Targeting phospholipase D in cancer, infection and neurodegenerative disorders

The transcription factor Myc controls metabolic reprogramming upon T lymphocyte activation

Wang, R., Dillon, C. P., Shi, L. Z., Milasta, S., Carter, R., Finkelstein, D., McCormick, L. L., Fitzgerald, P., Chi, H., Munger, J., et al. (2011) · Immunity · doi:10.1016/j.immuni.2011.09.021 · Cited by 2,140 · see citing works

The Effect of Raloxifene on Risk of Breast Cancer in Postmenopausal Women: Results From the MORE Randomized Trial

Cummings, S. R., Eckert, S., Krueger, K. A., Grady, D., Powles, T. J., Cauley, J. A., Norton, L., Nickelsen, T., Bjarnason, N. H., Morrow, M., et al. (1999) · JAMA · doi:10.1001/jama.281.23.2189 · Cited by 1,872 · see citing works

ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity

Brown, H. A., Gutowski, S., Moomaw, C. R., Slaughter, C. A., & Sternwels, P. C. (1993) · Cell · doi:10.1016/0092-8674(93)90323-i · Cited by 901 · see citing works

Phosphatidylinositol 4-Phosphate 5-Kinase α Is a Downstream Effector of the Small G Protein ARF6 in Membrane Ruffle Formation

Honda, A., Nogami, M., Yokozeki, T., Yamazaki, M., Nakamura, H., Watanabe, H., Kawamoto, K., Nakayama, K., Morris, A. J., Frohman, M. A., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)81540-8 · Cited by 798 · see citing works

The effect of raloxifene on risk of breast cancer in postmenopausal women : results from the MORE randomized trial. Multiple Outcomes of Raloxifene Evaluation

Cummings, S. R. (1999) · Medical Entomology and Zoology · Cited by 797 · see citing works

Phospholipase D: a Downstream Effector of ARF in Granulocytes

Cockcroft, S., Thomas, G. M. H., Fensome, A. C., Geny, B., Cunningham, E., Gout, I. T., Hiles, I. D., Totty, N. F., Truong, O., & Hsuan, J. J. (1994) · Science · doi:10.1126/science.8290961 · Cited by 631 · see citing works

Allosteric Akt (PKB) inhibitors: discovery and SAR of isozyme selective inhibitors

Lindsley, C. W., Zhao, Z., Leister, W., Robinson, R., Barnett, S. F., Defeo-Jones, D., Jones, R. E., Hartman, G. D., Huff, J. R., Huber, H. E., et al. (2004) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2004.11.011 · Cited by 504 · see citing works

Rare coding variants in the phospholipase D3 gene confer risk for Alzheimer’s disease

Cruchaga, C., Karch, C. M., Jin, S. C., Benitez, B. A., Cai, Y., Guerreiro, R., Harari, O., Norton, J., Budde, J., Bertelsen, S., et al. (2014) · Nature · doi:10.1038/nature12825 · Cited by 461 · see citing works

Diverse type VI secretion phospholipases are functionally plastic antibacterial effectors

Russell, A. B., LeRoux, M., Hathazi, K., Agnello, D. M., Ishikawa, T., Wiggins, P. A., Wai, S. N., & Mougous, J. D. (2013) · Nature · doi:10.1038/nature12074 · Cited by 415 · see citing works

Modulation of Membrane Curvature by Phosphatidic Acid and Lysophosphatidic Acid

Kooijman, E. E., Chupin, V., KRUIJFF, B. D., & Burger, K. N. J. (2003) · Traffic · doi:10.1034/j.1600-0854.2003.00086.x · Cited by 404 · see citing works

Phospholipase D: Enzymology, Functionality, and Chemical Modulation

Selvy, P. E., Lavieri, R. R., Lindsley, C. W., & Brown, H. A. (2011) · Chemical Reviews · doi:10.1021/cr200296t · Cited by 392 · see citing works

Coronavirus Cell Entry Occurs through the Endo-/Lysosomal Pathway in a Proteolysis-Dependent Manner

Tait‐Burkard, C., Verheije, M. H., Wicht, O., van Kasteren, S. I., van Kuppeveld, F. J. M., Haagmans, B. L., Pelkmans, L., Rottier, P. J. M., Bosch, B., & de Haan, C. A. M. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004502 · Cited by 389 · see citing works

Regulation of phospholipase D

Exton, J. H. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(99)00089-x · Cited by 366 · see citing works

Alteration of mTOR signaling occurs early in the progression of Alzheimer disease (AD): analysis of brain from subjects with pre‐clinical AD, amnestic mild cognitive impairment and late‐stage AD

Tramutola, A., Triplett, J. C., Di Domenico, F., Niedowicz, D. M., Murphy, M. P., Coccia, R., Perluigi, M., & Butterfield, D. A. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13037 · Cited by 347 · see citing works

A novel family of phospholipase D homologues that includes phospholipid synthases and putative endonucleases: Identification of duplicated repeats and potential active site residues

Ponting, C. P., & Kerr, I. D. (1996) · Protein Science · doi:10.1002/pro.5560050513 · Cited by 328 · see citing works

Role of Yersinia Murine Toxin in Survival of Yersinia pestis in the Midgut of the Flea Vector

Hinnebusch, B. J., Rudolph, A. E., Cherepanov, P., Dixon, J. E., Schwan, T. G., & Försberg, Å. (2002) · Science · doi:10.1126/science.1069972 · Cited by 315 · see citing works

Phospholipase D2-generated phosphatidic acid couples EGFR stimulation to Ras activation by Sos

Zhao, C., Du, G., Skowronek, K., Frohman, M. A., & Bar‐Sagi, D. (2007) · Nature Cell Biology · doi:10.1038/ncb1594 · Cited by 295 · see citing works

Design of isoform-selective phospholipase D inhibitors that modulate cancer cell invasiveness

Scott, S. A., Selvy, P. E., Buck, J. R., Cho, H. P., Criswell, T. L., Thomas, A. L., Armstrong, M. D., Arteaga, C. L., Lindsley, C. W., & Brown, H. A. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.140 · Cited by 283 · see citing works

Phospholipase D Signaling Pathways and Phosphatidic Acid as Therapeutic Targets in Cancer

Bruntz, R. C., Lindsley, C. W., & Brown, H. A. (2014) · Pharmacological Reviews · doi:10.1124/pr.114.009217 · Cited by 275 · see citing works

5-Fluoro-2-indolyl des-chlorohalopemide (FIPI), a Phospholipase D Pharmacological Inhibitor That Alters Cell Spreading and Inhibits Chemotaxis

Su, W., Yeku, O., Srinivas, O., Genna, A., Park, J.-S., Ren, H., Du, G., Gelb, M. H., Morris, A. J., & Frohman, M. A. (2008) · Molecular Pharmacology · doi:10.1124/mol.108.053298 · Cited by 251 · see citing works

Molecular determinants of tissue selectivity in estrogen receptor modulators

Grese, T. A., Sluka, J. P., Bryant, H. U., Cullinan, G. J., Glasebrook, A. L., Jones, C. D., Matsumoto, K., Palkowitz, A. D., Sato, M., Termine, J. D., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.25.14105 · Cited by 243 · see citing works

Activation of Phosphatidylcholine Cycle Enzymes in Human Epithelial Ovarian Cancer Cells

Iorio, E., Ricci, A. L., Bagnoli, M., Pisanu, M. E., Castellano, G., Vito, M. D., Venturini, E., Glunde, K., Bhujwalla, Z. M., Mezzanzanica, D., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-3833 · Cited by 228 · see citing works

Inactivation of Phospholipase D DiminishesAcinetobacter baumanniiPathogenesis

Jacobs, A. C., Hood-Pishchany, M. I., Boyd, K. L., Olson, P. D., Morrison, J. M., Carson, S. D., Sayood, K., Iwen, P. C., Skaar, E. P., & Dunman, P. M. (2010) · Infection and Immunity · doi:10.1128/iai.00889-09 · Cited by 215 · see citing works

Compartmentalized Replication of R5 T Cell-Tropic HIV-1 in the Central Nervous System Early in the Course of Infection

Sturdevant, C. B., Joseph, S., Schnell, G., Price, R. W., Swanstrom, R. I., & Spudich, S. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004720 · Cited by 200 · see citing works

Phospholipase D confers rapamycin resistance in human breast cancer cells

Chen, Y., Yang, Z., & Foster, D. A. (2003) · Oncogene · doi:10.1038/sj.onc.1206565 · Cited by 196 · see citing works

Impaired αIIbβ3Integrin Activation and Shear-Dependent Thrombus Formation in Mice Lacking Phospholipase D1

Elvers, M., Stegner, D., Hagedorn, I., Kleinschnitz, C., Braun, A., Kuijpers, M. J. E., Boesl, M. R., Chen, Q., Heemskerk, J. W. M., Stoll, G., et al. (2010) · Science Signaling · doi:10.1126/scisignal.2000551 · Cited by 193 · see citing works

Phospholipase D2 Ablation Ameliorates Alzheimer's Disease-Linked Synaptic Dysfunction and Cognitive Deficits

Oliveira, T. G., Chan, R., Tian, H., Laredo, M., Shui, G., Staniszewski, A., Zhang, H., Wang, L., Kim, T., Duff, K., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.3317-10.2010 · Cited by 179 · see citing works

Constitutive and lysophosphatidic acid (LPA)-induced LPA production: role of phospholipase D and phospholipase A2.

