The Role of the Phosphorus Atom in Drug Design

Fluorine in medicinal chemistry

Purser, S., Moore, P. R., Swallow, S., & Gouverneur, V. (2008) · Chem. Soc. Rev. · doi:10.1039/b610213c · Cited by 7,570

Metabotropic Glutamate Receptors: Physiology, Pharmacology, and Disease

Niswender, C. M., & Conn, P. J. (2010) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.011008.145533 · Cited by 1,892

Hallucinogens

Nichols, D. E. (2004) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2003.11.002 · Cited by 1,211

TRP Channels and Pain

Julius, D. (2013) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155833 · Cited by 1,140

Bisphosphonates: The first 40years

Russell, R. G. G. (2011) · Bone · doi:10.1016/j.bone.2011.04.022 · Cited by 1,124

Regulation of cellulose synthesis in Acetobacter xylinum by cyclic diguanylic acid

Ross, P., Weinhouse, H., Aloni, Y., Michaeli, D., Weinberger-Ohana, P., Mayer, R., Braun, S., de Vroom, E., van der Marel, G. A., van Boom, J. H., et al. (1987) · Nature · doi:10.1038/325279a0 · Cited by 1,022

Hybrid Molecules with a Dual Mode of Action: Dream or Reality?

Meunier, B. (2008) · Accounts of Chemical Research · doi:10.1021/ar7000843 · Cited by 929

Adenosine receptors as drug targets — what are the challenges?

Chen, J.-F., Eltzschig, H. K., & Fredholm, B. B. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd3955 · Cited by 895

Purinergic regulation of the immune system

Cekic, C., & Linden, J. (2016) · Nature Reviews Immunology · doi:10.1038/nri.2016.4 · Cited by 787

Remarkable Potential of the α-Aminophosphonate/Phosphinate Structural Motif in Medicinal Chemistry

Mucha, A., Kafarski, P., & Berlicki, Ł. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200587f · Cited by 672

Structure of the TRPA1 ion channel suggests regulatory mechanisms

Paulsen, C. E., Armache, J.-P., Gao, Y., Cheng, Y., & Julius, D. (2015) · Nature · doi:10.1038/nature14367 · Cited by 660

Diphosphonates Inhibit Formation of Calcium Phosphate Crystals in vitro and Pathological Calcification in vivo

Francis, M. D., Graham, R., Russell, G., & Fleisch, H. (1969) · Science · doi:10.1126/science.165.3899.1264 · Cited by 608

The molecular mechanism of nitrogen-containing bisphosphonates as antiosteoporosis drugs

Kavanagh, K. L., Guo, K., Dunford, J. E., Wu, X., Knapp, S., Ebetino, F. H., Rogers, M. J., Russell, R. G. G., & Oppermann, U. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601643103 · Cited by 536

Acetylcholinesterase: ‘classical’ and ‘non-classical’ functions and pharmacology

Silman, I., & Sussman, J. L. (2005) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2005.01.014 · Cited by 524

Eukaryotic mRNA Decapping

Coller, J., & Parker, R. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074032 · Cited by 482

Acidocalcisomes ? conserved from bacteria to man

Docampo, R., de Souza, W., Miranda, K., Rohloff, P., & Moreno, S. N. J. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1097 · Cited by 468

Large-Scale Structural Analysis of the Classical Human Protein Tyrosine Phosphatome

Barr, A. J., Ugochukwu, E., Lee, W. H., King, O. N. F., Filippakopoulos, P., Alfano, I., Savitsky, P., Burgess-Brown, N. A., Müller, S., & Knapp, S. (2009) · Cell · doi:10.1016/j.cell.2008.11.038 · Cited by 467

Fluorinated Carbonyl and Olefinic Compounds: Basic Character and Asymmetric Catalytic Reactions

Mikami, K., Itoh, Y., & Yamanaka, M. (2003) · Chemical Reviews · doi:10.1021/cr030685w · Cited by 437

Phosphinate Chemistry in the 21st Century: A Viable Alternative to the Use of Phosphorus Trichloride in Organophosphorus Synthesis.

