記事
Digital data available(Crossref)
Begin reading now
CiNii Research
Regulation of the release of damage-associated molecular patterns from necroptotic cells
- Material type
- 記事
- Author
- Hiroyasu Nakanoほか
- Publisher
- Portland Press Ltd.
- Publication date
- 2022-03-16
- Material Format
- Digital
- Journal name
- Biochemical Journal 479 5
- Publication Page
- p.677-685
Detailed bibliographic record
Summary, etc.:
- <jats:p>Damage-associated molecular patterns (DAMPs) are molecules within living cells that are released when cell membranes are ruptured. Although DA...
Holdings of Libraries in Japan
This page shows libraries in Japan other than the National Diet Library that hold the material.
Please contact your local library for information on how to use materials or whether it is possible to request materials from the holding libraries.
Bibliographic Record
You can check the details of this material, its authority (keywords that refer to materials on the same subject, author's name, etc.), etc.
Digital
- Material Type
- 記事
- Author Heading
- Publication Date
- 2022-03-16
- Publication Date (W3CDTF)
- 2022-03-16
- Periodical title
- Biochemical Journal
- No. or year of volume/issue
- 479 5
- Volume
- 479
- Issue
- 5
- Pages
- 677-685
- Publication date of volume/issue (W3CDTF)
- 2022-03-16
- ISSN (Periodical Title)
- 02646021
- Publication (Periodical Title)
- Portland Press Ltd.
- Subject Heading
- Target Audience
- 一般
- DOI
- 10.1042/bcj20210604
- Date Created (W3CDTF)
- 2022-03-16
- Related Material (URI)
- Is Referenced By
- Generation of transgenic mice expressing a FRET biosensor, SMART, that responds to necroptosis
- References
- Single-Cell Imaging of Caspase-1 Dynamics Reveals an All-or-None Inflammasome Signaling ResponseA FRET biosensor for necroptosis uncovers two different modes of the release of DAMPsThe Endotoxin Delivery Protein HMGB1 Mediates Caspase-11-Dependent Lethality in SepsisMLKL trafficking and accumulation at the plasma membrane control the kinetics and threshold for necroptosisReceptor Interacting Protein Kinase-3 Determines Cellular Necrotic Response to TNF-αPhosphorylation-Driven Assembly of the RIP1-RIP3 Complex Regulates Programmed Necrosis and Virus-Induced InflammationTime-Lapse Imaging of Necroptosis and DAMP Release at Single-Cell ResolutionNINJ1 mediates plasma membrane rupture during lytic cell deathOligomerization‐driven MLKL ubiquitylation antagonizes necroptosisRIPK1 Regulates RIPK3-MLKL-Driven Systemic Inflammation and Emergency HematopoiesisGasdermins: Effectors of PyroptosisThe in vivo evidence for regulated necrosisGasdermin D pore structure reveals preferential release of mature interleukin-1Viral Z-RNA triggers ZBP1-dependent cell deathReal-time single-cell imaging of protein secretionDepletion of myeloid cells exacerbates hepatitis and induces an aberrant increase in histone H3 in mouse serumToll-like Receptor 3-mediated Necrosis via TRIF, RIP3, and MLKLImmunogenic cell death and DAMPs in cancer therapyHMGB1 promotes cellular chemokine synthesis and potentiates mesenchymal stromal cell migration via Rap1 activationPlasma Membrane Pores Drive Inflammatory Cell DeathPrinciples of membrane remodeling by dynamic ESCRT-III polymersRIPK1 can mediate apoptosis in addition to necroptosis during embryonic developmentQuantitative and Dynamic Catalogs of Proteins Released during Apoptotic and Necroptotic Cell DeathProgrammed Cell Death in Immune Defense: Knowledge and PresumptionsLive-Cell Imaging Technique to Visualize DAMPs Release During Regulated Cell DeathCellular FLICE-Inhibitory Protein Regulates Tissue HomeostasisChallenges in Developing Protein Secretion Assays at a Single-Cell LevelMLKL forms cation channelsRIPK1 Blocks Early Postnatal Lethality Mediated by Caspase-8 and RIPK3A Translocation Pathway for Vesicle-Mediated Unconventional Protein SecretionDeath Receptors and Their Ligands in Inflammatory Disease and CancerFerroptotic pores induce Ca2+ fluxes and ESCRT-III activation to modulate cell death kineticsLocation, location, location: A compartmentalized view of TNF-induced necroptotic signalingKnocking ’em Dead: Pore-Forming Proteins in Immune DefenseConformational switching of the pseudokinase domain promotes human MLKL tetramerization and cell death by necroptosisRIP1 suppresses innate immune necrotic as well as apoptotic cell death during mammalian parturitionRIPK1 counteracts ZBP1-mediated necroptosis to inhibit inflammationActivation of the pseudokinase MLKL unleashes the four-helix bundle domain to induce membrane localization and necroptotic cell deathDamage control: cellular mechanisms of plasma membrane repairEvolutionary divergence of the necroptosis effector MLKLNecroptosis in development, inflammation and diseaseCell death and inflammation: the case for <scp>IL</scp>‐1 family cytokines as the canonical <scp>DAMP</scp>s of the immune systemCleavage of RIPK1 by caspase-8 is crucial for limiting apoptosis and necroptosisDAI/ZBP1/DLM-1 Complexes with RIP3 to Mediate Virus-Induced Programmed Necrosis that Is Targeted by Murine Cytomegalovirus vIRAIdentification of the hallmarks of necroptosis and ferroptosis by transmission electron microscopyMembrane Repair: Mechanisms and PathophysiologyMLKL, the Protein that Mediates Necroptosis, Also Regulates Endosomal Trafficking and Extracellular Vesicle GenerationToll-like receptors activate programmed necrosis in macrophages through a receptor-interacting kinase-3–mediated pathwayNecroptosis in health and diseasesThe Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling ComplexESCRT-III Acts Downstream of MLKL to Regulate Necroptotic Cell Death and Its ConsequencesMixed Lineage Kinase Domain-like Protein MLKL Causes Necrotic Membrane Disruption upon Phosphorylation by RIP3Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosisMLKL forms disulfide bond-dependent amyloid-like polymers to induce necroptosisProgrammed Necrosis in the Cross Talk of Cell Death and InflammationMLKL Compromises Plasma Membrane Integrity by Binding to Phosphatidylinositol PhosphatesConsensus guidelines for the detection of immunogenic cell deathMixed Lineage Kinase Domain-like Protein Mediates Necrosis Signaling Downstream of RIP3 KinaseInduction of TNF Receptor I-Mediated Apoptosis via Two Sequential Signaling ComplexesZ-nucleic-acid sensing triggers ZBP1-dependent necroptosis and inflammationCryo-EM structure of the gasdermin A3 membrane poreTranslocation of mixed lineage kinase domain-like protein to plasma membrane leads to necrotic cell deathRIPK1 inhibits ZBP1-driven necroptosis during developmentMixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosisCheckpoints in TNF-Induced Cell Death: Implications in Inflammation and CancerFlotillin-mediated endocytosis and ALIX–syntenin-1–mediated exocytosis protect the cell membrane from damage caused by necroptosisRelease of chromatin protein HMGB1 by necrotic cells triggers inflammationTNF-α Induces Two Distinct Caspase-8 Activation PathwaysThe RIP1/RIP3 Necrosome Forms a Functional Amyloid Signaling Complex Required for Programmed NecrosisGut stem cell necroptosis by genome instability triggers bowel inflammationNecroptosis: The Release of Damage-Associated Molecular Patterns and Its Physiological RelevanceThe MLKL Channel in Necroptosis Is an Octamer Formed by Tetramers in a Dyadic ProcessNucleotides released by apoptotic cells act as a find-me signal to promote phagocytic clearanceA Plug Release Mechanism for Membrane Permeation by MLKLMechanism of membrane pore formation by human gasdermin‐DHMG-1 as a Late Mediator of Endotoxin Lethality in MiceCleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell deathRIP3: a molecular switch for necrosis and inflammationActive MLKL triggers the NLRP3 inflammasome in a cell-intrinsic mannerInitiation and execution mechanisms of necroptosis: an overviewNecroptosis Execution Is Mediated by Plasma Membrane Nanopores Independent of CalciumCellular Functions and Molecular Mechanisms of the ESCRT Membrane-Scission MachineryCaspase-1-dependent processing of pro-interleukin-1β is cytosolic and precedes cell death
- Data Provider (Database)
- 国立情報学研究所 : CiNii Research
- Original Data Provider (Database)
- Crossref科学研究費助成事業データベース科学研究費助成事業データベース科学研究費助成事業データベースCrossref