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Artículos de revistas sobre el tema "Analogues biomimétiques de nicotinamide"

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Publicado: 25 de mayo de 2024

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1

Lipka, Pawel, Andrzej Zatorski, Kyoichi A. Watanabe y Krzysztof W. Pankeiwicz. "Synthesis of Methylene-Bridged Analogues of Nicotinamide Riboside, Nicotinamide Mononucleotide and Nicotinamide Adenine Dinucleotide". Nucleosides and Nucleotides 15, n.º 1-3 (enero de 1996): 149–67. http://dx.doi.org/10.1080/07328319608002377.

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2

Pankiewicz, Krzysztof W., Marek M. Kabat, Elzbieta Sochacka, Lech Ciszewski, Joanna Zeidler y Kyoichi A. Watanabe. "C-Nucleoside Analogues of Nicotinamide Mononucleotide (NMN)". Nucleosides and Nucleotides 7, n.º 5-6 (octubre de 1988): 589–93. http://dx.doi.org/10.1080/07328318808056291.

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3

Campbell, P. I., M. I. Abraham y S. A. Kempson. "Increased cAMP in proximal tubules is acute effect of nicotinamide analogues". American Journal of Physiology-Renal Physiology 257, n.º 6 (1 de diciembre de 1989): F1021—F1026. http://dx.doi.org/10.1152/ajprenal.1989.257.6.f1021.

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The possible role of adenosine 3',5'-cyclic monophosphate (cAMP) in the mechanism of the acute inhibitory effects of nicotinamide and analogues on brush-border membrane (BBM) phosphate transport was investigated. Compared with basal values, cAMP content of rat renal proximal tubule suspensions was elevated two- to fivefold when incubated at 37 degrees C for 1 h with nicotinamide, 5-methylnicotinamide, or picolinamide at 1–3 mM and in the presence of a phosphodiesterase inhibitor. Thymidine had no effect on cAMP content. There was significant and specific inhibition of BBM transport of phosphate when proximal tubules were incubated with either nicotinamide or picolinamide at concentrations that increased tubule cAMP content. Thymidine had no effect on BBM transport of phosphate. These findings were independent of the dietary Pi intake of the rats. The absence of any effect of thymidine on phosphate transport strongly suggests that inhibition of poly(adenosine diphosphate ribose) polymerase does not play a role in nicotinamide action on phosphate transport. The change in phosphate transport induced by nicotinamide occurred with no change in NAD content. These findings indicate that an increase in cAMP, rather than NAD, is the important change that may mediate the acute inhibition of Na(+)-dependent phosphate transport by nicotinamide.
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4

Pankiewicz, K. W., A. Zatorski y K. A. Watanabe. "NAD-analogues as potential anticancer agents: conformational restrictions as basis for selectivity." Acta Biochimica Polonica 43, n.º 1 (31 de marzo de 1996): 183–93. http://dx.doi.org/10.18388/abp.1996_4552.

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Cofactor type inhibitors (NAD-analogues) of IMP-dehydrogenase (IMPDH) were synthesized and their application as potential anticancer agents are discussed. C-nucleoside isosteres of NAD, C-NAD and C-PAD, showed an effective competitive inhibition of IMPDH, C-NAD but not C-PAD caused extremely potent inhibition of alcohol dehydrogenase. We also synthesized compounds in which nicotinamide riboside was replaced with tiazofurin (TAD-analogues) and the 2' and 3'-positions of adenosine part were fluorinated. The ribose ring of 2'-deoxy-2'-fluoroadenosine is in the C3'-endo conformation whereas 3'-deoxy-3'-fluoroadenosine favors the C2'-endo sugar pucker. These derivatives are good inhibitors of IMPDH type II, the isoenzyme dominant in neoplastic cells. In contrast, all these analogues showed rather week inhibitory activity against alcohol dehydrogenase. Nicotinamide riboside derivatives in which the base and the sugar are linked through an oxygen or a methylene bridge were synthesized. NAD-analogues containing such conformationally restricted nicotinamide nucleoside moiety (syn or anti) are expected to be selective inhibitors of B-specific (IMPDH) or A-specific dehydrogenases, respectively.
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5

Goulioukina, Natasha, Johny Wehbe, Damien Marchand, Roger Busson, Eveline Lescrinier, Dieter Heindl y Piet Herdewijn. "Synthesis of Nicotinamide Adenine Dinucleotide (NAD) Analogues with a Sugar Modified Nicotinamide Moiety". Helvetica Chimica Acta 90, n.º 7 (julio de 2007): 1266–78. http://dx.doi.org/10.1002/hlca.200790127.

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6

Migaud, Marie, Philip Redpath, Jolanta Haluszczak y Simon Macdonald. "Nicotinamide Benzimidazolide Dinucleotides, Non-Cyclisable Analogues of NAD+". Synlett 25, n.º 16 (26 de agosto de 2014): 2331–36. http://dx.doi.org/10.1055/s-0034-1379000.

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7

Hocková, Dana y Antonín Holý. "Synthesis of Some "Abbreviated" NAD+ Analogues". Collection of Czechoslovak Chemical Communications 62, n.º 6 (1997): 948–56. http://dx.doi.org/10.1135/cccc19970948.

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Four new "abbreviated" NAD+ analogues with hydroxymethyl or carboxyl function as a substituent of an aliphatic chain linking the adenine and nicotinamide moieties were prepared using the Zincke reaction as the key step. As intermediates several new acyclic nucleoside analogues containing hydroxy, carboxyl, azido and amino group were prepared.
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8

Kongmuang, Somlak. "Hydrotropic Solubilization of Riboflavin by Urea, Nicotinamide and Nicotinamide Analogues in Aqueous Systems(การละลายในนํ้าฃองไรโบฟลาวินโดยสารไฮโดรโทรปิค: ยูเ..." Thai Journal of Pharmaceutical Sciences 26, n.º 1 (1 de enero de 2002): 61–68. http://dx.doi.org/10.56808/3027-7922.2288.