Montchamp, J.-L. (2014) · Accounts of Chemical Research · doi:10.1021/ar400071v · Cited by 435

Propofol in Anesthesia. Mechanism of Action, Structure-Activity Relationships, and Drug Delivery

Trapani, G., Altomare, C., Sanna, E., Biggio, G., & Liso, G. (2000) · Current Medicinal Chemistry · doi:10.2174/0929867003375335 · Cited by 423

Kinomics: methods for deciphering the kinome

Johnson, S. A., & Hunter, T. (2005) · Nature Methods · doi:10.1038/nmeth731 · Cited by 419

Prodrugs of Phosphates and Phosphonates

Hecker, S. J., & Erion, M. D. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm701260b · Cited by 414

Structure of the human P2Y12 receptor in complex with an antithrombotic drug

Zhang, K., Zhang, J., Gao, Z.-G., Zhang, D., Zhu, L., Han, G. W., Moss, S. M., Paoletta, S., Kiselev, E., Lu, W., et al. (2014) · Nature · doi:10.1038/nature13083 · Cited by 397

Butyrophilin 3A1 binds phosphorylated antigens and stimulates human γδ T cells

Vavassori, S., Kumar, A., Wan, G. S., Ramanjaneyulu, G. S., Cavallari, M., El Daker, S., Beddoe, T., Theodossis, A., Williams, N. K., Gostick, E., et al. (2013) · Nature Immunology · doi:10.1038/ni.2665 · Cited by 392

The relationship between the chemistry and biological activity of the bisphosphonates

Ebetino, F. H., Hogan, A.-M. L., Sun, S., Tsoumpra, M. K., Duan, X., Triffitt, J. T., Kwaasi, A. A., Dunford, J. E., Barnett, B. L., Oppermann, U., et al. (2011) · Bone · doi:10.1016/j.bone.2011.03.774 · Cited by 391

Fluorinated Phosphonates: Synthesis and Biomedical Application

Romanenko, V. D., & Kukhar, V. P. (2006) · Chemical Reviews · doi:10.1021/cr051000q · Cited by 366

An Allosteric Self-Splicing Ribozyme Triggered by a Bacterial Second Messenger

Lee, E. R., Baker, J. L., Weinberg, Z., Sudarsan, N., & Breaker, R. R. (2010) · Science · doi:10.1126/science.1190713 · Cited by 347

The ProTide Prodrug Technology: From the Concept to the Clinic

Mehellou, Y., Rattan, H. S., & Balzarini, J. M. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00734 · Cited by 345

MECHANISMS OF ACTION OF BISPHOSPHONATES

Rodan, G. A. (1998) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.38.1.375 · Cited by 304

A new endogenous ATP analog (ApppI) inhibits the mitochondrial adenine nucleotide translocase (ANT) and is responsible for the apoptosis induced by nitrogen‐containing bisphosphonates

Mönkkönen, H., Auriola, S., Lehenkari, P., Kellinsalmi, M., Hassinen, I. E., Vepsäläinen, J., & Mönkkönen, J. (2006) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706628 · Cited by 280

Organization and functions of mGlu and GABAB receptor complexes

Pin, J.-P., & Bettler, B. (2016) · Nature · doi:10.1038/nature20566 · Cited by 274

Medicinal chemistry of adenosine, P2Y and P2X receptors

Jacobson, K. A., & Müller, C. E. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.12.001 · Cited by 262

Inhibitors of Acetylcholinesterase and Butyrylcholinesterase Meet Immunity

Pohanka, M. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15069809 · Cited by 245

Bisphosphonates and Estrogens Inhibit Osteocyte Apoptosis via Distinct Molecular Mechanisms Downstream of Extracellular Signal-regulated Kinase Activation

Plotkin, L. I., Aguirre, J. I., Kousteni, S., Manolagas, S. C., & Bellido, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412817200 · Cited by 240

Molecular mechanisms of action of bisphosphonates

Rogers, M. J., Frith, J. C., Luckman, S. P., Coxon, F. P., Benford, H. L., M̈onkk̈onen, J., Auriola, S., Chilton, K. M., & Russell, R. G. G. (1999) · Bone · doi:10.1016/s8756-3282(99)00070-8 · Cited by 237

Studies on the Biosynthesis of Cholesterol

Cornforth, J. W., Cornforth, R. H., Popják, G., & Yengoyan, L. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99800-5 · Cited by 230