Eder, A. M., Sasagawa, T., Mao, M., Aoki, J., & Mills, G. B. (2000) · PubMed · Cited by 175 · see citing works

Structure and regulation of phospholipase D

Morris, A. J., Engebrecht, J., & Frohman, M. A. (1996) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(96)10016-x · Cited by 175 · see citing works

Tumor cell sensitization to apoptotic stimuli by selective inhibition of specific Akt/PKB family members

Defeo-Jones, D., Barnett, S. F., Fu, S., Hancock, P. J., Haskell, K., Leander, K. R., McAvoy, E., Robinson, R., Duggan, M. E., Lindsley, C. W., et al. (2005) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.271.4.2 · Cited by 173 · see citing works

Overexpression of phospholipase D1 in human breast cancer tissues

Noh, D. (2000) · Cancer Letters · doi:10.1016/s0304-3835(00)00612-1 · Cited by 166 · see citing works

Biophysics and function of phosphatidic acid: A molecular perspective

Kooijman, E. E., & Burger, K. N. J. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.04.001 · Cited by 164 · see citing works

Partial Purification and Characterization of Arf-sensitive Phospholipase D from Porcine Brain

Brown, H. A., Gutowski, S., Kahn, R., & Sternweis, P. C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.25.14935 · Cited by 148 · see citing works

Mammalian phospholipase D physiological and pathological roles

Peng, X., & Frohman, M. A. (2011) · Acta Physiologica · doi:10.1111/j.1748-1716.2011.02298.x · Cited by 141 · see citing works

Increased Activity and Intranuclear Expression of Phospholipase D2 in Human Renal Cancer

Zhao, Y., Ehara, H., Akao, Y., Shamoto, M., Nakagawa, Y., Banno, Y., Deguchi, T., Ohishi, N., Yagi, K., & Nozawa, Y. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3719 · Cited by 137 · see citing works

Nonproductive Human Immunodeficiency Virus Type 1 Infection in Nucleoside-Treated G 0 Lymphocytes

Korin, Y. D., & Zack, J. A. (1999) · Journal of Virology · doi:10.1128/jvi.73.8.6526-6532.1999 · Cited by 134 · see citing works

Phospholipase D and the Maintenance of Phosphatidic Acid Levels for Regulation of Mammalian Target of Rapamycin (mTOR)

Foster, D. A., Salloum, D., Menon, D., & Frías, M. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.566091 · Cited by 133 · see citing works

Lipid Composition of the Viral Envelope of Three Strains of Influenza Virus—Not All Viruses Are Created Equal

Ivanova, P. T., Myers, D. S., Milne, S. B., McClaren, J. L., Thomas, P. G., & Brown, H. A. (2015) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.5b00040 · Cited by 116 · see citing works

Dynamic phospholipid signaling by G protein-coupled receptors

Weernink, P. A. O., Li, H., Jakobs, K. H., & Schmidt, M. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.09.012 · Cited by 114 · see citing works

Small Interfering RNA Profiling Reveals Key Role of Clathrin-Mediated Endocytosis and Early Endosome Formation for Infection by Respiratory Syncytial Virus

Kolokoltsov, A. A., Deniger, D. C., Fleming, E. H., Roberts, N. J., Karpilow, J. M., & Davey, R. A. (2007) · Journal of Virology · doi:10.1128/jvi.02780-06 · Cited by 113 · see citing works

FAM83B mediates EGFR- and RAS-driven oncogenic transformation

Cipriano, R., Graham, J., Miskimen, K. L. S., Bryson, B. L., Bruntz, R. C., Scott, S. A., Brown, H. A., Stark, G. R., & Jackson, M. W. (2012) · Journal of Clinical Investigation · doi:10.1172/jci60517 · Cited by 111 · see citing works

Localization of <i>N</i>‐acyl phosphatidylethanolamine phospholipase D (NAPE‐PLD) expression in mouse brain: A new perspective on <i>N</i>‐acylethanolamines as neural signaling molecules

Egertová, M., Simon, G. M., Cravatt, B. F., & Elphick, M. R. (2008) · Journal of Comparative Neurology · doi:10.1002/cne.21568 · Cited by 111 · see citing works

Presenilin-1 uses phospholipase D1 as a negative regulator of β-amyloid formation

Cai, D., Netzer, W. J., Zhong, M., Lin, Y., Du, G., Frohman, M. A., Foster, D. A., Sisodia, S. S., Xu, H., Gorelick, F. S., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510708103 · Cited by 110 · see citing works

Role of Phospholipase D Activation in Nervous System Physiology and Pathophysiology

Klein, J., Caspi, V. C., Liscovitch, M., & Löffelholz, K. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.65041445.x · Cited by 108 · see citing works

Expression, Characterization, and Mutagenesis of theYersinia pestis Murine Toxin, a Phospholipase D Superfamily Member

Rudolph, A. E., Stuckey, J. A., Zhao, Y. C., Matthews, H. R., Patton, W. A., Moss, J., & Dixon, J. E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.17.11824 · Cited by 108 · see citing works

ADP-ribosylation Factor Functions Synergistically with a 50-kDa Cytosolic Factor in Cell-free Activation of Human Neutrophil Phospholipase D

Lambeth, J. D., Kwak, J.-Y., Bowman, E. P., Perry, D., Uhlinger, D. J., & Lopez, I. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.6.2431 · Cited by 104 · see citing works

Optimization of Halopemide for Phospholipase D2 inhibition

Monovich, L. G., Mugrage, B. B., Quadros, E., Toscano, K., Tommasi, R., LaVoie, S., Liu, E. W., Du, Z., LaSala, D., Boyar, W. C., et al. (2007) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.01.059 · Cited by 102 · see citing works

Design and synthesis of isoform-selective phospholipase D (PLD) inhibitors. Part I: Impact of alternative halogenated privileged structures for PLD1 specificity

Lewis, J. A., Scott, S. A., Lavieri, R. R., Buck, J. R., Selvy, P. E., Stoops, S. L., Armstrong, M. D., Brown, H. A., & Lindsley, C. W. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.02.057 · Cited by 102 · see citing works

Rapid Mitogenic Regulation of the mTORC1 Inhibitor, DEPTOR, by Phosphatidic Acid

Yoon, M., Rosenberger, C. L., Wu, C., Truong, N., Sweedler, J. V., & Chen, J. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.03.028 · Cited by 101 · see citing works

Synaptic vesicle-like lipidome of human cytomegalovirus virions reveals a role for SNARE machinery in virion egress

Liu, S. T. H., Sharon-Friling, R., Ivanova, P. T., Milne, S. B., Myers, D. S., Rabinowitz, J. D., Brown, H. A., & Shenk, T. E. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1109796108 · Cited by 100 · see citing works

Phospholipase D in brain function and Alzheimer's disease

Oliveira, T. G., & Paolo, G. D. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2010.04.004 · Cited by 97 · see citing works

Biochemical Analysis of Phospholipase D

Brown, H. A., Henage, L. G., Preininger, A. M., Xiang, Y., & Exton, J. H. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)34004-4 · Cited by 91 · see citing works

Phospholipase D in Cell Signaling: From a Myriad of Cell Functions to Cancer Growth and Metastasis

Gómez-Cambronero, J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.574152 · Cited by 91 · see citing works

Design, Synthesis, and Biological Evaluation of Halogenated N-(2-(4-Oxo-1-phenyl-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)benzamides: Discovery of an Isoform-Selective Small Molecule Phospholipase D2 Inhibitor

