ACS Publications. Most Trusted. Most Cited. Most Read
Design and Pharmacological Activity of Phosphinic Acid Based NAALADase Inhibitors

OR SEARCH CITATIONS

My Activity
Publications

Figure 1Loading Img
Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Med. Chem. 2001, 44, 24, 4170-4175
    Article

    Design and Pharmacological Activity of Phosphinic Acid Based NAALADase Inhibitors
    Click to copy article linkArticle link copied!

    View Author Information
    Guilford Pharmaceuticals Inc., 6611 Tributary Street, Baltimore, Maryland 21224
    Other Access Options

    Journal of Medicinal Chemistry

    Cite this: J. Med. Chem. 2001, 44, 24, 4170–4175
    Click to copy citationCitation copied!
    https://doi.org/10.1021/jm0001774
    Published October 18, 2001
    Copyright © 2001 American Chemical Society
    Request reuse permissions

    Abstract

    Click to copy section linkSection link copied!
    Abstract Image

    A novel series of phosphinic acid based inhibitors of the neuropeptidase NAALADase are described in this work. This series of compounds is the most potent series of inhibitors of the enzyme described to date. In addition, we have shown that these compounds are protective in animal models of neurodegeneration. Compound 34 significantly prevented neurodegeneration in a middle cerebral artery occlusion model of cerebral ischemia. In addition, in the chronic constrictive model of neuropathic pain, compound 34 significantly attenuated the hypersensitivity observed with saline-treated animals. These data suggest that NAALADase inhibition may provide a new approach for the treatment of both neurodegenerative disorders and peripheral neuropathies.

    Copyright © 2001 American Chemical Society

    Subjects

    what are subjects

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. Add or change your institution or let them know you’d like them to include access.

    *

    In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.

    †

     Current address:  The R. W. Johnson Pharmaceutical Research Institute, Route 202, P.O. Box 300, Raritan, NJ 08869.

    ‡

     Current address:  The R. W. Johnson Pharmaceutical Research Institute, 3210 Merryfield Row, San Diego, CA 92121.

    Cited By

    Click to copy section linkSection link copied!

    This article is cited by 77 publications.

