about
Pyroptotic cell death defends against intracellular pathogensTLR5 and Ipaf: dual sensors of bacterial flagellin in the innate immune systemCytoplasmic flagellin activates caspase-1 and secretion of interleukin 1beta via IpafThe Prostaglandin E2-EP3 Receptor Axis Regulates Anaplasma phagocytophilum-Mediated NLRC4 Inflammasome ActivationBacteriophages in the evolution of pathogen-host interactionsInvB is a type III secretion chaperone specific for SspA.Inflammasome-mediated pyroptotic and apoptotic cell death, and defense against infection.Detection of cytosolic bacteria by inflammatory caspases.Innate immune detection of bacterial virulence factors via the NLRC4 inflammasomeCutting edge: Cytosolic bacterial DNA activates the inflammasome via Aim2.Guanylate binding proteins promote caspase-11-dependent pyroptosis in response to cytoplasmic LPS.Activation of the NLRP3 inflammasome by intracellular poly I:CCaspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria.Salmonella typhimurium impedes innate immunity with a mast-cell-suppressing protein tyrosine phosphatase, SptP.Yersinia pestis activates both IL-1β and IL-1 receptor antagonist to modulate lung inflammation during pneumonic plagueNLRC4 and TLR5 each contribute to host defense in respiratory melioidosis.Canonical Inflammasomes Drive IFN-γ to Prime Caspase-11 in Defense against a Cytosol-Invasive Bacterium.Guanylate binding proteins enable rapid activation of canonical and noncanonical inflammasomes in Chlamydia-infected macrophages.Inflammasomes Coordinate Pyroptosis and Natural Killer Cell Cytotoxicity to Clear Infection by a Ubiquitous Environmental Bacterium.Interferon-β therapy against EAE is effective only when development of the disease depends on the NLRP3 inflammasome.Pseudomonas aeruginosa activates caspase 1 through Ipaf.Pyroptosis triggers pore-induced intracellular traps (PITs) that capture bacteria and lead to their clearance by efferocytosisSalmonella and Caspase-1: A complex Interplay of Detection and Evasion.Caspase-1-induced pyroptotic cell death.Mechanisms of NOD-like receptor-associated inflammasome activation.Reassessing the Evolutionary Importance of Inflammasomes.Dietary Salt Exacerbates Experimental Colitis.IL-1β, IL-18, and eicosanoids promote neutrophil recruitment to pore-induced intracellular traps following pyroptosis.Salmonella effectors translocated across the vacuolar membrane interact with the actin cytoskeleton.Down with doublespeak: NAIP/NLRC4 inflammasomes get specificYopM puts caspase-1 on ice.Caspase-11 protects against bacteria that escape the vacuole.Salmonella typhimurium leucine-rich repeat proteins are targeted to the SPI1 and SPI2 type III secretion systems.Cutting edge: Mouse NAIP1 detects the type III secretion system needle protein.Cytoplasmic LPS activates caspase-11: implications in TLR4-independent endotoxic shock.miniMAVS, You Complete Me!Generation of a Listeria vaccine strain by enhanced caspase-1 activation.The RIP1-RIP3 complex initiates mitochondrial fission to fuel NLRP3.Detection of pyroptosis by measuring released lactate dehydrogenase activity.Virus binding to a plasma membrane receptor triggers interleukin-1 alpha-mediated proinflammatory macrophage response in vivo.
P50
Q27022620-E00F2298-5CEB-429D-A563-CC23C8C17D12Q28240172-B7F72F3E-ED4F-48F6-A748-2D6D6BC35161Q28506503-8E588215-EDE0-49DC-BB91-AAABE7D6EAD6Q28553346-B4E17A36-868D-458D-8A1C-CD92B22FDB0EQ33712790-C0282314-7D77-4CF7-B923-1768232388F4Q33792217-1C09F92E-2F14-48FD-A941-A69F49E682EFQ34036902-B5D491DA-C432-4513-9E99-C24C48D9AA64Q34039994-406D9B91-7880-4846-8847-52B2C06C553BQ34357994-4452492B-AFD9-4182-ACB8-8B92C471D347Q34361030-48522FDD-ACA1-4064-9297-01916E29AB05Q34414371-C7C522BB-C68D-43F4-B1CF-381D1E3E7822Q34421170-0FD5AB8F-B661-45EF-BB60-949116B9CFD8Q34678595-C95D09C6-C295-4F40-ACD4-C3BD89DDDEEAQ35077679-7F19AC40-0011-49FB-88EF-157E9A815730Q35189003-7BB083B8-31B4-42C9-913F-78C59AB3E862Q35260658-FDAE9BE8-015A-44DF-91DE-EBB61583FFBAQ36053123-1EBBCFA0-3CA4-465F-95FC-7BD7C2F3AFC0Q36281253-64BBC890-B695-4DB6-8C85-BE1A6551EDFEQ36304356-0EC98FF0-BE9C-445F-9AFC-FD37AC0CBA64Q36431053-39841AA5-684F-4B6E-B40C-88AACB14020BQ36497402-484D93D1-D805-4F8C-A1CA-34F6CF026EF3Q37272072-451C22AF-8C21-4D15-BB4D-571E5623F65EQ37915291-AE41EF1E-C58E-4F5D-A9BC-724F1A06FCB3Q37925075-6B56E4A6-B11B-4D01-8CC1-CE1514545EDDQ38140207-106D4CF8-B86D-4A32-BA29-622043F07B8CQ38708563-67B0E155-B816-4D8A-AB69-47876A0B00ECQ40163090-3D61713C-E106-4DB3-8BA8-C2F4BF2EA951Q40499874-D77EEDCC-726A-42F4-A195-842A523D363DQ40658475-86641C09-9CE0-4E29-97A7-2561D98702CBQ40928906-A119B0D7-CADC-4C7F-8401-440E50F6156AQ41404512-B444A977-7459-4969-BF60-6EF9AB34F206Q41452200-F3F13B9B-99D3-4D05-9585-014726C6FE3DQ41481295-F7DE76DE-A31D-4D52-B306-5E4B092D7CC7Q41883043-E62C8319-BC9B-4201-81CF-ECC7EA57B750Q41970918-935A4A59-7EF9-4AF2-B3BA-319CB8596B5DQ42156567-ED8F0C49-9739-4480-BCF2-335D1D133756Q42181071-76813315-2BA8-4323-827A-EA6E595BE4D9Q42365903-94480B5C-45E1-470B-A1C0-8FCB3769DF16Q42576230-1583FC44-6D2A-4EEA-A94A-DBE802C57B2BQ42579980-1D8FFA4C-C622-47EC-BF5B-9F34DDB5EFDD
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Edward A. Miao
@ast
Edward A. Miao
@en
Edward A. Miao
@es
Edward A. Miao
@sl
type
label
Edward A. Miao
@ast
Edward A. Miao
@en
Edward A. Miao
@es
Edward A. Miao
@sl
prefLabel
Edward A. Miao
@ast
Edward A. Miao
@en
Edward A. Miao
@es
Edward A. Miao
@sl
P106
P1153
6603412614
P21
P31
P496
0000-0001-7295-3490