Lavieri, R. R., Scott, S. A., Selvy, P. E., Kim, K., Jadhav, S. B., Morrison, R. D., Daniels, J. S., Brown, H. A., & Lindsley, C. W. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100814g · Cited by 90 · see citing works

Silibinin inhibits hepatitis C virus entry into hepatocytes by hindering clathrin-dependent trafficking

Blaising, J., Levy, P. L., Gondeau, C., Phelip, C., Varbanov, M., Teissier, É., Ruggiero, F., Polyak, S. J., Oberlies, N. H., Ivanovic, T., et al. (2013) · Cellular Microbiology · doi:10.1111/cmi.12155 · Cited by 87 · see citing works

Increased phospholipase D activity in human breast cancer

Uchida, N., Okamura, S.-I., Nagamachi, Y., & Yamashita, S. (1997) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/bf01208639 · Cited by 87 · see citing works

mTOR signaling: PLD takes center stage

Sun, Y., & Chen, J. (2008) · Cell Cycle · doi:10.4161/cc.7.20.6881 · Cited by 84 · see citing works

Phospholipase D2 Mediates Survival Signaling through Direct Regulation of Akt in Glioblastoma Cells

Bruntz, R. C., Taylor, H. E., Lindsley, C. W., & Brown, H. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.532978 · Cited by 83 · see citing works

Pseudomonas aeruginosa Synthesizes Phosphatidylcholine by Use of the Phosphatidylcholine Synthase Pathway

Wilderman, P. J., Vasil, A. I., Martin, W. E., Murphy, R. C., & Vasil, M. L. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.17.4792-4799.2002 · Cited by 81 · see citing works

Development of Dual PLD1/2 and PLD2 Selective Inhibitors from a Common 1,3,8-Triazaspiro[4.5]decane Core: Discovery of ML298 and ML299 That Decrease Invasive Migration in U87-MG Glioblastoma Cells

O’Reilly, M. C., Scott, S. A., Brown, K. A., Oguin, T. H., Thomas, P. G., Daniels, J. S., Morrison, R. D., Brown, H. A., & Lindsley, C. W. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm301782e · Cited by 75 · see citing works

Functional Regulation of Phospholipase D Expression in Cancer and Inflammation

Kang, D. W., Choi, K. Y., & Min, D. S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.569822 · Cited by 75 · see citing works

Solubilization and properties of a membrane-bound enzyme from rat brain catalyzing a base-exchange reaction

Saito, M., & Kanfer, J. N. (1973) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(73)90674-8 · Cited by 72 · see citing works

RhoA and a Cytosolic 50-kDa Factor Reconstitute GTPγS-dependent Phospholipase D Activity in Human Neutrophil Subcellular Fractions

Kwak, J.-Y., López, I., Uhlinger, D. J., Ryu, S. H., & Lambeth, J. D. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.27093 · Cited by 70 · see citing works

Association of a polymorphism of the phospholipase D2 gene with the prevalence of colorectal cancer

Yamada, Y., Hamajima, N., Kato, T., Iwata, H., Yamamura, Y., Shinoda, M., Suyama, M., Mitsudomi, T., Tajima, K., Kusakabe, S., et al. (2003) · Journal of Molecular Medicine · doi:10.1007/s00109-002-0411-x · Cited by 69 · see citing works

Requirement of phospholipase D1 activity in H-Ras V12 -induced transformation

Buchanan, F. G., McReynolds, M., Couvillon, A. D., Kam, Y., Holla, V. R., DuBois, R. N., & Exton, J. H. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406698102 · Cited by 66 · see citing works

PLD3 gene variants and Alzheimer's disease

Hooli, B. V., Lill, C. M., Mullin, K., Qiao, D., Lange, C., Bertram, L., & Tanzi, R. E. (2015) · Nature · doi:10.1038/nature14040 · Cited by 64 · see citing works

Design and synthesis of isoform-selective phospholipase D (PLD) inhibitors. Part II. Identification of the 1,3,8-triazaspiro[4,5]decan-4-one privileged structure that engenders PLD2 selectivity

Lavieri, R. R., Scott, S., Lewis, J. A., Selvy, P. E., Armstrong, M. D., Brown, H. A., & Lindsley, C. W. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.02.125 · Cited by 64 · see citing works

Phospholipase D Facilitates Efficient Entry of Influenza Virus, Allowing Escape from Innate Immune Inhibition

Oguin, T. H., Sharma, S., Stuart, A. D., Duan, S., Scott, S. A., Jones, C. K., Daniels, J. S., Lindsley, C. W., Thomas, P. G., & Brown, H. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.558817 · Cited by 63 · see citing works

Molecular Mechanisms of N -Formyl-Methionyl-Leucyl-Phenylalanine-Induced Superoxide Generation and Degranulation in Mouse Neutrophils: Phospholipase D Is Dispensable

Sato, T., Hongu, T., Sakamoto, M., Funakoshi, Y., & Kanaho, Y. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00869-12 · Cited by 63 · see citing works

PLD3 and sporadic Alzheimer's disease risk

Lambert, J., Grenier‐Boley, B., Bellenguez, C., Pasquier, F., Campion, D., Dartigues, J., Berr, C., Tzourio, C., & Amouyel, P. (2015) · Nature · doi:10.1038/nature14036 · Cited by 61 · see citing works

Addition of Deoxynucleosides Enhances Human Immunodeficiency Virus Type 1 Integration and 2LTR Formation in Resting CD4+T Cells

Plesa, G., Dai, J., Baytop, C., Riley, J. L., June, C. H., & O’Doherty, U. (2007) · Journal of Virology · doi:10.1128/jvi.01745-07 · Cited by 59 · see citing works

Pharmacological Inhibition of Phospholipase D Protects Mice From Occlusive Thrombus Formation and Ischemic Stroke—Brief Report

Stegner, D., Thielmann, I., Kraft, P., Frohman, M., Stoll, G., & Nieswandt, B. (2013) · Arteriosclerosis, Thrombosis and Vascular Biology · doi:10.1161/atvbaha.113.302030 · Cited by 58 · see citing works

Definition of the Protein Kinase C Interaction Site of Phospholipase D

Park, S.-K., Min, D. S., & Exton, J. H. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8275 · Cited by 58 · see citing works

PLD3 variants in population studies

van der Lee, S. J., Holstege, H. H., Wong, T. H., Jakobsdóttir, J., Bis, J. C., Chouraki, V. A., van Rooij, J., Grove, M. L., Smith, A. V., Amin, N., et al. (2015) · Nature · doi:10.1038/nature14038 · Cited by 55 · see citing works

Lactation status influences expression of CCAAT/enhancer binding protein isoform mRNA in the mouse mammary gland

Gigliotti, A. P., & DeWille, J. W. (1998) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(199802)174:2 · Cited by 55 · see citing works

Phospholipase D signaling pathway is involved in lung cancer-derived IL-8 increased osteoclastogenesis

Hsu, Y., Hung, J., Ko, Y., Hung, C., Huang, M., & Kuo, P. (2010) · Carcinogenesis · doi:10.1093/carcin/bgq030 · Cited by 54 · see citing works

Legionella pneumophila Effector LpdA Is a Palmitoylated Phospholipase D Virulence Factor

Schroeder, G. N., Auraß, P., Oates, C. V. L., Tate, E. W., Hartland, E. L., Flieger, A., & Frankel, G. M. (2015) · Infection and Immunity · doi:10.1128/iai.00785-15 · Cited by 52 · see citing works

Gonococcal Phospholipase D Modulates the Expression and Function of Complement Receptor 3 in Primary Cervical Epithelial Cells

Edwards, J. L., Entz, D. D., & Apicella, M. A. (2003) · Infection and Immunity · doi:10.1128/iai.71.11.6381-6391.2003 · Cited by 52 · see citing works

Phospholipase D1 is associated with amyloid precursor protein in Alzheimer's disease

Jin, J.-K., Ahn, B., Na, Y., Kim, J.-I., Kim, Y., Choi, E., Ko, Y., Chung, K. C., Kozlowski, P. B., & Min, D. S. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.05.022 · Cited by 51 · see citing works

Phosphatidic Acid Produced by Phospholipase D Promotes RNA Replication of a Plant RNA Virus

Hyodo, K., Taniguchi, T., Manabe, Y., Kaido, M., Mise, K., Sugawara, T., Taniguchi, H., & Okuno, T. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004909 · Cited by 49 · see citing works

Cellular and Physiological Roles for Phospholipase D1 in Cancer

Zhang, Y., & Frohman, M. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.576876 · Cited by 48 · see citing works