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9

Röllig, Robert, Caroline E. Paul, Magalie Claeys-Bruno, Katia Duquesne, Selin Kara y Véronique Alphand. "Divorce in the two-component BVMO family: the single oxygenase for enantioselective chemo-enzymatic Baeyer–Villiger oxidations". Organic & Biomolecular Chemistry 19, n.º 15 (2021): 3441–50. http://dx.doi.org/10.1039/d1ob00015b.

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10

Pankiewicz, Krzysztof, Kyoichi Watanabe, Krystyna Lesiak-Watanabe, Barry Goldstein y Hiremagalur Jayaram. "The Chemistry of Nicotinamide Adenine Dinucleotide (NAD) Analogues Containing C-Nucleosides Related to Nicotinamide Riboside [1]". Current Medicinal Chemistry 9, n.º 7 (1 de abril de 2002): 733–41. http://dx.doi.org/10.2174/0929867024606920.

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11

Petrelli, Riccardo, Yuk Yin Sham, Liqiang Chen, Krzysztof Felczak, Eric Bennett, Daniel Wilson, Courtney Aldrich et al. "Selective inhibition of nicotinamide adenine dinucleotide kinases by dinucleoside disulfide mimics of nicotinamide adenine dinucleotide analogues". Bioorganic & Medicinal Chemistry 17, n.º 15 (agosto de 2009): 5656–64. http://dx.doi.org/10.1016/j.bmc.2009.06.013.

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12

Hocková, Dana, Milena Masojídková y Antonín Holý. ""Abbreviated" NAD+ Analogues Containinga Phosphonate Function". Collection of Czechoslovak Chemical Communications 61, n.º 10 (1996): 1538–48. http://dx.doi.org/10.1135/cccc19961538.

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"Abbreviated" NAD+ analogues with anionic phosphonate function as a part of the link between the adenine and nicotinamide moieties, 9-(2-phosphonomethoxyethyl)adenine 2-(3-carbamoylpyridinium)ethyl ester (1a), (R)- and (S)-9-(2-phosphonomethoxypropyl)adenine 2-(3-carbamoylpyridinium)ethyl ester (1b and 1c), (RS)-9-(3-hydroxy-2-phosphonomethoxypropyl)adenine 2-(3-carbamoylpyridinium)ethyl ester (1d), and (S)- and (R)-1-[3-(adenin-9-yl)-2-phosphonatomethoxypropyl]-3-carbamoylpyridinium (2a and 2b), were prepared by multistep syntheses using the Zincke reaction in the last step.
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13

Sicsic, Sames, Mohamed Ikbal y François Le Goffic. "Chemoenzymatic approach to carbocyclic analogues of ribonucleosides and nicotinamide ribose." Tetrahedron Letters 28, n.º 17 (enero de 1987): 1887–88. http://dx.doi.org/10.1016/s0040-4039(00)96001-5.

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14

Tanimori, Shinji, Takeshi Ohta y Mitsunori Kirihata. "An efficient chemical synthesis of nicotinamide riboside (NAR) and analogues". Bioorganic & Medicinal Chemistry Letters 12, n.º 8 (abril de 2002): 1135–37. http://dx.doi.org/10.1016/s0960-894x(02)00125-7.

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15

Paul, Caroline E., Isabel W. C. E. Arends y Frank Hollmann. "Is Simpler Better? Synthetic Nicotinamide Cofactor Analogues for Redox Chemistry". ACS Catalysis 4, n.º 3 (5 de febrero de 2014): 788–97. http://dx.doi.org/10.1021/cs4011056.

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16

Pankiewicz, K. W., K. Malinowski, H. N. Jayaram, K. Lesiak­ Watanabe y K. A. Watanabe. "Novel Mycophenolic Adenine Bis{phosphonate)s as Potential Immunosuppressants". Current Medicinal Chemistry 6, n.º 7 (julio de 1999): 629–34. http://dx.doi.org/10.2174/092986730607220401124820.

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Abstracts: Mycophenolic acid (MPA) is the most potent and specific inhibitor of inosine monophosphate dehydrogenase (IMPDH). This compound was reported to bind the NAD site of IMPDH and mimic the binding of nicotinamide moiety of nicotinamide adenine dinucleotide. We linked MPA derivatives with the adenine moiety of NAD through a methylenebis(phosphonate) bridge to form novel mycophenolic adenine dinucleotides (MADs) which resemble well the intact natural cofactor. The MAD analogues differ by the length of the side chain (linker) between the aromatic ring of mycophenolic derivative and the -phosphorus atom of the adenosine bis(phosphonate) moiety. Regardless of the linker size, MADs were found to be potent inhibitors of human IMPDH type I and type II with Ki's = 0.25-0.52 f..LM, an order of magnitude less potent than MPA itself (Ki = 0.01-0.04 f..LM). The growth of K562 cells was inhibited by MPA (IC50 = 0.3 f..LM) and the MAD analogues (IC50 = 0.1-1.5 f..LM) with a similar potency. Accordingly, a suppression of alloantigen-induced proliferation of human lymphocytes by the MAD analogues at concentration of 10-20 f..LM was equally effective as that observed for MPA. In contrast to MPA, MAD analogues were found to be resistant to glucuronidation in vitro. Since therapeutic potential of MPA is limited by its undesirable glucuronidation, the glucuronidation-resistant MAD analogues may be superior immunosuppressants if they are not glucuronidated in vivo.
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17

Makarov, Mikhail V. y Marie E. Migaud. "Syntheses and chemical properties of β-nicotinamide riboside and its analogues and derivatives". Beilstein Journal of Organic Chemistry 15 (13 de febrero de 2019): 401–30. http://dx.doi.org/10.3762/bjoc.15.36.

