2023
Progranulinopathy: A diverse realm of disorders linked to progranulin imbalances
Huang G, Jian J, Liu C. Progranulinopathy: A diverse realm of disorders linked to progranulin imbalances. Cytokine & Growth Factor Reviews 2023, 76: 142-159. PMID: 37981505, PMCID: PMC10978308, DOI: 10.1016/j.cytogfr.2023.11.001.Peer-Reviewed Original ResearchDiverse functionsRegulation of tumorigenesisChaperone activityMultiple membrane receptorsMultitude of processesGrowth factor-like moleculesExtracellular functionsNeuronal degenerative diseasesLysosomal proteinsIntricate mechanismsLysosomal functionMembrane receptorsIntracellular componentsLysosomal hydrolasesDiverse arrayLysosomal storage diseaseProteinNeural proliferationGRN geneCritical roleGrowth factorIntricate interplayRole of progranulinPathophysiological processesStorage diseaseAllosteric inhibition of the T cell receptor by a designed membrane ligand
Ye Y, Morita S, Chang J, Buckley P, Wilhelm K, DiMaio D, Groves J, Barrera F. Allosteric inhibition of the T cell receptor by a designed membrane ligand. ELife 2023, 12: e82861. PMID: 37796108, PMCID: PMC10554751, DOI: 10.7554/elife.82861.Peer-Reviewed Original ResearchConceptsT cell receptorTCR activationCD3ζ subunitsTM ligandsComplex molecular machinesReceptor tyrosine kinase EphA2Cell receptorTM domainTransmembrane domainNative nanodiscsTCR subunitsAllosteric changesTM bundleCytoplasmic sideTM regionMolecular mechanismsExtracellular domainAllosteric inhibitionLck phosphorylationMolecular machinesMembrane receptorsAberrant activationSubunitsMembrane ligandsDecades of investigation
2021
Dormant spores sense amino acids through the B subunits of their germination receptors
Artzi L, Alon A, Brock K, Green A, Tam A, Ramírez-Guadiana F, Marks D, Kruse A, Rudner D. Dormant spores sense amino acids through the B subunits of their germination receptors. Nature Communications 2021, 12: 6842. PMID: 34824238, PMCID: PMC8617281, DOI: 10.1038/s41467-021-27235-2.Peer-Reviewed Original ResearchConceptsAmino acid-polyamine-organocation superfamilyEvolutionary co-variation analysisL-alanine recognitionB subunitStress-resistant sporesSuperfamily of transportersPutative membrane receptorL-alanineResponse to L-alanineGerABNutrient sensingBacillus subtilisGerminant receptorsBulky residuesAmino acidsMembrane receptorsPrototypic receptorNutrient detectionSporesGerminationCo-variance analysisL-serineMutationsL-leucineBacillalesThe butyrophilin 1a1 knockout mouse revisited: Ablation of Btn1a1 leads to concurrent cell death and renewal in the mammary epithelium during lactation
Jeong J, Kadegowda AKG, Meyer TJ, Jenkins LM, Dinan JC, Wysolmerski JJ, Weigert R, Mather IH. The butyrophilin 1a1 knockout mouse revisited: Ablation of Btn1a1 leads to concurrent cell death and renewal in the mammary epithelium during lactation. FASEB BioAdvances 2021, 3: 971-997. PMID: 34938960, PMCID: PMC8664049, DOI: 10.1096/fba.2021-00059.Peer-Reviewed Original ResearchWild-type cellsAcute phase response genesCell death pathwaysMouse linesFos/JunMutant mouse linesMammary epitheliumMammary epithelial cellsButyrophilin 1A1Secretion complexDeath routeProteomic analysisNuclear DNADeath pathwaysResponse genesOptimal milk productionExpression of cyclinsCaspase-8Upregulation of Ki67Cell deathMembrane receptorsType cellsLipid dropletsRedox enzymesLysosomal lysis
2020
Sperm ion channels and transporters in male fertility and infertility
Wang H, McGoldrick LL, Chung JJ. Sperm ion channels and transporters in male fertility and infertility. Nature Reviews Urology 2020, 18: 46-66. PMID: 33214707, PMCID: PMC7852504, DOI: 10.1038/s41585-020-00390-9.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsSperm ion channelsIon channelsSperm cellsMammalian sperm cellsIon signalingDynamic regulationDefective sperm functionFemale reproductive tractChannel CatSperHuman geneticsMembrane receptorsMale fertilityHealth careAttractive targetDirect electrophysiological recordingsOverall health careHuman infertilityReproductive health careSperm functionPrincipal Ca2Development of contraceptivesSperm activityGene variantsReproductive tractGenetic abnormalities
2016
Rapid steroid hormone actions via membrane receptors