Phospholipase D-mediated autophagic regulation is a potential target for cancer therapy

Jang, Y., Choi, K.-S., & Min, D. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.174 · Cited by 47 · see citing works

Phospholipase D1 is up-regulated in the mitochondrial fraction from the brains of Alzheimer's disease patients

Jin, J.-K., Kim, N., Lee, Y.-J., Kim, Y., Choi, E., Kozlowski, P. B., Park, M. H., Kim, H., & Min, D. S. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2006.08.062 · Cited by 47 · see citing works

Entry of Influenza Virus

Sun, X., & Whittaker, G. R. (2006) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-7651-1_4 · Cited by 46 · see citing works

Biological Characterization ofChlamydia trachomatisPlasticity Zone MACPF Domain Family Protein CT153

Taylor, L. D., Nelson, D. E., Dorward, D. W., Whitmire, W. M., & Caldwell, H. D. (2010) · Infection and Immunity · doi:10.1128/iai.01455-09 · Cited by 46 · see citing works

Discovery of Desketoraloxifene Analogues as Inhibitors of Mammalian, Pseudomonas aeruginosa , and NAPE Phospholipase D Enzymes

Scott, S., Spencer, C. T., O’Reilly, M. C., Brown, K. A., Lavieri, R. R., Cho, C., Jung, D., Larock, R. C., Brown, H. A., & Lindsley, C. W. (2014) · ACS Chemical Biology · doi:10.1021/cb500828m · Cited by 46 · see citing works

Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells

Kang, D. W., Park, M. H., Lee, Y. J., Kim, H. S., Lindsley, C. W., Brown, H. A., & Min, D. S. (2010) · International Journal of Cancer · doi:10.1002/ijc.25402 · Cited by 45 · see citing works

Chemical modulation of glycerolipid signaling and metabolic pathways

Scott, S., Mathews, T. P., Ivanova, P. T., Lindsley, C. W., & Brown, H. A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.01.009 · Cited by 43 · see citing works

Neisseria gonorrhoeae PLD directly interacts with Akt kinase upon infection of primary, human, cervical epithelial cells

Edwards, J. L., & Apicella, M. A. (2006) · Cellular Microbiology · doi:10.1111/j.1462-5822.2006.00707.x · Cited by 42 · see citing works

Phospholipase D1 Couples CD4+ T Cell Activation to c-Myc-Dependent Deoxyribonucleotide Pool Expansion and HIV-1 Replication

Taylor, H. E., Simmons, G. E., Jr., Mathews, T. P., Khatua, A. K., Popik, W., Lindsley, C. W., D’Aquila, R. T., & Brown, H. A. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004864 · Cited by 42 · see citing works

PLD1 rather than PLD2 regulates phorbol-ester-, adhesion-dependent and Fcγ-receptor-stimulated ROS production in neutrophils

Norton, L. J., Zhang, Q., Saqib, K. M., Schrewe, H., Macura, K., Anderson, K. E., Lindsley, C. W., Brown, H. A., Rudge, S. A., & Wakelam, M. J. O. (2011) · Journal of Cell Science · doi:10.1242/jcs.082008 · Cited by 42 · see citing works

Hyperactivation of EGFR and downstream effector phospholipase D1 by oncogenic FAM83B

Cipriano, R., Bryson, B. L., Miskimen, K. L. S., Bartel, C. A., Hernandez-Sanchez, W. M., Bruntz, R. C., Scott, S. A., Lindsley, C. W., Brown, H. A., & Jackson, M. W. (2013) · Oncogene · doi:10.1038/onc.2013.293 · Cited by 41 · see citing works

Selective Estrogen Receptor (ER) Modulators Differentially Regulate Phospholipase D Catalytic Activity in ER-Negative Breast Cancer Cells

Eisen, S. F., & Brown, H. A. (2002) · Molecular Pharmacology · doi:10.1124/mol.62.4.911 · Cited by 40 · see citing works

Biochemical Characterization of a Pseudomonas aeruginosa Phospholipase D

Spencer, C. T., & Brown, H. A. (2015) · Biochemistry · doi:10.1021/bi501291t · Cited by 38 · see citing works

Growth Effects of Regulatory Peptides and Intracellular Signaling Routes in Human Pancreatic Cancer Cell Lines

Douziech, N., Lajas, A. I., Coulombe, Z., Calvo, E. L., Lainé, J., & Morisset, J. (1998) · Endocrine · doi:10.1385/endo:9:2:171 · Cited by 37 · see citing works

Upregulation of phospholipase D1 in the spinal cords of rats with clip compression injury

Jung, K., Min, D. S., Sim, K.-B., Ahn, M., Kim, H., Cheong, J., & Shin, T. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(02)01155-2 · Cited by 37 · see citing works

Role of Phospholipase D2/Phosphatidic Acid Signal Transduction in μ- and δ-Opioid Receptor Endocytosis

Yang, L., Seifert, A., Wu, D., Wang, X., Rankovic, V., Schröder, H., Brandenburg, L. O., Höllt, V., & Koch, T. (2010) · Molecular Pharmacology · doi:10.1124/mol.109.063107 · Cited by 35 · see citing works

Phosphoryl Transfers of the Phospholipase D Superfamily: A Quantum Mechanical Theoretical Study

DeYonker, N. J., & Webster, C. E. (2013) · Journal of the American Chemical Society · doi:10.1021/ja4042753 · Cited by 33 · see citing works

Two sites of action for PLD2 inhibitors: The enzyme catalytic center and an allosteric, phosphoinositide biding pocket

Ganesan, R., Mahankali, M., Alter, G. M., & Gómez-Cambronero, J. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.12.007 · Cited by 33 · see citing works

[33] Stimulation of phospholipase D by ADP-ribosylation factor

Brown, H. A., & Sternweis, P. C. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(95)57035-7 · Cited by 32 · see citing works

Stable adhesion and migration of human neutrophils requires phospholipase D-mediated activation of the integrin CD11b/CD18

Powner, D., Pettitt, T. R., Anderson, R., Nash, G. B., & Wakelam, M. J. O. (2007) · Molecular Immunology · doi:10.1016/j.molimm.2007.01.033 · Cited by 31 · see citing works

Tamoxifen as Adjuvant Therapy in Breast Cancer

Plowman, P. N. (1993) · Drugs · doi:10.2165/00003495-199346050-00003 · Cited by 31 · see citing works

STUDIES ON PLAGUE

Ajl, S. J., Reedal, J. S., DURRUM, E. L., & Warren, J. D. (1955) · Journal of Bacteriology · doi:10.1128/jb.70.2.158-169.1955 · Cited by 31 · see citing works

Regulation of Phospholipase D Activity and Phosphatidic Acid Production after Purinergic (P2Y6) Receptor Stimulation

Scott, S. A., Xiang, Y., Mathews, T. P., Cho, H. P., Myers, D. S., Armstrong, M. D., Tallman, K. A., O’Reilly, M. C., Lindsley, C. W., & Brown, H. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.451708 · Cited by 29 · see citing works

Phospholipase D as a Therapeutic Target in Brain Disorders

Lindsley, C. W., & Brown, H. A. (2011) · Neuropsychopharmacology · doi:10.1038/npp.2011.178 · Cited by 27 · see citing works

Increased expression of phospholipase D1 in the spinal cords of rats with experimental autoimmune encephalomyelitis

Ahn, M., Min, D. S., Kang, J., Jung, K., & Shin, T. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)02383-7 · Cited by 26 · see citing works

Enhanced levels of oleate-dependent and Arf-dependent phospholipase D isoforms in experimental colon cancer.

