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Enrique M. De La Cruz, PhD

Professor and Chair of Molecular Biophysics and Biochemistry; Head, Branford College

Contact Information

Enrique M. De La Cruz, PhD

Mailing Address

  • Molecular Biophysics and Biochemistry

    PO Box 208114, 266 Whitney Avenue

    New Haven, CT 06520-8114

    United States

De La Cruz Lab
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Research Summary

Identifying the chemical and physical principles of work production by molecular motor protein enzymes and polymers has emerged as a major area in contemporary Biochemistry and Biophysics. My research program integrates comprehensive kinetic and thermodynamic analyses of catalytic reaction pathways with computational and mathematical modeling to develop and test predictive models of work output by molecular motor proteins, enzyme function and adaptation, and biopolymer fragmentation. Our work has revealed how enzymatic adaptations among evolutionary related molecular motor proteins determine their biological function, and how cells regulate the length and assembly dynamics of polymers that drive cell movement.

Our current and future efforts focus primarily in three areas:

  1. identifying the molecular origins of actin filament elasticity and the mechanical basis of filament severing by regulatory proteins;
  2. defining how ATP utilization by DEAD-box proteins (DBPs) is coupled to duplex rRNA unwinding; and
  3. determining the catalytic pathways, specificities and biological activities of nucleotide pyrophosphatase/phosphodiesterase (NPP) enzymes.

Specialized Terms: Cytoskeleton; RNA helicases; Kinetics; Thermodynamics; Polymer Mechanics; Processivity

Extensive Research Description

Persistence software can be found on our Lab page.

