About
Titles
Hospital Resident
Appointments
Departments & Organizations
Education & Training
- PhD
- Boston University, Pathology & Laboratory Medicine (2023)
- MSc
- Boston University, Pathology & Laboratory Medicine (2019)
- MD
- Shahid Beheshti University of Medical Sciences (2013)
Research
Research at a Glance
Publications Timeline
A big-picture view of Razie Amraei, MD, PhD's research output by year.
22Publications
686Citations
Publications
2023
Calreticulin Regulates SARS-CoV-2 Spike Protein Turnover and Modulates SARS-CoV-2 Infectivity
Rahimi N, White M, Amraei R, Lotfollahzadeh S, Xia C, Michalak M, Costello C, Mühlberger E. Calreticulin Regulates SARS-CoV-2 Spike Protein Turnover and Modulates SARS-CoV-2 Infectivity. Cells 2023, 12: 2694. PMID: 38067122, PMCID: PMC10705507, DOI: 10.3390/cells12232694.Peer-Reviewed Original ResearchAltmetricMeSH Keywords and ConceptsConceptsSARS-CoV-2 infectivityCardiovascular complicationsS-RBDSARS-CoV-2 infectionEndothelial cellsMajor clinical hallmarksSpike proteinCOVID-19 patientsCoronavirus disease 2019SARS-CoV-2 spike proteinSARS-CoV-2S proteinProteasomal inhibitor bortezomibHuman endothelial cellsShRNA-mediated knockdownCalcium hemostasisClinical hallmarkDisease 2019Inhibitor bortezomibCalcium homeostasisAcidification of lysosomesRole of calreticulinTreatment of cellsProtein levelsComplicationsInactivation of Minar2 in mice hyperactivates mTOR signaling and results in obesity
Lotfollahzadeh S, Xia C, Amraei R, Hua N, Kandror K, Farmer S, Wei W, Costello C, Chitalia V, Rahimi N. Inactivation of Minar2 in mice hyperactivates mTOR signaling and results in obesity. Molecular Metabolism 2023, 73: 101744. PMID: 37245847, PMCID: PMC10267597, DOI: 10.1016/j.molmet.2023.101744.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsMTOR activationHigh-fat dietObesity-associated diseasesGlucose toleranceKO miceChronic diseasesPathophysiological roleBody fatMetabolic disordersHypertrophic adipocytesKnockout miceObesityAdipose tissuePhysiological negative regulatorType 2HEK-293 cellsImpaired expressionComplex disorderCell culture studiesAdipocytesDiseaseMiceDisordersMTORUnknown role
2022
PRMT4-mediated arginine methylation promotes tyrosine phosphorylation of VEGFR-2 and regulates filopodia protrusions
Hartsough E, Shelke R, Amraei R, Aryan Z, Lotfollahzadeh S, Rahimi N. PRMT4-mediated arginine methylation promotes tyrosine phosphorylation of VEGFR-2 and regulates filopodia protrusions. IScience 2022, 25: 104736. PMID: 35942094, PMCID: PMC9356023, DOI: 10.1016/j.isci.2022.104736.Peer-Reviewed Original ResearchCitationsAltmetricConceptsSrc homology domain 2Protein arginine methyltransferase 4N-terminal domain bindsFilopodia protrusionsVEGFR-2Arginine methylationDomain bindsVascular endothelial growth factor receptor 2 activationSignal transductionTyrosine phosphorylationC-SrcMolecular mechanismsDomain 2MethylationPhosphorylationAngiogenic signalingPathological angiogenesisReceptor 2 activationAngiogenic responseTumor angiogenesisVEGFR-2 inhibitorsEVH1AngiogenesisTransductionSignalingCentral Gαi2 Protein Mediated Neuro-Hormonal Control of Blood Pressure and Salt Sensitivity
