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Research Associate 3, MS
Research
Research at a Glance
Yale Co-Authors
Frequent collaborators of Peili Wang's published research.
Publications Timeline
A big-picture view of Peili Wang's research output by year.
Gary Désir, MD
3Publications
433Citations
Publications
2018
Long-Term Use of GLP-1 Receptor Agonists Alter GLP-1 Receptor mRNA Expression in Hindbrain Pathways That Regulate Gastric Motility in Mice
WANG P, MAMILLAPALLI R, ZHU W, CHAN O. Long-Term Use of GLP-1 Receptor Agonists Alter GLP-1 Receptor mRNA Expression in Hindbrain Pathways That Regulate Gastric Motility in Mice. Diabetes 2018, 67 DOI: 10.2337/db18-1088-p.Peer-Reviewed Original ResearchAltmetricConceptsGLP-1R expressionGLP-1R mRNA expressionGastric motilityGLP-1RAsMRNA expressionGLP-1 receptor mRNA expressionSuppressive effectGLP-1 receptor agonistsPost-prandial glucose levelsType 2 diabetesReceptor mRNA expressionAdeno-associated viral vectorLong-term useHindbrain pathwaysIncretin systemSolitary tractGlucagon releaseReceptor agonistC57BL6 micePretreatment levelsGLP-1RGlucose levelsTherapeutic strategiesReceptor desensitizationGLP-1R.
2006
Voltage-gated potassium channel Kv1.3 regulates GLUT4 trafficking to the plasma membrane via a Ca2+-dependent mechanism
Li Y, Wang P, Xu J, Desir GV. Voltage-gated potassium channel Kv1.3 regulates GLUT4 trafficking to the plasma membrane via a Ca2+-dependent mechanism. American Journal Of Physiology - Cell Physiology 2006, 290: c345-c351. PMID: 16403947, DOI: 10.1152/ajpcell.00091.2005.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsPlasma membraneKv1.3 channel activityAmount of GLUT4GLUT4 protein translocationInsulin sensitivityChannel activityChannel inhibitionAddition of wortmanninGLUT4 traffickingInsulin-dependent pathwayProtein translocationPeripheral insulin sensitivityVoltage-gated potassium channel Kv1.3GLUT4 translocationPotassium channel Kv1.3Gene inactivationInsulin-sensitive tissuesGLUT4 proteinKv1.3 inhibitionGlucose transportPsora-4Channel Kv1.3Adipose tissueBody weightPharmacological inhibition
2005
Renalase is a novel, soluble monoamine oxidase that regulates cardiac function and blood pressure
Xu J, Li G, Wang P, Velazquez H, Yao X, Li Y, Wu Y, Peixoto A, Crowley S, Desir GV. Renalase is a novel, soluble monoamine oxidase that regulates cardiac function and blood pressure. Journal Of Clinical Investigation 2005, 115: 1275-1280. PMID: 15841207, PMCID: PMC1074681, DOI: 10.1172/jci24066.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsEnd-stage renal diseaseBlood pressureRenal diseaseCardiac functionNovel flavin adenine dinucleotide-dependent amine oxidaseFlavin adenine dinucleotide-dependent amine oxidaseSystemic blood pressurePeripheral vascular toneRenalase gene expressionCardiovascular morbiditySoluble monoamine oxidaseVascular toneAvailable therapiesPlasma concentrationsCardiac contractilityEndocrine functionEndocrine organHealthy subjectsHeart rateElectrolyte balanceCompensatory increaseSmall intestineKidneyRenalaseMonoamine oxidase
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