Cyclic Dinucleotides and the Innate Immune Response

Danilchanka, O., & Mekalanos, J. J. (2013) · Cell · doi:10.1016/j.cell.2013.08.014 · Cited by 228

Structural Basis for the Exceptional in vivo Efficacy of Bisphosphonate Drugs

Rondeau, J., Bitsch, F., Bourgier, E., Geiser, M., Hemmig, R., Kroemer, M., Lehmann, S., Ramage, P., Rieffel, S., Strauss, A., et al. (2006) · ChemMedChem · doi:10.1002/cmdc.200500059 · Cited by 226

Risks and benefits of bisphosphonates

Coleman, R. E. (2008) · British Journal of Cancer · doi:10.1038/sj.bjc.6604382 · Cited by 212

Recent Trends in Nucleotide Synthesis

Roy, B., Depaix, A., Périgaud, C., & Peyrottes, S. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00174 · Cited by 212

Farnesyltransferase inhibition causes morphological reversion of ras-transformed cells by a complex mechanism that involves regulation of the actin cytoskeleton.

Prendergast, G. C., Davide, J. P., deSolms, S. J., Giuliani, E. A., Graham, S. L., Gibbs, J. B., Oliff, A., & Kohl, N. E. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.6.4193 · Cited by 209

Enzymatic Synthesis of Psilocybin

Fricke, J., Blei, F., & Hoffmeister, D. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201705489 · Cited by 200

An introduction to the roles of purinergic signalling in neurodegeneration, neuroprotection and neuroregeneration

Burnstock, G. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.05.031 · Cited by 199

Targeting Bone Metastases with a Bispecific Anticancer and Antiangiogenic Polymer–Alendronate–Taxane Conjugate

Miller, K., Erez, R., Segal, E., Shabat, D., & Satchi‐Fainaro, R. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200805133 · Cited by 179

Lipophilic Bisphosphonates as Dual Farnesyl/Geranylgeranyl Diphosphate Synthase Inhibitors: An X-ray and NMR Investigation

Zhang, Y., Cao, R., Yin, F., Hudock, M. P., Guo, R.-T., Krysiak, K., Mukherjee, S., Gao, Y.-G., Robinson, H., Song, Y., et al. (2009) · Journal of the American Chemical Society · doi:10.1021/ja808285e · Cited by 178

Acidocalcisomes

Docampo, R., & Moreno, S. N. J. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.05.012 · Cited by 160

Therapeutic Implications for Striatal-Enriched Protein Tyrosine Phosphatase (STEP) in Neuropsychiatric Disorders

Goebel-Goody, S. M., Baum, M., Paspalas, C. D., Fernandez, S. M., Carty, N. C., Kurup, P., & Lombroso, P. J. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.003053 · Cited by 159

Phosphorothioate cap analogs stabilize mRNA and increase translational efficiency in mammalian cells

Grudzien‐Nogalska, E., Jemielity, J., Kowalska, J., Darżynkiewicz, E., & Rhoads, R. E. (2007) · RNA · doi:10.1261/rna.701307 · Cited by 157

Trypanosoma cruzi Contains Major Pyrophosphate Stores, and Its Growth in Vitro and in Vivo Is Blocked by Pyrophosphate Analogs

Urbina, J. A., Moreno, B., Vierkotter, S., Oldfield, E., Payares, G., Sanoja, C., Bailey, B. N., Yan, W., Scott, D. A., Moreno, S. N. J., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.47.33609 · Cited by 151

Aspartyl-tRNA Synthetase Is the Target of Peptide Nucleotide Antibiotic Microcin C

Metlitskaya, A. Z., Kazakov, T., Kommer, A., Pavlova, O., Prætorius-Ibba, M., Ibba, M., Krasheninnikov, I. A., Kolb, V. A., Khmel, I. A., & Severinov, K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513174200 · Cited by 151

Bisphosphonates Are Potent Inhibitors of Trypanosoma cruzi Farnesyl Pyrophosphate Synthase

Montalvetti, A., Bailey, B. N., Martin, M., Severin, G. W., Oldfield, E., & Docampo, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103950200 · Cited by 149