Schwartz N, Verma A, Bivens CB, Schwartz Z, Boyan BD. Rapid steroid hormone actions via membrane receptors. Biochimica Et Biophysica Acta 2016, 1863: 2289-2298. PMID: 27288742, DOI: 10.1016/j.bbamcr.2016.06.004.Peer-Reviewed Original ResearchConceptsDNA-binding sitesPhosphoinositide-3 kinaseClassical steroid hormone receptorsMembrane-bound receptorsNumber of pathwaysDevelopmental functionsGene transcriptionSteroid hormone actionSteroid hormonesImpact tumorigenesisCell cycleCellular activitiesMembrane receptorsPhospholipase DSteroid hormone receptorsPhospholipase CReceptor counterpartsRapid steroidCancer cellsNovel receptorPathwayDihydroxy vitamin D3Cytosolic receptorHormone actionHormone receptors
2015
Signaling pathways in biliary epithelial cells
Leite M, Guerra M, Andrade V, Nathanson M. Signaling pathways in biliary epithelial cells. 2015, 15-33. DOI: 10.1002/9781118663387.ch2.Peer-Reviewed Original ResearchBiliary epithelial cellsEpithelial cellsFormation of bileSurface membrane receptorsBiliary treeDuctal bileIntracellular signal transduction pathwaysCanalicular bileGrowth factorCholangiocytesBileCell functionPeptide hormonesBile saltsDetoxification of xenobioticsMembrane receptorsSignal transduction pathwaysTransduction pathwaysReceptors and Transduction Mechanisms II: Indirectly Coupled Receptor/Ion Channel Systems
Levitan I, Kaczmarek L. Receptors and Transduction Mechanisms II: Indirectly Coupled Receptor/Ion Channel Systems. 2015, 263-294. DOI: 10.1093/med/9780199773893.003.0012.ChaptersProtein phosphorylationSecond messenger-dependent protein kinasesReceptor-channel couplingIon channel proteinsAppropriate biological responseExtracellular signalsDirect phosphorylationSpecific membrane receptorsProtein kinaseRegulatory componentsChannel proteinsSecond messenger systemsMembrane receptorsTransduction mechanismsIon channelsPhosphorylationBiological responsesMessenger systemsIon channel systemsDiversityTarget cellsSignal recognitionNeuronal excitabilityCellsKinaseRole of Mechanotransduction in Vascular Biology
Humphrey JD, Schwartz MA, Tellides G, Milewicz DM. Role of Mechanotransduction in Vascular Biology. Circulation Research 2015, 116: 1448-1461. PMID: 25858068, PMCID: PMC4420625, DOI: 10.1161/circresaha.114.304936.Peer-Reviewed Original ResearchConceptsExtracellular matrixRole of mechanotransductionExtracellular matrix constituentsActomyosin filamentsMembrane receptorsDysfunctional mechanosensingVascular biologyAortic aneurysmNew therapeutic strategiesContractile proteinsThoracic aortic aneurysmIntramural cellsCellsMechanobiological processesMatrix constituentsAcute dissectionAortic cellsAortic diseaseMechanosensingTherapeutic strategiesHemodynamic loadGenesProgressive enlargementReceptorsMechanoregulation
2012
Modulation of gap junction channels and hemichannels by growth factors
Schalper K, Riquelme M, Brañes M, Martínez A, Vega J, Berthoud V, Bennett M, Sáez J. Modulation of gap junction channels and hemichannels by growth factors. Molecular Omics 2012, 8: 685-698. PMID: 22218428, DOI: 10.1039/c1mb05294b.Peer-Reviewed Original ResearchConceptsGap junction channelsTransduction pathwaysGrowth factor signal transduction pathwaysJunction channelsNumerous cellular processesCell-cell communicationCell-cell channelsGrowth factorSignal transduction pathwaysProtein kinase-dependent mechanismNormal cellular responseCellular transduction pathwaysKinase-dependent mechanismCell membrane receptorsGap junction hemichannelsCellular coordinationCellular processesProtein kinaseCellular responsesCell stageMembrane receptorsMembrane channelsCell typesFunctional consequencesChannel insertion
2009
Signaling Pathways in Biliary Epithelial Cells
Leite M, Andrade V, Nathanson M. Signaling Pathways in Biliary Epithelial Cells. 2009, 25-39. DOI: 10.1007/978-3-642-00150-5_2.Peer-Reviewed Original ResearchBiliary epithelial cellsEpithelial cellsFormation of bileSurface membrane receptorsBiliary treeDuctal bileIntracellular signal transduction pathwaysCanalicular bileGrowth factorCholangiocytesBileCell functionPeptide hormonesBile saltsDetoxification of xenobioticsMembrane receptorsSignal transduction pathwaysTransduction pathwaysProtein-protein interactions among ion channels regulate ion transport in the kidney.
