Enrique M. De La Cruz, PhD

• Demetrios Braddock
• Ewa Folta-Stogniew
• Jimin Wang
• Joseph Madri
• Karin Reinisch
• Mark Hochstrasser
• Mark Mooseker
• Paul Stabach
• Stephanie Thorn
• Wenxiang Cao

Biochemistry; Biophysics; Cytoskeleton; Kinetics; Molecular Biology; Thermodynamics; RNA Helicases

• Cooperative ligand binding to a double-stranded Ising lattice—Application to cofilin binding to actin filamentsCao 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.
• Friction patterns guide actin network contractionColin A, Orhant-Prioux M, Guérin C, Savinov M, Cao W, Vianay B, Scarfone I, Roux A, De La Cruz E, Mogilner A, Théry M, Blanchoin L. Friction patterns guide actin network contraction. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2300416120. PMID: 37725653, PMCID: PMC10523593, DOI: 10.1073/pnas.2300416120.
• Twist response of actin filamentsBibeau J, Pandit N, Gray S, Nejad N, Sindelar C, Cao W, De La Cruz E. Twist response of actin filaments. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2208536120. PMID: 36656858, PMCID: PMC9942836, DOI: 10.1073/pnas.2208536120.
• Flagella-like beating of actin bundles driven by self-organized myosin wavesPochitaloff M, Miranda M, Richard M, Chaiyasitdhi A, Takagi Y, Cao W, De La Cruz E, Sellers J, Joanny J, Jülicher F, Blanchoin L, Martin P. Flagella-like beating of actin bundles driven by self-organized myosin waves. Nature Physics 2022, 18: 1240-1247. PMID: 37396880, PMCID: PMC10312380, DOI: 10.1038/s41567-022-01688-8.
• The nucleoporin Gle1 activates DEAD-box protein 5 (Dbp5) by promoting ATP binding and accelerating rate limiting phosphate releaseGray S, Cao W, Montpetit B, De La Cruz EM. The nucleoporin Gle1 activates DEAD-box protein 5 (Dbp5) by promoting ATP binding and accelerating rate limiting phosphate release. Nucleic Acids Research 2022, 50: 3998-4011. PMID: 35286399, PMCID: PMC9023272, DOI: 10.1093/nar/gkac164.
• Rab34 GTPase mediates ciliary membrane formation in the intracellular ciliogenesis pathwayGanga AK, Kennedy MC, Oguchi ME, Gray S, Oliver KE, Knight TA, De La Cruz EM, Homma Y, Fukuda M, Breslow DK. Rab34 GTPase mediates ciliary membrane formation in the intracellular ciliogenesis pathway. Current Biology 2021, 31: 2895-2905.e7. PMID: 33989527, PMCID: PMC8282722, DOI: 10.1016/j.cub.2021.04.075.
• Clusters of a Few Bound Cofilins Sever Actin FilamentsBibeau JP, Gray S, De La Cruz EM. Clusters of a Few Bound Cofilins Sever Actin Filaments. Journal Of Molecular Biology 2021, 433: 166833. PMID: 33524412, PMCID: PMC8689643, DOI: 10.1016/j.jmb.2021.166833.
• Structural basis of fast- and slow-severing actin–cofilactin boundariesHocky GM, Sindelar CV, Cao W, Voth GA, De La Cruz EM. Structural basis of fast- and slow-severing actin–cofilactin boundaries. Journal Of Biological Chemistry 2021, 296: 100337. PMID: 33508320, PMCID: PMC7961102, DOI: 10.1016/j.jbc.2021.100337.
• Improving the Pharmacodynamics and In Vivo Activity of ENPP1‐Fc Through Protein and Glycosylation EngineeringStabach PR, Zimmerman K, Adame A, Kavanagh D, Saeui CT, Agatemor C, Gray S, Cao W, De La Cruz EM, Yarema KJ, Braddock DT. Improving the Pharmacodynamics and In Vivo Activity of ENPP1‐Fc Through Protein and Glycosylation Engineering. Clinical And Translational Science 2020, 14: 362-372. PMID: 33064927, PMCID: PMC7877847, DOI: 10.1111/cts.12887.
• Force and phosphate release from Arp2/3 complex promote dissociation of actin filament branchesPandit 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.
• Directional allosteric regulation of protein filament lengthJermyn AS, Cao W, Elam WA, De La Cruz EM, Lin MM. Directional allosteric regulation of protein filament length. Physical Review E 2020, 101: 032409. PMID: 32290018, PMCID: PMC7758089, DOI: 10.1103/physreve.101.032409.
• Thermal fracture kinetics of heterogeneous semiflexible polymersLorenzo AM, De La Cruz EM, Koslover EF. Thermal fracture kinetics of heterogeneous semiflexible polymers. Soft Matter 2020, 16: 2017-2024. PMID: 31996875, PMCID: PMC7047574, DOI: 10.1039/c9sm01637f.
• Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filamentsHuehn AR, Bibeau JP, Schramm AC, Cao W, De La Cruz EM, Sindelar CV. Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 1478-1484. PMID: 31900364, PMCID: PMC6983403, DOI: 10.1073/pnas.1915987117.
• Severed Actin and Microtubules with Motors Walking All Over Them: Cryo-EM Studies of Seriously Perturbed Helical AssembliesDebs G, Huehn A, Cha M, Liu X, Elam W, Cao W, De La Cruz E, Sindelar C. Severed Actin and Microtubules with Motors Walking All Over Them: Cryo-EM Studies of Seriously Perturbed Helical Assemblies. Microscopy And Microanalysis 2019, 25: 1362-1363. DOI: 10.1017/s1431927619007542.
• Active cargo positioning in antiparallel transport networksRichard M, Blanch-Mercader C, Ennomani H, Cao W, De La Cruz EM, Joanny JF, Jülicher F, Blanchoin L, Martin P. Active cargo positioning in antiparallel transport networks. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 14835-14842. PMID: 31289230, PMCID: PMC6660773, DOI: 10.1073/pnas.1900416116.
• Plastic Deformation and Fragmentation of Strained Actin FilamentsSchramm AC, Hocky GM, Voth GA, Martiel JL, De La Cruz EM. Plastic Deformation and Fragmentation of Strained Actin Filaments. Biophysical Journal 2019, 117: 453-463. PMID: 31301801, PMCID: PMC6697348, DOI: 10.1016/j.bpj.2019.06.018.
