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Novel Genetic Mutations in the First Swedish Patient with Purine Nucleoside Phosphorylase Deficiency and Clinical Outcome After Hematopoietic Stem Cell Transplantation with HLA-Matched Unrelated Donor.

JIMD reports

Brodszki N, Svensson M, van Kuilenburg AB, Meijer J, Zoetekouw L, Truedsson L, Toporski J.
PMID: 25967230
JIMD Rep. 2015;24:83-9. doi: 10.1007/8904_2015_444. Epub 2015 May 13.

Purine nucleoside phosphorylase (PNP) is an enzyme active in the purine salvage pathway. PNP deficiency caused by autosomal recessive mutations in the PNP gene leads to severe combined immunodeficiency (SCID) and in two thirds of cases also to neurological...

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Brodszki N, Svensson M, van Kuilenburg AB, et al. Novel Genetic Mutations in the First Swedish Patient with Purine Nucleoside Phosphorylase Deficiency and Clinical Outcome After Hematopoietic Stem Cell Transplantation with HLA-Matched Unrelated Donor. JIMD Rep. 2015;24:83-9doi: 10.1007/8904_2015_444.
Brodszki, N., Svensson, M., van Kuilenburg, A. B., Meijer, J., Zoetekouw, L., Truedsson, L., & Toporski, J. (2015). Novel Genetic Mutations in the First Swedish Patient with Purine Nucleoside Phosphorylase Deficiency and Clinical Outcome After Hematopoietic Stem Cell Transplantation with HLA-Matched Unrelated Donor. JIMD reports, 2483-9. https://doi.org/10.1007/8904_2015_444
Brodszki, Nicholas, et al. "Novel Genetic Mutations in the First Swedish Patient with Purine Nucleoside Phosphorylase Deficiency and Clinical Outcome After Hematopoietic Stem Cell Transplantation with HLA-Matched Unrelated Donor." JIMD reports vol. 24 (2015): 83-9. doi: https://doi.org/10.1007/8904_2015_444
Brodszki N, Svensson M, van Kuilenburg AB, Meijer J, Zoetekouw L, Truedsson L, Toporski J. Novel Genetic Mutations in the First Swedish Patient with Purine Nucleoside Phosphorylase Deficiency and Clinical Outcome After Hematopoietic Stem Cell Transplantation with HLA-Matched Unrelated Donor. JIMD Rep. 2015;24:83-9. doi: 10.1007/8904_2015_444. Epub 2015 May 13. PMID: 25967230; PMCID: PMC4582029.
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1,N6-ethenoadenine and other Fluorescent Nucleobase Analogues as Substrates for Purine-Nucleoside Phosphorylases: Spectroscopic and Kinetic Studies.

Current pharmaceutical design

Wierzchowski J, Stachelska-Wierzchowska A, Wielgus-Kutrowska B, Bzowska A.
PMID: 29022509
Curr Pharm Des. 2017 Oct 11; doi: 10.2174/1381612823666171011103551. Epub 2017 Oct 11.

BACKGROUND: Purine-nucleoside phosphorylase (PNP) is known as a tool for the synthesis of various nucleosides and nucleoside analogues. Mechanism, properties, molecular diversity and inhibitors of PNP, particularly these of pharmacological significance, are briefly characterized.METHODS: UV and fluorescence spectroscopy was...

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Wierzchowski J, Stachelska-Wierzchowska A, Wielgus-Kutrowska B, et al. 1,N6-ethenoadenine and other Fluorescent Nucleobase Analogues as Substrates for Purine-Nucleoside Phosphorylases: Spectroscopic and Kinetic Studies. Curr Pharm Des. 2017;doi: 10.2174/1381612823666171011103551.
Wierzchowski, J., Stachelska-Wierzchowska, A., Wielgus-Kutrowska, B., & Bzowska, A. (2017). 1,N6-ethenoadenine and other Fluorescent Nucleobase Analogues as Substrates for Purine-Nucleoside Phosphorylases: Spectroscopic and Kinetic Studies. Current pharmaceutical design, . https://doi.org/10.2174/1381612823666171011103551
Wierzchowski, Jacek, et al. "1,N6-ethenoadenine and other Fluorescent Nucleobase Analogues as Substrates for Purine-Nucleoside Phosphorylases: Spectroscopic and Kinetic Studies." Current pharmaceutical design vol. (2017). doi: https://doi.org/10.2174/1381612823666171011103551
Wierzchowski J, Stachelska-Wierzchowska A, Wielgus-Kutrowska B, Bzowska A. 1,N6-ethenoadenine and other Fluorescent Nucleobase Analogues as Substrates for Purine-Nucleoside Phosphorylases: Spectroscopic and Kinetic Studies. Curr Pharm Des. 2017 Oct 11; doi: 10.2174/1381612823666171011103551. Epub 2017 Oct 11. PMID: 29022509.
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An Improved Synthesis of 7-Substituted Pyrrolo[3,2-d]pyrimidines.

