2020
Force and phosphate release from Arp2/3 complex promote dissociation of actin filament branches
Pandit NG, Cao W, Bibeau J, Johnson-Chavarria EM, Taylor EW, Pollard TD, De La Cruz EM. Force and phosphate release from Arp2/3 complex promote dissociation of actin filament branches. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 13519-13528. PMID: 32461373, PMCID: PMC7306818, DOI: 10.1073/pnas.1911183117.Peer-Reviewed Original ResearchConceptsActin filament branchesArp2/3 complexMother filamentFilament branchesTotal internal reflection fluorescence microscopyEssential cellular functionsMechanical forcesActin filament networkReflection fluorescence microscopyCellular functionsActin networkCell motilityComplex generatesActin filamentsArp2/3Filament networkFluorescence microscopyState 1Branch junctionsState 2FilamentsComplexesPhosphate releaseMuscle actinADP
2008
The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering Complexes
Cai Y, Chin HF, Lazarova D, Menon S, Fu C, Cai H, Sclafani A, Rodgers DW, De La Cruz EM, Ferro-Novick S, Reinisch KM. The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering Complexes. Cell 2008, 133: 1202-1213. PMID: 18585354, PMCID: PMC2465810, DOI: 10.1016/j.cell.2008.04.049.Peer-Reviewed Original ResearchThe Roles of Thymosin β4 in Cell Migration and Cell-to-Cell Signaling in Disease
Au J, Krendel M, Safer D, De La Cruz E. The Roles of Thymosin β4 in Cell Migration and Cell-to-Cell Signaling in Disease. Protein Reviews 2008, 218-228. DOI: 10.1007/978-0-387-71749-4_9.Peer-Reviewed Original ResearchΒ-thymosinsMetazoan cellsExtracellular cuesCell signalingFree actin monomersFilament elongationMonomeric actinActin monomersCell migrationInduction of angiogenesisRegulatory effectsTumor metastasisThymosin β4CellsTherapeutic applicationsSignalingPolypeptideActinΒ4High concentrationsAngiogenesisInductionFamilyComplexesTβ4
2007
Contributions from All Over
AU JK, DE LA CRUZ EM, SAFER D. Contributions from All Over. Annals Of The New York Academy Of Sciences 2007, 1112: 38-44. PMID: 17468230, DOI: 10.1196/annals.1415.015.Peer-Reviewed Original ResearchConceptsProline residuesActin bindingWild-type complexHydrophobic contactsSite-directed mutagenesisStrong actin bindingHydrophobic residuesAlanine residuesCysteine 374Slow association rateRate of associationResiduesMutantsComplex variesTbeta4Association rateSulfo-1BindingCis-trans isomerizationKinetic basisComplexesPro27Pro29Lys19MutagenesisFluorescence of 2-aminopurine reveals rapid conformational changes in the RB69 DNA polymerase-primer/template complexes upon binding and incorporation of matched deoxynucleoside triphosphates
Zhang H, Cao W, Zakharova E, Konigsberg W, De La Cruz EM. Fluorescence of 2-aminopurine reveals rapid conformational changes in the RB69 DNA polymerase-primer/template complexes upon binding and incorporation of matched deoxynucleoside triphosphates. Nucleic Acids Research 2007, 35: 6052-6062. PMID: 17766250, PMCID: PMC2094073, DOI: 10.1093/nar/gkm587.Peer-Reviewed Original ResearchConceptsHydroxyl groupsNucleotidyl transfer reactionMinimal kinetic schemeConformational changesDetectable fluorescence changeChemical quenchTransfer reactionsDependent fluorescence enhancementFluorescence enhancementFluorescence quenchingFluorescent probeRapid conformational changesTemplate complexN-positionRate constantsFluorescence changesRapid fluorescenceTernary complexKinetic schemeComplexesTemplating baseDependent conformational changesDp/TTemplateFluorescence