Yoshida, M., Okamura, S.-I., Kodaki, T., Mori, M., & Yamashita, S. (1998) · PubMed · Cited by 26 · see citing works

Human Phospholipase D Activity Transiently Regulates Pyrimidine Biosynthesis in Malignant Gliomas

Mathews, T. P., Hill, S., Rose, K. L., Ivanova, P. T., Lindsley, C. W., & Brown, H. A. (2015) · ACS Chemical Biology · doi:10.1021/cb500772c · Cited by 23 · see citing works

Discovery of a Highly Selective PLD2 Inhibitor (ML395): A New Probe with Improved Physiochemical Properties and Broad‐Spectrum Antiviral Activity against Influenza Strains

O’Reilly, M. C., Oguin, T. H., Scott, S. A., Thomas, P. G., Locuson, C. W., Morrison, R. D., Daniels, J. S., Brown, H. A., & Lindsley, C. W. (2014) · ChemMedChem · doi:10.1002/cmdc.201402333 · Cited by 20 · see citing works

Halopemide, a new psychotropic agent

LOONEN, A. J. M., & Soudijn, W. (1985) · Pharmacy World & Science · doi:10.1007/bf01962862 · Cited by 18 · see citing works

Discovery of Compounds Blocking the Proliferation of Toxoplasma gondii and Plasmodium falciparum in a Chemical Space Based on Piperidinyl-Benzimidazolone Analogs

Saïdani, N., Botté, C. Y., Deligny, M., Bonneau, A.-L., Reader, J., Lasselin, R., Merer, G., Niepceron, A., Brossier, F., Cintrat, J., et al. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01445-13 · Cited by 11 · see citing works

Effects of halopemide on GABA receptor binding, uptake and release

LOONEN, A. J. M., Soe-Agnie, C., & Soudijn, W. (1981) · Brain Research · doi:10.1016/0006-8993(81)90932-x · Cited by 10 · see citing works

Assays and Characterization of Mammalian Phosphatidylinositol 4,5-Bisphosphate-Sensitive Phospholipase D

Jiang, X., Gutowski, S., Singer, W. D., & Sternweis, P. C. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)45026-4 · Cited by 9 · see citing works

Further evaluation of novel structural modifications to scaffolds that engender PLD isoform selective inhibition

O’Reilly, M. C., Scott, S., Brown, H. A., & Lindsley, C. W. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.11.017 · Cited by 6 · see citing works

Using O-(n-alkyl)-N-(N,N′-dimethylethyl)phosphoramidates to investigate the role of Ca2+ and interfacial binding in a bacterial phospholipase D

Oh, M.-K., Yang, H., & Roberts, M. F. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/s1570-9639(03)00166-3 · Cited by 4 · see citing works

Toxic Mechanisms of Five Heavy Metals: Mercury, Lead, Chromium, Cadmium, and Arsenic

Balali‐Mood, M., Naseri, K., Tahergorabi, Z., Khazdair, M. R., & Sadeghi, M. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.643972 · Cited by 3,154 · see citing works

Lipid metabolism in cancer progression and therapeutic strategies

Fu, Y., Zou, T., Shen, X., Nelson, P. J., Li, J., Wu, C., Yang, J., Zheng, Y., Bruns, C. J., Zhao, Y., et al. (2020) · MedComm · doi:10.1002/mco2.27 · Cited by 406 · see citing works

Extracellular vesicles: lipids as key components of their biogenesis and functions

Record, M., Silvente-Poirot, S., Poirot, M., & Wakelam, M. O. (2018) · Journal of Lipid Research · doi:10.1194/jlr.e086173 · Cited by 328 · see citing works

Analytical Challenges and Recent Advances in Mass Spectrometry Based Lipidomics

Rustam, Y. H., & Reid, G. E. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b04836 · Cited by 284 · see citing works

Systemic impact of heavy metals and their role in cancer development: a review

Parida, L., & Patel, T. (2023) · Environmental Monitoring and Assessment · doi:10.1007/s10661-023-11399-z · Cited by 233 · see citing works

Lipid Mediators Regulate Pulmonary Fibrosis: Potential Mechanisms and Signaling Pathways

Suryadevara, V., Ramchandran, R., Kamp, D. W., & Natarajan, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124257 · Cited by 164 · see citing works

MARCKS and MARCKS-like proteins in development and regeneration

Amri, M. E., FitzGerald, U., & Schlosser, G. (2018) · Journal of Biomedical Science · doi:10.1186/s12929-018-0445-1 · Cited by 150 · see citing works

Plant-derived nanovesicles: Current understanding and applications for cancer therapy

Ly, N. P., Han, H. S., Kim, M., Park, J. H., & Choi, K. Y. (2022) · Bioactive Materials · doi:10.1016/j.bioactmat.2022.10.005 · Cited by 114 · see citing works

Lipids at the Crossroad of α-Synuclein Function and Dysfunction: Biological and Pathological Implications

Alza, N. P., González, P. A. I., Conde, M. A., Uranga, R. M., & Salvador, G. A. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00175 · Cited by 111 · see citing works

Curcumin downregulates the PI3K–AKT–mTOR pathway and inhibits growth and progression in head and neck cancer cells

Borges, G. Á., Elias, S. T., Amorim, B. R., de Lima, C. L., Coletta, R. D., CASTILHO, R. M., SQUARIZE, C. H., & Guerra, E. N. S. (2020) · Phytotherapy Research · doi:10.1002/ptr.6780 · Cited by 100 · see citing works

A real-time, click chemistry imaging approach reveals stimulus-specific subcellular locations of phospholipase D activity

Liang, D., Wu, K., Tei, R., Bumpus, T. W., Ye, J., & Baskin, J. M. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1903949116 · Cited by 95 · see citing works

Clickable Substrate Mimics Enable Imaging of Phospholipase D Activity

Bumpus, T. W., & Baskin, J. M. (2017) · ACS Central Science · doi:10.1021/acscentsci.7b00222 · Cited by 80 · see citing works

Pseudomonas aeruginosa Toxin ExoU as a Therapeutic Target in the Treatment of Bacterial Infections

Foulkes, D. M., McLean, K., Haneef, A. S., Fernig, D. G., Winstanley, C., Berry, N. G., & Kaye, S. B. (2019) · Microorganisms · doi:10.3390/microorganisms7120707 · Cited by 80 · see citing works

Greasing the Wheels of Lipid Biology with Chemical Tools

Bumpus, T. W., & Baskin, J. M. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.09.011 · Cited by 68 · see citing works

Interaction and Regulation Between Lipid Mediator Phosphatidic Acid and Circadian Clock Regulators

Kim, S., Nusinow, D. A., Sorkin, M. L., Pruneda-Paz, J. L., & Wang, X. (2019) · The Plant Cell · doi:10.1105/tpc.18.00675 · Cited by 63 · see citing works

c-Jun/AP-1 overexpression reprograms ERα signaling related to tamoxifen response in ERα-positive breast cancer

He, H., Sinha, I., Fan, R., Haldosén, L.-A., Yan, F., Zhao, C., & Dahlman‐Wright, K. (2018) · Oncogene · doi:10.1038/s41388-018-0165-8 · Cited by 62 · see citing works

The Ligand Binding Landscape of Diacylglycerol Kinases

Franks, C. E., Campbell, S., Purow, B. W., Harris, T. E., & Hsu, K. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.06.007 · Cited by 61 · see citing works

Sphingosine 1-Phosphate (S1P) Signaling in Glioblastoma Multiforme—A Systematic Review

Mahajan, S. G., Bien-Möller, S., Marx, S., Schroeder, H. W. S., & Rauch, B. H. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18112448 · Cited by 61 · see citing works

Prostate cancer-derived exosomes promote osteoblast differentiation and activity through phospholipase D2

Borel, M., Lollo, G., Magne, D., Buchet, R., Brizuela, L., & Mebarek, S. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165919 · Cited by 62 · see citing works

PLD3 is a neuronal lysosomal phospholipase D associated with β-amyloid plaques and cognitive function in Alzheimer’s disease

Nackenoff, A. G., Hohman, T. J., Neuner, S. M., Akers, C. S., Weitzel, N. C., Shostak, A., Ferguson, S. M., Mobley, B., Bennett, D. A., Schneider, J. A., et al. (2021) · PLOS Genetics · doi:10.1371/journal.pgen.1009406 · Cited by 59 · see citing works

Phospholipase D as a key modulator of cancer progression

Yao, Y., Wang, X., Li, H., Fan, J., Qian, X., Li, H., & Xu, Y. (2020) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12592 · Cited by 58 · see citing works

Recent in vivo advances of spirocyclic scaffolds for drug discovery

Batista, V. F., Pinto, D. C. G. A., & Silva, A. M. S. (2022) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2022.2055544 · Cited by 59 · see citing works

Phospholipase D inhibitors reduce human prostate cancer cell proliferation and colony formation

Noble, A. R., Maitland, N. J., Berney, D. M., & Rumsby, M. G. (2017) · British Journal of Cancer · doi:10.1038/bjc.2017.391 · Cited by 57 · see citing works

Exercise mimetics: a novel strategy to combat neuroinflammation and Alzheimer’s disease

Zhao, R. (2024) · Journal of Neuroinflammation · doi:10.1186/s12974-024-03031-9 · Cited by 62 · see citing works

Comparative lipidomics of 5-Fluorouracil–sensitive and –resistant colorectal cancer cells reveals altered sphingomyelin and ceramide controlled by acid sphingomyelinase (SMPD1)