Amraei R, Moreira J, Wainford R. Central Gαi2 Protein Mediated Neuro-Hormonal Control of Blood Pressure and Salt Sensitivity. Frontiers In Endocrinology 2022, 13: 895466. PMID: 35837296, PMCID: PMC9275552, DOI: 10.3389/fendo.2022.895466.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsDietary sodium intakeG protein-coupled receptorsParaventricular nucleusBlood pressureSodium intakeElectrolyte homeostasisCentral angiotensin II type 1 receptorsAcute isotonic volume expansionAngiotensin II type 1 receptorII type 1 receptorSalt sensitivityMajor public health issueAcute pharmacological activationAfferent renal nervesNeuro-hormonal responseSalt-sensitive animalsDevelopment of hypertensionSalt-resistant ratsIsotonic volume expansionHypothalamic paraventricular nucleusMultiple G protein-coupled receptorsType 1 receptorNeuro-hormonal controlGαi/oPublic health issueExtracellular vimentin is an attachment factor that facilitates SARS-CoV-2 entry into human endothelial cells
Amraei R, Xia C, Olejnik J, White M, Napoleon M, Lotfollahzadeh S, Hauser B, Schmidt A, Chitalia V, Mühlberger E, Costello C, Rahimi N. Extracellular vimentin is an attachment factor that facilitates SARS-CoV-2 entry into human endothelial cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2113874119. PMID: 35078919, PMCID: PMC8833221, DOI: 10.1073/pnas.2113874119.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsSARS-CoV-2 infectionHuman endothelial cellsSARS-CoV-2 entrySARS-CoV-2S-protein interactionEndothelial cellsIdentification of vimentinShRNA-mediated knockdownIntermediate filament proteinsBinding of vimentinHEK-293 cellsAttachment factorsViral entrySARS-CoV-2 S proteinDevelopment of therapeuticsExtracellular vimentinS protein receptorInfectious SARS-CoV-2Host cellsCellular componentsCoexpression of vimentinFilament proteinsPrimary entry receptorSARS-CoV-2 spike proteinS protein
2021
The cell adhesion molecule TMIGD1 binds to moesin and regulates tubulin acetylation and cell migration
Rahimi N, Ho R, Chandler K, De La Cena K, Amraei R, Mitchel A, Engblom N, Costello C. The cell adhesion molecule TMIGD1 binds to moesin and regulates tubulin acetylation and cell migration. Journal Of Biomedical Science 2021, 28: 61. PMID: 34503512, PMCID: PMC8427838, DOI: 10.1186/s12929-021-00757-z.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsMitotic spindle organizationERM familyΑ-tubulinSpindle organizationCell migrationApical localizationN-terminal ERM domainCRISPR/Cas9-mediated knockoutMitotic spindle assemblyCell-cell adhesionCas9-mediated knockoutFilopodia-like protrusionsNovel tumor suppressorComplex functional interplayActin organizationERM domainLysine acetylationTMIGD1Spindle assemblyCarboxyl terminusFunctional interplayMoesinCell cycleTumor suppressorEzrinCD209L/L-SIGN and CD209/DC-SIGN Act as Receptors for SARS-CoV‑2
Amraei R, Yin W, Napoleon M, Suder E, Berrigan J, Zhao Q, Olejnik J, Chandler K, Xia C, Feldman J, Hauser B, Caradonna T, Schmidt A, Gummuluru S, Mühlberger E, Chitalia V, Costello C, Rahimi N. CD209L/L-SIGN and CD209/DC-SIGN Act as Receptors for SARS-CoV‑2. ACS Central Science 2021, 7: 1156-1165. PMID: 34341769, PMCID: PMC8265543, DOI: 10.1021/acscentsci.0c01537.Peer-Reviewed Original ResearchCitationsAltmetricConceptsSARS-CoV-2 spike receptor-binding domainSARS-CoV-2SARS-CoV-2 entryL-SIGNSARS-CoV-2 infectionCD209/DC-SIGNSpike receptor-binding domainAntiviral drug developmentReceptor-binding domainCell typesHuman endothelial cellsDC-SIGNAlternative receptorLow expressionEndothelial cellsImmunofluorescence stainingCD209Virus entryACE2Disease-relevant cell typesProminent expressionCD209LKidney epitheliumReceptorsDrug developmentNEDD4 regulates ubiquitination and stability of the cell adhesion molecule IGPR-1 via lysosomal pathway