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The β-anomeric form of nicotinamide riboside (NR+) is a precursor for nicotinamide adenine dinucleotide (NAD+), a redox cofactor playing a critical role in cell metabolism. Recently, it has been demonstrated that its chloride salt (NR+Cl−) has beneficial effects, and now NR+Cl−is available as a dietary supplement. Syntheses and studies of analogues and derivatives of NR+are of high importance to unravel the role of NR+in biochemical processes in living cells and to elaborate the next generation of NR+derivatives and conjugates with the view of developing novel drug and food supplement candidates. This review provides an overview of the synthetic approaches, the chemical properties, and the structural and functional modifications which have been undertaken on the nicotinoyl riboside scaffold.
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18

Arora, Mandeep Kumar, Parul Grover, Syed Mohammed Basheeruddin Asdaq, Lovekesh Mehta, Ritu Tomar, Mohd Imran, Anuj Pathak et al. "Potential role of nicotinamide analogues against SARS-COV-2 target proteins". Saudi Journal of Biological Sciences 28, n.º 12 (diciembre de 2021): 7567–74. http://dx.doi.org/10.1016/j.sjbs.2021.09.072.

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19

Larocque, Elizabeth, Elizabeth Fei Yin Chu, Nimmashetti Naganna y Herman O. Sintim. "Nicotinamide–Ponatinib Analogues as Potent Anti-CML and Anti-AML Compounds". ACS Omega 5, n.º 6 (4 de febrero de 2020): 2690–98. http://dx.doi.org/10.1021/acsomega.9b03223.

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20

Nashawi, Asma A. y Richard Hartley. "New Vitamin E Analogues". Journal of King Abdulaziz University - Medical Sciences 23, n.º 4 (31 de diciembre de 2016): 25–42. http://dx.doi.org/10.4197/med.23-4.4.

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Lipid peroxidation is the mediator of several pathophysiological events such atherosclerosis, neurodegenerative disease and others. It is induced by reactive oxygen species that react with biological substrates, leading to cell damage. It is thought that Nicotinamide Adenine Dinucleotide Phosphate Hydrogen oxidases, as well as mitochondria dysfunction and other sources, are at the centre of these events, so it becomes an important therapeutic target. In order to retard this damage and the progression of the disease, the natural and synthetic antioxidant vitamin E (Tocopherol) has been studied extensively. In this study, we briefly address current knowledge on the function of vitamin E and try to emphasize its antioxidant properties versus its other properties. The purpose of this study is to design and synthesize a new vitamin E analogue that is placed outside cells. The precursor to a new vitamin E analogue bearing two charges is prepared from the reaction of the corresponding (6acetoxy-2,5,7,8- tetramethylchroman-2-yl) acyl chloride compound that was directly treated with an aniline-2,5-disulfonic acid tetrabutylammonium salt. The latter, a newly prepared compound, is considered a target. The new tocopherol analogue of the product was expected to exhibit protection of lipid membrane from the oxidative damage behavior of reactive oxygen species.
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21

Lee, H. J. y G. G. Chang. "Interactions of nicotinamide-adenine dinucleotide phosphate analogues and fragments with pigeon liver malic enzyme. Synergistic effect between the nicotinamide and adenine moieties". Biochemical Journal 245, n.º 2 (15 de julio de 1987): 407–14. http://dx.doi.org/10.1042/bj2450407.

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The structural requirements of the NADP+ molecule as a coenzyme in the oxidative decarboxylation reaction catalysed by pigeon liver malic enzyme were studied by kinetic and fluorimetric analyses with various NADP+ analogues and fragments. The substrate L-malate had little effect on the nucleotide binding. Etheno-NADP+, 3-acetylpyridine-adenine dinucleotide phosphate, and nicotinamide-hypoxanthine dinucleotide phosphate act as alternative coenzymes for the enzyme. Their kinetic parameters were similar to that of NADP+. Thionicotinamide-adenine dinucleotide phosphate, 3-aminopyridine-adenine dinucleotide phosphate, 5′-adenylyl imidodiphosphate, nicotinamide-adenine dinucleotide 3′-phosphate and NAD+ act as inhibitors for the enzyme. The first two were competitive with respect to NADP+ and non-competitive with respect to L-malate; the other inhibitors were non-competitive with NADP+. All NADP+ fragments were inhibitory to the enzyme, with a wide range of affinity, depending on the presence or absence of a 2′-phosphate group. Compounds with this group bind to the enzyme 2-3 orders of magnitude more tightly than those without this group. Only compounds with this group were competitive inhibitors with respect to NADP+. We conclude that the 2′-phosphate group is crucial for the nucleotide binding of this enzyme, whereas the carboxyamide carbonyl group of the nicotinamide moiety is important for the coenzyme activity. There is a strong synergistic effect between the binding of the nicotinamide and adenosine moieties of the nucleotide molecule.
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22

Brown, J. M., M. J. Lemmon, M. R. Horsman y W. W. Lee. "Structure–activity Relationships for Tumour Radiosensitization by Analogues of Nicotinamide and Benzamide". International Journal of Radiation Biology 59, n.º 3 (enero de 1991): 739–48. http://dx.doi.org/10.1080/09553009114550651.

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23

Hargenrader, George N., Ravindra B. Weerasooriya, Stefan Ilic, Jens Niklas, Oleg G. Poluektov y Ksenija D. Glusac. "Photoregeneration of Biomimetic Nicotinamide Adenine Dinucleotide Analogues via a Dye-Sensitized Approach". ACS Applied Energy Materials 2, n.º 1 (26 de noviembre de 2018): 80–91. http://dx.doi.org/10.1021/acsaem.8b01574.