    1. Zora Novakova, Zahra Aliakbar Tehrani, Radek Jurok, Lucia Motlova, Zsofia Kutil, Jiri Pavlicek, Shivam Shukla, Cindy J. Choy, Barbora Havlinova, Petra Baranova, Clifford E. Berkman, Martin Kuchar, Jiri Cerny, Cyril Barinka. Structural, Biochemical, and Computational Characterization of Sulfamides as Bimetallic Peptidase Inhibitors. Journal of Chemical Information and Modeling 2024, 64 (3) , 1030-1042. https://doi.org/10.1021/acs.jcim.3c01542
    2. Xinlin Wang, Yimin Chen, Yuqing Xiong, Longfei Zhang, Beibei Wang, Yajun Liu, Mengchao Cui. Design and Characterization of Squaramic Acid-Based Prostate-Specific Membrane Antigen Inhibitors for Prostate Cancer. Journal of Medicinal Chemistry 2023, 66 (10) , 6889-6904. https://doi.org/10.1021/acs.jmedchem.3c00309
    3. Dimitris Georgiadis, Nikolaos Skoulikas, Athanasios Papakyriakou, Efstratios Stratikos. Phosphinic Peptides as Tool Compounds for the Study of Pharmacologically Relevant Zn-Metalloproteases. ACS Pharmacology & Translational Science 2022, 5 (12) , 1228-1253. https://doi.org/10.1021/acsptsci.2c00183
    4. Xiaojiang Duan, Futao Liu, Hongmok Kwon, Youngjoo Byun, Il Minn, Xuekang Cai, Jingming Zhang, Martin G. Pomper, Zhi Yang, Zhen Xi, Xing Yang. (S)-3-(Carboxyformamido)-2-(3-(carboxymethyl)ureido)propanoic Acid as a Novel PSMA Targeting Scaffold for Prostate Cancer Imaging. Journal of Medicinal Chemistry 2020, 63 (7) , 3563-3576. https://doi.org/10.1021/acs.jmedchem.9b02031
    5. Albertus Wijnand Hensbergen, Danny M. van Willigen, Florian van Beurden, Pim J. van Leeuwen, Tessa Buckle, Margret Schottelius, Tobias Maurer, Hans-Jürgen Wester, Fijs W. B. van Leeuwen. Image-Guided Surgery: Are We Getting the Most Out of Small-Molecule Prostate-Specific-Membrane-Antigen-Targeted Tracers?. Bioconjugate Chemistry 2020, 31 (2) , 375-395. https://doi.org/10.1021/acs.bioconjchem.9b00758
    6. Michael Nedelcovych, Ranjeet P. Dash, Lukáš Tenora, Sarah C. Zimmermann, Alexandra J. Gadiano, Caroline Garrett, Jesse Alt, Kristen R. Hollinger, Elie Pommier, Andrej Jančařík, Camilo Rojas, Ajit G. Thomas, Ying Wu, Krystyna Wozniak, Pavel Majer, Barbara S. Slusher, and Rana Rais . Enhanced Brain Delivery of 2-(Phosphonomethyl)pentanedioic Acid Following Intranasal Administration of Its γ-Substituted Ester Prodrugs. Molecular Pharmaceutics 2017, 14 (10) , 3248-3257. https://doi.org/10.1021/acs.molpharmaceut.7b00231
    7. Rana Rais, Jan Vávra, Tomáš Tichý, Ranjeet P. Dash, Alexandra J. Gadiano, Lukáš Tenora, Lenka Monincová, Cyril Bařinka, Jesse Alt, Sarah C. Zimmermann, C. Ethan Slusher, Ying Wu, Krystyna Wozniak, Pavel Majer, Takashi Tsukamoto, and Barbara S. Slusher . Discovery of a para-Acetoxy-benzyl Ester Prodrug of a Hydroxamate-Based Glutamate Carboxypeptidase II Inhibitor as Oral Therapy for Neuropathic Pain. Journal of Medicinal Chemistry 2017, 60 (18) , 7799-7809. https://doi.org/10.1021/acs.jmedchem.7b00825
    8. Zora Novakova, Krystyna Wozniak, Andrej Jancarik, Rana Rais, Ying Wu, Jiri Pavlicek, Dana Ferraris, Barbora Havlinova, Jakub Ptacek, Jan Vavra, Niyada Hin, Camilo Rojas, Pavel Majer, Barbara S. Slusher, Takashi Tsukamoto, and Cyril Barinka . Unprecedented Binding Mode of Hydroxamate-Based Inhibitors of Glutamate Carboxypeptidase II: Structural Characterization and Biological Activity. Journal of Medicinal Chemistry 2016, 59 (10) , 4539-4550. https://doi.org/10.1021/acs.jmedchem.5b01806
    9. Xing Yang, Ronnie C. Mease, Mrudula Pullambhatla, Ala Lisok, Ying Chen, Catherine A. Foss, Yuchuan Wang, Hassan Shallal, Hannah Edelman, Adam T. Hoye, Giorgio Attardo, Sridhar Nimmagadda, and Martin G. Pomper . [18F]Fluorobenzoyllysinepentanedioic Acid Carbamates: New Scaffolds for Positron Emission Tomography (PET) Imaging of Prostate-Specific Membrane Antigen (PSMA). Journal of Medicinal Chemistry 2016, 59 (1) , 206-218. https://doi.org/10.1021/acs.jmedchem.5b01268