Jung, J. H., Taniguchi, K., Lee, H. M., Lee, M. Y., Bandu, R., Komura, K., Lee, K. Y., Akao, Y., & Kim, K. P. (2020) · Scientific Reports · doi:10.1038/s41598-020-62823-0 · Cited by 56 · see citing works

TBX3 functions as a tumor suppressor downstream of activated CTNNB1 mutants during hepatocarcinogenesis

Liang, B., Zhou, Y., Qian, M., Xu, M., Wang, J., Zhang, Y., Song, X., Wang, H., Lin, S., Ren, C., et al. (2021) · Journal of Hepatology · doi:10.1016/j.jhep.2021.01.044 · Cited by 55 · see citing works

BPDE, the Migration and Invasion of Human Trophoblast Cells, and Occurrence of Miscarriage in Humans: Roles of a Novel lncRNA-HZ09

Dai, M., Huang, W., Huang, X., Ma, C., Wang, R., Tian, P., Chen, W., Zhang, Y., Mi, C., & Zhang, H. (2023) · Environmental Health Perspectives · doi:10.1289/ehp10477 · Cited by 54 · see citing works

Crystal structure of human PLD1 provides insight into activation by PI(4,5)P2 and RhoA

Bowling, F. Z., Salazar, C. M., Bell, J. A., Huq, T. S., Frohman, M. A., & Airola, M. V. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0499-8 · Cited by 54 · see citing works

Improving the efficacy of hormone therapy in breast cancer: The role of cholesterol metabolism in SERM-mediated autophagy, cell differentiation and death

Leignadier, J., Dalenc, F., Poirot, M., & Silvente‐Poirot, S. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.06.120 · Cited by 52 · see citing works

Crystal structure of plant PLDα1 reveals catalytic and regulatory mechanisms of eukaryotic phospholipase D

Li, J., Yu, F., Guo, H., Xiong, R., Zhang, W., He, F., Zhang, M., & Zhang, P. (2019) · Cell Research · doi:10.1038/s41422-019-0244-6 · Cited by 47 · see citing works

Phospholipase D and Choline Metabolism

Onono, F. O., & Morris, A. J. (2019) · Handbook of experimental pharmacology · doi:10.1007/164_2019_320 · Cited by 47 · see citing works

Synthesis of Benzo[b]thiophenes through Rhodium‐Catalyzed Three‐Component Reaction using Elemental Sulfur

Moon, S., Kato, M., Nishii, Y., & Miura, M. (2020) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.202000112 · Cited by 44 · see citing works

Monitoring protein communities and their responses to therapeutics

Budayeva, H. G., & Kirkpatrick, D. S. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0063-y · Cited by 41 · see citing works

Role of phospholipase D in bleomycin-induced mitochondrial reactive oxygen species generation, mitochondrial DNA damage, and pulmonary fibrosis

Suryadevara, V., Huang, L., Kim, S.-J., Cheresh, P., Shaaya, M., Bandela, M., Fu, P., Feghali‐Bostwick, C. A., Paolo, G. D., Kamp, D. W., et al. (2019) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00320.2018 · Cited by 43 · see citing works

Coupling Lipid Nanoparticle Structure and Automated Single‐Particle Composition Analysis to Design Phospholipase‐Responsive Nanocarriers

Barriga, H. M. G., Pence, I. J., Holme, M. N., Doutch, J., Penders, J., Nele, V., Thomas, M. R., Carroni, M., & Stevens, M. M. (2022) · Advanced Materials · doi:10.1002/adma.202200839 · Cited by 41 · see citing works

Providing context for phosphatidylethanol as a biomarker of alcohol consumption with a pharmacokinetic model

Simon, T. W. (2018) · Regulatory Toxicology and Pharmacology · doi:10.1016/j.yrtph.2018.01.029 · Cited by 41 · see citing works

Human PLD structures enable drug design and characterization of isoenzyme selectivity

Metrick, C. M., Peterson, E. A., Santoro, J. C., Enyedy, I. J., Murugan, P., Chen, T., Michelsen, K., Cullivan, M. L., Spilker, K. A., Kumar, P. R., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-019-0458-4 · Cited by 41 · see citing works

Elevated phospholipase D isoform 1 in Alzheimer's disease patients' hippocampus: Relevance to synaptic dysfunction and memory deficits

Krishnan, B., Kayed, R., & Taglialatela, G. (2018) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.01.002 · Cited by 40 · see citing works

Hypoxia induced changes in miRNAs and their target mRNAs in extracellular vesicles of esophageal squamous cancer cells

Chen, F., Chu, L., Li, J., Shi, Y., Xu, B., Gu, J., Yao, X., Tian, M., Yang, X., & Sun, X. (2020) · Thoracic Cancer · doi:10.1111/1759-7714.13295 · Cited by 40 · see citing works

Proliferative and metastatic roles for Phospholipase D in mouse models of cancer

Roth, E., & Frohman, M. A. (2017) · Advances in Biological Regulation · doi:10.1016/j.jbior.2017.11.004 · Cited by 37 · see citing works

Inhibition of phospholipase D1 induces immunogenic cell death and potentiates cancer immunotherapy in colorectal cancer

Hwang, W. C., Song, D., Lee, H., Oh, C., Lim, S. H., Bae, H. J., Kim, N. D., Han, G., & Min, D. S. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00853-6 · Cited by 38 · see citing works

Fate of Liposomes in the Presence of Phospholipase C and D: From Atomic to Supramolecular Lipid Arrangement

Holme, M. N., Rashid, M. H., Thomas, M. R., Barriga, H. M. G., Herpoldt, K., Heenan, R. K., Dreiss, C. A., Bañuelos, J. L., Xie, H., Yarovsky, I., et al. (2018) · ACS Central Science · doi:10.1021/acscentsci.8b00286 · Cited by 36 · see citing works

High glucose-induced phospholipase D activity in retinal pigment epithelium cells: New insights into the molecular mechanisms of diabetic retinopathy

Tenconi, P. E., Bermúdez, V., Oresti, G. M., Giusto, N. M., Salvador, G. A., & Mateos, M. V. (2019) · Experimental Eye Research · doi:10.1016/j.exer.2019.04.028 · Cited by 36 · see citing works

Structural insights into phospholipase D function

Yao, Y., Li, J., Lin, Y., Zhou, J., Zhang, P., & Xu, Y. (2020) · Progress in Lipid Research · doi:10.1016/j.plipres.2020.101070 · Cited by 35 · see citing works

PLD1 and PLD2 differentially regulate the balance of macrophage polarization in inflammation and tissue injury

Hwang, W. C., Seo, S., Kang, M.-J., Kang, R. H., Paolo, G. D., Choi, K.-Y., & Min, D.-S. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.30224 · Cited by 28 · see citing works

Transcriptome and Metabolome Analyses Reveal Potential Salt Tolerance Mechanisms Contributing to Maintenance of Water Balance by the Halophytic Grass Puccinellia nuttalliana

Vaziriyeganeh, M., Khan, S. U., & Zwiazek, J. J. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.760863 · Cited by 33 · see citing works

DLGAP1-AS2–Mediated Phosphatidic Acid Synthesis Activates YAP Signaling and Confers Chemoresistance in Squamous Cell Carcinoma

Nan, Y., Luo, Q., Wu, X., Liu, S., Zhao, P., Chang, W., Zhou, A., & Liu, Z. (2022) · Cancer Research · doi:10.1158/0008-5472.can-22-0717 · Cited by 32 · see citing works

Phospholipase D1 downregulation by α-synuclein: Implications for neurodegeneration in Parkinson's disease

Conde, M. A., Alza, N. P., González, P. A. I., Bilbao, P., Campos, S. S., Uranga, R. M., & Salvador, G. A. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2018.03.006 · Cited by 32 · see citing works

Phosphatidic acid signaling and function in nuclei

Yao, S., Kim, S., Li, J., Tang, S., & Wang, X. (2023) · Progress in Lipid Research · doi:10.1016/j.plipres.2023.101267 · Cited by 31 · see citing works

Proteomic composition of Nipah virus-like particles

Vera-Velasco, N. M., García‐Murria, M. J., del Pino, M. M. S., Mingarro, I., & Martínez‐Gil, L. (2017) · Journal of Proteomics · doi:10.1016/j.jprot.2017.10.012 · Cited by 30 · see citing works

Phospholipase D2 promotes disease progression of renal cell carcinoma through the induction of angiogenin