Boulpaep E. Protein-protein interactions among ion channels regulate ion transport in the kidney. Bulletin Et Mémoires De L'Académie Royale De Médecine De Belgique 2009, 164: 133-41; discussion 141-2. PMID: 20120088.Peer-Reviewed Original ResearchConceptsAMP kinaseProtein CFTRCFTR channel gatingMembrane transport proteinsProtein-protein interactionsMembrane-attached proteinsSerine-threonine kinaseRegulation of transportKir 1.1Mg-ATPIon transportExtracellular agonistsMembrane proteinsTransport proteinsChannel gatingIntracellular ATP concentrationIntracellular messengerMembrane receptorsCFTRMetabolic signalsIon channelsChloride channelsEpithelial ion transportDirect interactionRenal K secretion
2007
Notch regulates cell fate and dendrite morphology of newborn neurons in the postnatal dentate gyrus
Breunig JJ, Silbereis J, Vaccarino FM, Šestan N, Rakic P. Notch regulates cell fate and dendrite morphology of newborn neurons in the postnatal dentate gyrus. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104: 20558-20563. PMID: 18077357, PMCID: PMC2154470, DOI: 10.1073/pnas.0710156104.Peer-Reviewed Original ResearchConceptsAbrogation of NotchCell cycle exitNeuronal fate determinationPrecursor cellsTransit-amplifying cellsFate determinationInducible gainCell fateCycle exitNeural precursor cellsModulates SurvivalMolecular controlPostnatal progenitor cellsLifelong additionHippocampal morphogenesisDifferentiation statePostnatal dentate gyrusNewborn granule cellsMembrane receptorsNeural stemGenetic ablationExpression of Notch1Structural plasticityProgenitor cellsEnvironmental modulators1,25-Dihydroxyvitamin D3 induces expression of the Wnt signaling co-regulator LRP5 via regulatory elements located significantly downstream of the gene's transcriptional start site
Fretz JA, Zella LA, Kim S, Shevde NK, Pike JW. 1,25-Dihydroxyvitamin D3 induces expression of the Wnt signaling co-regulator LRP5 via regulatory elements located significantly downstream of the gene's transcriptional start site. The Journal Of Steroid Biochemistry And Molecular Biology 2007, 103: 440-445. PMID: 17229572, PMCID: PMC1868540, DOI: 10.1016/j.jsbmb.2006.11.018.Peer-Reviewed Original ResearchConceptsTranscriptional start siteGene transcriptional start siteChIP-chip analysisLRP5/LRP6Chromatin structureHuman genomeRegulatory regionsStart siteRegulatory elementsWnt familyHeterologous promoterCanonical WntMembrane receptorsMRNA transcriptsWntSecreted memberOsteoblastic cellsLRP5GenesVDRELRP5 geneBone formationProteinLrp5 locusOsteoblast numberEmploying Systems Biology to Quantify Receptor Tyrosine Kinase Signaling in Time and Space
Kholodenko B. Employing Systems Biology to Quantify Receptor Tyrosine Kinase Signaling in Time and Space. 2007, 300-318. DOI: 10.1007/978-1-59745-531-2_16.Peer-Reviewed Original ResearchProtein phosphorylation networksReceptor tyrosine kinase signalingTrafficking of endosomesPivotal physiological processesTyrosine kinase signalingPlasma membrane receptorsPhosphorylation networksUltrasensitive switchPhosphorylated kinasesKinase signalingEnvironmental cuesCell motilitySystems biologyNegative feedback circuitPhysiological processesCellular responsesMembrane receptorsLiving cellsCellular architectureSpatiotemporal response patternsComputational approachIntricate relationshipEndosomesKinaseMitosis
2005
MIBG and somatostatin receptor analogs in children: current concepts on diagnostic and therapeutic use.