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24

Batoux, Nathalie E., Francesca Paradisi, Paul C. Engel y Marie E. Migaud. "Novel nicotinamide adenine dinucleotide analogues as selective inhibitors of NAD+-dependent enzymes". Tetrahedron 60, n.º 31 (julio de 2004): 6609–17. http://dx.doi.org/10.1016/j.tet.2004.05.091.

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25

Paul, Caroline E., Isabel W. C. E. Arends y Frank Hollmann. "ChemInform Abstract: Is Simpler Better? Synthetic Nicotinamide Cofactor Analogues for Redox Chemistry". ChemInform 45, n.º 18 (17 de abril de 2014): no. http://dx.doi.org/10.1002/chin.201418274.

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26

KROHN, K., H. HEINS y K. WIELCKENS. "ChemInform Abstract: Synthesis and Cytotoxic Activity of C-Glycosidic Nicotinamide Riboside Analogues." ChemInform 23, n.º 23 (22 de agosto de 2010): no. http://dx.doi.org/10.1002/chin.199223265.

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27

Tanimori, Shinji, Takeshi Ohta y Mitsunori Kirihata. "ChemInform Abstract: An Efficient Chemical Synthesis of Nicotinamide Riboside (NAR) and Analogues." ChemInform 33, n.º 33 (20 de mayo de 2010): no. http://dx.doi.org/10.1002/chin.200233231.

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28

Kolbin, A. S., A. A. Kurylev, Yu Ye Balykina, M. A. Proskurin y S. A. Mishinova. "Pharmacoeconomic analysis of insulin aspart+nicotinamide versus insulin aspart in patients with diabetes mellitus". Pharmacoeconomics: theory and practice 9, n.º 4 (15 de diciembre de 2021): 5–11. http://dx.doi.org/10.30809/phe.4.2021.1.

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Glycemic control is a clinical goal in the treatment of diabetes mellitus. Currently available bolus insulin analogues do not follow the physiological pattern of insulin secretion after meals because they are slowly absorbed from the injection site. Insulin aspart+nicotinamide is an ultra-fast acting human insulin analog that can be administered before or after meals and the nicotinamide (vitamin B3) molecule provides optimal glycemic control. Aim. To evaluate clinical and economic efficacy of the drug insulin aspart+nicotinamide in comparison with insulin aspart in patients with diabetes mellitus. Materials and Methods. Clinical and economic analysis was performed in accordance with the standards and recommendations valid in the Russian Federation, the method of cost-effectiveness analysis for the first model population of patients with type 1 diabetes and the method of cost-minimization analysis for the second model population of patients with type 2 diabetes, modeling horizon was 26 weeks. Since the study is conducted from the per- spective of the health care system only direct medical costs were considered, that is, the cost of insulin therapy and the cost of complications treatment (hypoglycemia). During the budget impact analysis, the source of data on the target population was the registry of patients with diabetes mellitus of the Russian Federation. Probabilistic sensitivity analysis was performed to assess the impact of changes in the input parameters of the models. Results. Insulin aspart+nicotinamide has a clinical advantage in the effective- ness of HbA1c reduction in type 1 diabetes population. In patients with type 2 diabetes, the effectiveness of insulin aspart+nicotinamide and insulin aspart is comparable by a similar criterion. Direct medical costs of insulin aspart+nicotinamide are 10.64% lower in comparison with insulin aspart use in type 1 and type 2 diabetes patients’ population. The CER value in type 1 diabetes patient population for insulin aspart is 70% higher compared to insulin aspart+nicotinamide (7,410,353.83 and 4,348,513.94 RUR respectively). Budget impact analysis results are the following: that complete replacement of insulin aspart with insulin aspart+nicotinamide over 3 years is accompanied by a 5.3% reduction of regional drug benefit budget costs. Conclusion. The clinical and economic analysis confirms the economic feasibility of insulin aspart + nicotinamide use
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29

Bezsudnova, Ekaterina Yu, Tatiana E. Petrova, Natalia V. Artemova, Konstantin M. Boyko, Ivan G. Shabalin, Tatiana V. Rakitina, Konstantin M. Polyakov y Vladimir O. Popov. "NADP-Dependent Aldehyde Dehydrogenase from Archaeon Pyrobaculum sp.1860: Structural and Functional Features". Archaea 2016 (2016): 1–14. http://dx.doi.org/10.1155/2016/9127857.

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We present the functional and structural characterization of the first archaeal thermostable NADP-dependent aldehyde dehydrogenase AlDHPyr1147. In vitro, AlDHPyr1147 catalyzes the irreversible oxidation of short aliphatic aldehydes at 60–85°С, and the affinity of AlDHPyr1147 to the NADP+ at 60°С is comparable to that for mesophilic analogues at 25°С. We determined the structures of the apo form of AlDHPyr1147 (3.04 Å resolution), three binary complexes with the coenzyme (1.90, 2.06, and 2.19 Å), and the ternary complex with the coenzyme and isobutyraldehyde as a substrate (2.66 Å). The nicotinamide moiety of the coenzyme is disordered in two binary complexes, while it is ordered in the ternary complex, as well as in the binary complex obtained after additional soaking with the substrate. AlDHPyr1147 structures demonstrate the strengthening of the dimeric contact (as compared with the analogues) and the concerted conformational flexibility of catalytic Cys287 and Glu253, as well as Leu254 and the nicotinamide moiety of the coenzyme. A comparison of the active sites of AlDHPyr1147 and dehydrogenases characterized earlier suggests that proton relay systems, which were previously proposed for dehydrogenases of this family, are blocked in AlDHPyr1147, and the proton release in the latter can occur through the substrate channel.
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30

Chen, Dongxing, Linjie Li, Krystal Diaz, Iredia D. Iyamu, Ravi Yadav, Nicholas Noinaj y Rong Huang. "Novel Propargyl-Linked Bisubstrate Analogues as Tight-Binding Inhibitors for Nicotinamide N-Methyltransferase". Journal of Medicinal Chemistry 62, n.º 23 (14 de noviembre de 2019): 10783–97. http://dx.doi.org/10.1021/acs.jmedchem.9b01255.