    10. Guiyang Hao, Amit Kumar, Timothy Dobin, Orhan K. Öz, Jer-Tsong Hsieh, and Xiankai Sun . A Multivalent Approach of Imaging Probe Design To Overcome an Endogenous Anion Binding Competition for Noninvasive Assessment of Prostate Specific Membrane Antigen. Molecular Pharmaceutics 2013, 10 (8) , 2975-2985. https://doi.org/10.1021/mp4000844
    11. Doris Stoermer, Dilrukshi Vitharana, Niyada Hin, Greg Delahanty, Bridget Duvall, Dana V. Ferraris, Brian S. Grella, Randall Hoover, Camilo Rojas, Megan K. Shanholtz, Kyle P. Smith, Marigo Stathis, Ying Wu, Krystyna M. Wozniak, Barbara S. Slusher, and Takashi Tsukamoto . Design, Synthesis, and Pharmacological Evaluation of Glutamate Carboxypeptidase II (GCPII) Inhibitors Based on Thioalkylbenzoic Acid Scaffolds. Journal of Medicinal Chemistry 2012, 55 (12) , 5922-5932. https://doi.org/10.1021/jm300488m
    12. Anna Plechanovová, Youngjoo Byun, Glenda Alquicer, L'ubica Škultétyová, Petra Mlčochová, Adriana Němcová, Hyung-Joon Kim, Michal Navrátil, Ronnie Mease, Jacek Lubkowski, Martin Pomper, Jan Konvalinka, Lubomír Rulíšek, and Cyril Bařinka . Novel Substrate-Based Inhibitors of Human Glutamate Carboxypeptidase II with Enhanced Lipophilicity. Journal of Medicinal Chemistry 2011, 54 (21) , 7535-7546. https://doi.org/10.1021/jm200807m
    13. Andrew X. Zhang, Ryan P. Murelli, Cyril Barinka, Julien Michel, Alexandra Cocleaza, William L. Jorgensen, Jacek Lubkowski and David A. Spiegel . A Remote Arene-Binding Site on Prostate Specific Membrane Antigen Revealed by Antibody-Recruiting Small Molecules. Journal of the American Chemical Society 2010, 132 (36) , 12711-12716. https://doi.org/10.1021/ja104591m
    14. Dao-Yong Wang, Xiang-Ping Hu, Chuan-Jin Hou, Jun Deng, Sai-Bo Yu, Zheng-Chao Duan, Jia-Di Huang and Zhuo Zheng. Enantioselective Rh-Catalyzed Hydrogenation of 3-Aryl-2-phosphonomethylpropenoates by a New Class of Chiral Ferrocenyl Diphosphine Ligands. Organic Letters 2009, 11 (15) , 3226-3229. https://doi.org/10.1021/ol9012469
    15. Cyril Barinka, Youngjoo Byun, Crystal L. Dusich, Sangeeta R. Banerjee, Ying Chen, Mark Castanares, Alan P. Kozikowski, Ronnie C. Mease, Martin G. Pomper and Jacek Lubkowski . Interactions between Human Glutamate Carboxypeptidase II and Urea-Based Inhibitors: Structural Characterization. Journal of Medicinal Chemistry 2008, 51 (24) , 7737-7743. https://doi.org/10.1021/jm800765e
    16. Ling-Wei Hsin, Li-Te Chang, Richard B. Rothman, Christina M. Dersch, Arthur E. Jacobson and Kenner C. Rice. Design and Synthesis of 2- and 3-Substituted-3-phenylpropyl Analogs of 1-[2-[Bis(4-fluorophenyl)methoxy]ethyl]-4-(3-phenylpropyl)piperazine and 1-[2-(Diphenylmethoxy)ethyl]-4-(3-phenylpropyl)piperazine: Role of Amino, Fluoro, Hydroxyl, Methoxyl, Methyl, Methylene, and Oxo Substituents on Affinity for the Dopamine and Serotonin Transporters. Journal of Medicinal Chemistry 2008, 51 (9) , 2795-2806. https://doi.org/10.1021/jm701270n
    17. Cyril Bařinka,, Miroslava Rovenská,, Petra Mlčochová,, Klára Hlouchová,, Anna Plechanovová,, Pavel Majer,, Takashi Tsukamoto,, Barbara S. Slusher,, Jan Konvalinka, and, Jacek Lubkowski. Structural Insight into the Pharmacophore Pocket of Human Glutamate Carboxypeptidase II. Journal of Medicinal Chemistry 2007, 50 (14) , 3267-3273. https://doi.org/10.1021/jm070133w