• Regulation of axon growth by myosin II–dependent mechanocatalysis of cofilin activityZhang XF, Ajeti V, Tsai N, Fereydooni A, Burns W, Murrell M, De La Cruz EM, Forscher P. Regulation of axon growth by myosin II–dependent mechanocatalysis of cofilin activity. Journal Of Cell Biology 2019, 218: 2329-2349. PMID: 31123185, PMCID: PMC6605792, DOI: 10.1083/jcb.201810054.
• Opening remarks from the EditorsDe La Cruz EM, Blanchoin L, Ostap EM. Opening remarks from the Editors. Biophysical Reviews 2018, 10: 1479-1480. PMID: 30488377, PMCID: PMC6297087, DOI: 10.1007/s12551-018-0487-3.
• 14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surfaceKarlberg T, Hornyak P, Pinto AF, Milanova S, Ebrahimi M, Lindberg M, Püllen N, Nordström A, Löverli E, Caraballo R, Wong EV, Näreoja K, Thorsell AG, Elofsson M, De La Cruz EM, Björkegren C, Schüler H. 14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface. Nature Communications 2018, 9: 3785. PMID: 30224724, PMCID: PMC6141617, DOI: 10.1038/s41467-018-06194-1.
• Insights into the Cooperative Nature of ATP Hydrolysis in Actin FilamentsKatkar HH, Davtyan A, Durumeric AEP, Hocky GM, Schramm AC, De La Cruz EM, Voth GA. Insights into the Cooperative Nature of ATP Hydrolysis in Actin Filaments. Biophysical Journal 2018, 115: 1589-1602. PMID: 30249402, PMCID: PMC6260209, DOI: 10.1016/j.bpj.2018.08.034.
• Nup159 Weakens Gle1 Binding to Dbp5 But Does Not Accelerate ADP ReleaseWong EV, Gray S, Cao W, Montpetit R, Montpetit B, De La Cruz EM. Nup159 Weakens Gle1 Binding to Dbp5 But Does Not Accelerate ADP Release. Journal Of Molecular Biology 2018, 430: 2080-2095. PMID: 29782832, PMCID: PMC6003625, DOI: 10.1016/j.jmb.2018.05.025.
• The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segmentsHuehn A, Cao W, Elam WA, Liu X, De La Cruz EM, Sindelar CV. The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments. Journal Of Biological Chemistry 2018, 293: 5377-5383. PMID: 29463680, PMCID: PMC5900768, DOI: 10.1074/jbc.ac118.001843.
• Cofilin Induces a Local Change in the Twist of Actin FilamentsHuehn A, Cao W, Elam W, De La Cruz E, Sindelar C. Cofilin Induces a Local Change in the Twist of Actin Filaments. Biophysical Journal 2018, 114: 145a. DOI: 10.1016/j.bpj.2017.11.812.
• Insights into the Cooperative Nature of ATP Hydrolysis in Actin FilamentsKatkar H, Davtyan A, Durumeric A, Hocky G, Schramm A, De La Cruz E, Voth G. Insights into the Cooperative Nature of ATP Hydrolysis in Actin Filaments. Biophysical Journal 2018, 114: 142a. DOI: 10.1016/j.bpj.2017.11.796.
• Self Organized Wave Like Beating of Actin Bundles in a Minimal Acto-Myosin System of Controlled ArchitecturePochitaloff M, Richard M, Yasuharu T, De La Cruz E, Sellers J, Joanny J, Jülicher F, Blanchoin L, Martin P. Self Organized Wave Like Beating of Actin Bundles in a Minimal Acto-Myosin System of Controlled Architecture. Biophysical Journal 2018, 114: 649a. DOI: 10.1016/j.bpj.2017.11.3505.
• Mechanoregulated inhibition of formin facilitates contractile actomyosin ring assemblyZimmermann D, Homa KE, Hocky GM, Pollard LW, De La Cruz EM, Voth GA, Trybus KM, Kovar DR. Mechanoregulated inhibition of formin facilitates contractile actomyosin ring assembly. Nature Communications 2017, 8: 703. PMID: 28951543, PMCID: PMC5614989, DOI: 10.1038/s41467-017-00445-3.
• Phosphomimetic S3D cofilin binds but only weakly severs actin filamentsElam WA, Cao W, Kang H, Huehn A, Hocky GM, Prochniewicz E, Schramm AC, Negrón K, Garcia J, Bonello TT, Gunning PW, Thomas DD, Voth GA, Sindelar CV, De La Cruz EM. Phosphomimetic S3D cofilin binds but only weakly severs actin filaments. Journal Of Biological Chemistry 2017, 292: 19565-19579. PMID: 28939776, PMCID: PMC5712599, DOI: 10.1074/jbc.m117.808378.
• Actin Filament Strain Promotes Severing and Cofilin DissociationSchramm AC, Hocky GM, Voth GA, Blanchoin L, Martiel JL, De La Cruz EM. Actin Filament Strain Promotes Severing and Cofilin Dissociation. Biophysical Journal 2017, 112: 2624-2633. PMID: 28636918, PMCID: PMC5479148, DOI: 10.1016/j.bpj.2017.05.016.
• Active Cargo Positioning from Actin-Polarity Sensing by Small Myosin AssembliesRichard M, Ennomani H, Blanch-Mercader C, de la Cruz E, Joanny J, Jülicher F, Blanchoin L, Martin P. Active Cargo Positioning from Actin-Polarity Sensing by Small Myosin Assemblies. Biophysical Journal 2017, 112: 562a. DOI: 10.1016/j.bpj.2016.11.3026.
• Neuronal Calcium Sensor 1 Has Two Variants with Distinct Calcium Binding CharacteristicsWang B, Boeckel GR, Huynh L, Nguyen L, Cao W, De La Cruz EM, Kaftan EJ, Ehrlich BE. Neuronal Calcium Sensor 1 Has Two Variants with Distinct Calcium Binding Characteristics. PLOS ONE 2016, 11: e0161414. PMID: 27575489, PMCID: PMC5004852, DOI: 10.1371/journal.pone.0161414.
• Cations Stiffen Actin Filaments by Adhering a Key Structural Element to Adjacent SubunitsHocky GM, Baker JL, Bradley MJ, Sinitskiy AV, De La Cruz EM, Voth GA. Cations Stiffen Actin Filaments by Adhering a Key Structural Element to Adjacent Subunits. The Journal Of Physical Chemistry B 2016, 120: 4558-4567. PMID: 27146246, PMCID: PMC4959277, DOI: 10.1021/acs.jpcb.6b02741.