Kandori, S., Kojima, T., Matsuoka, T., Yoshino, T., Sugiyama, A., Nakamura, E., Shimazui, T., Funakoshi, Y., Kanaho, Y., & Nishiyama, H. (2018) · Cancer Science · doi:10.1111/cas.13609 · Cited by 30 · see citing works

Targeting Phospholipase D4 Attenuates Kidney Fibrosis

Trivedi, P., Kumar, R. K., Iyer, A., Boswell, S. A., Gerarduzzi, C., Dadhania, V. P., Herbert, Z. T., Joshi, N., Luyendyk, J. P., Humphreys, B. D., et al. (2017) · Journal of the American Society of Nephrology · doi:10.1681/asn.2016111222 · Cited by 29 · see citing works

Phospholipase D: A new mediator during high phosphate‐induced vascular calcification associated with chronic kidney disease

Skafi, N., Abdallah, D., Soulage, C. O., Reibel, S., Vitale, N., Hamade, E., Faour, W. H., Magne, D., Badran, B. M., Hussein, N., et al. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27281 · Cited by 29 · see citing works

Phospholipase D1 Signaling: Essential Roles in Neural Stem Cell Differentiation

Park, S., & Han, J. (2018) · Journal of Molecular Neuroscience · doi:10.1007/s12031-018-1042-1 · Cited by 29 · see citing works

Curbing Lipids: Impacts ON Cancer and Viral Infection

Dutta, A., & Sharma-Walia, N. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030644 · Cited by 28 · see citing works

Altered hydroxymethylome in the substantia nigra of Parkinson’s disease

Min, S., Xu, Q., Qin, L., Li, Y., Li, Z., Chen, C., Wu, H., Han, J., Zhu, X., Jin, P., et al. (2022) · Human Molecular Genetics · doi:10.1093/hmg/ddac122 · Cited by 27 · see citing works

The transcriptional landscape of Alzheimer’s disease and its association with Wnt signaling pathway

Martínez, M., & Inestrosa, N. C. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.06.029 · Cited by 25 · see citing works

Effect of Prenatal Opioid Exposure on the Human Placental Methylome

Borrelli, K. N., Wachman, E. M., Beierle, J. A., Taglauer, E. S., Jain, M., Bryant, C. D., & Zhang, H. (2022) · Biomedicines · doi:10.3390/biomedicines10051150 · Cited by 25 · see citing works

PLD1 is a key player in cancer stemness and chemoresistance: Therapeutic targeting of cross-talk between the PI3K/Akt and Wnt/β-catenin pathways

Lim, S. H., Lee, H., Lee, H., Kim, K., Choi, J., Han, J. M., & Min, D. S. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01260-9 · Cited by 27 · see citing works

Preparation and Evaluation of Liposomes Co-Loaded with Doxorubicin, Phospholipase D Inhibitor 5-Fluoro-2-Indolyl Deschlorohalopemide (FIPI) and D-Alpha Tocopheryl Acid Succinate (α-TOS) for Anti-Metastasis

Song, M., Wang, J., Lei, J., Peng, G., Zhang, W., Zhang, Y., Yin, M., Li, J., Liu, Y., Wei, X., et al. (2019) · Nanoscale Research Letters · doi:10.1186/s11671-019-2964-4 · Cited by 24 · see citing works

Emergent Glycerophospholipid Fluorescent Probes: Synthesis and Applications

Varandas, P. A. M. M., Cobb, A. J. A., Segundo, M. A., & Silva, E. M. P. (2019) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.9b00660 · Cited by 24 · see citing works

Can a metabolism-targeted therapeutic intervention successfully subjugate SARS-COV-2? A scientific rational

Mansouri, K., Rastegari‐Pouyani, M., Ghanbari-Movahed, M., Safarzadeh, M., Kiani, S., & Ghanbari‐Movahed, Z. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110694 · Cited by 24 · see citing works

Phospholipase D1 is upregulated by vorinostat and confers resistance to vorinostat in glioblastoma

Kang, D. W., Hwang, W. C., Noh, Y. N., Kang, Y., Jang, Y., Kim, J., & Min, D. S. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.29882 · Cited by 23 · see citing works

MiR-638 suppresses the progression of oral squamous cell carcinoma through wnt/β-catenin pathway by targeting phospholipase D1

Tang, K., Han-Ying, T., Du, Y., Tian, T., & Xiong, S. (2019) · Artificial Cells Nanomedicine and Biotechnology · doi:10.1080/21691401.2019.1647222 · Cited by 23 · see citing works

Characterization of α‐synuclein N‐terminal domain as a novel cellular phosphatidic acid sensor

Yamada, H., Mizuno, S., Honda, S., Takahashi, D., & Sakane, F. (2019) · FEBS Journal · doi:10.1111/febs.15137 · Cited by 23 · see citing works

In vitro 6-hydroxydopamine-induced neurotoxicity: New insights on NFκB modulation

González, P. A. I., Conde, M. A., Pardo, V. G., Uranga, R. M., & Salvador, G. A. (2019) · Toxicology in Vitro · doi:10.1016/j.tiv.2019.06.019 · Cited by 22 · see citing works

Targeting of Phospholipase D1 Ameliorates Collagen-Induced Arthritis via Modulation of Treg and Th17 Cell Imbalance and Suppression of Osteoclastogenesis

Yoo, H. J., Hwang, W. C., & Min, D. S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093230 · Cited by 21 · see citing works

Lipin-1-derived diacylglycerol activates intracellular TRPC3 which is critical for inflammatory signaling

Casas, J., Meana, C., López‐López, J. R., Balsinde, J., & Balboa, M. A. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03999-0 · Cited by 22 · see citing works

Phospholipase Signaling in Breast Cancer

Lee, Y. J., Shin, K. J., Jang, H., Noh, D., Ryu, S. H., & Suh, P. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9620-6_2 · Cited by 21 · see citing works

Click chemistry–enabled CRISPR screening reveals GSK3 as a regulator of PLD signaling

Bumpus, T. W., Huang, S., Tei, R., & Baskin, J. M. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2025265118 · Cited by 21 · see citing works

Sexual dimorphism in gut microbiota dictates therapeutic efficacy of intravenous immunoglobulin on radiotherapy complications

Wang, Z., Xiao, H., Dong, J., Li, Y., Wang, B., Chen, Z., Zeng, X., Liu, J., Dong, Y., Ma, L., et al. (2022) · Journal of Advanced Research · doi:10.1016/j.jare.2022.06.002 · Cited by 21 · see citing works

Phospholipid metabolism in innate immunity and inflammation: from basic to clinic

Liu, J., Chen, Y., & O'Neill, L. A. J. (2025) · Immunity & Inflammation · doi:10.1007/s44466-025-00001-5 · Cited by 20 · see citing works

Diacylglycerols as biomarkers of sustained immune activation in Proteinopathies associated with dementia

Wood, P. L., Cebak, J. E., & Woltjer, R. L. (2017) · Clinica Chimica Acta · doi:10.1016/j.cca.2017.11.009 · Cited by 19 · see citing works

Exonucleases: Degrading DNA to Deal with Genome Damage, Cell Death, Inflammation and Cancer

Manils, J., Marruecos, L., & Soler, C. (2022) · Cells · doi:10.3390/cells11142157 · Cited by 19 · see citing works

Elevated phospholipase D activity in androgen-insensitive prostate cancer cells promotes both survival and metastatic phenotypes

Utter, M., Chakraborty, S., Goren, L., Feuser, L., Zhu, Y., & Foster, D. A. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.03.006 · Cited by 20 · see citing works

Phospholipase D functional ablation has a protective effect in an Alzheimer’s disease Caenorhabditis elegans model

Bravo, F. V., Silva, J. D. D., Chan, R., Paolo, G. D., Teixeira‐Castro, A., & Oliveira, T. G. (2018) · Scientific Reports · doi:10.1038/s41598-018-21918-5 · Cited by 20 · see citing works

Symmetrically substituted dichlorophenes inhibit N-acyl-phosphatidylethanolamine phospholipase D

Aggarwal, G., Zarrow, J. E., Mashhadi, Z., Flynn, C. R., Vinson, P. N., Weaver, C. D., & Davies, S. S. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013362 · Cited by 20 · see citing works

Targeting mTOR in the Context of Diet and Whole-body Metabolism

Koundouros, N., & Blenis, J. (2022) · Endocrinology · doi:10.1210/endocr/bqac041 · Cited by 19 · see citing works