    18. Pavel Majer,, Bunda Hin,, Doris Stoermer,, Jessica Adams,, Weizheng Xu,, Bridget R. Duvall,, Greg Delahanty,, Qun Liu,, Marigo J. Stathis,, Krystyna M. Wozniak,, Barbara S. Slusher, and, Takashi Tsukamoto. Structural Optimization of Thiol-Based Inhibitors of Glutamate Carboxypeptidase II by Modification of the P1‘ Side Chain. Journal of Medicinal Chemistry 2006, 49 (10) , 2876-2885. https://doi.org/10.1021/jm051019l
    19. David M. Bartley and, James K. Coward. Regioselective Synthesis of α-Methyl 2-Methyleneglutarate via a Novel Lactonization−Elimination Rearrangement. The Journal of Organic Chemistry 2006, 71 (1) , 372-374. https://doi.org/10.1021/jo051854a
    20. David M. Bartley and, James K. Coward. A Stereoselective Synthesis of Phosphinic Acid Phosphapeptides Corresponding to Glutamyl-γ-glutamate and Incorporation into Potent Inhibitors of Folylpoly-γ-glutamyl Synthetase. The Journal of Organic Chemistry 2005, 70 (17) , 6757-6774. https://doi.org/10.1021/jo0507439
    21. Takashi Tsukamoto,, Pavel Majer,, Dilrukshi Vitharana,, Chiyou Ni,, Bunda Hin,, Xi-Chun M. Lu,, Ajit G. Thomas,, Krystyna M. Wozniak,, David C. Calvin,, Ying Wu,, Barbara S. Slusher,, David Scarpetti, and, George W. Bonneville. Enantiospecificity of Glutamate Carboxypeptidase II Inhibition. Journal of Medicinal Chemistry 2005, 48 (7) , 2319-2324. https://doi.org/10.1021/jm049258g
    22. Pingyu Ding,, Marvin J. Miller,, Yi Chen,, Paul Helquist,, A. Jayne Oliver, and, Olaf Wiest. Syntheses of Conformationally Constricted Molecules as Potential NAALADase/PSMA Inhibitors. Organic Letters 2004, 6 (11) , 1805-1808. https://doi.org/10.1021/ol049473r
    23. Alan P. Kozikowski,, Jiazhong Zhang,, Fajun Nan,, Pavel A. Petukhov,, Ewa Grajkowska,, Jarda T. Wroblewski,, Tatsuo Yamamoto,, Tomasz Bzdega,, Barbara Wroblewska, and, Joseph H. Neale. Synthesis of Urea-Based Inhibitors as Active Site Probes of Glutamate Carboxypeptidase II:  Efficacy as Analgesic Agents. Journal of Medicinal Chemistry 2004, 47 (7) , 1729-1738. https://doi.org/10.1021/jm0306226
    24. Pavel Majer,, Paul F. Jackson,, Greg Delahanty,, Brian S. Grella,, Yao-Sen Ko,, Weixing Li,, Qun Liu,, Keith M. Maclin,, Jana Poláková,, Kathryn A Shaffer,, Doris Stoermer,, Dilrukshi Vitharana,, Eric Yanjun Wang,, Anthony Zakrzewski,, Camilo Rojas,, Barbara S. Slusher,, Krystyna M. Wozniak,, Eric Burak,, Tharin Limsakun, and, Takashi Tsukamoto. Synthesis and Biological Evaluation of Thiol-Based Inhibitors of Glutamate Carboxypeptidase II:  Discovery of an Orally Active GCP II Inhibitor. Journal of Medicinal Chemistry 2003, 46 (10) , 1989-1996. https://doi.org/10.1021/jm020515w
    25. Robyn Wiseman, Kristin L. Bigos, Amy F.T. Arnsten, Barbara S. Slusher. Inhibition of brain glutamate carboxypeptidase II (GCPII) to enhance cognitive function. 2024https://doi.org/10.1016/bs.apha.2024.10.018
    26. S. F. Malysheva, V. A. Kuimov, S. N. Arbuzova. Elemental Phosphorus in the Synthesis of Organophosphorus Compounds: The Recent Advances (A Review). Russian Journal of General Chemistry 2023, 93 (S1) , S238-S255. https://doi.org/10.1134/S1070363223140293
    27. Vladimir A. Kuimov, Svetlana F. Malysheva, Natalia A. Belogorlova, Ruslan I. Fattakhov, Alexander I. Albanov, Boris A. Trofimov. Triton-X-100 as an Organic Catalyst for One-Pot Synthesis of Arylmethyl-H-phosphinic Acids from Red Phosphorus and Arylmethyl Halides in the KOH/H2O/Toluene Multiphase Superbase System. Catalysts 2023, 13 (4) , 720. https://doi.org/10.3390/catal13040720
    28. Sadakatali S. Gori, Ajit G. Thomas, Arindom Pal, Robyn Wiseman, Dana V. Ferraris, Run-duo Gao, Ying Wu, Jesse Alt, Takashi Tsukamoto, Barbara S. Slusher, Rana Rais. D-DOPA Is a Potent, Orally Bioavailable, Allosteric Inhibitor of Glutamate Carboxypeptidase II. Pharmaceutics 2022, 14 (10) , 2018. https://doi.org/10.3390/pharmaceutics14102018
