure-kinetic relationships
10.1021/acs.jmedchem.7b01647 · doi-reference
RIP1 inhibition blocks inflammatory diseases but not tumor growth or metastases
10.1038/s41418-019-0347-0 · doi-reference
RIP1 kinase drives macrophage-mediated adaptive immune tolerance in pancreatic Cancer
10.1016/j.ccell.2018.10.006 · doi-reference
Comparison of the pharmacokinetics of RIPK1 inhibitor GSK2982772 in healthy Western and Japanese subjects
10.1007/s13318-020-00652-2 · doi-reference
A randomised, placebo-controlled study of RIPK1 inhibitor GSK2982772 in patients with active ulcerative colitis
10.1136/bmjgast-2021-000680 · doi-reference
Discovery of a first-in-class receptor interacting protein 1 (RIP1) kinase specific clinical candidate (GSK2982772) for the treatment of inflammatory diseases
10.1021/acs.jmedchem.6b01751 · doi-reference
Characterization of GSK’963: a structurally distinct, potent and selective inhibitor of RIP1 kinase
10.1038/cddiscovery.2015.9 · doi-reference
DNA-encoded library screening identifies benzo[b][1,4]oxazepin-4-ones as highly potent and Monoselective receptor interacting protein 1 kinase inhibitors
10.1021/acs.jmedchem.5b01898 · doi-reference
Necrostatin-1 analogues: critical issues on the specificity, activity and in vivo use in experimental disease models
10.1038/cddis.2012.176 · doi-reference
Necrostatin-1 prevents necroptosis in brains after ischemic stroke via inhibition of RIPK1-mediated RIPK3/MLKL signaling
10.14336/ad.2018.0728 · doi-reference
Receptor-interacting protein kinase 1 (RIPK1) as a therapeutic target
10.1038/s41573-020-0071-y · doi-reference
Necrostatin-1 and necroptosis inhibition: pathophysiology and therapeutic implications
10.1016/j.phrs.2020.105297 · doi-reference
RIPK1 contributes to cisplatin-induced apoptosis of esophageal squamous cell carcinoma cells via activation of JNK pathway
10.1016/j.lfs.2021.119064 · doi-reference
A decision point between transdifferentiation and programmed cell death priming controls KRAS-dependent pancreatic cancer development
10.1038/s41467-025-56493-7 · doi-reference
Tubular epithelial cells in renal clear cell carcinoma express high RIPK1/3 and show increased susceptibility to TNF receptor 1-induced necroptosis
10.1038/cddis.2016.184 · doi-reference
RIPK1-dependent necroptosis promotes vasculogenic mimicry formation via eIF4E in triple-negative breast cancer
10.1038/s41419-023-05841-w · doi-reference
RIPK1 is a negative mediator in aquaporin 1-driven triple-negative breast carcinoma progression and metastasis
10.1038/s41523-021-00261-5 · doi-reference