• Architecture and Connectivity Govern Actin Network ContractilityEnnomani H, Letort G, Guérin C, Martiel JL, Cao W, Nédélec F, De La Cruz EM, Théry M, Blanchoin L. Architecture and Connectivity Govern Actin Network Contractility. Current Biology 2016, 26: 616-626. PMID: 26898468, PMCID: PMC4959279, DOI: 10.1016/j.cub.2015.12.069.
• Specific Cation Binding Stiffens Actin Filaments by Adhering D-Loops to Adjacent MonomersHocky G, Baker J, Bradley M, Sinitskiy A, De La Cruz E, Voth G. Specific Cation Binding Stiffens Actin Filaments by Adhering D-Loops to Adjacent Monomers. Biophysical Journal 2016, 110: 125a. DOI: 10.1016/j.bpj.2015.11.721.
• Pi Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5)Wong EV, Cao W, Vörös J, Merchant M, Modis Y, Hackney DD, Montpetit B, De La Cruz EM. Pi Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5). Journal Of Molecular Biology 2015, 428: 492-508. PMID: 26730886, PMCID: PMC4744555, DOI: 10.1016/j.jmb.2015.12.018.
• ENPP1-Fc prevents mortality and vascular calcifications in rodent model of generalized arterial calcification of infancyAlbright RA, Stabach P, Cao W, Kavanagh D, Mullen I, Braddock AA, Covo MS, Tehan M, Yang G, Cheng Z, Bouchard K, Yu ZX, Thorn S, Wang X, Folta-Stogniew EJ, Negrete A, Sinusas AJ, Shiloach J, Zubal G, Madri JA, De La Cruz EM, Braddock DT. ENPP1-Fc prevents mortality and vascular calcifications in rodent model of generalized arterial calcification of infancy. Nature Communications 2015, 6: 10006. PMID: 26624227, PMCID: PMC4686714, DOI: 10.1038/ncomms10006.
• Metavinculin Tunes the Flexibility and the Architecture of Vinculin-Induced Bundles of Actin FilamentsDurer Z, McGillivary RM, Kang H, Elam WA, Vizcarra CL, Hanein D, De La Cruz EM, Reisler E, Quinlan ME. Metavinculin Tunes the Flexibility and the Architecture of Vinculin-Induced Bundles of Actin Filaments. Journal Of Molecular Biology 2015, 427: 2782-2798. PMID: 26168869, PMCID: PMC4540644, DOI: 10.1016/j.jmb.2015.07.005.
• Actin Mechanics and Fragmentation*De La Cruz EM, Gardel ML. Actin Mechanics and Fragmentation*. Journal Of Biological Chemistry 2015, 290: 17137-17144. PMID: 25957404, PMCID: PMC4498053, DOI: 10.1074/jbc.r115.636472.
• Mechanical Heterogeneity Favors Fragmentation of Strained Actin FilamentsDe La Cruz EM, Martiel JL, Blanchoin L. Mechanical Heterogeneity Favors Fragmentation of Strained Actin Filaments. Biophysical Journal 2015, 108: 2270-2281. PMID: 25954884, PMCID: PMC4423049, DOI: 10.1016/j.bpj.2015.03.058.
• Site-Specific Cation Release Drives Actin Filament Severing by Vertebrate CofilinKang H, Bradley M, Cao W, Zhou K, Grintsevich E, Michelot A, Reisler E, Sindelar C, Hochstrasser M, De La Cruz E. Site-Specific Cation Release Drives Actin Filament Severing by Vertebrate Cofilin. Biophysical Journal 2015, 108: 24a-25a. DOI: 10.1016/j.bpj.2014.11.159.
• Kinetics and Thermodynamics of the ATPase Cycle of the DEAD-Box Protein Dbp5Wong E, Cao W, Montpetit B, De La Cruz E. Kinetics and Thermodynamics of the ATPase Cycle of the DEAD-Box Protein Dbp5. Biophysical Journal 2015, 108: 225a. DOI: 10.1016/j.bpj.2014.11.1243.
• Phosphomimic S3D Cofilin Binds Actin Filaments but does not Sever themElam W, Kang H, Prochniewicz E, Nieves-Torres K, Thomas D, De La Cruz E. Phosphomimic S3D Cofilin Binds Actin Filaments but does not Sever them. Biophysical Journal 2015, 108: 300a. DOI: 10.1016/j.bpj.2014.11.1630.
• Site-specific cation release drives actin filament severing by vertebrate cofilinKang H, Bradley MJ, Cao W, Zhou K, Grintsevich EE, Michelot A, Sindelar CV, Hochstrasser M, De La Cruz EM. Site-specific cation release drives actin filament severing by vertebrate cofilin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 17821-17826. PMID: 25468977, PMCID: PMC4273407, DOI: 10.1073/pnas.1413397111.
• Navigating the cell: how motors function in vivoDe La Cruz EM, Holzbaur EL. Navigating the cell: how motors function in vivo. Journal Of Cell Science 2014, 127: 2997-2998. PMID: 25024456, DOI: 10.1242/jcs.156414.
• Multi-Platform Compatible Software for Analysis of Polymer Bending MechanicsGraham JS, McCullough BR, Kang H, Elam WA, Cao W, De La Cruz EM. Multi-Platform Compatible Software for Analysis of Polymer Bending Mechanics. PLOS ONE 2014, 9: e94766. PMID: 24740323, PMCID: PMC3989245, DOI: 10.1371/journal.pone.0094766.
• Actin Filament Severing by Vertebrate Cofilin is Driven by Linked Cation ReleaseKang H, Bradley M, McCullough B, Grintsevich E, Michelot A, Hochstrasser M, Reisler E, De La Cruz E. Actin Filament Severing by Vertebrate Cofilin is Driven by Linked Cation Release. Biophysical Journal 2014, 106: 164a-165a. DOI: 10.1016/j.bpj.2013.11.938.
• Molecular Basis of Purinergic Signal Metabolism by Ectonucleotide Pyrophosphatase/Phosphodiesterases 4 and 1 and Implications in Stroke*♦Albright RA, Ornstein DL, Cao W, Chang WC, Robert D, Tehan M, Hoyer D, Liu L, Stabach P, Yang G, De La Cruz EM, Braddock DT. Molecular Basis of Purinergic Signal Metabolism by Ectonucleotide Pyrophosphatase/Phosphodiesterases 4 and 1 and Implications in Stroke*♦. Journal Of Biological Chemistry 2013, 289: 3294-3306. PMID: 24338010, PMCID: PMC3916532, DOI: 10.1074/jbc.m113.505867.