    29. Zahra Nikfarjam, Farshid Zargari, Alireza Nowroozi, Omid Bavi. Metamorphosis of prostate specific membrane antigen (PSMA) inhibitors. Biophysical Reviews 2022, 14 (1) , 303-315. https://doi.org/10.1007/s12551-021-00919-1
    30. Hanane Lahnif, Tilmann Grus, Stefanie Pektor, Lukas Greifenstein, Mathias Schreckenberger, Frank Rösch. Hybrid Chelator-Based PSMA Radiopharmaceuticals: Translational Approach. Molecules 2021, 26 (21) , 6332. https://doi.org/10.3390/molecules26216332
    31. Mohamed El Fakiri, Nicolas M. Geis, Nawal Ayada, Matthias Eder, Ann-Christin Eder. PSMA-Targeting Radiopharmaceuticals for Prostate Cancer Therapy: Recent Developments and Future Perspectives. Cancers 2021, 13 (16) , 3967. https://doi.org/10.3390/cancers13163967
    32. Hyunsoo Ha, Hongmok Kwon, Taehyeong Lim, Jaebong Jang, Song-Kyu Park, Youngjoo Byun. Inhibitors of prostate-specific membrane antigen in the diagnosis and therapy of metastatic prostate cancer – a review of patent literature. Expert Opinion on Therapeutic Patents 2021, 31 (6) , 525-547. https://doi.org/10.1080/13543776.2021.1878145
    33. Andrew Siow, Renata Kowalczyk, Margaret A. Brimble, Paul W.R. Harris. Evolution of Peptide-Based Prostate-Specific Membrane Antigen (PSMA) Inhibitors: An Approach to Novel Prostate Cancer Therapeutics. Current Medicinal Chemistry 2021, 28 (19) , 3713-3752. https://doi.org/10.2174/0929867327666201006153847
    34. Hongmok Kwon, Hyunwoong Lim, Hyunsoo Ha, Doyoung Choi, Sang-Hyun Son, Hwanhee Nam, Il Minn, Youngjoo Byun. Structure-activity relationship studies of prostate-specific membrane antigen (PSMA) inhibitors derived from α-amino acid with (S)- or (R)-configuration at P1′ region. Bioorganic Chemistry 2020, 104 , 104304. https://doi.org/10.1016/j.bioorg.2020.104304
    35. K Nordengen, C Morland, B S Slusher, V Gundersen. Dendritic Localization and Exocytosis of NAAG in the Rat Hippocampus. Cerebral Cortex 2020, 30 (3) , 1422-1435. https://doi.org/10.1093/cercor/bhz176
    36. Sara Pastorino, Mattia Riondato, Licia Uccelli, Giampiero Giovacchini, Elisabetta Giovannini, Valerio Duce, Andrea Ciarmiello. Toward the Discovery and Development of PSMA Targeted Inhibitors for Nuclear Medicine Applications. Current Radiopharmaceuticals 2020, 13 (1) , 63-79. https://doi.org/10.2174/1874471012666190729151540
    37. Chunhai Wang, Xiaoling Huang, Xueting Liu, Suqian Gao, Bin Zhao, Shangdong Yang. Photo-induced phosphorus radical involved semipinacol rearrangement reaction: Highly synthesis of γ-oxo-phosphonates. Chinese Chemical Letters 2020, 31 (3) , 677-680. https://doi.org/10.1016/j.cclet.2019.08.011
    38. Susanne Lütje, Roger Slavik, Wolfgang Fendler, Ken Herrmann, Matthias Eiber. PSMA ligands in prostate cancer – Probe optimization and theranostic applications. Methods 2017, 130 , 42-50. https://doi.org/10.1016/j.ymeth.2017.06.026
    39. Jennifer D. Young, Vincenzo Abbate, Cinzia Imberti, Levente K. Meszaros, Michelle T. Ma, Samantha Y.A. Terry, Robert C. Hider, Greg E. Mullen, Philip J. Blower. 68 Ga-THP-PSMA: A PET Imaging Agent for Prostate Cancer Offering Rapid, Room-Temperature, 1-Step Kit-Based Radiolabeling. Journal of Nuclear Medicine 2017, 58 (8) , 1270-1277. https://doi.org/10.2967/jnumed.117.191882
    40. Peizhong Xie, Jinyu Wang, Jing Fan, Yanan Liu, Xiangyang Wo, Teck-Peng Loh. The C–OH/P–H dehydrative cross-coupling for the construction of the P–C bond under metal-free conditions. Green Chemistry 2017, 19 (9) , 2135-2139. https://doi.org/10.1039/C7GC00882A