P2Y nucleotide receptors: promise of therapeutic applications

Jacobson, K. A., & Boeynaems, J. (2010) · Drug Discovery Today · doi:10.1016/j.drudis.2010.05.011 · Cited by 148

Inhibitors of HIV-1 Attachment: The Discovery and Development of Temsavir and its Prodrug Fostemsavir

Meanwell, N. A., Krystal, M., Nowicka-Sans, B., Langley, D. R., Conlon, D. A., Eastgate, M. D., Grasela, D. M., Timmins, P., Wang, T., & Kadow, J. F. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01337 · Cited by 143

Molecular structure and function of P2X receptors

Habermacher, C., Dunning, K., Chataigneau, T., & Grütter, T. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.07.032 · Cited by 141

Phosphoric acid as a precursor to chemicals traditionally synthesized from white phosphorus

Geeson, M. B., & Cummins, C. C. (2018) · Science · doi:10.1126/science.aar6620 · Cited by 140

In Vitro Antiviral Characteristics of HIV-1 Attachment Inhibitor BMS-626529, the Active Component of the Prodrug BMS-663068

Nowicka-Sans, B., Gong, Y.-F., McAuliffe, B. V., Dicker, I. B., Ho, H., Zhou, N., Eggers, B. J., Lin, P., Ray, N., Wind‐Rotolo, M., et al. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00426-12 · Cited by 139

Chemical Structure and Translation Inhibition Studies of the Antibiotic Microcin C7

Guijarro, J. I., González‐Pastor, J. E., Baleux, F., Millán, J. L. S., Castilla, M. A., Rico, M., Moreno, F., & Delepierre, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.40.23520 · Cited by 137

Farnesyl pyrophosphate synthase: a key enzyme in isoprenoid biosynthetic pathway and potential molecular target for drug development

Dhar, M. K., Koul, A., & Kaul, S. (2012) · New Biotechnology · doi:10.1016/j.nbt.2012.07.001 · Cited by 135

Structure and mechanism of the farnesyl diphosphate synthase from Trypanosoma cruzi: Implications for drug design

Gabelli, S. B., McLellan, J. S., Montalvetti, A., et al. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20754 · Cited by 133

Regulatory Mechanisms and Novel Therapeutic Targeting Strategies for Protein Tyrosine Phosphatases

Yu, Z.-H., & Zhang, Z. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00105 · Cited by 131

Defective macromolecule biosynthesis and cell-cycle progression in a mammalian cell starved for mevalonate.

Sinensky, M. S., & Logel, J. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.10.3257 · Cited by 130

Allosteric non-bisphosphonate FPPS inhibitors identified by fragment-based discovery

Jahnke, W., Rondeau, J., Cotesta, S., Marzinzik, A. L., Pellé, X., Geiser, M., Strauss, A., Götte, M., Bitsch, F., Hemmig, R., et al. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.421 · Cited by 129

Synthesis and P2Y receptor activity of a series of uridine dinucleoside 5′-polyphosphates

Pendergast, W., Yerxa, B. R., Douglass, J. G., Shaver, S. R., Dougherty, R. W., Redick, C. C., Sims, I. F., & Rideout, J. L. (2001) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(00)00612-0 · Cited by 127

A Single Enzyme Catalyses Formation of Trypanothione from Glutathione and Spermidine in Trypanosoma cruzi

Oza, S. L., Tétaud, E., Ariyanayagam, M. R., Warnon, S. S., & Fairlamb, A. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204403200 · Cited by 124

Fragment-Based Substrate Activity Screening Method for the Identification of Potent Inhibitors of the Mycobacterium tuberculosis Phosphatase PtpB

Soellner, M. B., Rawls, K. A., Grundner, C., Alber, T., & Ellman, J. A. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0727520 · Cited by 110

Synthesis of a Phosphoantigen Prodrug that Potently Activates Vγ9Vδ2 T-Lymphocytes

Hsiao, C. C., Lin, X., Barney, R. J., Shippy, R. R., Li, J., Vinogradova, O., Wiemer, D. F., & Wiemer, A. J. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.06.006 · Cited by 107

Nucleotide pyrophosphatase/phosphodiesterase 1 (NPP1) and its inhibitors

Lee, S.-Y., & Müller, C. E. (2017) · MedChemComm · doi:10.1039/c7md00015d · Cited by 103