The Journal of organic chemistry

Elliott AJ, Morris PE, Petty SL, Williams CH.
PMID: 11671913
J Org Chem. 1997 Nov 14;62(23):8071-8075. doi: 10.1021/jo971062j.

Base (NaOMe)-catalyzed condensation of 3,3-dimethoxypropionitrile with aldehydes followed by hydrolysis with 6 N HCl gives the unsaturated cyano aldehydes 5. Catalytic reduction of the double bond followed by reaction with diethyl aminomalonate affords the enamines 7, which cyclize to...

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Elliott AJ, Morris PE, Petty SL, et al. An Improved Synthesis of 7-Substituted Pyrrolo[3,2-d]pyrimidines. J Org Chem. 1997;62(23):8071-8075doi: 10.1021/jo971062j.
Elliott, A. J., Morris, P. E., Petty, S. L., & Williams, C. H. (1997). An Improved Synthesis of 7-Substituted Pyrrolo[3,2-d]pyrimidines. The Journal of organic chemistry, 62(23), 8071-8075. https://doi.org/10.1021/jo971062j
Elliott, Arthur J., et al. "An Improved Synthesis of 7-Substituted Pyrrolo[3,2-d]pyrimidines." The Journal of organic chemistry vol. 62,23 (1997): 8071-8075. doi: https://doi.org/10.1021/jo971062j
Elliott AJ, Morris PE, Petty SL, Williams CH. An Improved Synthesis of 7-Substituted Pyrrolo[3,2-d]pyrimidines. J Org Chem. 1997 Nov 14;62(23):8071-8075. doi: 10.1021/jo971062j. PMID: 11671913.
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Refined structure of purine nucleoside phosphorylase at 2.75 A resolution.

Acta crystallographica. Section D, Biological crystallography

Narayana SV, Bugg CE, Ealick SE.
PMID: 15299947
Acta Crystallogr D Biol Crystallogr. 1997 Mar 01;53:131-42. doi: 10.1107/S0907444996012619.

Human purine nucleoside phosphorylase (PNP) catalyzes the reversible phosphorolysis of ribonucleosides and 2'-deoxyribonucleosides to the free base and (2'-deoxy)ribose-l-phosphate. The crystal structure previously determined at 3.2 A resolution by multiple isomorphous replacement methods [Ealick, Rule, Carter, Greenhough, Babu, Cook,...

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Narayana SV, Bugg CE, Ealick SE. Refined structure of purine nucleoside phosphorylase at 2.75 A resolution. Acta Crystallogr D Biol Crystallogr. 1997;53:131-42doi: 10.1107/S0907444996012619.
Narayana, S. V., Bugg, C. E., & Ealick, S. E. (1997). Refined structure of purine nucleoside phosphorylase at 2.75 A resolution. Acta crystallographica. Section D, Biological crystallography, 53131-42. https://doi.org/10.1107/S0907444996012619
Narayana, S V, et al. "Refined structure of purine nucleoside phosphorylase at 2.75 A resolution." Acta crystallographica. Section D, Biological crystallography vol. 53 (1997): 131-42. doi: https://doi.org/10.1107/S0907444996012619
Narayana SV, Bugg CE, Ealick SE. Refined structure of purine nucleoside phosphorylase at 2.75 A resolution. Acta Crystallogr D Biol Crystallogr. 1997 Mar 01;53:131-42. doi: 10.1107/S0907444996012619. PMID: 15299947.
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Gut bacteria recycle uric acid nitrogen in termites: A strategy for nutrient conservation.

Proceedings of the National Academy of Sciences of the United States of America

Potrikus CJ, Breznak JA.
PMID: 16593064
Proc Natl Acad Sci U S A. 1981 Jul;78(7):4601-5. doi: 10.1073/pnas.78.7.4601.

Reticulitermes flavipes termites synthesize uric acid via purine-nucleoside phosphorylase (purine-nucleoside: orthophosphate ribosyltransferase, EC 2.4.2.1) and xanthine dehydrogenase (xanthine:NAD(+) oxidoreductase, EC 1.2.1.37), but their tissues lack uricase (urate:oxygen oxidoreductase, EC 1.7.3.3) or any other enzyme that degrades uric acid. Nevertheless,...