    41. Maroor Raghavan Ambikalmajan Pillai, Raviteja Nanabala, Ajith Joy, Arun Sasikumar, Furn F. (Russ) Knapp. Radiolabeled enzyme inhibitors and binding agents targeting PSMA: Effective theranostic tools for imaging and therapy of prostate cancer. Nuclear Medicine and Biology 2016, 43 (11) , 692-720. https://doi.org/10.1016/j.nucmedbio.2016.08.006
    42. Alexey E. Machulkin, Yan A. Ivanenkov, Anastasia V. Aladinskaya, Mark S. Veselov, Vladimir A. Aladinskiy, Elena K. Beloglazkina, Victor E. Koteliansky, Artem G. Shakhbazyan, Yuri B. Sandulenko, Alexander G. Majouga. Small-molecule PSMA ligands. Current state, SAR and perspectives. Journal of Drug Targeting 2016, 24 (8) , 679-693. https://doi.org/10.3109/1061186X.2016.1154564
    43. Rana Rais, Weiwei Jiang, Huihong Zhai, Krystyna M. Wozniak, Marigo Stathis, Kristen R. Hollinger, Ajit G. Thomas, Camilo Rojas, James J. Vornov, Michael Marohn, Xuhang Li, Barbara S. Slusher. FOLH1/GCPII is elevated in IBD patients, and its inhibition ameliorates murine IBD abnormalities. JCI Insight 2016, 1 (12) https://doi.org/10.1172/jci.insight.88634
    44. J.J. Vornov, K.R. Hollinger, P.F. Jackson, K.M. Wozniak, M.H. Farah, P. Majer, R. Rais, B.S. Slusher. Still NAAG’ing After All These Years. 2016, 215-255. https://doi.org/10.1016/bs.apha.2016.01.007
    45. Yu‐Chang Chang, Chia‐Ming Weng, Tanveer M. Shaikh, Fung‐E Hong. Magnesium Halide‐promoted Ring‐opening Reaction of Cyclic Ether in the Presence of Phosphine Halide. Journal of the Chinese Chemical Society 2015, 62 (8) , 703-711. https://doi.org/10.1002/jccs.201500154
    46. Rana Rais, Krystyna Wozniak, Ying Wu, Minae Niwa, Marigo Stathis, Jesse Alt, Marc Giroux, Akira Sawa, Camilo Rojas, Barbara S. Slusher, . Selective CNS Uptake of the GCP-II Inhibitor 2-PMPA following Intranasal Administration. PLOS ONE 2015, 10 (7) , e0131861. https://doi.org/10.1371/journal.pone.0131861
    47. Clemens Kratochwil, Frederik L. Giesel, Karin Leotta, Matthias Eder, Torsten Hoppe-Tich, Hagop Youssoufian, Klaus Kopka, John W. Babich, Uwe Haberkorn. PMPA for Nephroprotection in PSMA-Targeted Radionuclide Therapy of Prostate Cancer. Journal of Nuclear Medicine 2015, 56 (2) , 293-298. https://doi.org/10.2967/jnumed.114.147181
    48. Chunlong Zhong, Qizhong Luo, Jiyao Jiang. Blockade of N -acetylaspartylglutamate peptidases: a novel protective strategy for brain injuries and neurological disorders. International Journal of Neuroscience 2014, 124 (12) , 867-873. https://doi.org/10.3109/00207454.2014.890935
    49. James J. Vornov, Krystyna M. Wozniak, Ying Wu, Camilo Rojas, Rana Rais, Barbara S. Slusher. Pharmacokinetics and Pharmacodynamics of the Glutamate Carboxypeptidase II Inhibitor 2-MPPA Show Prolonged Alleviation of Neuropathic Pain through an Indirect Mechanism. Journal of Pharmacology and Experimental Therapeutics 2013, 346 (3) , 406-413. https://doi.org/10.1124/jpet.113.205039
    50. Rana Rais, Randall Hoover, Krystyna Wozniak, Michelle A. Rudek, Takashi Tsukamoto, Jesse Alt, Camilo Rojas, Barbara S. Slusher. Reversible Disulfide Formation of the Glutamate Carboxypeptidase II Inhibitor E2072 Results in Prolonged Systemic Exposures In Vivo. Drug Metabolism and Disposition 2012, 40 (12) , 2315-2323. https://doi.org/10.1124/dmd.112.046821
    51. Krystyna M. Wozniak, Ying Wu, James J. Vornov, Rena Lapidus, Rana Rais, Camilo Rojas, Takashi Tsukamoto, Barbara S. Slusher. The Orally Active Glutamate Carboxypeptidase II Inhibitor E2072 Exhibits Sustained Nerve Exposure and Attenuates Peripheral Neuropathy. Journal of Pharmacology and Experimental Therapeutics 2012, 343 (3) , 746-754. https://doi.org/10.1124/jpet.112.197665
    52. Artur Mucha. Synthesis and Modifications of Phosphinic Dipeptide Analogues. Molecules 2012, 17 (11) , 13530-13568. https://doi.org/10.3390/molecules171113530