• Regulation of Actin by Ion-Linked EquilibriaKang H, Bradley MJ, Elam WA, De La Cruz EM. Regulation of Actin by Ion-Linked Equilibria. Biophysical Journal 2013, 105: 2621-2628. PMID: 24359734, PMCID: PMC3882474, DOI: 10.1016/j.bpj.2013.10.032.
• Quantitative full time course analysis of nonlinear enzyme cycling kineticsCao W, De La Cruz EM. Quantitative full time course analysis of nonlinear enzyme cycling kinetics. Scientific Reports 2013, 3: 2658. PMID: 24029878, PMCID: PMC3772379, DOI: 10.1038/srep02658.
• Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamicsXia S, Wood M, Bradley MJ, De La Cruz EM, Konigsberg WH. Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics. Nucleic Acids Research 2013, 41: 9077-9089. PMID: 23921641, PMCID: PMC3799440, DOI: 10.1093/nar/gkt674.
• Competitive displacement of cofilin can promote actin filament severingElam WA, Kang H, De La Cruz EM. Competitive displacement of cofilin can promote actin filament severing. Biochemical And Biophysical Research Communications 2013, 438: 728-731. PMID: 23911787, PMCID: PMC3785092, DOI: 10.1016/j.bbrc.2013.07.109.
• Take advantage of time in your experiments: a guide to simple, informative kinetics assaysPollard TD, De La Cruz EM. Take advantage of time in your experiments: a guide to simple, informative kinetics assays. Molecular Biology Of The Cell 2013, 24: 1103-1110. PMID: 23580192, PMCID: PMC3623632, DOI: 10.1091/mbc.e13-01-0030.
• Actin organization and dynamics: novel regulatory mechanisms from the biophysical to the tissue levelMiller AL, De La Cruz EM. Actin organization and dynamics: novel regulatory mechanisms from the biophysical to the tissue level. Molecular Biology Of The Cell 2013, 24: 677-677. PMID: 23486401, PMCID: PMC3596237, DOI: 10.1091/mbc.e12-12-0879.
• Biophysics of actin filament severing by cofilinElam WA, Kang H, De La Cruz EM. Biophysics of actin filament severing by cofilin. FEBS Letters 2013, 587: 1215-1219. PMID: 23395798, PMCID: PMC4079045, DOI: 10.1016/j.febslet.2013.01.062.
• Molecular Origins of Cofilin-Linked Changes in Actin Filament MechanicsFan J, Saunders MG, Haddadian EJ, Freed KF, De La Cruz EM, Voth GA. Molecular Origins of Cofilin-Linked Changes in Actin Filament Mechanics. Journal Of Molecular Biology 2013, 425: 1225-1240. PMID: 23352932, PMCID: PMC3740545, DOI: 10.1016/j.jmb.2013.01.020.
• Molecular Origins of Cofilin-Linked Changes in Actin Filament MechanicsFan J, Saunders M, Haddadian E, Freed K, De La Cruz E, Voth G. Molecular Origins of Cofilin-Linked Changes in Actin Filament Mechanics. Biophysical Journal 2013, 104: 549a-550a. DOI: 10.1016/j.bpj.2012.11.3047.
• Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffnessKang H, Bradley MJ, McCullough BR, Pierre A, Grintsevich EE, Reisler E, De La Cruz EM. Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 16923-16927. PMID: 23027950, PMCID: PMC3479481, DOI: 10.1073/pnas.1211078109.
• NPP4 is a procoagulant enzyme on the surface of vascular endotheliumAlbright RA, Chang WC, Robert D, Ornstein DL, Cao W, Liu L, Redick ME, Young JI, De La Cruz EM, Braddock DT. NPP4 is a procoagulant enzyme on the surface of vascular endothelium. Blood 2012, 120: 4432-4440. PMID: 22995898, PMCID: PMC4017314, DOI: 10.1182/blood-2012-04-425215.
• Actin Network Architecture Can Determine Myosin Motor ActivityReymann AC, Boujemaa-Paterski R, Martiel JL, Guérin C, Cao W, Chin HF, De La Cruz EM, Théry M, Blanchoin L. Actin Network Architecture Can Determine Myosin Motor Activity. Science 2012, 336: 1310-1314. PMID: 22679097, PMCID: PMC3649007, DOI: 10.1126/science.1221708.
• ATP Utilization and RNA Conformational Rearrangement by DEAD-Box ProteinsHenn A, Bradley MJ, De La Cruz EM. ATP Utilization and RNA Conformational Rearrangement by DEAD-Box Proteins. Annual Review Of Biophysics 2012, 41: 247-267. PMID: 22404686, PMCID: PMC7761782, DOI: 10.1146/annurev-biophys-050511-102243.
• Plus‐end directed myosins accelerate actin filament sliding by single‐headed myosin VIRamamurthy B, Cao W, De La Cruz EM, Mooseker MS. Plus‐end directed myosins accelerate actin filament sliding by single‐headed myosin VI. Cytoskeleton 2012, 69: 59-69. PMID: 22213699, PMCID: PMC3327287, DOI: 10.1002/cm.21002.
• Chapter Two Analyzing ATP Utilization by DEAD-Box RNA Helicases Using Kinetic and Equilibrium MethodsBradley MJ, De La Cruz EM. Chapter Two Analyzing ATP Utilization by DEAD-Box RNA Helicases Using Kinetic and Equilibrium Methods. 2012, 511: 29-63. PMID: 22713314, PMCID: PMC7768905, DOI: 10.1016/b978-0-12-396546-2.00002-4.
• Molecular Structure and Biological Activity of NPP-4, An Endothelial Cell Surface Pyrophosphatase/ Phosphodiesterase That Stimulates Platelet Aggregation and Secretion Via Liberation of ADP Upon Hydrolysis of Diadenosine TriphosphateOrnstein D, Albright R, Chang W, Robert D, Cao W, De La Cruz E, Braddock D. Molecular Structure and Biological Activity of NPP-4, An Endothelial Cell Surface Pyrophosphatase/ Phosphodiesterase That Stimulates Platelet Aggregation and Secretion Via Liberation of ADP Upon Hydrolysis of Diadenosine Triphosphate. Blood 2011, 118: 701. DOI: 10.1182/blood.v118.21.701.701.
• Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrateWu X, Bradley MJ, Cai Y, Kümmel D, De La Cruz EM, Barr FA, Reinisch KM. Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 18672-18677. PMID: 22065758, PMCID: PMC3219131, DOI: 10.1073/pnas.1110415108.
• Actin Filament Dynamics in the Actomyosin VI Complex Is Regulated Allosterically by Calcium–Calmodulin Light ChainProchniewicz E, Pierre A, McCullough BR, Chin HF, Cao W, Saunders LP, Thomas DD, De La Cruz EM. Actin Filament Dynamics in the Actomyosin VI Complex Is Regulated Allosterically by Calcium–Calmodulin Light Chain. Journal Of Molecular Biology 2011, 413: 584-592. PMID: 21910998, PMCID: PMC3633491, DOI: 10.1016/j.jmb.2011.08.058.
• Cofilin-Linked Changes in Actin Filament Flexibility Promote SeveringMcCullough BR, Grintsevich EE, Chen CK, Kang H, Hutchison AL, Henn A, Cao W, Suarez C, Martiel JL, Blanchoin L, Reisler E, De La Cruz EM. Cofilin-Linked Changes in Actin Filament Flexibility Promote Severing. Biophysical Journal 2011, 101: 151-159. PMID: 21723825, PMCID: PMC3127193, DOI: 10.1016/j.bpj.2011.05.049.
• Kinetic Analysis of Autotaxin Reveals Substrate-specific Catalytic Pathways and a Mechanism for Lysophosphatidic Acid Distribution*Saunders LP, Cao W, Chang WC, Albright RA, Braddock DT, De La Cruz EM. Kinetic Analysis of Autotaxin Reveals Substrate-specific Catalytic Pathways and a Mechanism for Lysophosphatidic Acid Distribution*. Journal Of Biological Chemistry 2011, 286: 30130-30141. PMID: 21719699, PMCID: PMC3191052, DOI: 10.1074/jbc.m111.246884.
• Cofilin Tunes the Nucleotide State of Actin Filaments and Severs at Bare and Decorated Segment BoundariesSuarez C, Roland J, Boujemaa-Paterski R, Kang H, McCullough B, Reymann A, Guérin C, Martiel J, De La Cruz E, Blanchoin L. Cofilin Tunes the Nucleotide State of Actin Filaments and Severs at Bare and Decorated Segment Boundaries. Current Biology 2011, 21: 904. DOI: 10.1016/j.cub.2011.05.019.
• Cofilin Tunes the Nucleotide State of Actin Filaments and Severs at Bare and Decorated Segment BoundariesSuarez C, Roland J, Boujemaa-Paterski R, Kang H, McCullough BR, Reymann AC, Guérin C, Martiel JL, De La Cruz EM, Blanchoin L. Cofilin Tunes the Nucleotide State of Actin Filaments and Severs at Bare and Decorated Segment Boundaries. Current Biology 2011, 21: 862-868. PMID: 21530260, PMCID: PMC3100394, DOI: 10.1016/j.cub.2011.03.064.
• Direct Observation of the Myosin Va Recovery Stroke That Contributes to Unidirectional Stepping along ActinShiroguchi K, Chin HF, Hannemann DE, Muneyuki E, De La Cruz EM, Kinosita K. Direct Observation of the Myosin Va Recovery Stroke That Contributes to Unidirectional Stepping along Actin. PLOS Biology 2011, 9: e1001031. PMID: 21532738, PMCID: PMC3075224, DOI: 10.1371/journal.pbio.1001031.
• Mechanism of Mss116 ATPase Reveals Functional Diversity of DEAD-Box ProteinsCao W, Coman MM, Ding S, Henn A, Middleton ER, Bradley MJ, Rhoades E, Hackney DD, Pyle AM, De La Cruz EM. Mechanism of Mss116 ATPase Reveals Functional Diversity of DEAD-Box Proteins. Journal Of Molecular Biology 2011, 409: 399-414. PMID: 21501623, PMCID: PMC3125984, DOI: 10.1016/j.jmb.2011.04.004.
• A Myosin V Inhibitor Based on Privileged Chemical ScaffoldsIslam K, Chin HF, Olivares AO, Saunders LP, De La Cruz EM, Kapoor TM. A Myosin V Inhibitor Based on Privileged Chemical Scaffolds. Angewandte Chemie International Edition 2010, 49: 8484-8488. PMID: 20878825, PMCID: PMC3063097, DOI: 10.1002/anie.201004026.
• A Myosin V Inhibitor Based on Privileged Chemical ScaffoldsIslam K, Chin H, Olivares A, Saunders L, De La Cruz E, Kapoor T. A Myosin V Inhibitor Based on Privileged Chemical Scaffolds. Angewandte Chemie 2010, 122: 8662-8666. DOI: 10.1002/ange.201004026.
• Structure-Based Analysis of Toxoplasma gondii Profilin: A Parasite-Specific Motif Is Required for Recognition by Toll-Like Receptor 11Kucera K, Koblansky AA, Saunders LP, Frederick KB, De La Cruz EM, Ghosh S, Modis Y. Structure-Based Analysis of Toxoplasma gondii Profilin: A Parasite-Specific Motif Is Required for Recognition by Toll-Like Receptor 11. Journal Of Molecular Biology 2010, 403: 616-629. PMID: 20851125, PMCID: PMC2957522, DOI: 10.1016/j.jmb.2010.09.022.
• Origin of Twist-Bend Coupling in Actin FilamentsDe La Cruz EM, Roland J, McCullough BR, Blanchoin L, Martiel JL. Origin of Twist-Bend Coupling in Actin Filaments. Biophysical Journal 2010, 99: 1852-1860. PMID: 20858430, PMCID: PMC2941021, DOI: 10.1016/j.bpj.2010.07.009.
• The Kinetics of Cooperative Cofilin Binding Reveals Two States of the Cofilin-Actin FilamentDe La Cruz EM, Sept D. The Kinetics of Cooperative Cofilin Binding Reveals Two States of the Cofilin-Actin Filament. Biophysical Journal 2010, 98: 1893-1901. PMID: 20441753, PMCID: PMC2862197, DOI: 10.1016/j.bpj.2010.01.023.
• Actin filament remodeling by actin depolymerization factor/cofilinPfaendtner J, De La Cruz EM, Voth GA. Actin filament remodeling by actin depolymerization factor/cofilin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 7299-7304. PMID: 20368459, PMCID: PMC2867716, DOI: 10.1073/pnas.0911675107.