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31

WALL, Katherine A., Mariola KLIS, John KORNET, Donna COYLE, Jean-Christophe AMÉ, Myron K. JACOBSON y James T. SLAMA. "Inhibition of the intrinsic NAD+ glycohydrolase activity of CD38 by carbocyclic NAD analogues". Biochemical Journal 335, n.º 3 (1 de noviembre de 1998): 631–36. http://dx.doi.org/10.1042/bj3350631.

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Carba-NAD and pseudocarba-NAD are carbocyclic analogues of NAD+ in which a 2,3-dihydroxycyclopentane methanol replaces the β-d-ribonucleotide ring of the nicotinamide riboside moiety of NAD+ [Slama and Simmons (1988) Biochemistry 27, 183–193]. These carbocyclic NAD+ analogues, related to each other as diastereomers, have been tested as inhibitors of the intrinsic NAD+ glycohydrolase activity of human CD38, dog spleen NAD+ glycohydrolase, mouse CD38 and Aplysia californicacADP-ribose synthetase. Pseudocarba-NAD, the carbocyclic dinucleotide in which l-2,3-dihydroxycyclopentane methanol replaces the d-ribose of the nicotinamide riboside moiety of NAD+, was found to be the more potent inhibitor. Pseudocarba-NAD was shown to inhibit the intrinsic NAD+ glycohydrolase activity of human CD38 competitively, with Ki = 148 µM determined for the recombinant extracellular protein domain and Ki = 180 µM determined for the native protein expressed as a cell-surface enzyme on cultured Jurkat cells. Pseudocarba-NAD was shown to be a non-competitive inhibitor of the purified dog spleen NAD+ glycohydrolase, with Kis = 47 µM and Kii = 198 µM. Neither pseudocarba-NAD nor carba-NAD inhibited mouse CD38 or Aplysia californicacADP-ribose synthetase significantly at concentrations up to 1 mM. The results underscore significant species differences in the sensitivity of these enzymes to inhibition, and indicate that pseudocarba-NAD will be useful as an inhibitor of the enzymic activity of human but not mouse CD38 in studies using cultured cells.
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32

Pankiewicz, Krzysztof W. y Krzysztof Felczak. "From ribavirin to NAD analogues and back to ribavirin in search for anticancer agents". Heterocyclic Communications 21, n.º 5 (1 de octubre de 2015): 249–57. http://dx.doi.org/10.1515/hc-2015-0133.

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AbstractRibavirin, a broad-spectrum antiviral agent is used in the clinic alone or in combination with other antivirals and/or interferons. Numerous structural analogues of ribavirin have been developed, among them tiazofurin, which is inactive against viruses but is a potent anticancer drug. Tiazofurin was found to inhibit nicotinamide adenine dinucleotide (NAD)-dependent inosine monophosphate dehydrogenase (IMPDH) after metabolic conversion into tiazofurin adenine dinucleotide (TAD), which binds well but could not serve as IMPDH cofactor. TAD showed high selectivity against human IMPDH vs. other cellular dehydrogenases. Mycophenolic acid (MPA) was even more specific, binding at the cofactor-binding domain of IMPDH. Ribavirin adenine dinucleotide, however, did not show any significant inhibition at the enzymatic level. We synthesized numerous NAD analogues in which natural nicotinamide riboside was replaced by tiazofurin, MPA moiety, or benzamide riboside, and the adenosine moiety as well as the pyrophosphate linker were broadly modified. Some of these compounds were found to be low nanomolar inhibitors of the enzyme and sub-micromolar inhibitors of cancer cell line proliferation. The best were as potent as tyrosine kinase inhibitor gleevec heralded as a ‘magic bullet’ against chronic myelogenous leukemia. In recent years, ribavirin was rediscovered as a potential anticancer agent against number of tumors including leukemia. It was clearly established that its antitumor activity is related to the inhibition of an oncogene, the eukaryotic translation initiation factor (eIF4E).
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33

Nayak, Yogendra, Venkatachalam Hillemane, Vijay Kumar Daroji, B. S. Jayashree y M. K. Unnikrishnan. "Antidiabetic Activity of Benzopyrone Analogues in Nicotinamide-Streptozotocin Induced Type 2 Diabetes in Rats". Scientific World Journal 2014 (2014): 1–12. http://dx.doi.org/10.1155/2014/854267.

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Benzopyrones are proven antidiabetic drug candidate in diabetic drug discovery. In this view novel synthetic benzopyrone analogues were selected for testing in experimental diabetes. Type 2 diabetes (T2D) was induced in Wistar rats by streptozotocin (60 mg/kg, i.p.) followed by nicotinamide (120 mg/kg i.p.). Rats having fasting blood glucose (FBG) >200 mg/dL, 7 days after T2D-induction, are selected for the study. Test compounds and standard treatment were continued for 15 days. FBG, oral glucose tolerance test (OGTT), and insulin tolerance test (ITT) were determined on 21st day after induction of T2D. Plasma lipids and serum insulin were estimated. Homeostatic model assessment (HOMA-IR) was then calculated from serum insulin. Rats were sacrificed and pancreas was isolated for histopathological observations. Oxidative stress markers were estimated in liver homogenate. Quercetin, a natural product with benzopyrone ring, showed significant hypoglycemic activity comparable to glibenclamide. Treatment with test compounds lowered the FBG and insulin resistance was significant alleviated as determined by OGTT, HOMA-IR, and ITT. There was significant normalisation of liver antioxidant enzymes compared to diabetic rats indicating that all the synthesised benzopyrone analogues are beneficial in reducing oxidative stress and are on par with the standard quercetin and glibenclamide in experimental T2D.
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34

Wang, Lei, Bin Liu, Yuxue Liu, Yue Sun, Wujun Liu, Dayu Yu y Zongbao K. Zhao. "Escherichia coli Strain Designed for Characterizing in Vivo Functions of Nicotinamide Adenine Dinucleotide Analogues". Organic Letters 21, n.º 9 (17 de abril de 2019): 3218–22. http://dx.doi.org/10.1021/acs.orglett.9b00935.