    53. Derong Ding, Guang Yan. A Convenient Method for the Synthesis of Aminomethylmonoalkylphosphinate. Chinese Journal of Chemistry 2012, 30 (8) , 1906-1908. https://doi.org/10.1002/cjoc.201200123
    54. Xinning Wang, Haibin Tian, Zhenghong Lee, Warren D. W. Heston. Structure-Activity Relationships of 2′,5′-Oligoadenylate Analogue Modifications of Prostate-Specific Membrane Antigen (PSMA) Antagonists. Nucleosides, Nucleotides and Nucleic Acids 2012, 31 (5) , 432-444. https://doi.org/10.1080/15257770.2012.671988
    55. Jeroen R Mesters, Rolf Hilgenfeld. Glutamate Carboxypeptidase II. 2011https://doi.org/10.1002/9781119951438.eibc0649
    56. Li-Bin Luo, Dao-Yong Wang, Xiao-Mao Zhou, Zhuo Zheng, Xiang-Ping Hu. Asymmetric synthesis of 2-alkyl-3-phosphonopropanoic acid derivatives via Rh-catalyzed asymmetric hydrogenation. Tetrahedron: Asymmetry 2011, 22 (24) , 2117-2123. https://doi.org/10.1016/j.tetasy.2011.12.002
    57. Klára Hlouchová, Cyril BaŘinka, Jan Konvalinka. Glutamate Carboxypeptidase II as a Therapeutic Target. 2011, 62-95. https://doi.org/10.1039/9781849733151-00062
    58. Cyril Barinka, Klara Hlouchova, Miroslava Rovenska, Pavel Majer, Miroslawa Dauter, Niyada Hin, Yao-Sen Ko, Takashi Tsukamoto, Barbara S. Slusher, Jan Konvalinka, Jacek Lubkowski. Structural Basis of Interactions between Human Glutamate Carboxypeptidase II and Its Substrate Analogs. Journal of Molecular Biology 2008, 376 (5) , 1438-1450. https://doi.org/10.1016/j.jmb.2007.12.066
    59. Yunpeng Ye, Min Liu, Jeff L.‐F. Kao, Garland R. Marshall. Design, synthesis, and metal binding of novel Pseudo‐ oligopeptides containing two phosphinic acid groups. Biopolymers 2008, 89 (1) , 72-85. https://doi.org/10.1002/bip.20855
    60. Hagen Cramer, James R. Okicki, Taikyun Rho, Xinning Wang, Robert H. Silverman, Warren D. W. Heston. 2-5A Ligands—A New Concept for the Treatment of Prostate Cancer. Nucleosides, Nucleotides and Nucleic Acids 2007, 26 (10-12) , 1471-1477. https://doi.org/10.1080/15257770701542652
    61. M. Teus, A. Jirgensons, M. Dambrova, R. Mezhapuke. Synthesis and GCP II inhibitory activity of 4[4-(3-bromobenzyl)-5-hydroxyisoxazol-3-yl]benzoic acid heterocyclic analogs. Chemistry of Heterocyclic Compounds 2007, 43 (11) , 1440-1444. https://doi.org/10.1007/s10593-007-0222-7
    62. Takashi Tsukamoto, Krystyna M. Wozniak, Barbara S. Slusher. Progress in the discovery and development of glutamate carboxypeptidase II inhibitors. Drug Discovery Today 2007, 12 (17-18) , 767-776. https://doi.org/10.1016/j.drudis.2007.07.010
    63. Petra Mlčochová, Anna Plechanovová, Cyril Bařinka, Daruka Mahadevan, Jose W. Saldanha, Lubomír Rulíšek, Jan Konvalinka. Mapping of the active site of glutamate carboxypeptidase II by site‐directed mutagenesis. The FEBS Journal 2007, 274 (18) , 4731-4741. https://doi.org/10.1111/j.1742-4658.2007.06021.x
    64. P. Šácha, J. Zámečník, C. Bařinka, K. Hlouchová, A. Vícha, P. Mlčochová, I. Hilgert, T. Eckschlager, J. Konvalinka. Expression of glutamate carboxypeptidase II in human brain. Neuroscience 2007, 144 (4) , 1361-1372. https://doi.org/10.1016/j.neuroscience.2006.10.022
    65. Pingyu Ding, Paul Helquist, Marvin J. Miller. Design, synthesis and pharmacological activity of novel enantiomerically pure phosphonic acid-based NAALADase inhibitors. Organic & Biomolecular Chemistry 2007, 5 (5) , 826. https://doi.org/10.1039/b615603g
    66. Jens Nagel, Irina Belozertseva, Sergio Greco, Vladimir Kashkin, Andrey Malyshkin, Aigars Jirgensons, Elena Shekunova, Bernd Eilbacher, Anton Bespalov, Wojciech Danysz. Effects of NAAG peptidase inhibitor 2-PMPA in model chronic pain – relation to brain concentration. Neuropharmacology 2006, 51 (7-8) , 1163-1171. https://doi.org/10.1016/j.neuropharm.2006.07.018