Coauthors

Research Interests

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

Selected Publications

  • Improving the Pharmacodynamics and In Vivo Activity of ENPP1-Fc Through Protein and Glycosylation Engineering.Stabach 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 2021, 14: 362-372 PubMed ID: 33064927, PMCID: PMC7877847, DOI: 10.1111/cts.12887.
  • Structural basis of fast- and slow-severing actin-cofilactin boundaries.Hocky GM, Sindelar CV, Cao W, Voth GA, De La Cruz EM. Structural basis of fast- and slow-severing actin-cofilactin boundaries. The Journal Of Biological Chemistry 2021, 296: 100337 PubMed ID: 33508320, PMCID: PMC7961102, DOI: 10.1016/j.jbc.2021.100337.
  • Clusters of a Few Bound Cofilins Sever Actin Filaments.Bibeau JP, Gray S, De La Cruz EM. Clusters of a Few Bound Cofilins Sever Actin Filaments. Journal Of Molecular Biology 2021, 433: 166833 PubMed ID: 33524412, PMCID: PMC8689643, DOI: 10.1016/j.jmb.2021.166833.
  • Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments.Huehn 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 PubMed ID: 31900364, PMCID: PMC6983403, DOI: 10.1073/pnas.1915987117.
  • Thermal fracture kinetics of heterogeneous semiflexible polymers.Lorenzo AM, De La Cruz EM, Koslover EF. Thermal fracture kinetics of heterogeneous semiflexible polymers. Soft Matter 2020, 16: 2017-2024 PubMed ID: 31996875, PMCID: PMC7047574, DOI: 10.1039/c9sm01637f.
  • Directional allosteric regulation of protein filament length.Jermyn AS, Cao W, Elam WA, De La Cruz EM, Lin MM. Directional allosteric regulation of protein filament length. Physical Review. E 2020, 101: 032409 PubMed ID: 32290018, PMCID: PMC7758089, DOI: 10.1103/PhysRevE.101.032409.
  • 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 PubMed ID: 32461373, PMCID: PMC7306818, DOI: 10.1073/pnas.1911183117.
  • Regulation of axon growth by myosin II-dependent mechanocatalysis of cofilin activity.Zhang 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. The Journal Of Cell Biology 2019, 218: 2329-2349 PubMed ID: 31123185, PMCID: PMC6605792, DOI: 10.1083/jcb.201810054.
  • Plastic Deformation and Fragmentation of Strained Actin Filaments.Schramm 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 PubMed ID: 31301801, PMCID: PMC6697348, DOI: 10.1016/j.bpj.2019.06.018.
  • Active cargo positioning in antiparallel transport networks.Richard 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 PubMed ID: 31289230, PMCID: PMC6660773, DOI: 10.1073/pnas.1900416116.
  • 14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface.Karlberg 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 PubMed ID: 30224724, PMCID: PMC6141617, DOI: 10.1038/s41467-018-06194-1.
  • The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments.Huehn 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. The Journal Of Biological Chemistry 2018, 293: 5377-5383 PubMed ID: 29463680, PMCID: PMC5900768, DOI: 10.1074/jbc.AC118.001843.
  • Nup159 Weakens Gle1 Binding to Dbp5 But Does Not Accelerate ADP Release.Wong 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 PubMed ID: 29782832, PMCID: PMC6003625, DOI: 10.1016/j.jmb.2018.05.025.
  • Insights into the Cooperative Nature of ATP Hydrolysis in Actin Filaments.Katkar 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 PubMed ID: 30249402, PMCID: PMC6260209, DOI: 10.1016/j.bpj.2018.08.034.
  • Opening remarks from the Editors.De La Cruz EM, Blanchoin L, Ostap EM. Opening remarks from the Editors. Biophysical Reviews 2018, 10: 1479-1480 PubMed ID: 30488377, PMCID: PMC6297087, DOI: 10.1007/s12551-018-0487-3.
  • Mechanoregulated inhibition of formin facilitates contractile actomyosin ring assembly.Zimmermann 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 PubMed ID: 28951543, PMCID: PMC5614989, DOI: 10.1038/s41467-017-00445-3.
  • Phosphomimetic S3D cofilin binds but only weakly severs actin filaments.Elam 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. The Journal Of Biological Chemistry 2017, 292: 19565-19579 PubMed ID: 28939776, PMCID: PMC5712599, DOI: 10.1074/jbc.M117.808378.
  • Actin Filament Strain Promotes Severing and Cofilin Dissociation.Schramm 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 PubMed ID: 28636918, PMCID: PMC5479148, DOI: 10.1016/j.bpj.2017.05.016.
  • Architecture and Connectivity Govern Actin Network Contractility.Ennomani 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 : CB 2016, 26: 616-26 PubMed ID: 26898468, PMCID: PMC4959279, DOI: 10.1016/j.cub.2015.12.069.