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35

Kam, Bernard L., Olaf Malver, Thomas M. Marschner y Norman J. Oppenheimer. "Pyridine coenzyme analogues. Synthesis and characterization of .alpha.- and .beta.-nicotinamide arabinoside adenine dinucleotides". Biochemistry 26, n.º 12 (16 de junio de 1987): 3453–61. http://dx.doi.org/10.1021/bi00386a031.

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36

SLEATH, P. R., A. L. HANDLON y N. J. OPPENHEIMER. "ChemInform Abstract: Pyridine Coenzyme Analogues. Part 3. Synthesis of Three NAD+ Analogues Containing a 2′-Deoxy-2′-Substituted Nicotinamide Arabinofuranosyl Moiety." ChemInform 22, n.º 41 (22 de agosto de 2010): no. http://dx.doi.org/10.1002/chin.199141250.

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37

ZIEGLER, Mathias, Dierk JORCKE y Manfred SCHWEIGER. "Identification of bovine liver mitochondrial NAD+ glycohydrolase as ADP-ribosyl cyclase". Biochemical Journal 326, n.º 2 (1 de septiembre de 1997): 401–5. http://dx.doi.org/10.1042/bj3260401.

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The present investigation identifies bovine liver mitochondrial NADase (NAD+ glycohydrolase) as a member of the class of bifunctional ADP-ribosyl cyclases/cyclic ADP-ribose hydrolases, known to be potential second messenger enzymes. These enzymes catalyse the synthesis and degradation of cyclic ADP-ribose, a potent intracellular calcium-mobilizing agent. The mitochondrial enzyme utilized the NAD+ analogues nicotinamide guanine dinucleotide (NGD+) and nicotinamide hypoxanthine dinucleotide (NHD+) to form fluorescent cyclic purine nucleoside diphosphoriboses. ADP-ribosyl cyclase activity was also demonstrated using 32P-labelled NAD+ as substrate. The identity of NADase and ADP-ribosyl cyclase was supported by their co-migration in SDS/polyacrylamide gels. Cyclase activity was visualized directly within the gel by detecting the formation of fluorescent cyclic IDP-ribose from NHD+. The enzyme catalysed the hydrolysis of cyclic ADP-ribose to ADP-ribose. Moreover, in the presence of nicotinamide and cyclic ADP-ribose the enzyme synthesized NAD+. Both the ADP-ribosyl cyclase and NADase activities of the enzyme were strongly inhibited by reducing agents. Treatment of the NADase with dithiothreitol caused the apparent inactivation of the enzyme. Subsequent removal of the reducing agent and addition of oxidized glutathione led to a partial recovery of enzymic activity. The results support a model for pro-oxidant-induced calcium release from mitochondria involving cyclic ADP-ribose as a specific messenger, rather than the non-enzymic modification of proteins by ADP-ribose.
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38

Conforti, Irene, Andrea Benzi, Irene Caffa, Santina Bruzzone, Alessio Nencioni y Alberto Marra. "Iminosugar-Based Nicotinamide Phosphoribosyltransferase (NAMPT) Inhibitors as Potential Anti-Pancreatic Cancer Agents". Pharmaceutics 15, n.º 5 (11 de mayo de 2023): 1472. http://dx.doi.org/10.3390/pharmaceutics15051472.

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The nicotinamide phosphoribosyltransferase (NAMPT) is considered a very promising therapeutic target because it is overexpressed in pancreatic cancer. Although many inhibitors have been prepared and tested, clinical trials have shown that NAMPT inhibition may result in severe haematological toxicity. Therefore, the development of conceptually new inhibitors is an important and challenging task. We synthesized ten β-d-iminoribofuranosides bearing various heterocycle-based chains carbon-linked to the anomeric position starting from non-carbohydrate derivatives. They were then submitted to NAMPT inhibition assays, as well as to pancreatic tumor cells viability and intracellular NAD+ depletion evaluation. The biological activity of the compounds was compared to that of the corresponding analogues lacking the carbohydrate unit to assess, for the first time, the contribution of the iminosugar moiety to the properties of these potential antitumor agents.
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39

Felczak, Krzysztof y Krzysztof W. Pankiewicz. "Synthesis of Methylenebis(Phosphonate) Analogues of 2-, 4-, and 6-Pyridones of Nicotinamide Adenine Dinucleotide". Nucleosides, Nucleotides and Nucleic Acids 30, n.º 7-8 (julio de 2011): 512–23. http://dx.doi.org/10.1080/15257770.2011.575909.

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40

OHTA, Tatuya, Syuhei ISHIKURA, Syunichi SHINTANI, Noriyuki USAMI y Akira HARA. "Kinetic alteration of a human dihydrodiol/3α-hydroxysteroid dehydrogenase isoenzyme, AKR1C4, by replacement of histidine-216 with tyrosine or phenylalanine". Biochemical Journal 352, n.º 3 (8 de diciembre de 2000): 685–91. http://dx.doi.org/10.1042/bj3520685.