• Robust processivity of myosin V under off-axis loadsOguchi Y, Mikhailenko SV, Ohki T, Olivares AO, De La Cruz EM, Ishiwata S. Robust processivity of myosin V under off-axis loads. Nature Chemical Biology 2010, 6: 300-305. PMID: 20228794, PMCID: PMC2917589, DOI: 10.1038/nchembio.322.
• Pathway of ATP utilization and duplex rRNA unwinding by the DEAD-box helicase, DbpAHenn A, Cao W, Licciardello N, Heitkamp SE, Hackney DD, De La Cruz EM. Pathway of ATP utilization and duplex rRNA unwinding by the DEAD-box helicase, DbpA. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 4046-4050. PMID: 20160110, PMCID: PMC2840157, DOI: 10.1073/pnas.0913081107.
• Myosin Isoform Determines the Conformational Dynamics and Cooperativity of Actin Filaments in the Strongly Bound Actomyosin ComplexProchniewicz E, Chin HF, Henn A, Hannemann DE, Olivares AO, Thomas DD, De La Cruz EM. Myosin Isoform Determines the Conformational Dynamics and Cooperativity of Actin Filaments in the Strongly Bound Actomyosin Complex. Journal Of Molecular Biology 2009, 396: 501-509. PMID: 19962990, PMCID: PMC2834967, DOI: 10.1016/j.jmb.2009.11.063.
• How cofilin severs an actin filamentDe La Cruz EM. How cofilin severs an actin filament. Biophysical Reviews 2009, 1: 51-59. PMID: 20700473, PMCID: PMC2917815, DOI: 10.1007/s12551-009-0008-5.
• Kinetic Analysis of the Guanine Nucleotide Exchange Activity of TRAPP, a Multimeric Ypt1p Exchange FactorChin HF, Cai Y, Menon S, Ferro-Novick S, Reinisch KM, De La Cruz EM. Kinetic Analysis of the Guanine Nucleotide Exchange Activity of TRAPP, a Multimeric Ypt1p Exchange Factor. Journal Of Molecular Biology 2009, 389: 275-288. PMID: 19361519, PMCID: PMC2770256, DOI: 10.1016/j.jmb.2009.03.068.
• Watching the walk: Observing chemo‐mechanical coupling in a processive myosin motorDe La Cruz EM, Olivares AO. Watching the walk: Observing chemo‐mechanical coupling in a processive myosin motor. All Life 2009, 3: 67-70. PMID: 19794813, PMCID: PMC2707789, DOI: 10.2976/1.3095425.
• Chapter 6 Kinetic and Equilibrium Analysis of the Myosin ATPaseDe La Cruz EM, Ostap EM. Chapter 6 Kinetic and Equilibrium Analysis of the Myosin ATPase. 2009, 455: 157-192. PMID: 19289206, PMCID: PMC2921708, DOI: 10.1016/s0076-6879(08)04206-7.
• Identification of small-molecule inhibitors of autotaxin that inhibit melanoma cell migration and invasionSaunders LP, Ouellette A, Bandle R, Chang WC, Zhou H, Misra RN, De La Cruz EM, Braddock DT. Identification of small-molecule inhibitors of autotaxin that inhibit melanoma cell migration and invasion. Molecular Cancer Therapeutics 2008, 7: 3352-3362. PMID: 18852138, PMCID: PMC7857123, DOI: 10.1158/1535-7163.mct-08-0463.
• How the Load and the Nucleotide State Affect the Actin Filament Binding Mode of the Molecular Motor Myosin V.Mikhailenko SV, Oguchi Y, Ohki T, Shimozawa T, Olivares AO, De La Cruz EM, Ishiwata S. How the Load and the Nucleotide State Affect the Actin Filament Binding Mode of the Molecular Motor Myosin V. Journal Of The Korean Physical Society 2008, 53: 1726-1730. PMID: 20552037, PMCID: PMC2884403, DOI: 10.3938/jkps.53.1726.
• Structural and Energetic Analysis of Activation by a Cyclic Nucleotide Binding DomainAltieri SL, Clayton GM, Silverman WR, Olivares AO, De La Cruz EM, Thomas LR, Morais-Cabral JH. Structural and Energetic Analysis of Activation by a Cyclic Nucleotide Binding Domain. Journal Of Molecular Biology 2008, 381: 655-669. PMID: 18619611, PMCID: PMC2555981, DOI: 10.1016/j.jmb.2008.06.011.
• Load-dependent ADP binding to myosins V and VI: Implications for subunit coordination and functionOguchi Y, Mikhailenko SV, Ohki T, Olivares AO, De La Cruz EM, Ishiwata S. Load-dependent ADP binding to myosins V and VI: Implications for subunit coordination and function. Proceedings Of The National Academy Of Sciences Of The United States Of America 2008, 105: 7714-7719. PMID: 18509050, PMCID: PMC2409399, DOI: 10.1073/pnas.0800564105.
• The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering ComplexesCai 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.
• Cofilin Increases the Bending Flexibility of Actin Filaments: Implications for Severing and Cell MechanicsMcCullough BR, Blanchoin L, Martiel JL, De La Cruz EM. Cofilin Increases the Bending Flexibility of Actin Filaments: Implications for Severing and Cell Mechanics. Journal Of Molecular Biology 2008, 381: 550-558. PMID: 18617188, PMCID: PMC2753234, DOI: 10.1016/j.jmb.2008.05.055.
• Widely Distributed Residues in Thymosin β4 Are Critical for Actin BindingAu JK, Olivares AO, Henn A, Cao W, Safer D, De La Cruz EM. Widely Distributed Residues in Thymosin β4 Are Critical for Actin Binding. Biochemistry 2008, 47: 4181-4188. PMID: 18327913, PMCID: PMC2587058, DOI: 10.1021/bi701769u.
• Effects of Solution Crowding on Actin Polymerization Reveal the Energetic Basis for Nucleotide-Dependent Filament StabilityFrederick KB, Sept D, De La Cruz EM. Effects of Solution Crowding on Actin Polymerization Reveal the Energetic Basis for Nucleotide-Dependent Filament Stability. Journal Of Molecular Biology 2008, 378: 540-550. PMID: 18374941, PMCID: PMC2424216, DOI: 10.1016/j.jmb.2008.02.022.
• The Roles of Thymosin β4 in Cell Migration and Cell-to-Cell Signaling in DiseaseAu J, Krendel M, Safer D, De La Cruz E. The Roles of Thymosin β4 in Cell Migration and Cell-to-Cell Signaling in Disease. 2008, 218-228. DOI: 10.1007/978-0-387-71749-4_9.