Pashankar FD, O'Dorisio MS, Menda Y. MIBG and somatostatin receptor analogs in children: current concepts on diagnostic and therapeutic use. Journal Of Nuclear Medicine 2005, 46 Suppl 1: 55s-61s. PMID: 15653652.Peer-Reviewed Original ResearchMeSH Keywords3-IodobenzylguanidineAnimalsChildChild, PreschoolClinical Trials as TopicHumansInfantInfant, NewbornNeuroblastomaOctreotidePatient SelectionPentetic AcidPractice Guidelines as TopicPractice Patterns, Physicians'Radiation InjuriesRadionuclide ImagingRadiopharmaceuticalsSomatostatinTreatment OutcomeConceptsSolid tumorsCertain pediatric tumorsSomatostatin receptor analoguesPediatric solid tumorsMetaiodobenzylguanidine scanNuclear imaging techniquesBone scanPediatric tumorsFalse transmitterTherapeutic useCell membrane receptorsReceptor analoguesYoung adultsTumorsMolecular targetsCurrent conceptsMIBGScansMembrane receptorsSpecific ligandsImaging techniquesChildrenSubcellular organellesCellular proteinsDiagnosis
2003
Tyr-317 Phosphorylation Increases Shc Structural Rigidity and Reduces Coupling of Domain Motions Remote from the Phosphorylation Site as Revealed by Molecular Dynamics Simulations*
Suenaga A, Kiyatkin AB, Hatakeyama M, Futatsugi N, Okimoto N, Hirano Y, Narumi T, Kawai A, Susukita R, Koishi T, Furusawa H, Yasuoka K, Takada N, Ohno Y, Taiji M, Ebisuzaki T, Hoek JB, Konagaya A, Kholodenko BN. Tyr-317 Phosphorylation Increases Shc Structural Rigidity and Reduces Coupling of Domain Motions Remote from the Phosphorylation Site as Revealed by Molecular Dynamics Simulations*. Journal Of Biological Chemistry 2003, 279: 4657-4662. PMID: 14613932, DOI: 10.1074/jbc.m310598200.Peer-Reviewed Original ResearchConceptsPhosphotyrosine bindingTyr-317Shc phosphorylationSH2 domainC-terminal Src homology 2 domainSrc homology 2 domainRAS/RAF/MEK/ERK pathwayShc adaptor proteinRaf/MEK/ERK pathwayMEK/ERK pathwayReceptor tyrosine kinasesShc functionPhosphorylated ShcPhosphorylation sitesAdaptor proteinLinker regionShcTyrosine kinaseERK pathwayMembrane receptorsPhosphorylationDomain motionMolecular dynamics simulationsNumerous partnersDomain couplingAssessment of Insulin-Like Growth Factors and Mutagen Sensitivity as Predictors of Lung Cancer Risk
Wu X, Yu H, Makan N, Spitz M. Assessment of Insulin-Like Growth Factors and Mutagen Sensitivity as Predictors of Lung Cancer Risk. Methods In Molecular Medicine 2003, 75: 279-287. PMID: 12407747, DOI: 10.1385/1-59259-324-0:279.Peer-Reviewed Original ResearchMeSH Keywords7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxideBleomycinChromatidsChromosome AberrationsEnzyme-Linked Immunosorbent AssayHumansInsulin-Like Growth Factor Binding Protein 3Insulin-Like Growth Factor IInsulin-Like Growth Factor IILung NeoplasmsLymphocytesMutagenicity TestsMutagensPredictive Value of TestsRisk FactorsConceptsInsulin-like growth factorSignal transduction pathwaysGrowth factorCell cycle progressionCell membrane receptorsTransduction pathwaysBcl proteinsMAP kinaseLung cancer cellsIGF-1 receptorCell deathMembrane receptorsS phaseAntiproliferative moleculesBinding of IGFBax proteinCell proliferationLung cancer riskImportant functionsProteinCancer cellsCyclin D1Retinoic acidTypes of peptidesMitogenic action
2002
Rapid vascular cell responses to estrogen and membrane receptors
Haynes MP, Li L, Russell KS, Bender JR. Rapid vascular cell responses to estrogen and membrane receptors. Vascular Pharmacology 2002, 38: 99-108. PMID: 12379956, DOI: 10.1016/s0306-3623(02)00133-7.Peer-Reviewed Original ResearchConceptsSignal transduction cascadeTransduction cascadeG protein-coupled receptorsMembrane-localized estrogen receptorsEstrogen receptorTranscription factorsMAP kinaseApparent coronary heart diseaseRapid consequencesCellular responsesCellular localizationMembrane receptorsCoronary heart diseaseAge-matched malesEffects of estrogenVascular cell responsesSmooth muscle cellsVariety of estrogenVascular cellsMuscle cellsComplex formationPremenopausal womenHeart diseaseVascular wallMarked gender differences
2001
A serum prolactin-binding protein: implications for growth hormone
Dannies P. A serum prolactin-binding protein: implications for growth hormone. Trends In Endocrinology And Metabolism 2001, 12: 427-428. PMID: 11701331, DOI: 10.1016/s1043-2760(01)00497-0.Peer-Reviewed Original Research
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