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Human dihydrodiol dehydrogenase with 3α-hydroxysteroid dehydrogenase activity exists in four forms (AKR1C1Ő1C4) that belong to the aldoŐketo reductase (AKR) family. Recent crystallographic studies on the other proteins in this family have indicated a role for a tyrosine residue (corresponding to position 216 in these isoenzymes) in stacking the nicotinamide ring of the coenzyme. This tyrosine residue is conserved in most AKR family members including AKR1C1Ő1C3, but is replaced with histidine in AKR1C4 and phenylalanine in some AKR members. In the present study we prepared mutant enzymes of AKR1C4 in which His-216 was replaced with tyrosine or phenylalanine. The two mutations decreased 3-fold the Km for NADP+ and differently influenced the Km and kcat for substrates depending on their structures. The kinetic constants for bile acids with a 12α-hydroxy group were decreased 1.5Ő7-fold and those for the other substrates were increased 1.3Ő9-fold. The mutation also yielded different changes in sensitivity to competitive inhibitors such as hexoestrol analogues, 17β-oestradiol, phenolphthalein and flufenamic acid and 3,5,3´,5´-tetraiodothyropropionic acid analogues. Furthermore, the mutation decreased the stimulatory effects of the enzyme activity by sulphobromophthalein, clofibric acid and thyroxine, which increased the Km for the coenzyme and substrate of the mutant enzymes more highly than those of the wild-type enzyme. These results indicate the importance of this histidine residue in creating the cavity of the substrate-binding site of AKR1C4 through the orientation of the nicotinamide ring of the coenzyme, as well as its involvement in the conformational change by binding non-essential activators.
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41

Galloway, T. S. y S. van Heyningen. "Binding of NAD+ by cholera toxin". Biochemical Journal 244, n.º 1 (15 de mayo de 1987): 225–30. http://dx.doi.org/10.1042/bj2440225.

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1. The Km for NAD+ of cholera toxin working as an NAD+ glycohydrolase is 4 mM, and this is increased to about 50 mM in the presence of low-Mr ADP-ribose acceptors. Only molecules having both the adenine and nicotinamide moieties of NAD+ with minor alterations in the nicotinamide ring can be competitive inhibitors of this reaction. 2. This high Km for NAD+ is also reflected in the dissociation constant, Kd, which was determined by a variety of methods. 3. Results from equilibrium dialysis were subject to high error, but showed one binding site and a Kd of about 3 mM. 4. The A1 peptide of the toxin is digested by trypsin, and this digestion is completely prevented by concentrations of NAD+ above 50 mM. Measurement (by densitometric scanning of polyacrylamide-gel electrophoretograms) of the rate of tryptic digestion at different concentrations of NAD+ allowed a more accurate determination of Kd = 4.0 +/- 0.4 mM. Some analogues of NAD+ that are competitive inhibitors of the glycohydrolase reaction also prevented digestion.
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42

Zhang, Liangren, Anna Ka Yee Kwong, Zhenjun Yang, Zhe Chen, Hon Cheung Lee y Lihe Zhang. "Studies on the Synthesis of Nicotinamide Nucleoside and Nucleotide Analogues and Their Inhibitions towards CD38 NADase". HETEROCYCLES 83, n.º 12 (2011): 2837. http://dx.doi.org/10.3987/com-11-12361.

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43

Tanuma, Sei-ichi, Kiyotaka Katsuragi, Takahiro Oyama, Atsushi Yoshimori, Yuri Shibasaki, Yasunobu Asawa, Hiroaki Yamazaki et al. "Structural Basis of Beneficial Design for Effective Nicotinamide Phosphoribosyltransferase Inhibitors". Molecules 25, n.º 16 (10 de agosto de 2020): 3633. http://dx.doi.org/10.3390/molecules25163633.

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Inhibition of nicotinamide phosphoribosyltransferase (NAMPT) is an attractive therapeutic strategy for targeting cancer metabolism. So far, many potent NAMPT inhibitors have been developed and shown to bind to two unique tunnel-shaped cavities existing adjacent to each active site of a NAMPT homodimer. However, cytotoxicities and resistances to NAMPT inhibitors have become apparent. Therefore, there remains an urgent need to develop effective and safe NAMPT inhibitors. Thus, we designed and synthesized two close structural analogues of NAMPT inhibitors, azaindole–piperidine (3a)- and azaindole–piperazine (3b)-motif compounds, which were modified from the well-known NAMPT inhibitor FK866 (1). Notably, 3a displayed considerably stronger enzyme inhibitory activity and cellular potency than did 3b and 1. The main reason for this phenomenon was revealed to be due to apparent electronic repulsion between the replaced nitrogen atom (N1) of piperazine in 3b and the Nδ atom of His191 in NAMPT by our in silico binding mode analyses. Indeed, 3b had a lower binding affinity score than did 3a and 1, although these inhibitors took similar stable chair conformations in the tunnel region. Taken together, these observations indicate that the electrostatic enthalpy potential rather than entropy effects inside the tunnel cavity has a significant impact on the different binding affinity of 3a from that of 3b in the disparate enzymatic and cellular potencies. Thus, it is better to avoid or minimize interactions with His191 in designing further effective NAMPT inhibitors.
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44

Czarnecka, Kamila, Małgorzata Girek, Paweł Kręcisz, Robert Skibiński, Kamil Łątka, Jakub Jończyk, Marek Bajda et al. "Discovery of New Cyclopentaquinoline Analogues as Multifunctional Agents for the Treatment of Alzheimer’s Disease". International Journal of Molecular Sciences 20, n.º 3 (24 de enero de 2019): 498. http://dx.doi.org/10.3390/ijms20030498.