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Potrikus CJ, Breznak JA. Gut bacteria recycle uric acid nitrogen in termites: A strategy for nutrient conservation. Proc Natl Acad Sci U S A. 1981;78(7):4601-5doi: 10.1073/pnas.78.7.4601.
Potrikus, C. J., & Breznak, J. A. (1981). Gut bacteria recycle uric acid nitrogen in termites: A strategy for nutrient conservation. Proceedings of the National Academy of Sciences of the United States of America, 78(7), 4601-5. https://doi.org/10.1073/pnas.78.7.4601
Potrikus, C J, and Breznak, J A. "Gut bacteria recycle uric acid nitrogen in termites: A strategy for nutrient conservation." Proceedings of the National Academy of Sciences of the United States of America vol. 78,7 (1981): 4601-5. doi: https://doi.org/10.1073/pnas.78.7.4601
Potrikus CJ, Breznak JA. Gut bacteria recycle uric acid nitrogen in termites: A strategy for nutrient conservation. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4601-5. doi: 10.1073/pnas.78.7.4601. PMID: 16593064; PMCID: PMC319841.
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Simultaneous determination of sulfite and phosphate in wine by means of immobilized enzyme reactions and amperometric detection in a flow-injection system.

Talanta

Yao T, Satomura M, Nakahara T.
PMID: 18966179
Talanta. 1994 Dec;41(12):2113-9. doi: 10.1016/0039-9140(94)00188-x.

A flow-injection system is proposed for the simultaneous determination of sulfite and phosphate in wine. A sulfite oxidase immobilized reactor and purine nucleoside phosphorylase-xanthine oxidase co-immobilized reactor are incorporated at fixed positions (parallel configuration) in the flow line, which...

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Yao T, Satomura M, Nakahara T. Simultaneous determination of sulfite and phosphate in wine by means of immobilized enzyme reactions and amperometric detection in a flow-injection system. Talanta. 1994;41(12):2113-9doi: 10.1016/0039-9140(94)00188-x.
Yao, T., Satomura, M., & Nakahara, T. (1994). Simultaneous determination of sulfite and phosphate in wine by means of immobilized enzyme reactions and amperometric detection in a flow-injection system. Talanta, 41(12), 2113-9. https://doi.org/10.1016/0039-9140(94)00188-x
Yao, T, et al. "Simultaneous determination of sulfite and phosphate in wine by means of immobilized enzyme reactions and amperometric detection in a flow-injection system." Talanta vol. 41,12 (1994): 2113-9. doi: https://doi.org/10.1016/0039-9140(94)00188-x
Yao T, Satomura M, Nakahara T. Simultaneous determination of sulfite and phosphate in wine by means of immobilized enzyme reactions and amperometric detection in a flow-injection system. Talanta. 1994 Dec;41(12):2113-9. doi: 10.1016/0039-9140(94)00188-x. PMID: 18966179.
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Clinical Trials and Treatment of ATL.

Leukemia research and treatment

Tsukasaki K, Tobinai K.
PMID: 23259064
Leuk Res Treatment. 2012;2012:101754. doi: 10.1155/2012/101754. Epub 2012 Jan 16.

ATL is a distinct peripheral T-lymphocytic malignancy associated with human T-cell lymphotropic virus type I (HTLV-1). The diversity in clinical features and prognosis of patients with this disease has led to its subtype-classification into four categories, acute, lymphoma, chronic,...

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Tsukasaki K, Tobinai K. Clinical Trials and Treatment of ATL. Leuk Res Treatment. 2012;2012:101754doi: 10.1155/2012/101754.
Tsukasaki, K., & Tobinai, K. (2012). Clinical Trials and Treatment of ATL. Leukemia research and treatment, 2012101754. https://doi.org/10.1155/2012/101754
Tsukasaki, Kunihiro, and Tobinai, Kensei. "Clinical Trials and Treatment of ATL." Leukemia research and treatment vol. 2012 (2012): 101754. doi: https://doi.org/10.1155/2012/101754
Tsukasaki K, Tobinai K. Clinical Trials and Treatment of ATL. Leuk Res Treatment. 2012;2012:101754. doi: 10.1155/2012/101754. Epub 2012 Jan 16. PMID: 23259064; PMCID: PMC3505932.
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The effects of forodesine in murine and human multiple myeloma cells.