Design, Synthesis, and Antimicrobial Evaluation of a Novel Bone-Targeting Bisphosphonate-Ciprofloxacin Conjugate for the Treatment of Osteomyelitis Biofilms

Sedghizadeh, P. P., Sun, S., Junka, A., Richard, E., Sadrerafi, K., Mahabady, S., Bakhshalian, N., Tjokro, N. O., Bartoszewicz, M., Oleksy-Wawrzyniak, M., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01615 · Cited by 99

Antimalarial and Antitumor Evaluation of Novel C-10 Non-Acetal Dimers of 10β-(2-Hydroxyethyl)deoxoartemisinin

Jeyadevan, J. P., Bray, P. G., Chadwick, J., Chadwick, A. E., Byrne, A., Ward, S. A., Park, B. K., Williams, D. P., Cosstick, R., Davies, J. D., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm030974c · Cited by 96

5′-Phosphorothiolate Dinucleotide Cap Analogues: Reagents for Messenger RNA Modification and Potent Small-Molecular Inhibitors of Decapping Enzymes

Wojtczak, B. A., Sikorski, P. J., Fac-Dabrowska, K., Nowicka, A. M., Warmiński, M., Kubacka, D., Nowak, E., Nowotny, M., Kowalska, J., & Jemielity, J. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b02597 · Cited by 95

2‐Chloro N6‐methyl‐(N)‐methanocarba‐2′‐deoxyadenosine‐3′,5′‐bisphosphate is a selective high affinity P2Y1 receptor antagonist

Boyer, J. L., Adams, M., Ravi, R. G., Jacobson, K. A., & Harden, T. K. (2002) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0704673 · Cited by 94

Potent and Selective Inhibition of Acid Sphingomyelinase by Bisphosphonates

Roth, A. G., Drescher, D., Yang, Y., Redmer, S., Uhlig, S., & Arenz, C. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200903288 · Cited by 94

Biosynthesis of non-head-to-tail terpenes. Formation of 1'-1 and 1'-3 linkages

Poulter, C. (1990) · Accounts of Chemical Research · doi:10.1021/ar00171a003 · Cited by 87

Allosteric modulation of ATP-gated P2X receptor channels

Coddou, C., Stojilković, S. S., & Huidobro-Toro, J. P. (2011) · Reviews in the Neurosciences · doi:10.1515/rns.2011.014 · Cited by 86

Bisphosphonate-modified biomaterials for drug delivery and bone tissue engineering

Ossipov, D. A. (2015) · Expert Opinion on Drug Delivery · doi:10.1517/17425247.2015.1021679 · Cited by 85

Toxoplasma gondii Relies on Both Host and Parasite Isoprenoids and Can Be Rendered Sensitive to Atorvastatin

Li, Z., Ramakrishnan, S., Striepen, B., & Moreno, S. N. J. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003665 · Cited by 82

A Virtual Screening Hit Reveals New Possibilities for Developing Group III Metabotropic Glutamate Receptor Agonists

Selvam, C., Oueslati, N., Lemasson, I., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901523t · Cited by 73

Synthesis and Biological Evaluation of α-Halogenated Bisphosphonate and Phosphonocarboxylate Analogues of Risedronate

Marma, M. S., Xia, Z., Stewart, C. A., Coxon, F. P., Dunford, J. E., Baron, R., Kashemirov, B. A., Ebetino, F. H., Triffitt, J. T., Russell, R. G. G., et al. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm0702884 · Cited by 67

Location-Dependent Signaling of the Group 1 Metabotropic Glutamate Receptor mGlu5

Jong, Y.-J. I., Sergin, I., Purgert, C. A., & O’Malley, K. L. (2014) · Molecular Pharmacology · doi:10.1124/mol.114.094763 · Cited by 66

The Acidocalcisome as a Target for Chemotherapeutic Agents in Protozoan Parasites

Docampo, R., & Moreno, S. N. J. (2008) · Current Pharmaceutical Design · doi:10.2174/138161208784041079 · Cited by 63

A Pyridoxine Cyclic Phosphate and Its 6-Azoaryl Derivative Selectively Potentiate and Antagonize Activation of P2X1 Receptors