  • Cations Stiffen Actin Filaments by Adhering a Key Structural Element to Adjacent Subunits.Hocky 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: 4558-67 PubMed ID: 27146246, PMCID: PMC4959277, DOI: 10.1021/acs.jpcb.6b02741.
  • P(I) 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. P(I) Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5). Journal Of Molecular Biology 2016, 428: 492-508 PubMed ID: 26730886, PMCID: PMC4744555, DOI: 10.1016/j.jmb.2015.12.018.
  • Neuronal Calcium Sensor 1 Has Two Variants with Distinct Calcium Binding Characteristics.Wang 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 PubMed ID: 27575489, PMCID: PMC5004852, DOI: 10.1371/journal.pone.0161414.
  • Metavinculin Tunes the Flexibility and the Architecture of Vinculin-Induced Bundles of Actin Filaments.Oztug Durer ZA, 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: 2782-98 PubMed ID: 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. The Journal Of Biological Chemistry 2015, 290: 17137-44 PubMed ID: 25957404, PMCID: PMC4498053, DOI: 10.1074/jbc.R115.636472.
  • ENPP1-Fc prevents mortality and vascular calcifications in rodent model of generalized arterial calcification of infancy.Albright 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 PubMed ID: 26624227, PMCID: PMC4686714, DOI: 10.1038/ncomms10006.
  • Mechanical heterogeneity favors fragmentation of strained actin filaments.De La Cruz EM, Martiel JL, Blanchoin L. Mechanical heterogeneity favors fragmentation of strained actin filaments. Biophysical Journal 2015, 108: 2270-81 PubMed ID: 25954884, PMCID: PMC4423049, DOI: 10.1016/j.bpj.2015.03.058.
  • 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. The Journal Of Biological Chemistry 2014, 289: 3294-306 PubMed ID: 24338010, PMCID: PMC3916532, DOI: 10.1074/jbc.M113.505867.
  • Multi-platform compatible software for analysis of polymer bending mechanics.Graham 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 PubMed ID: 24740323, PMCID: PMC3989245, DOI: 10.1371/journal.pone.0094766.
  • Site-specific cation release drives actin filament severing by vertebrate cofilin.Kang 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: 17821-6 PubMed ID: 25468977, PMCID: PMC4273407, DOI: 10.1073/pnas.1413397111.
  • Navigating the cell: how motors function in vivo.De La Cruz EM, Holzbaur EL. Navigating the cell: how motors function in vivo. Journal Of Cell Science 2014, 127: 2997-8 PubMed ID: 25024456, DOI: 10.1242/jcs.156414.
  • Quantitative full time course analysis of nonlinear enzyme cycling kinetics.Cao W, De La Cruz EM. Quantitative full time course analysis of nonlinear enzyme cycling kinetics. Scientific Reports 2013, 3: 2658 PubMed ID: 24029878, PMCID: PMC3772379, DOI: 10.1038/srep02658.
  • Take advantage of time in your experiments: a guide to simple, informative kinetics assays.Pollard 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: 1103-10 PubMed ID: 23580192, PMCID: PMC3623632, DOI: 10.1091/mbc.E13-01-0030.
  • Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics.Xia 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: 9077-89 PubMed ID: 23921641, PMCID: PMC3799440, DOI: 10.1093/nar/gkt674.
  • Molecular origins of cofilin-linked changes in actin filament mechanics.Fan 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: 1225-40 PubMed ID: 23352932, PMCID: PMC3740545, DOI: 10.1016/j.jmb.2013.01.020.
  • Biophysics of actin filament severing by cofilin.Elam WA, Kang H, De la Cruz EM. Biophysics of actin filament severing by cofilin. FEBS Letters 2013, 587: 1215-9 PubMed ID: 23395798, PMCID: PMC4079045, DOI: 10.1016/j.febslet.2013.01.062.
  • Actin organization and dynamics: novel regulatory mechanisms from the biophysical to the tissue level.Miller 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 PubMed ID: 23486401, PMCID: PMC3596237, DOI: 10.1091/mbc.E12-12-0879.
  • Competitive displacement of cofilin can promote actin filament severing.Elam WA, Kang H, De La Cruz EM. Competitive displacement of cofilin can promote actin filament severing. Biochemical And Biophysical Research Communications 2013, 438: 728-31 PubMed ID: 23911787, PMCID: PMC3785092, DOI: 10.1016/j.bbrc.2013.07.109.
  • Regulation of actin by ion-linked equilibria.Kang H, Bradley MJ, Elam WA, De La Cruz EM. Regulation of actin by ion-linked equilibria. Biophysical Journal 2013, 105: 2621-8 PubMed ID: 24359734, PMCID: PMC3882474, DOI: 10.1016/j.bpj.2013.10.032.
  • Actin network architecture can determine myosin motor activity.Reymann 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 (New York, N.Y.) 2012, 336: 1310-4 PubMed ID: 22679097, PMCID: PMC3649007, DOI: 10.1126/science.1221708.