Advances in hematology

Bieghs L, Caers J, De Bruyne E, Van Valckenborgh E, Higginbotham F, Vanderkerken K, Menu E.
PMID: 20981156
Adv Hematol. 2010;2010:131895. doi: 10.1155/2010/131895. Epub 2010 Oct 19.

Multiple myeloma (MM) is the second most commonly diagnosed hematological malignancy, characterized by a monoclonal proliferation of malignant cells in the bone marrow. Despite recent advances in treatment strategies, MM remains incurable and new therapeutical targets are needed. Recently...

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Bieghs L, Caers J, De Bruyne E, et al. The effects of forodesine in murine and human multiple myeloma cells. Adv Hematol. 2010;2010:131895doi: 10.1155/2010/131895.
Bieghs, L., Caers, J., De Bruyne, E., Van Valckenborgh, E., Higginbotham, F., Vanderkerken, K., & Menu, E. (2010). The effects of forodesine in murine and human multiple myeloma cells. Advances in hematology, 2010131895. https://doi.org/10.1155/2010/131895
Bieghs, Liesbeth, et al. "The effects of forodesine in murine and human multiple myeloma cells." Advances in hematology vol. 2010 (2010): 131895. doi: https://doi.org/10.1155/2010/131895
Bieghs L, Caers J, De Bruyne E, Van Valckenborgh E, Higginbotham F, Vanderkerken K, Menu E. The effects of forodesine in murine and human multiple myeloma cells. Adv Hematol. 2010;2010:131895. doi: 10.1155/2010/131895. Epub 2010 Oct 19. PMID: 20981156; PMCID: PMC2963119.
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Substrate spectra of nucleoside phosphorylases and their potential in the production of pharmaceutically active compounds.

Current pharmaceutical design

Yehia H, Kamel S, Paulick K, Wagner A, Neubauer P.
PMID: 29076414
Curr Pharm Des. 2017 Oct 24; doi: 10.2174/1381612823666171024155811. Epub 2017 Oct 24.

BACKGROUND: Nucleoside phosphorylases catalyze the reversible phosphorolysis of pyrimidine and purine nucleosides in the presence of phosphate. They are relevant to the appropriate function of the immune system in mammals and interesting drug targets for cancer treatment. Next to...

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Yehia H, Kamel S, Paulick K, et al. Substrate spectra of nucleoside phosphorylases and their potential in the production of pharmaceutically active compounds. Curr Pharm Des. 2017;doi: 10.2174/1381612823666171024155811.
Yehia, H., Kamel, S., Paulick, K., Wagner, A., & Neubauer, P. (2017). Substrate spectra of nucleoside phosphorylases and their potential in the production of pharmaceutically active compounds. Current pharmaceutical design, . https://doi.org/10.2174/1381612823666171024155811
Yehia, Heba, et al. "Substrate spectra of nucleoside phosphorylases and their potential in the production of pharmaceutically active compounds." Current pharmaceutical design vol. (2017). doi: https://doi.org/10.2174/1381612823666171024155811
Yehia H, Kamel S, Paulick K, Wagner A, Neubauer P. Substrate spectra of nucleoside phosphorylases and their potential in the production of pharmaceutically active compounds. Curr Pharm Des. 2017 Oct 24; doi: 10.2174/1381612823666171024155811. Epub 2017 Oct 24. PMID: 29076414.
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Use of E. coli Purine Nucleoside Phosphorylase in the Treatment of Solid Tumors.

Current pharmaceutical design

Parker WB, Sorscher EJ.
PMID: 29119917
Curr Pharm Des. 2017 Nov 08; doi: 10.2174/1381612823666171109101851. Epub 2017 Nov 08.

BACKGROUND: The selective expression of non-human genes in tumor tissue to activate non-toxic compounds (Gene Directed Prodrug Enzyme Therapy, GDEPT) is a novel strategy designed for killing tumor cells in patients with little or no systemic toxicity. Numerous non-human...

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Parker WB, Sorscher EJ. Use of E. coli Purine Nucleoside Phosphorylase in the Treatment of Solid Tumors. Curr Pharm Des. 2017;doi: 10.2174/1381612823666171109101851.
Parker, W. B., & Sorscher, E. J. (2017). Use of E. coli Purine Nucleoside Phosphorylase in the Treatment of Solid Tumors. Current pharmaceutical design, . https://doi.org/10.2174/1381612823666171109101851
Parker, William B, and Sorscher, Eric J. "Use of E. coli Purine Nucleoside Phosphorylase in the Treatment of Solid Tumors." Current pharmaceutical design vol. (2017). doi: https://doi.org/10.2174/1381612823666171109101851
Parker WB, Sorscher EJ. Use of E. coli Purine Nucleoside Phosphorylase in the Treatment of Solid Tumors. Curr Pharm Des. 2017 Nov 08; doi: 10.2174/1381612823666171109101851. Epub 2017 Nov 08. PMID: 29119917; PMCID: PMC6224313.
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A Novel Assay for Phosphoserine Phosphatase Exploiting Serine Acetyltransferase as the Coupling Enzyme.

