Wenxiang Cao, PhD
Research ScientistCards
About
Research
Publications
2026
A direct, real-time, spectrophotometric assay for measuring ENPP1-catalyzed cGAMP hydrolysis
Michalchik M, Lombardo Z, Braddock D, Cao W, De La Cruz E. A direct, real-time, spectrophotometric assay for measuring ENPP1-catalyzed cGAMP hydrolysis. Journal Of Biological Chemistry 2026, 113078. PMID: 42055331, DOI: 10.1016/j.jbc.2026.113078.Peer-Reviewed Original ResearchReal-time assayP-nitrophenyl 5'-thymidine monophosphateResistance to cancer immunotherapyNon-hydrolyzable ATP analogTime courseNucleotide substratesExtracellular hydrolasesProduct formationCancer immunotherapySpectrophotometric assayATP analogImmune surveillanceTumor microenvironmentEnzymatic activityNative substrateCancer therapyQuench-flowGMP productionENPP1Colorimetric readoutSpectroscopic assaysHigh-throughputCGAMPTumorBinding affinity
2025
Kinetic mechanism of ENPP1 ATPase: Implications for aberrant calcification disorders and enzyme replacement therapy
Michalchik M, Potchernikov T, Lester E, Braddock D, Cao W, De La Cruz E. Kinetic mechanism of ENPP1 ATPase: Implications for aberrant calcification disorders and enzyme replacement therapy. Journal Of Biological Chemistry 2025, 301: 110558. PMID: 40769408, PMCID: PMC12446537, DOI: 10.1016/j.jbc.2025.110558.Peer-Reviewed Original ResearchEctonucleotide pyrophosphatase phosphodiesterase 1ATPase cycleMolecular mechanismsExtracellular catalytic domainEnzyme replacement therapyPhysiological regulationReplacement therapyCatalytic domainATP substrateCalcification disordersATP cleavageProduct inhibitionRegulatory feedbackGlycoprotein enzymeMichaelis constantATP levelsProduct releaseATPPhosphodiesterase 1EnzymePredicting OutcomeSerum ATP levelsPhysiological concentrationsAMPKinetic analysis
2024
Bending stiffness of Toxoplasma gondii actin filaments
Cao W, Sladewski T, Heaslip A, De La Cruz E. Bending stiffness of Toxoplasma gondii actin filaments. Journal Of Biological Chemistry 2024, 301: 108101. PMID: 39706262, PMCID: PMC11786770, DOI: 10.1016/j.jbc.2024.108101.Peer-Reviewed Original ResearchConceptsActin filamentsD-loopMechanical properties of actin filamentsFilament subunitsSkeletal muscle actin filamentsProperties of actin filamentsSkeletal muscle actinMuscle actin filamentsFilament length distributionApicomplexan parasite Toxoplasma gondiiIntersubunit salt bridgesOrganelle inheritancePointed-endSubunit interactionsNeighboring subunitUnique assembly propertiesSalt bridgesSubunitFunctional consequencesSubunit dissociationVisible densityActinSubunit incorporationParasite Toxoplasma gondiiFilamentsHigh-resolution yeast actin structures indicate the molecular mechanism of actin filament stiffening by cations
Xu X, Cao W, Swift M, Pandit N, Huehn A, Sindelar C, De La Cruz E, Hanein D, Volkmann N. High-resolution yeast actin structures indicate the molecular mechanism of actin filament stiffening by cations. Communications Chemistry 2024, 7: 164. PMID: 39079963, PMCID: PMC11289367, DOI: 10.1038/s42004-024-01243-x.Peer-Reviewed Original ResearchActin filamentsVertebrate actinsActin structuresDNase I binding loopActin filament assemblyEukaryotic cell functionStructures of wild-typeNear-atomic resolution structuresPotential binding sitesActin subunitsFilament assemblyRegulatory proteinsDNase IA167ActinAdjacent subunitsRegulatory roleMolecular mechanismsVertebratesWild-typeGlutamic acidCell functionFilamentsSubunitResiduesQuantitative correlation of ENPP1 pathogenic variants with disease phenotype