  • NPP4 is a procoagulant enzyme on the surface of vascular endothelium.Albright 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: 4432-40 PubMed ID: 22995898, PMCID: PMC4017314, DOI: 10.1182/blood-2012-04-425215.
  • Plus-end directed myosins accelerate actin filament sliding by single-headed myosin VI.Ramamurthy B, Cao W, De la Cruz EM, Mooseker MS. Plus-end directed myosins accelerate actin filament sliding by single-headed myosin VI. Cytoskeleton (Hoboken, N.J.) 2012, 69: 59-69 PubMed ID: 22213699, PMCID: PMC3327287, DOI: 10.1002/cm.21002.
  • Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness.Kang 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: 16923-7 PubMed ID: 23027950, PMCID: PMC3479481, DOI: 10.1073/pnas.1211078109.
  • Analyzing ATP utilization by DEAD-Box RNA helicases using kinetic and equilibrium methods.Bradley MJ, De La Cruz EM. Analyzing ATP utilization by DEAD-Box RNA helicases using kinetic and equilibrium methods. Methods In Enzymology 2012, 511: 29-63 PubMed ID: 22713314, PMCID: PMC7768905, DOI: 10.1016/B978-0-12-396546-2.00002-4.
  • ATP utilization and RNA conformational rearrangement by DEAD-box proteins.Henn A, Bradley MJ, De La Cruz EM. ATP utilization and RNA conformational rearrangement by DEAD-box proteins. Annual Review Of Biophysics 2012, 41: 247-67 PubMed ID: 22404686, PMCID: PMC7761782, DOI: 10.1146/annurev-biophys-050511-102243.
  • Mechanism of Mss116 ATPase reveals functional diversity of DEAD-Box proteins.Cao 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 PubMed ID: 21501623, PMCID: PMC3125984, DOI: 10.1016/j.jmb.2011.04.004.
  • Cofilin-linked changes in actin filament flexibility promote severing.McCullough 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: 151-9 PubMed ID: 21723825, PMCID: PMC3127193, DOI: 10.1016/j.bpj.2011.05.049.
  • Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate.Wu 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: 18672-7 PubMed ID: 22065758, PMCID: PMC3219131, DOI: 10.1073/pnas.1110415108.
  • 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. The Journal Of Biological Chemistry 2011, 286: 30130-41 PubMed ID: 21719699, PMCID: PMC3191052, DOI: 10.1074/jbc.M111.246884.
  • Actin filament dynamics in the actomyosin VI complex is regulated allosterically by calcium-calmodulin light chain.Prochniewicz 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: 584-92 PubMed ID: 21910998, PMCID: PMC3633491, DOI: 10.1016/j.jmb.2011.08.058.
  • Cofilin tunes the nucleotide state of actin filaments and severs at bare and decorated segment boundaries.Suarez 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 : CB 2011, 21: 862-8 PubMed ID: 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 actin.Shiroguchi 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 PubMed ID: 21532738, PMCID: PMC3075224, DOI: 10.1371/journal.pbio.1001031.
  • Origin of twist-bend coupling in actin filaments.De La Cruz EM, Roland J, McCullough BR, Blanchoin L, Martiel JL. Origin of twist-bend coupling in actin filaments. Biophysical Journal 2010, 99: 1852-60 PubMed ID: 20858430, PMCID: PMC2941021, DOI: 10.1016/j.bpj.2010.07.009.
  • Pathway of ATP utilization and duplex rRNA unwinding by the DEAD-box helicase, DbpA.Henn 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: 4046-50 PubMed ID: 20160110, PMCID: PMC2840157, DOI: 10.1073/pnas.0913081107.
  • A myosin V inhibitor based on privileged chemical scaffolds.Islam 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 Ed. In English) 2010, 49: 8484-8 PubMed ID: 20878825, PMCID: PMC3063097, DOI: 10.1002/anie.201004026.
  • Structure-based analysis of Toxoplasma gondii profilin: a parasite-specific motif is required for recognition by Toll-like receptor 11.Kucera 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: 616-29 PubMed ID: 20851125, PMCID: PMC2957522, DOI: 10.1016/j.jmb.2010.09.022.
  • Robust processivity of myosin V under off-axis loads.Oguchi 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: 300-5 PubMed ID: 20228794, PMCID: PMC2917589, DOI: 10.1038/nchembio.322.
  • Actin filament remodeling by actin depolymerization factor/cofilin.Pfaendtner 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: 7299-304 PubMed ID: 20368459, PMCID: PMC2867716, DOI: 10.1073/pnas.0911675107.
  • The kinetics of cooperative cofilin binding reveals two states of the cofilin-actin filament.De La Cruz EM, Sept D. The kinetics of cooperative cofilin binding reveals two states of the cofilin-actin filament. Biophysical Journal 2010, 98: 1893-901 PubMed ID: 20441753, PMCID: PMC2862197, DOI: 10.1016/j.bpj.2010.01.023.