Sun L, Amraei R, Rahimi N. NEDD4 regulates ubiquitination and stability of the cell adhesion molecule IGPR-1 via lysosomal pathway. Journal Of Biomedical Science 2021, 28: 35. PMID: 33962630, PMCID: PMC8103646, DOI: 10.1186/s12929-021-00731-9.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsCell adhesion molecule IGPR-1IGPR-1Lysosomal-dependent degradationUbiquitin E3Vivo co-immunoprecipitation assaysWild-type Nedd4Knockdown of NEDD4Polyproline-rich motifCritical cellular processesCell-cell adhesionCo-immunoprecipitation assaysTreatment of cellsCell surface levelsHEK-293 cellsA375 melanoma cellsWW domainsCellular processesRich motifLysosomal pathwayC-terminusNedd4Key regulatorLysosomal inhibitorsMolecular mechanismsMelanoma cell lines
2020
Transmembrane and Immunoglobulin Domain Containing 1, a Putative Tumor Suppressor, Induces G2/M Cell Cycle Checkpoint Arrest in Colon Cancer Cells
De La Cena K, Ho R, Amraei R, Woolf N, Tashjian J, Zhao Q, Richards S, Walker J, Huang J, Chitalia V, Rahimi N. Transmembrane and Immunoglobulin Domain Containing 1, a Putative Tumor Suppressor, Induces G2/M Cell Cycle Checkpoint Arrest in Colon Cancer Cells. American Journal Of Pathology 2020, 191: 157-167. PMID: 33129760, PMCID: PMC7788663, DOI: 10.1016/j.ajpath.2020.09.015.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsCell cycleColorectal cancerCell cycle checkpoint arrestCell cycle inhibitor proteinsNovel tumor suppressor geneFull molecular mechanismsPutative tumor suppressorColon cancer cellsTumor suppressor geneG2/M phaseSporadic human colorectal cancerNormal intestinal epithelial cellsEpigenetic mechanismsCheckpoint arrestTMIGD1Inhibitor proteinNovel potential therapeutic targetIntestinal epithelial cellsMolecular mechanismsTumor suppressorPoor overall survivalSuppressor geneDevelopment of adenomasImmunoglobulin domainHuman colorectal cancerCell adhesion molecule IGPR-1 activates AMPK connecting cell adhesion to autophagy
Amraei R, Alwani T, Ho R, Aryan Z, Wang S, Rahimi N. Cell adhesion molecule IGPR-1 activates AMPK connecting cell adhesion to autophagy. Journal Of Biological Chemistry 2020, 295: 16691-16699. PMID: 32978258, PMCID: PMC7864065, DOI: 10.1074/jbc.ra120.014790.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsMeSH KeywordsAmino Acid MotifsAMP-Activated Protein KinasesAnimalsAutophagyAutophagy-Related Protein-1 HomologBeclin-1CD28 AntigensCell AdhesionHEK293 CellsHumansI-kappa B KinaseIntracellular Signaling Peptides and ProteinsLipopolysaccharidesMicroscopy, FluorescenceMicrotubule-Associated ProteinsPhosphorylationPrimatesRNA, Guide, KinetoplastidaSirolimusSubstrate SpecificityConceptsIGPR-1Cell adhesionCell adhesion molecule IGPR-1Proline-rich receptor-1Serine/threonine kinaseKey serine/threonine kinaseAmino acid starvationBeclin-1Phosphorylation of AMPThreonine kinaseAutophagy stimuliKinase assaysLC3-II levelsCellular stressNutrient deprivationProtein kinaseCell adhesion moleculeProtein ULK1IκB kinase βEndothelial barrier functionKinase βCellular assaysPhosphorylationSubsequent activationCell detachment