Phospholipase D2 controls bone homeostasis by modulating M-CSF-dependent osteoclastic cell migration and microtubule stability

Kim, H., Lee, D.-K., Jin, X., Che, X., Ryu, S. H., & Choi, J. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00820-1 · Cited by 19 · see citing works

Effects of phospholipase D during cultured osteoblast mineralization and bone formation

Abdallah, D., Skafi, N., Hamade, E., Borel, M., Reibel, S., Vitale, N., Jamal, A. E., Bougault, C., Laroche, N., Vico, L., et al. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.27881 · Cited by 19 · see citing works

Lipidomic analysis of immune activation in equine leptospirosis and Leptospira-vaccinated horses

Wood, P. L., Steinman, M., Erol, E., Carter, C. N., Christmann, U., & Verma, A. (2018) · PLoS ONE · doi:10.1371/journal.pone.0193424 · Cited by 18 · see citing works

IMPACT: Imaging phospholipase d activity with clickable alcohols via transphosphatidylation

Bumpus, T. W., Liang, D., & Baskin, J. M. (2020) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2020.04.037 · Cited by 18 · see citing works

A polydiacetylenes-based sensor for the efficient detection of phospholipase D activity

Zhang, Z., Li, J., Wang, F., Wei, T., Chen, Y., Qiang, J., Xiao, T., & Chen, X. (2018) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2018.11.117 · Cited by 17 · see citing works

Phospholipase Family Enzymes in Lung Cancer: Looking for Novel Therapeutic Approaches

Salucci, S., Aramini, B., Bartoletti‐Stella, A., Versari, I., Martinelli, G., Blalock, W. L., Stella, F., & Faenza, I. (2023) · Cancers · doi:10.3390/cancers15123245 · Cited by 16 · see citing works

PLD-dependent phosphatidic acid microdomains are signaling platforms for podosome formation

Bolomini‐Vittori, M., Mennens, S. F. B., Joosten, B., Fransen, J. A. M., Du, G., van den Dries, K., & Cambi, A. (2019) · Scientific Reports · doi:10.1038/s41598-019-39358-0 · Cited by 16 · see citing works

Phospholipase D1 inhibition sensitizes glioblastoma to temozolomide and suppresses its tumorigenicity

Kang, D. W., Hwang, W. C., Noh, Y. N., Park, K. S., & Min, D. S. (2020) · The Journal of Pathology · doi:10.1002/path.5519 · Cited by 16 · see citing works

Understanding abiotic stress tolerance mechanisms in non-food grass species through omics approaches

Mondal, S., Seelam, R. T., Mondal, B., & Jespersen, D. (2024) · Plant Stress · doi:10.1016/j.stress.2024.100516 · Cited by 15 · see citing works

Marcks and Marcks-like 1 proteins promote spinal cord development and regeneration in Xenopus

Amri, M. E., Pandit, A. S., & Schlosser, G. (2024) · eLife · doi:10.7554/elife.98277 · Cited by 15 · see citing works

Suppressing aberrant phospholipase D1 signaling in 3xTg Alzheimer’s disease mouse model promotes synaptic resilience

Bourne, K. Z., Natarajan, C., Perez, C., Tumurbaatar, B., Taglialatela, G., & Krishnan, B. (2019) · Scientific Reports · doi:10.1038/s41598-019-54974-6 · Cited by 15 · see citing works

A Smart “Sense-and-Treat” Nanoplatform Based on Semiconducting Polymer Nanoparticles for Precise Photothermal-Photodynamic Combined Therapy

Bao, B., Su, P., Song, K., Cui, Y., Zhai, X., Xu, Y., Liu, J., & Wang, L. (2021) · Biomacromolecules · doi:10.1021/acs.biomac.0c01567 · Cited by 15 · see citing works

Discovery of Phospholipase D Inhibitors with Improved Drug-like Properties and Central Nervous System Penetrance

May‐Dracka, T. L., Gao, F., Hopkins, B. T., Hronowski, X. L., Chen, T., Chodaparambil, J. V., Metrick, C. M., Cullivan, M., Enyedy, I. J., Kaliszczak, M. A., et al. (2022) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.1c00682 · Cited by 14 · see citing works

Phospholipase D2 is a positive regulator of sirtuin 1 and modulates p53-mediated apoptosis via sirtuin 1

Lee, H., Jung, T.-Y., Lim, S. H., Choi, E. J., Lee, J., & Min, D. S. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00659-y · Cited by 14 · see citing works

Metabolomics in combination with network pharmacology reveals the potential anti-neuroinflammatory mechanism of essential oils from four Curcuma species

Huang, Z., Yuan, Y., Tan, Z., Zheng, J., Zhang, W., Huang, S., Wang, Y., Chen, M., Zhang, L., & Li, H. (2023) · Industrial Crops and Products · doi:10.1016/j.indcrop.2023.116411 · Cited by 13 · see citing works

Canonical phospholipase D isoforms in visual function and ocular response to stress

Bermúdez, V., Tenconi, P. E., Giusto, N. M., & Mateos, M. V. (2022) · Experimental Eye Research · doi:10.1016/j.exer.2022.108976 · Cited by 13 · see citing works

Dickkopf1 (Dkk1) Alleviates Vascular Calcification by Regulating the Degradation of Phospholipase D1 (PLD1)

Li, X., Liu, X., Li, X., Zhao, Y., Wang, Q., Zhong, H., Liu, D., Yuan, C., Zheng, T.-F., & Zhang, M. (2022) · Journal of Cardiovascular Translational Research · doi:10.1007/s12265-022-10251-y · Cited by 13 · see citing works

Untargeted Metabolomics Yields Insights Into the Lipidome of Botrylloides niger Herdman, 1886, An Ascidian Invading the Mediterranean Sea

Sala, G. D., Coppola, D., Virgili, R., Vitale, G. A., Tanduo, V., Teta, R., Crocetta, F., & de Pascale, D. (2022) · Frontiers in Marine Science · doi:10.3389/fmars.2022.865751 · Cited by 13 · see citing works

Role of phospholipase D in the lifespan of Caenorhabditis elegans

Park, J.-H., Park, J., Lee, J., Kim, D.-Y., Hahm, J., & Bae, Y. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-017-0015-8 · Cited by 13 · see citing works

Isoform selective PLD inhibition by novel, chiral 2,8-diazaspiro[4.5]decan-1-one derivatives

Waterson, A. G., Scott, S. A., Kett, N. R., Blobaum, A. L., Brown, H. A., & Lindsley, C. W. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.10.033 · Cited by 13 · see citing works

Designing New Natural‐Mimetic Phosphatidic Acid: A Versatile and Innovative Synthetic Strategy for Glycerophospholipid Research

Schlichter, A., Wolf, A., Ferrand, T., Cocq, A., Riachy, L., Vertueux, S., Beauvais, B., Courvalet, M., Henry, P., Tanguy, É., et al. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202510412 · Cited by 12 · see citing works

Metal Ion Toxicity in Human Body: Sources, Effects, Mechanisms and Detoxification Methods

Islam, M., Roy, D., & Singha, D. (2025) · Chemistry Africa · doi:10.1007/s42250-025-01233-z · Cited by 13 · see citing works

Phospholipase D and the Mitogen Phosphatidic Acid in Human Disease: Inhibitors of PLD at the Crossroads of Phospholipid Biology and Cancer

Gómez-Cambronero, J., & Shah, K. N. (2019) · Handbook of experimental pharmacology · doi:10.1007/164_2019_216 · Cited by 8 · see citing works

Underpinning the role of phospholipase D as a therapeutic target in cancer

Gopal, P. K., Mukherjee, K., & Das, A. K. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-95697-0.00005-4

Phospholipase D: its role in metabolism processes and disease development

Ramenskaya, G. V., Melnik, E. V., & Петухов, А. Е. (2018) · Biomeditsinskaya Khimiya · doi:10.18097/pbmc20186401084 · Cited by 4 · see citing works

Phospholipase D: Its Role in Metabolic Processes and Development of Diseases

Ramenskaya, G. V., Melnik, E. V., & Петухов, А. Е. (2018) · Biochemistry (Moscow) Supplement Series B Biomedical Chemistry · doi:10.1134/s199075081803006x

Design of isoform-selective phospholipase D inhibitors that modulate cancer cell invasiveness

Scott, S. A., Selvy, P. E., Buck, J. R., Cho, H. P., Criswell, T. L., Thomas, A. L., Armstrong, M. D., Arteaga, C. L., Lindsley, C. W., & Brown, H. A. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.140 · Cited by 283 · see citing works