  • Myosin isoform determines the conformational dynamics and cooperativity of actin filaments in the strongly bound actomyosin complex.Prochniewicz 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 2010, 396: 501-9 PubMed ID: 19962990, PMCID: PMC2834967, DOI: 10.1016/j.jmb.2009.11.063.
  • Kinetic analysis of the guanine nucleotide exchange activity of TRAPP, a multimeric Ypt1p exchange factor.Chin 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: 275-88 PubMed ID: 19361519, PMCID: PMC2770256, DOI: 10.1016/j.jmb.2009.03.068.
  • How cofilin severs an actin filament.De La Cruz EM. How cofilin severs an actin filament. Biophysical Reviews 2009, 1: 51-59 PubMed ID: 20700473, PMCID: PMC2917815, DOI: 10.1007/s12551-009-0008-5.
  • Watching the walk: observing chemo-mechanical coupling in a processive myosin motor.De La Cruz EM, Olivares AO. Watching the walk: observing chemo-mechanical coupling in a processive myosin motor. HFSP Journal 2009, 3: 67-70 PubMed ID: 19794813, PMCID: PMC2707789, DOI: 10.2976/1.3095425.
  • Kinetic and equilibrium analysis of the myosin ATPase.De La Cruz EM, Ostap EM. Kinetic and equilibrium analysis of the myosin ATPase. Methods In Enzymology 2009, 455: 157-92 PubMed ID: 19289206, PMCID: PMC2921708, DOI: 10.1016/S0076-6879(08)04206-7.
  • Dimerization of FIR upon FUSE DNA binding suggests a mechanism of c-myc inhibition.Crichlow 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 2008, 27: 277-89 PubMed ID: 18059478, PMCID: PMC2206118, DOI: 10.1038/sj.emboj.7601936.
  • Load-dependent ADP binding to myosins V and VI: implications for subunit coordination and function.Oguchi 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: 7714-9 PubMed ID: 18509050, PMCID: PMC2409399, DOI: 10.1073/pnas.0800564105.
  • The ATPase cycle mechanism of the DEAD-box rRNA helicase, DbpA.Henn A, Cao W, Hackney DD, De La Cruz EM. The ATPase cycle mechanism of the DEAD-box rRNA helicase, DbpA. Journal Of Molecular Biology 2008, 377: 193-205 PubMed ID: 18237742, PMCID: PMC2359651, DOI: 10.1016/j.jmb.2007.12.046.
  • Effects of solution crowding on actin polymerization reveal the energetic basis for nucleotide-dependent filament stability.Frederick 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: 540-50 PubMed ID: 18374941, PMCID: PMC2424216, DOI: 10.1016/j.jmb.2008.02.022.
  • Widely distributed residues in thymosin beta4 are critical for actin binding.Au JK, Olivares AO, Henn A, Cao W, Safer D, De La Cruz EM. Widely distributed residues in thymosin beta4 are critical for actin binding. Biochemistry 2008, 47: 4181-8 PubMed ID: 18327913, PMCID: PMC2587058, DOI: 10.1021/bi701769u.
  • Cofilin increases the bending flexibility of actin filaments: implications for severing and cell mechanics.McCullough 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: 550-8 PubMed ID: 18617188, PMCID: PMC2753234, DOI: 10.1016/j.jmb.2008.05.055.
  • 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: 1202-13 PubMed ID: 18585354, PMCID: PMC2465810, DOI: 10.1016/j.cell.2008.04.049.
  • Identification of small-molecule inhibitors of autotaxin that inhibit melanoma cell migration and invasion.Saunders 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: 3352-62 PubMed ID: 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. The Journal Of The Korean Physical Society 2008, 53: 1726-1730 PubMed ID: 20552037, PMCID: PMC2884403, DOI: 10.3938/jkps.53.1726.
  • Structural and energetic analysis of activation by a cyclic nucleotide binding domain.Altieri 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: 655-69 PubMed ID: 18619611, PMCID: PMC2555981, DOI: 10.1016/j.jmb.2008.06.011.
  • Fluorescence 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: 6052-62 PubMed ID: 17766250, PMCID: PMC2094073, DOI: 10.1093/nar/gkm587.
  • Contributions from all over: widely distributed residues in thymosin beta-4 affect the kinetics and stability of actin binding.Au JK, De La Cruz EM, Safer D. Contributions from all over: widely distributed residues in thymosin beta-4 affect the kinetics and stability of actin binding. Annals Of The New York Academy Of Sciences 2007, 1112: 38-44 PubMed ID: 17468230, DOI: 10.1196/annals.1415.015.
  • The tail domain of myosin Va modulates actin binding to one head.Olivares AO, Chang W, Mooseker MS, Hackney DD, De La Cruz EM. The tail domain of myosin Va modulates actin binding to one head. The Journal Of Biological Chemistry 2006, 281: 31326-36 PubMed ID: 16921171, DOI: 10.1074/jbc.M603898200.