• Overview: Actin-Binding Protein Function and Its Relation to Disease PathologyKrendel M, De La Cruz E. Overview: Actin-Binding Protein Function and Its Relation to Disease Pathology. 2008, 65-82. DOI: 10.1007/978-0-387-71749-4_5.
• The ATPase Cycle Mechanism of the DEAD-box rRNA Helicase, DbpAHenn A, Cao W, Hackney DD, De La Cruz EM. The ATPase Cycle Mechanism of the DEAD-box rRNA Helicase, DbpA. Journal Of Molecular Biology 2007, 377: 193-205. PMID: 18237742, PMCID: PMC2359651, DOI: 10.1016/j.jmb.2007.12.046.
• Dimerization of FIR upon FUSE DNA binding suggests a mechanism of c‐myc inhibitionCrichlow GV, Zhou H, Hsiao HH, Frederick KB, Debrosse M, Yang Y, Folta-Stogniew EJ, Chung HJ, Fan C, De La Cruz EM, Levens D, Lolis E, Braddock D. Dimerization of FIR upon FUSE DNA binding suggests a mechanism of c‐myc inhibition. The EMBO Journal 2007, 27: 277-289. PMID: 18059478, PMCID: PMC2206118, DOI: 10.1038/sj.emboj.7601936.
• Contributions from All OverAU 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.
• Fluorescence of 2-aminopurine reveals rapid conformational changes in the RB69 DNA polymerase-primer/template complexes upon binding and incorporation of matched deoxynucleoside triphosphatesZhang 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.
• The Tail Domain of Myosin Va Modulates Actin Binding to One Head*Olivares A, Chang W, Mooseker M, Hackney D, De La Cruz E. The Tail Domain of Myosin Va Modulates Actin Binding to One Head*. Journal Of Biological Chemistry 2006, 281: 31326-31336. DOI: 10.1016/s0021-9258(19)84045-0.
• The Tail Domain of Myosin Va Modulates Actin Binding to One HeadOlivares AO, Chang W, Mooseker MS, Hackney DD, De La Cruz EM. The Tail Domain of Myosin Va Modulates Actin Binding to One Head. Journal Of Biological Chemistry 2006, 281: 31326-31336. PMID: 16921171, DOI: 10.1074/jbc.m603898200.
• Energetics and Kinetics of Cooperative Cofilin–Actin Filament InteractionsCao W, Goodarzi JP, De La Cruz EM. Energetics and Kinetics of Cooperative Cofilin–Actin Filament Interactions. Journal Of Molecular Biology 2006, 361: 257-267. PMID: 16843490, DOI: 10.1016/j.jmb.2006.06.019.
• Hydrodynamic Characterization of the DEAD-box RNA Helicase DbpATalavera MA, Matthews EE, Eliason WK, Sagi I, Wang J, Henn A, De La Cruz EM. Hydrodynamic Characterization of the DEAD-box RNA Helicase DbpA. Journal Of Molecular Biology 2005, 355: 697-707. PMID: 16325852, DOI: 10.1016/j.jmb.2005.10.058.
• Thymosin β4 Induces a Conformational Change in Actin MonomersDedova IV, Nikolaeva OP, Safer D, De La Cruz EM, dos Remedios CG. Thymosin β4 Induces a Conformational Change in Actin Monomers. Biophysical Journal 2005, 90: 985-992. PMID: 16272441, PMCID: PMC1367123, DOI: 10.1529/biophysj.105.063081.
• Cofilin Increases the Torsional Flexibility and Dynamics of Actin FilamentsProchniewicz E, Janson N, Thomas DD, De La Cruz EM. Cofilin Increases the Torsional Flexibility and Dynamics of Actin Filaments. Journal Of Molecular Biology 2005, 353: 990-1000. PMID: 16213521, DOI: 10.1016/j.jmb.2005.09.021.
• Vertebrate Myosin VIIb Is a High Duty Ratio Motor Adapted for Generating and Maintaining Tension*Henn A, De La Cruz EM. Vertebrate Myosin VIIb Is a High Duty Ratio Motor Adapted for Generating and Maintaining Tension*. Journal Of Biological Chemistry 2005, 280: 39665-39676. PMID: 16186105, DOI: 10.1074/jbc.m507667200.
• Holding the reins on Myosin VOlivares AO, De La Cruz EM. Holding the reins on Myosin V. Proceedings Of The National Academy Of Sciences Of The United States Of America 2005, 102: 13719-13720. PMID: 16172373, PMCID: PMC1236595, DOI: 10.1073/pnas.0507068102.
• Equilibrium and Kinetic Analysis of Nucleotide Binding to the DEAD-Box RNA Helicase DbpATalavera M, De La Cruz E. Equilibrium and Kinetic Analysis of Nucleotide Binding to the DEAD-Box RNA Helicase DbpA. Biochemistry 2005, 44: 12620-12620. DOI: 10.1021/bi058021z.
• Thermodynamics of Nucleotide Binding to Actomyosin V and VI: A Positive Heat Capacity Change Accompanies Strong ADP Binding †Robblee JP, Cao W, Henn A, Hannemann DE, De La Cruz EM. Thermodynamics of Nucleotide Binding to Actomyosin V and VI: A Positive Heat Capacity Change Accompanies Strong ADP Binding †. Biochemistry 2005, 44: 10238-10249. PMID: 16042401, DOI: 10.1021/bi050232g.
• Magnesium, ADP, and Actin Binding Linkage of Myosin V: Evidence for Multiple Myosin V−ADP and Actomyosin V−ADP States †Hannemann DE, Cao W, Olivares AO, Robblee JP, De La Cruz EM. Magnesium, ADP, and Actin Binding Linkage of Myosin V: Evidence for Multiple Myosin V−ADP and Actomyosin V−ADP States †. Biochemistry 2005, 44: 8826-8840. PMID: 15952789, DOI: 10.1021/bi0473509.
• Cofilin Binding to Muscle and Non-muscle Actin Filaments: Isoform-dependent Cooperative InteractionsDe La Cruz EM. Cofilin Binding to Muscle and Non-muscle Actin Filaments: Isoform-dependent Cooperative Interactions. Journal Of Molecular Biology 2004, 346: 557-564. PMID: 15670604, DOI: 10.1016/j.jmb.2004.11.065.