Jacobson, K. A., Kim, Y. C., Wildman, S. S. P., Mohanram, A., Harden, T. K., Boyer, J. L., King, B. F., & Burnstock, G. (1998) · Journal of Medicinal Chemistry · doi:10.1021/jm980183o · Cited by 62

New antibacterials for the treatment of toxoplasmosis; a patent review

Rodríguez, J. B., & Szajnman, S. H. (2012) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2012.668886 · Cited by 62

Structure-Based Optimization of Nonquaternary Reactivators of Acetylcholinesterase Inhibited by Organophosphorus Nerve Agents

Santoni, G., de Sousa, J., la Mora, E. D., Dias, J., Jean, L., Sussman, J. L., Silman, I., Renard, P., Brown, R. C. D., Weik, M., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00592 · Cited by 60

Cyclosaligenyl-2′,3′-didehydro-2′,3′-dideoxythymidine Monophosphate: Efficient Intracellular Delivery of d4TMP

Balzarini, J. M., Aquaro, S., Knispel, T., Rampazzo, C., Bianchi, V., Perno, C. F., Clercq, E. D., & Meier, C. (2000) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)12464-9 · Cited by 59

Structures and Conformational Properties of Bases, Furanose Sugars, and Phosphate Groups

Saenger, W. (1984) · Springer advanced texts in chemistry · doi:10.1007/978-1-4612-5190-3_4 · Cited by 58

Synthesis of All Possible Canonical (3′–5′-Linked) Cyclic Dinucleotides and Evaluation of Riboswitch Interactions and Immune-Stimulatory Effects

Wang, C., Sinn, M., Stifel, J., Heiler, A. C., Sommershof, A., & Hartig, J. S. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b06141 · Cited by 57

The inhibition of human farnesyl pyrophosphate synthase by nitrogen-containing bisphosphonates. Elucidating the role of active site threonine 201 and tyrosine 204 residues using enzyme mutants

Tsoumpra, M. K., Muniz, J. R. C., Barnett, B. L., et al. (2015) · Bone · doi:10.1016/j.bone.2015.08.020 · Cited by 56

Current Status and Progresses Made in Malaria Chemotherapy

Liñares, G. G., & Rodríguez, J. B. (2007) · Current Medicinal Chemistry · doi:10.2174/092986707779941096 · Cited by 52

New insights in Chagas disease treatment

Urbina, J. A. (2010) · Drugs of the Future · doi:10.1358/dof.2010.35.5.1484391 · Cited by 52

Mixed Aryl Phosphonate Prodrugs of a Butyrophilin Ligand

Foust, B. J., Poe, M. M., Lentini, N. A., Hsiao, C. C., Wiemer, A. J., & Wiemer, D. F. (2017) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.7b00245 · Cited by 51

The l-AP4 receptor

Thomsen, C. (1997) · General Pharmacology The Vascular System · doi:10.1016/s0306-3623(96)00417-x · Cited by 49

Bisphosphonates derived from fatty acids are potent growth inhibitors of Trypanosoma cruzi

Szajnman, S. H., Bailey, B. N., Docampo, R., & Rodríguez, J. B. (2001) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(01)00057-9 · Cited by 48

Purinergic P2X receptors: Structural models and analysis of ligand-target interaction

Ben, D. D., Buccioni, M., Lambertucci, C., Marucci, G., Thomas, A., & Volpini, R. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.10.071 · Cited by 45

Nitrogen-Containing Bisphosphonates and Cancer Immunotherapy

Clézardin, P., & Massaia, M. (2010) · Current Pharmaceutical Design · doi:10.2174/138161210793563545 · Cited by 44

Farnesyl pyrophosphate synthase modulators: a patent review (2006 – 2010)

Sun, S., & McKenna, C. E. (2011) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2011.593511 · Cited by 43

Role of psilocybin in the treatment of depression

Mahapatra, A., & Gupta, R. G. (2016) · Therapeutic Advances in Psychopharmacology · doi:10.1177/2045125316676092 · Cited by 42

Discovery of a Potent (4R,5S)-4-Fluoro-5-methylproline Sulfonamide Transient Receptor Potential Ankyrin 1 Antagonist and Its Methylene Phosphate Prodrug Guided by Molecular Modeling

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