Life (Basel, Switzerland)

Marchesani F, Zangelmi E, Bruno S, Bettati S, Peracchi A, Campanini B.
PMID: 34073563
Life (Basel). 2021 May 26;11(6). doi: 10.3390/life11060485.

Phosphoserine phosphatase (PSP) catalyzes the final step of de novo L-serine biosynthesis-the hydrolysis of phosphoserine to serine and inorganic phosphate-in humans, bacteria, and plants. In published works, the reaction is typically monitored through the discontinuous malachite green phosphate assay...

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Marchesani F, Zangelmi E, Bruno S, et al. A Novel Assay for Phosphoserine Phosphatase Exploiting Serine Acetyltransferase as the Coupling Enzyme. Life (Basel). 2021;11(6)doi: 10.3390/life11060485.
Marchesani, F., Zangelmi, E., Bruno, S., Bettati, S., Peracchi, A., & Campanini, B. (2021). A Novel Assay for Phosphoserine Phosphatase Exploiting Serine Acetyltransferase as the Coupling Enzyme. Life (Basel, Switzerland), 11(6), . https://doi.org/10.3390/life11060485
Marchesani, Francesco, et al. "A Novel Assay for Phosphoserine Phosphatase Exploiting Serine Acetyltransferase as the Coupling Enzyme." Life (Basel, Switzerland) vol. 11,6 (2021). doi: https://doi.org/10.3390/life11060485
Marchesani F, Zangelmi E, Bruno S, Bettati S, Peracchi A, Campanini B. A Novel Assay for Phosphoserine Phosphatase Exploiting Serine Acetyltransferase as the Coupling Enzyme. Life (Basel). 2021 May 26;11(6). doi: 10.3390/life11060485. PMID: 34073563; PMCID: PMC8229081.
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The comparative analysis of the properties and structures of purine nucleoside phosphorylases from thermophilic bacterium .

Journal of biomolecular structure & dynamics

Timofeev VI, Fateev IV, Kostromina MA, Abramchik YA, Konstantinova ID, Volkov VV, Lykoshin DD, Mikheeva OO, Muravieva TI, Esipov RS, Kuranova IP.
PMID: 33225840
J Biomol Struct Dyn. 2020 Nov 23;1-16. doi: 10.1080/07391102.2020.1848628. Epub 2020 Nov 23.

Two recombinant purine nucleoside phosphorylases from thermophilic bacterium

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Timofeev VI, Fateev IV, Kostromina MA, et al. The comparative analysis of the properties and structures of purine nucleoside phosphorylases from thermophilic bacterium . J Biomol Struct Dyn. 2020;1-16doi: 10.1080/07391102.2020.1848628.
Timofeev, V. I., Fateev, I. V., Kostromina, M. A., Abramchik, Y. A., Konstantinova, I. D., Volkov, V. V., Lykoshin, D. D., Mikheeva, O. O., Muravieva, T. I., Esipov, R. S., & Kuranova, I. P. (2020). The comparative analysis of the properties and structures of purine nucleoside phosphorylases from thermophilic bacterium . Journal of biomolecular structure & dynamics, 1-16. https://doi.org/10.1080/07391102.2020.1848628
Timofeev, Vladimir I, et al. "The comparative analysis of the properties and structures of purine nucleoside phosphorylases from thermophilic bacterium ." Journal of biomolecular structure & dynamics vol. (2020): 1-16. doi: https://doi.org/10.1080/07391102.2020.1848628
Timofeev VI, Fateev IV, Kostromina MA, Abramchik YA, Konstantinova ID, Volkov VV, Lykoshin DD, Mikheeva OO, Muravieva TI, Esipov RS, Kuranova IP. The comparative analysis of the properties and structures of purine nucleoside phosphorylases from thermophilic bacterium . J Biomol Struct Dyn. 2020 Nov 23;1-16. doi: 10.1080/07391102.2020.1848628. Epub 2020 Nov 23. PMID: 33225840.
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Showing 1 to 12 of 74 entries