• Equilibrium and Kinetic Analysis of Nucleotide Binding to the DEAD-Box RNA Helicase DbpA †Talavera MA, De La Cruz EM. Equilibrium and Kinetic Analysis of Nucleotide Binding to the DEAD-Box RNA Helicase DbpA †. Biochemistry 2004, 44: 959-970. PMID: 15654752, DOI: 10.1021/bi048253i.
• Mechanochemical coupling of two substeps in a single myosin V motorUemura S, Higuchi H, Olivares AO, De La Cruz EM, Ishiwata S. Mechanochemical coupling of two substeps in a single myosin V motor. Nature Structural & Molecular Biology 2004, 11: 877-883. PMID: 15286720, DOI: 10.1038/nsmb806.
• Mechanism of Nucleotide Binding to Actomyosin VI EVIDENCE FOR ALLOSTERIC HEAD-HEAD COMMUNICATION*Robblee JP, Olivares AO, De La Cruz EM. Mechanism of Nucleotide Binding to Actomyosin VI EVIDENCE FOR ALLOSTERIC HEAD-HEAD COMMUNICATION*. Journal Of Biological Chemistry 2004, 279: 38608-38617. PMID: 15247304, DOI: 10.1074/jbc.m403504200.
• Relating biochemistry and function in the myosin superfamilyDe La Cruz EM, Ostap EM. Relating biochemistry and function in the myosin superfamily. Current Opinion In Cell Biology 2004, 16: 61-67. PMID: 15037306, DOI: 10.1016/j.ceb.2003.11.011.
• Kinetic Characterization of the Weak Binding States of Myosin V †Yengo CM, De La Cruz EM, Safer D, Ostap EM, Sweeney HL. Kinetic Characterization of the Weak Binding States of Myosin V †. Biochemistry 2002, 41: 8508-8517. PMID: 12081502, DOI: 10.1021/bi015969u.
• Actin-induced Closure of the Actin-binding Cleft of Smooth Muscle Myosin*Yengo CM, De La Cruz EM, Chrin LR, Gaffney DP, Berger CL. Actin-induced Closure of the Actin-binding Cleft of Smooth Muscle Myosin*. Journal Of Biological Chemistry 2002, 277: 24114-24119. PMID: 11959853, DOI: 10.1074/jbc.m111253200.
• Structural biology. Actin' up.De La Cruz E, Pollard T. Structural biology. Actin' up. Science 2001, 293: 616-8. PMID: 11474090, DOI: 10.1126/science.1063558.
• Kinetic Mechanism and Regulation of Myosin VI*De La Cruz E, Ostap E, Sweeney H. Kinetic Mechanism and Regulation of Myosin VI*. Journal Of Biological Chemistry 2001, 276: 32373-32381. PMID: 11423557, DOI: 10.1074/jbc.m104136200.
• Actin-Binding Proteins: An OverviewDe La Cruz E. Actin-Binding Proteins: An Overview. 2001, 32: 123-134. PMID: 11131827, DOI: 10.1007/978-3-540-46560-7_9.
• Actin and Light Chain Isoform Dependence of Myosin V Kinetics †De La Cruz E, Wells A, Sweeney H, Ostap E. Actin and Light Chain Isoform Dependence of Myosin V Kinetics †. Biochemistry 2000, 39: 14196-14202. PMID: 11087368, DOI: 10.1021/bi001701b.
• ADP Inhibition of Myosin V ATPase ActivityDe La Cruz E, Sweeney H, Ostap E. ADP Inhibition of Myosin V ATPase Activity. Biophysical Journal 2000, 79: 1524-1529. PMID: 10969013, PMCID: PMC1301045, DOI: 10.1016/s0006-3495(00)76403-4.
• Thymosin-β4 Changes the Conformation and Dynamics of Actin MonomersDe La Cruz E, Ostap E, Brundage R, Reddy K, Sweeney H, Safer D. Thymosin-β4 Changes the Conformation and Dynamics of Actin Monomers. Biophysical Journal 2000, 78: 2516-2527. PMID: 10777749, PMCID: PMC1300842, DOI: 10.1016/s0006-3495(00)76797-x.
• Polymerization and structure of nucleotide-free actin filaments11Edited by W. BaumeisterDe La Cruz E, Mandinova A, Steinmetz M, Stoffler D, Aebi U, Pollard T. Polymerization and structure of nucleotide-free actin filaments11Edited by W. Baumeister. Journal Of Molecular Biology 2000, 295: 517-526. PMID: 10623543, DOI: 10.1006/jmbi.1999.3390.
• The kinetic mechanism of myosin VDe La Cruz E, Wells A, Rosenfeld S, Ostap E, Sweeney H. The kinetic mechanism of myosin V. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 13726-13731. PMID: 10570140, PMCID: PMC24132, DOI: 10.1073/pnas.96.24.13726.
• Regulation of G protein-coupled Receptor Kinase 5 (GRK5) by Actin*Freeman J, De La Cruz E, Pollard T, Lefkowitz R, Pitcher J. Regulation of G protein-coupled Receptor Kinase 5 (GRK5) by Actin*. Journal Of Biological Chemistry 1998, 273: 20653-20657. PMID: 9685424, DOI: 10.1074/jbc.273.32.20653.
• Interactions of Acanthamoeba Profilin with Actin and Nucleotides Bound to Actin †Vinson V, De La Cruz E, Higgs H, Pollard T. Interactions of Acanthamoeba Profilin with Actin and Nucleotides Bound to Actin †. Biochemistry 1998, 37: 10871-10880. PMID: 9692980, DOI: 10.1021/bi980093l.
• Kinetics and Thermodynamics of Phalloidin Binding to Actin Filaments from Three Divergent Species †De La Cruz E, Pollard T. Kinetics and Thermodynamics of Phalloidin Binding to Actin Filaments from Three Divergent Species †. Biochemistry 1996, 35: 14054-14061. PMID: 8916890, DOI: 10.1021/bi961047t.
• Nucleotide-free actin: stabilization by sucrose and nucleotide binding kinetics.De La Cruz EM, Pollard TD. Nucleotide-free actin: stabilization by sucrose and nucleotide binding kinetics. Biochemistry 1995, 34: 5452-61. PMID: 7727403, DOI: 10.1021/bi00016a016.
• Transient kinetic analysis of rhodamine phalloidin binding to actin filaments.De La Cruz EM, Pollard TD. Transient kinetic analysis of rhodamine phalloidin binding to actin filaments. Biochemistry 1994, 33: 14387-92. PMID: 7981198, DOI: 10.1021/bi00252a003.