Ansh A, Stabach P, Ciccone C, Cao W, De La Cruz E, Sabbagh Y, Carpenter T, Ferreira C, Braddock D. Quantitative correlation of ENPP1 pathogenic variants with disease phenotype. Bone 2024, 186: 117136. PMID: 38806089, PMCID: PMC11227391, DOI: 10.1016/j.bone.2024.117136.Peer-Reviewed Original ResearchEctonucleotide pyrophosphatase/phosphodiesterase 1Pathogenic variantsDisease phenotypeEnzyme velocityCompound heterozygotesEnzyme activityVariable enzyme activityAutosomal dominant phenotypeHigh-throughput assayAutosomal recessive formInnate immune responseENPP1 variantsDamaging variantsENPP1 deficiencyCole diseaseDominant phenotypeAutosomal dominant diseaseCatalytic velocityRecessive formEnzymePhenotypeWT levelsBio-active moleculesClinical phenotypeDominant diseasePublisher Correction: Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex
Chavali S, Chou S, Cao W, Pollard T, De La Cruz E, Sindelar C. Publisher Correction: Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex. Nature Communications 2024, 15: 2354. PMID: 38491023, PMCID: PMC10943100, DOI: 10.1038/s41467-024-46804-9.Commentaries, Editorials and LettersCryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex
Chavali S, Chou S, Cao W, Pollard T, De La Cruz E, Sindelar C. Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex. Nature Communications 2024, 15: 2059. PMID: 38448439, PMCID: PMC10918085, DOI: 10.1038/s41467-024-46179-x.Peer-Reviewed Original ResearchConceptsArp2/3 complexActin filamentsCryo-EM structureMother filamentDaughter filamentArp2/3 complex nucleates branched actin filamentsActin filament branchingBranched actin filamentsDissociation of PiADP-PiFilament branchingOrganelle movementADP stateBranch junctionsArp3A-resolutionActinArp2/3ADP-BeFxFilamentsADPPhosphate releaseFilament mechanismArp2OrganellesDistinct functional constraints driving conservation of the cofilin N-terminal regulatory tail
Sexton J, Potchernikov T, Bibeau J, Casanova-Sepúlveda G, Cao W, Lou H, Boggon T, De La Cruz E, Turk B. Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail. Nature Communications 2024, 15: 1426. PMID: 38365893, PMCID: PMC10873347, DOI: 10.1038/s41467-024-45878-9.Peer-Reviewed Original ResearchConceptsN-terminal regionActin bindingSequence requirementsLIM kinaseAnalysis of individual variantsInactivates cofilinS. cerevisiaeRegulatory tailFamily proteinsActin depolymerizationPhosphorylation sitesKinase recognitionSequence variantsInhibitory phosphorylationCofilinN-terminusIndividual variantsFunctional constraintsActinDisordered sequencesPhosphorylationSequenceBiochemical analysisSequence constraintsKinase
2023
Cofilin-mediated actin filament network flexibility facilitates 2D to 3D actomyosin shape change
Sun Z, Yadav V, Amiri S, Cao W, De La Cruz E, Murrell M. Cofilin-mediated actin filament network flexibility facilitates 2D to 3D actomyosin shape change. European Journal Of Cell Biology 2023, 103: 151379. PMID: 38168598, PMCID: PMC12128893, DOI: 10.1016/j.ejcb.2023.151379.Peer-Reviewed Original ResearchCooperative ligand binding to a double-stranded Ising lattice—Application to cofilin binding to actin filaments
Cao W, Taylor E, De La Cruz E. Cooperative ligand binding to a double-stranded Ising lattice—Application to cofilin binding to actin filaments. PNAS Nexus 2023, 2: pgad331. PMID: 37885622, PMCID: PMC10599439, DOI: 10.1093/pnasnexus/pgad331.Peer-Reviewed Original ResearchExact solutionCluster sizeIsing latticeLattice systemsBest fit parametersTransfer matrix methodInfinite onesChemical physicsMatrix methodCooperative ligandFit parametersLigand binding interactionsLinear polymersAdditional experimental informationBinding interactionsIsingSolutionDouble-stranded modelAnalysis of varietyLigandsElectron microscopyPolymersExperimental informationExperimental observationsPhysics
Academic Achievements & Community Involvement
Get In Touch
Contacts
Mailing Address
Molecular Biophysics and Biochemistry
266 Whitney Ave. , 335 Bass Building
New Haven, CT 06511
United States