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Here we report the two-step synthesis of 8 new cyclopentaquinoline derivatives as modifications of the tetrahydroacridine structure. Next, the biological assessment of each of them was performed. Based on the obtained results we identified 6-chloro-N-[2-(2,3-dihydro-1H-cyclopenta[b]quinolin-9-ylamino)-hexyl]]-nicotinamide hydrochloride (3e) as the most promising compound with inhibitory potencies against EeAChE and EqBuChE in the low nanomolar level 67 and 153 nM, respectively. Moreover, 3e compound is non-hepatotoxic, able to inhibit amyloid beta aggregation, and shows a mix-type of cholinesterase’s inhibition. The mixed type of inhibition of the compound was confirmed by molecular modeling. Then, yeast three-hybrid (Y3H) technology was used to confirm the known ligand-receptor interactions. New derivatives do not show antioxidant activity (confirmed by the use of two different tests). A pKa assay method was developed to identify the basic physicochemical properties of 3e compound. A LogP assay confirmed that 3e compound fulfills Lipinsky’s rule of five
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45

Galloway, T. S., R. M. Tait y S. van Heyningen. "Photolabelling of cholera toxin by NAD+". Biochemical Journal 242, n.º 3 (15 de marzo de 1987): 927–30. http://dx.doi.org/10.1042/bj2420927.

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When cholera toxin is incubated under u.v. light with NAD+ labelled in either the adenine or the nicotinamide moiety, radioactivity becomes covalently bound to the protein. The reaction is specific for cholera toxin, and is inhibited by excess unlabelled NAD+ or NAD analogues. Only the active A 1 chain of the toxin is labelled. The u.v.-absorption spectrum of the product is very similar to that of NAD+, and shows the same reaction with cyanide. The nature of the product is therefore different from that found when diphtheria toxin is photolabelled [Carroll & Collier (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 3307-3311] in that the yield is lower, but both moieties of the NAD molecule become bound.
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46

Jiang, Jie, Hongjun Kang, Xiaoliang Song, Sichao Huang, Sha Li y Jun Xu. "A Model of Interaction between Nicotinamide Adenine Dinucleotide Phosphate (NADPH) Oxidase and Apocynin Analogues by Docking Method". International Journal of Molecular Sciences 14, n.º 1 (4 de enero de 2013): 807–17. http://dx.doi.org/10.3390/ijms14010807.

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47

Pankiewicz, Krzysztof W. "Novel nicotinamide adenine dinucleotide analogues as potential anticancer agents: Quest for specific inhibition of inosine monophosphate dehydrogenase". Pharmacology & Therapeutics 76, n.º 1-3 (octubre de 1997): 89–100. http://dx.doi.org/10.1016/s0163-7258(97)00092-2.

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48

Whyte, B. J. y W. T. Griffiths. "8-vinyl reduction and chlorophyll a biosynthesis in higher plants". Biochemical Journal 291, n.º 3 (1 de mayo de 1993): 939–44. http://dx.doi.org/10.1042/bj2910939.

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A technique involving solid-phase extractions and polyethylene h.p.l.c. suitable for the routine compositional analysis of the total protochlorophyllide pool of plants is described. The resynthesis kinetics of the individual components of the pool have been studied in briefly illuminated etiolated tissue of wheat (Triticum aestivum) and cucumber (Cucumis sativus) during subsequent redarkening. The data are interpreted in terms of a precursor-product relationship between the di- and mono-vinyl analogues of protochlorophyllide during their reaccumulation in darkness. The interconversion is assumed to be catalysed by an 8-vinyl reductase, which shows greater activity in wheat than in cucumber. Analyses of the redox state of the nicotinamide nucleotide of the pool during the process are compatible with NADPH as the cofactor of the putative reductase.
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49

Chen, Zhe, Anna Ka Yee Kwong, Zhenjun Yang, Liangren Zhang, Hon Cheung Lee y Lihe Zhang. "ChemInform Abstract: Studies of the Synthesis of Nicotinamide Nucleoside and Nucleotide Analogues and Their Inhibitions Towards CD38 NADase." ChemInform 43, n.º 15 (15 de marzo de 2012): no. http://dx.doi.org/10.1002/chin.201215205.

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50

Zhang, Yanmin, Arnaud Chevalier, Omar Khdour, Larisa Soto y Sidney Hecht. "Inhibition of Human Cancer Cell Growth by Analogues of Antimycin A". Planta Medica 83, n.º 18 (8 de junio de 2017): 1377–83. http://dx.doi.org/10.1055/s-0043-112343.

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AbstractIn a recent study, several new derivatives of antimycin A (AMA) were produced by means of a novel transacylation reaction, and these were shown to mediate selective toxicity toward cultured A549 human lung epithelial adenocarcinoma cells, as compared with WI-38 normal human lung fibroblasts. The purpose of our study was to investigate whether the analogues all expressed their cytotoxicity by the same mechanism. This was done by studying the effects of the compounds in several types of cell lines. In comparison with 2-O-methylantimycin, which acts at the locus of Bcl-2, none of the new derivatives exhibited a difference in cytotoxicity toward cells expressing different levels of Bcl-2. In cell lines that over- or underexpress estrogen or Her2 receptors, AMA analogue 2 exhibited Her2 receptor dependency at low concentration. Three compounds (1, 4, and 6) exhibited concentration-dependent increases in reactive oxygen species, with 6 being especially potent. Compounds 5 and 6 diminished mitochondrial membrane potential more potently than AMA, and 1 also displayed enhanced activity relative to 2–4. Interestingly, only 1 and AMA displayed strong inhibition of the respiratory chain, as measured by monitoring NADH (reduced nicotinamide adenine dinucleotide) oxidase. Because four of the analogues have positively charged substituents, two of these (4 and 6) were studied to see whether the observed effects were due to much higher level of accumulation within the mitochondria. Their presence in the mitochondria was not dramatically enhanced. Neither of the two presently characterized mechanisms of cell killing by AMA can fully account for the observed results.
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