2024
The human CD47 checkpoint is targeted by an immunosuppressive Aedes aegypti salivary factor to enhance arboviral skin infectivity
Marin-Lopez A, Huck J, Esterly A, Azcutia V, Rosen C, Garcia-Milian R, Sefik E, Vidal-Pedrola G, Raduwan H, Chen T, Arora G, Halene S, Shaw A, Palm N, Flavell R, Parkos C, Thangamani S, Ring A, Fikrig E. The human CD47 checkpoint is targeted by an immunosuppressive Aedes aegypti salivary factor to enhance arboviral skin infectivity. Science Immunology 2024, 9: eadk9872. PMID: 39121194, DOI: 10.1126/sciimmunol.adk9872.Peer-Reviewed Original ResearchConceptsSuppress antiviral responsesArthropod proteinsPathogen replicationAntiviral responseProtein AVertebrate hostsMosquito salivary proteinsUp-regulatedBlood feedingHuman macrophagesPleomorphic effectsSkin infectionsZika virus disseminationInhibit proinflammatory responsesSalivary proteinsProteinNatural ligandWhite blood cellsHuman skin explantsProinflammatory responseMosquito salivaVirus disseminationHuman CD47Salivary factorsArbovirus infection
2008
Defective signal transduction in B lymphocytes lacking presenilin proteins
Yagi T, Giallourakis C, Mohanty S, Scheidig C, Shen J, Zheng H, Xavier RJ, Shaw AC. Defective signal transduction in B lymphocytes lacking presenilin proteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 2008, 105: 979-984. PMID: 18195359, PMCID: PMC2242696, DOI: 10.1073/pnas.0707755105.Peer-Reviewed Original ResearchConceptsPresenilin proteinsDiverse cellular processesMultiple genomic datasetsPS proteinsSignal transduction eventsWhole-genome datasetsDefective signal transductionNotch family membersCalcium-dependent signalingCellular processesProtein substratesSignal transductionTransduction eventsProtein interactionsPS2 functionUnanticipated roleConditional alleleGenomic datasetsToll-like receptor signalingPathway analysisIntegrative analysisPosttranslational cleavageReceptor signalingRecombinase expressionProtein
1991
Cytoplasmic tail deletion converts membrane immunoglobulin to a phosphatidylinositol-linked form lacking signaling and efficient antigen internalization functions
Mitchell RN, Shaw AC, Weaver YK, Leder P, Abbas AK. Cytoplasmic tail deletion converts membrane immunoglobulin to a phosphatidylinositol-linked form lacking signaling and efficient antigen internalization functions. Journal Of Biological Chemistry 1991, 266: 8856-8860. PMID: 2026599, DOI: 10.1016/s0021-9258(18)31524-2.Peer-Reviewed Original ResearchConceptsPhosphatidylinositol-linked formSignal transduction functionsPhosphatidylinositol-linked proteinsB cell lymphoma A20Cytoplasmic domainCytoplasmic tailMembrane proteinsSignal transductionTransmembrane proteinTransmembrane residuesTransduction functionMolecular massInternalization functionProteinAntigen receptorAntigen presentationEarly eventsMembrane immunoglobulinIg moleculesMode of expressionTransductionMIgMB lymphocytesSignalingResidues
1987
Allelic Exclusion in Transgenic Mice That Express the Membrane form of Immunoglobulin μ
Nussenzweig M, Shaw A, Sinn E, Danner D, Holmes K, Morse H, Leder P. Allelic Exclusion in Transgenic Mice That Express the Membrane form of Immunoglobulin μ. Science 1987, 236: 816-819. PMID: 3107126, DOI: 10.1126/science.3107126.Peer-Reviewed Original ResearchConceptsMembrane-bound formAllelic exclusionMembrane-bound proteinsMu chainsMu chain geneHeavy chainHeavy chain allelesHuman genesTransgenic miceImmunoglobulin μMessenger RNAMembrane formChain geneAntibody genesB cellsGenesImmunoglobulin M heavy chainHuman mu chainsMouse systemCellsRegulationMolecular formsRNATransgeneProtein