  • Energetics and kinetics of cooperative cofilin-actin filament interactions.Cao W, Goodarzi JP, De La Cruz EM. Energetics and kinetics of cooperative cofilin-actin filament interactions. Journal Of Molecular Biology 2006, 361: 257-67 PubMed ID: 16843490, DOI: 10.1016/j.jmb.2006.06.019.
  • Hydrodynamic characterization of the DEAD-box RNA helicase DbpA.Talavera 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 2006, 355: 697-707 PubMed ID: 16325852, DOI: 10.1016/j.jmb.2005.10.058.
  • Thymosin beta4 induces a conformational change in actin monomers.Dedova IV, Nikolaeva OP, Safer D, De La Cruz EM, dos Remedios CG. Thymosin beta4 induces a conformational change in actin monomers. Biophysical Journal 2006, 90: 985-92 PubMed ID: 16272441, PMCID: PMC1367123, DOI: 10.1529/biophysj.105.063081.
  • 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: 10238-49 PubMed ID: 16042401, DOI: 10.1021/bi050232g.
  • Cofilin binding to muscle and non-muscle actin filaments: isoform-dependent cooperative interactions.De La Cruz EM. Cofilin binding to muscle and non-muscle actin filaments: isoform-dependent cooperative interactions. Journal Of Molecular Biology 2005, 346: 557-64 PubMed ID: 15670604, DOI: 10.1016/j.jmb.2004.11.065.
  • 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. The Journal Of Biological Chemistry 2005, 280: 39665-76 PubMed ID: 16186105, DOI: 10.1074/jbc.M507667200.
  • 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: 8826-40 PubMed ID: 15952789, DOI: 10.1021/bi0473509.
  • Cofilin increases the torsional flexibility and dynamics of actin filaments.Prochniewicz 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 PubMed ID: 16213521, DOI: 10.1016/j.jmb.2005.09.021.
  • Holding the reins on myosin V.Olivares 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: 13719-20 PubMed ID: 16172373, PMCID: PMC1236595, DOI: 10.1073/pnas.0507068102.
  • 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 2005, 44: 959-70 PubMed ID: 15654752, DOI: 10.1021/bi048253i.
  • 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. The Journal Of Biological Chemistry 2004, 279: 38608-17 PubMed ID: 15247304, DOI: 10.1074/jbc.M403504200.
  • Mechanochemical coupling of two substeps in a single myosin V motor.Uemura 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: 877-83 PubMed ID: 15286720, DOI: 10.1038/nsmb806.
  • Relating biochemistry and function in the myosin superfamily.De La Cruz EM, Ostap EM. Relating biochemistry and function in the myosin superfamily. Current Opinion In Cell Biology 2004, 16: 61-7 PubMed ID: 15037306, DOI: 10.1016/j.ceb.2003.11.011.
  • 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. The Journal Of Biological Chemistry 2002, 277: 24114-9 PubMed ID: 11959853, DOI: 10.1074/jbc.M111253200.
  • 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: 8508-17 PubMed ID: 12081502, DOI: 10.1021/bi015969u.
  • Structural biology. Actin' up.De La Cruz EM, Pollard TD. Structural biology. Actin' up. Science (New York, N.Y.) 2001, 293: 616-8 PubMed ID: 11474090, DOI: 10.1126/science.1063558.
  • Polymerization and structure of nucleotide-free actin filaments.De La Cruz EM, Mandinova A, Steinmetz MO, Stoffler D, Aebi U, Pollard TD. Polymerization and structure of nucleotide-free actin filaments. Journal Of Molecular Biology 2000, 295: 517-26 PubMed ID: 10623543, DOI: 10.1006/jmbi.1999.3390.
  • Regulation of G protein-coupled receptor kinase 5 (GRK5) by actin.Freeman JL, De La Cruz EM, Pollard TD, Lefkowitz RJ, Pitcher JA. Regulation of G protein-coupled receptor kinase 5 (GRK5) by actin. The Journal Of Biological Chemistry 1998, 273: 20653-7 PubMed ID: 9685424, DOI: 10.1074/jbc.273.32.20653.
  • Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin.Vinson VK, De La Cruz EM, Higgs HN, Pollard TD. Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin. Biochemistry 1998, 37: 10871-80 PubMed ID: 9692980, DOI: 10.1021/bi980093l.
  • Kinetics and thermodynamics of phalloidin binding to actin filaments from three divergent species.De La Cruz EM, Pollard TD. Kinetics and thermodynamics of phalloidin binding to actin filaments from three divergent species. Biochemistry 1996, 35: 14054-61 PubMed ID: 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 PubMed ID: 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 PubMed ID: 7981198, DOI: 10.1021/bi00252a003.
  • Rab34 GTPase mediates ciliary membrane formation in the intracellular ciliogenesis pathway.Ganga 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 : CB 2021, 31: 2895-2905.e7 PubMed ID: 33989527, PMCID: PMC8282722, DOI: 10.1016/j.cub.2021.04.075.
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