    67. Alberto Scrivanti, Sara Bovo, Alessandra Ciappa, Ugo Matteoli. The asymmetric hydrogenation of 2-phenethylacrylic acid as the key step for the enantioselective synthesis of Citralis Nitrile®. Tetrahedron Letters 2006, 47 (52) , 9261-9265. https://doi.org/10.1016/j.tetlet.2006.10.129
    68. Jeroen R Mesters, Cyril Barinka, Weixing Li, Takashi Tsukamoto, Pavel Majer, Barbara S Slusher, Jan Konvalinka, Rolf Hilgenfeld. Structure of glutamate carboxypeptidase II, a drug target in neuronal damage and prostate cancer. The EMBO Journal 2006, 25 (6) , 1375-1384. https://doi.org/10.1038/sj.emboj.7600969
    69. Jia Zhou, Joseph H. Neale, Martin G. Pomper, Alan P. Kozikowski. NAAG peptidase inhibitors and their potential for diagnosis and therapy. Nature Reviews Drug Discovery 2005, 4 (12) , 1015-1026. https://doi.org/10.1038/nrd1903
    70. Dean J. Bacich, Krystyna M. Wozniak, X.‐C. May Lu, Denize S. O'Keefe, Noelle Callizot, Warren D. W. Heston, Barbara S. Slusher. Mice lacking glutamate carboxypeptidase II are protected from peripheral neuropathy and ischemic brain injury. Journal of Neurochemistry 2005, 95 (2) , 314-323. https://doi.org/10.1111/j.1471-4159.2005.03361.x
    71. J. P. Van Der Post, S. J. De Visser, M. L. De Kam, M. Woelfler, D. C. Hilt, J. Vornov, E. S. Burak, E. Bortey, B. S. Slusher, T. Limsakun, A. F. Cohen, J. M. A. Van Gerven. The central nervous system effects, pharmacokinetics and safety of the NAALADase‐inhibitor GPI 5693. British Journal of Clinical Pharmacology 2005, 60 (2) , 128-136. https://doi.org/10.1111/j.1365-2125.2005.02396.x
    72. Jeroen R Mesters, Rolf Hilgenfeld. Glutamate Carboxypeptidase II. 2004https://doi.org/10.1002/0470028637.met222
    73. G. Losi, S. Vicini, J. Neale. NAAG fails to antagonize synaptic and extrasynaptic NMDA receptors in cerebellar granule neurons. Neuropharmacology 2004, 46 (4) , 490-496. https://doi.org/10.1016/j.neuropharm.2003.10.007
    74. Ruth E. Carter, Joseph T. Coyle. Glutamate carboxypeptidase II. 2004, 960-963. https://doi.org/10.1016/B978-0-12-079611-3.50298-6
    75. Christos M. Tolias, M. Ross Bullock. Critical appraisal of neuroprotection trials in head injury: What have we learned?. NeuroRX 2004, 1 (1) , 71-79. https://doi.org/10.1602/neurorx.1.1.71
    76. Doris Stoermer, Qun Liu, Monicia R Hall, Juliet M Flanary, Ajit G Thomas, Camilo Rojas, Barbara S Slusher, Takashi Tsukamoto. Synthesis and biological evaluation of hydroxamate-Based inhibitors of glutamate carboxypeptidase II. Bioorganic & Medicinal Chemistry Letters 2003, 13 (13) , 2097-2100. https://doi.org/10.1016/S0960-894X(03)00407-4
    77. Takashi Tsukamoto, Juliet M. Flanary, Camilo Rojas, Barbara S. Slusher, Nadya Valiaeva, James K. Coward. Phosphonate and phosphinate analogues of N-Acylated γ-glutamylglutamate. Bioorganic & Medicinal Chemistry Letters 2002, 12 (16) , 2189-2192. https://doi.org/10.1016/S0960-894X(02)00360-8
    Download PDF
    Go to Journal of Medicinal Chemistry
    Get e-Alerts
    Get e-Alerts

    Journal of Medicinal Chemistry

    Cite this: J. Med. Chem. 2001, 44, 24, 4170–4175
    Click to copy citationCitation copied!
    https://doi.org/10.1021/jm0001774
    Published October 18, 2001
    Copyright © 2001 American Chemical Society
    Request reuse permissions

    Article Views

    1459

    Altmetric

    -

    Citations

    77
    Learn about these metrics

    Article Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.

    Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.

    The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated.