39 results on '"Kaminski, Pierre-Alexandre"'
Search Results
2. How cyanophage S-2L rejects adenine and incorporates 2-aminoadenine to saturate hydrogen bonding in its DNA
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Czernecki, Dariusz, Legrand, Pierre, Tekpinar, Mustafa, Rosario, Sandrine, Kaminski, Pierre-Alexandre, and Delarue, Marc
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- 2021
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3. Characterization of a triad of genes in cyanophage S-2L sufficient to replace adenine by 2-aminoadenine in bacterial DNA
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Czernecki, Dariusz, Bonhomme, Frédéric, Kaminski, Pierre-Alexandre, and Delarue, Marc
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- 2021
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4. The natural cytokinin 2OH3MeOBAR induces cell death by a mechanism that is different from that of the “classical” cytokinin ribosides
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Voller, Jiří, Béres, Tibor, Zatloukal, Marek, Kaminski, Pierre Alexandre, Niemann, Percy, Doležal, Karel, Džubák, Petr, Hajdúch, Marián, and Strnad, Miroslav
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- 2017
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5. The c‐di‐ AMP ‐binding protein CbpB modulates the level of ppGpp alarmone in Streptococcus agalactiae
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Covaleda‐Cortés, Giovanni, primary, Mechaly, Ariel, additional, Brissac, Terry, additional, Baehre, Heike, additional, Devaux, Laura, additional, England, Patrick, additional, Raynal, Bertrand, additional, Hoos, Sylviane, additional, Gominet, Myriam, additional, Firon, Arnaud, additional, Trieu‐Cuot, Patrick, additional, and Kaminski, Pierre Alexandre, additional
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- 2023
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6. 6-(Hetero)Arylpurine nucleotides as inhibitors of the oncogenic target DNPH1: Synthesis, structural studies and cytotoxic activities
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Amiable, Claire, Paoletti, Julie, Haouz, Ahmed, Padilla, André, Labesse, Gilles, Kaminski, Pierre-Alexandre, and Pochet, Sylvie
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- 2014
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7. L’alphabet génétique élargi
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Kaminski, Pierre-Alexandre, primary
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- 2022
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8. The CovR regulatory network drives the evolution of Group B Streptococcus virulence
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Mazzuoli, Maria-Vittoria, primary, Daunesse, Maëlle, additional, Varet, Hugo, additional, Rosinski-Chupin, Isabelle, additional, Legendre, Rachel, additional, Sismeiro, Odile, additional, Gominet, Myriam, additional, Kaminski, Pierre Alexandre, additional, Glaser, Philippe, additional, Chica, Claudia, additional, Trieu-Cuot, Patrick, additional, and Firon, Arnaud, additional
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- 2021
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9. A third purine biosynthetic pathway encoded by aminoadenine-based viral DNA genomes
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Sleiman, Dona, primary, Garcia, Pierre Simon, additional, Lagune, Marion, additional, Loc’h, Jerome, additional, Haouz, Ahmed, additional, Taib, Najwa, additional, Röthlisberger, Pascal, additional, Gribaldo, Simonetta, additional, Marlière, Philippe, additional, and Kaminski, Pierre Alexandre, additional
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- 2021
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10. Noncanonical DNA polymerization by aminoadenine-based siphoviruses
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Pezo, Valerie, primary, Jaziri, Faten, additional, Bourguignon, Pierre-Yves, additional, Louis, Dominique, additional, Jacobs-Sera, Deborah, additional, Rozenski, Jef, additional, Pochet, Sylvie, additional, Herdewijn, Piet, additional, Hatfull, Graham F., additional, Kaminski, Pierre-Alexandre, additional, and Marliere, Philippe, additional
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- 2021
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11. L'alphabet génétique élargi: Une déviation explorée par la nature chez une famille de bactériophages.
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Kaminski, Pierre-Alexandre
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- 2022
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12. Genetic and biochemical characterization of Salmonella enterica serovar Typhi deoxyribokinase
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Tourneux, Lise, Bucurenci, Nadia, Saveanu, Cosmin, Kaminski, Pierre Alexandre, Bouzon, Madeleine, Pistotnik, Elisabeth, Namane, Abdelkader, Marliere, Philippe, Barzu, Octavian, Sierra, Ines Li de la, Neuhard, Jan, and Gilles, Anne-Marie
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Bacteriology -- Research ,Salmonella typhosa -- Research ,Genomes -- Research ,Gene expression -- Research ,Biological sciences - Abstract
Research has been conducted on the Salonella enterica serovar Typhi genome. The identification of the gene that encodes deoxyribokinase is discussed.
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- 2000
13. Directed enzyme evolution and selections for catalysis based on product formation
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Jestin, Jean-Luc and Kaminski, Pierre Alexandre
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- 2004
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14. Insights into the structure and assembly of a bacterial cellulose secretion system
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Krasteva, Petya Violinova, Bernal-Bayard, Joaquin, Travier, Laetitia, Martin, Fernando Ariel, Kaminski, Pierre-Alexandre, Karimova, Gouzel, Fronzes, Rémi, Ghigo, Jean-Marc, SITBON, Pascale, Integrative Biology of Emerging Infectious Diseases - - IBEID2010 - ANR-10-LABX-0062 - LABX - VALID, Molecular and Structural Biology of Bacterial Transformation - MOLSTRUCTTRANSFO - - EC:FP7:ERC2012-01-01 - 2016-12-31 - 281149 - VALID, Biologie Structurale de la Sécrétion Bactérienne, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Biologie Structurale des Biofilms (SBB), Département Biochimie, Biophysique et Biologie Structurale (B3S), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Génétique des Biofilms, Institut Pasteur [Paris] (IP), Biologie des Bactéries pathogènes à Gram-positif, Biochimie des Interactions Macromoléculaires / Biochemistry of Macromolecular Interactions, Microbiologie Fondamentale et Pathogénicité (MFP), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Institut Européen de Chimie et Biologie (IECB), Université de Bordeaux (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), This work was supported by the Institut Pasteur, the Institute for Integrative Biology of the Cell (I2BC), the Centre National de la Recherche Scientifique (CNRS), the French Government’s Investissement d’Avenir program: Laboratoire d’Excellence 'Integrative Biology of Emerging Infectious Diseases' (Grant No. ANR-10-LABX-62-IBEID to J.-M.G.), the Fondation pour la Recherche Médicale (Grant No. DEQ20140329508 to J.-M.G.), the European Research Council (Grant MolStructTransfo to R.F.), and the ATIP-Avenir 2016 Program (to P.V.K.). In addition, P.V.K. was the recipient of a post-doctoral 'Roux-Cantarini' fellowship from the Institut Pasteur and J.B.-B. was the recipient of a long-term post-doctoral fellowship from the Federation of European Biochemical Societies (FEBS)., ANR-10-LABX-0062,IBEID,Integrative Biology of Emerging Infectious Diseases(2010), European Project: 281149,EC:FP7:ERC,ERC-2011-StG_20101109,MOLSTRUCTTRANSFO(2012), Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris], Institut Pasteur [Paris], Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), and Microbiologie cellulaire et moléculaire et pathogénicité (MCMP)
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Science ,[SDV]Life Sciences [q-bio] ,DNA Mutational Analysis ,Models, Biological ,Article ,Structure-Activity Relationship ,Bacterial secretion ,Protein Domains ,Escherichia coli ,Electron microscopy ,[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Protein Interaction Maps ,Cellulose ,lcsh:Science ,Bacterial Secretion Systems ,Cyclic GMP ,Bacterial structural biology ,Escherichia coli Proteins ,Membrane Proteins ,biochemical phenomena, metabolism, and nutrition ,Adaptation, Physiological ,Recombinant Proteins ,[SDV] Life Sciences [q-bio] ,Microscopy, Electron ,Biofilms ,lcsh:Q ,Software ,Protein Binding - Abstract
Secreted exopolysaccharides present important determinants for bacterial biofilm formation, survival, and virulence. Cellulose secretion typically requires the concerted action of a c-di-GMP-responsive inner membrane synthase (BcsA), an accessory membrane-anchored protein (BcsB), and several additional Bcs components. Although the BcsAB catalytic duo has been studied in great detail, its interplay with co-expressed subunits remains enigmatic. Here we show that E. coli Bcs proteins partake in a complex protein interaction network. Electron microscopy reveals a stable, megadalton-sized macromolecular assembly, which encompasses most of the inner membrane and cytosolic Bcs components and features a previously unobserved asymmetric architecture. Heterologous reconstitution and mutational analyses point toward a structure–function model, where accessory proteins regulate secretion by affecting both the assembly and stability of the system. Altogether, these results lay the foundation for more comprehensive models of synthase-dependent exopolysaccharide secretion in biofilms and add a sophisticated secretory nanomachine to the diverse bacterial arsenal for virulence and adaptation., Many Gram-negative bacteria secrete exopolysaccharides via functionally homologous synthase-dependent systems. Here the authors use electron microscopy to reveal that biofilm-promoting cellulose in E. coli is secreted by a conserved multi-component secretion system with a megadalton-sized asymmetric architecture.
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- 2017
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15. Cyclic di-AMP regulation of osmotic homeostasis is essential in Group B Streptococcus
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Devaux, Laura, primary, Sleiman, Dona, additional, Mazzuoli, Maria-Vittoria, additional, Gominet, Myriam, additional, Lanotte, Philippe, additional, Trieu-Cuot, Patrick, additional, Kaminski, Pierre-Alexandre, additional, and Firon, Arnaud, additional
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- 2018
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16. Cyclic di-AMP in host–pathogen interactions
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Devaux, Laura, primary, Kaminski, Pierre-Alexandre, additional, Trieu-Cuot, Patrick, additional, and Firon, Arnaud, additional
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- 2018
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17. Lectin-gene expression in pea (Pisum sativum L.) roots
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Buffard, Dominique, Kaminski, Pierre-Alexandre, and Strosberg, A. Donny
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- 1988
18. PbsP, a cell wall-anchored protein that binds plasminogen to promote hematogenous dissemination of Group B Streptococcus
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Buscetta, Marco, Firon, Arnaud, Pietrocola, Giampiero, Biondo, Carmelo, Mancuso, Giuseppe, Midiri, Angelina, Romeo, Letizia, Galbo, Roberta, Venza, Mario, Venza, Isabella, Kaminski, Pierre-Alexandre, Gominet, Myriam, Teti, Giuseppe, Speziale, Pietro, Trieu-Cuot, Patrick, Beninati, Concetta, Biologie des Bactéries pathogènes à Gram-positif, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Elie Metchnikoff Laboratory, University of Messina, University of Pavia, Scylla Biotech [Messina], Ministero dell'Università e della Ricerca Scientifica of Italy - Institut Pasteur, CNRS, French Government's Investissement d'Avenir program, Laboratoire d'Excellence 'Integrative Biology of Emerging Infectious Diseases' . Grant Number: (Grant ANR-10-LABX-62-IBEID) - Fondation pour la Recherche Médicale . Grant Number: (Grant DEQ20130326538), ANR-10-LABX-0062,IBEID,Integrative Biology of Emerging Infectious Diseases(2010), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), and Università degli Studi di Pavia = University of Pavia (UNIPV)
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Virulence ,GBS, SSURE repeat, CC17-strains, plasminogen binding protein ,Endothelial Cells ,Streptococcus ,Plasminogen ,[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology ,GBS ,[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology ,Bacterial Adhesion ,Streptococcus agalactiae ,Mice ,Cell Wall ,[SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases ,Streptococcal Infections ,CC17-strains ,[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN] ,Animals ,Humans ,Amino Acid Sequence ,Fibrinolysin ,plasminogen binding protein ,[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM] ,Adhesins, Bacterial ,Protein Binding ,SSURE repeat - Abstract
International audience; Streptococcus agalactiae (Group B Streptococcus or GBS) is a leading cause of invasive infections in neonates whose virulence is dependent on its ability to interact with cells and host components. We here characterized a surface protein with a critical function in GBS pathophysiology. This adhesin, designated PbsP, possesses two Streptococcal Surface Repeat domains, a methionine and lysine-rich region, and a LPXTG cell wall-anchoring motif. PbsP mediates plasminogen (Plg) binding both in vitro and in vivo and we showed that cell surface-bound Plg can be activated into plasmin by tissue plasminogen activator to increase the bacterial extracellular proteolytic activity. Absence of PbsP results in a decreased bacterial transmigration across brain endothelial cells and impaired virulence in a murine model of infection. PbsP is conserved among the main GBS lineages and is a major plasminogen adhesin in non-CC17 GBS strains. Importantly, immunization of mice with recombinant PbsP confers protective immunity. Our results indicate that GBS have evolved different strategies to recruit Plg which indicates that the ability to acquire cell surface proteolytic activity is essential for the invasiveness of this bacterium.
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- 2016
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19. MP87-08 ROLE OF THE C-MYC TARGET DNPH1, A NEW N-HYDROLASE, IN KIDNEY AND PROSTATE CANCERS
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Danilin, Sabrina, primary, Amiable, Claire, additional, Coquard, Catherine, additional, Kaminski, Pierre-Alexandre, additional, Paoletti, Julie, additional, Rothhut, Sylvie, additional, Hamaidi, Iméne, additional, Béraud, Claire, additional, Lindner, Véronique, additional, Lang, Hervé, additional, Pochet, Sylvie, additional, and Massfelder, Thierry, additional
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- 2017
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20. Group B Streptococcus Degrades Cyclic-di-AMP to Modulate STING-Dependent Type I Interferon Production
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Andrade, Warrison A., primary, Firon, Arnaud, additional, Schmidt, Tobias, additional, Hornung, Veit, additional, Fitzgerald, Katherine A., additional, Kurt-Jones, Evelyn A., additional, Trieu-Cuot, Patrick, additional, Golenbock, Douglas T., additional, and Kaminski, Pierre-Alexandre, additional
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- 2016
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21. Extracellular Nucleotide Catabolism by the Group B Streptococcus Ectonucleotidase NudP Increases Bacterial Survival in Blood
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Firon, Arnaud, primary, Dinis, Marcia, additional, Raynal, Bertrand, additional, Poyart, Claire, additional, Trieu-Cuot, Patrick, additional, and Kaminski, Pierre Alexandre, additional
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- 2014
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22. Correction: N6-Substituted AMPs Inhibit Mammalian Deoxynucleotide N-Hydrolase DNPH1
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Amiable, Claire, primary, Pochet, Sylvie, additional, Padilla, André, additional, Labesse, Gilles, additional, and Kaminski, Pierre Alexandre, additional
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- 2014
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23. CMS : the TriDAS Project Technical Design Report; v.1, the Trigger Systems
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L. Bayatyan, G., Grigorian, N., G. Khachatrian, V., T. Margarian, A., M. Sirunyan, A., Adam, W., Brügger, M., Erö, J., Fierro, M., Friedl, M., Frühwirth, R., Hrubec, J., Jeitler, A., Krammer, M., Pernicka, M., Porth, P., Rohringer, H., Rurua, L., Taurok, A., Walzel, G., Wedenig, R., E. Wulz, C., G. Baryshevsky, V., Fedorov, A., L. Gorodishenin, N., V. Korzhik, M., V. Missevitch, O., Panov, V., Zuyeuski, R., B. Zalessky, V., Ermalitsky, F., Kuchinskii, P., M. Lomako, V., Prosolovich, V., Devroede, O., Goorens, R., Lemonne, J., Tavernier, S., Udo, F., W. K. Van, Doninck, L. Van, Lancker, Bertrand, D., G. De, Lentdecker, Stefanescu, J., Velde C. Van, Der, Vanlaer, P., Favart, D., Govaerts, J., Grégoire, G., Lemaître, V., Ninane, A., Piotrzkowski, K., Aa O. Van, Der, Boulogne, I., Daubie, E., Herquet, P., Beaumont, W., Beckers, T., E. De, Langhe, Moortgat, F., Verbeure, F., Zhukov, V., Abadjiev, K., Anguelov, T., H. Atanasov, I., Damgov, J., Dimitrov, L., Genchev, V., Georgiev, G., Iaydjiev, P., Kounov, B., Penchev, L., Raykov, P., G. Sultanov, G., Vankov, I., Vankov, P., Darmenov, N., Gritskov, A., Jordanov, A., B. Litov, L., Mateev, M., Petev, P., Spassov, V., Tchijov, M., Tsenov, R., V. Velev, G., G. Bian, J., Chen, C., M. Chen, G., N. Guo, Y., T. He, J., H. Jiang, C., N. Jin, B., J. Ke, Z., Li, J., G. Li, W., Nan Li, Xiao, F. Qiu, J., W. Shen, B., Y. Shen, X., Y. Sheng, H., Wang, Y.Y., Sheng Xu, Rong, Yang, M., Yun Zhang, Bing, W. Zhang, J., Q. Zhang, S., Ren Zhao, Wei, Zhao, Z., Ping Zheng, Jian, Y. Zhu, G., S. Zhu, Y., Ban, Y., Cai, J., Erh Chen, Jia, Tao Liu, Hong, Qiu Liu, Song, Qiao Lou, Bin, J. Qian, S., Lin Ye, Yan, An, Q., Bian, Z., Chen, H., F. Gong, Z., Li, Chuan, S. Shri, C., Z. Sun, L., L. Wang, X., M. Wang, Z., Wu, J., Wei Ye, Shu, P. Zhang, Z., Deng, Q., J. Li, P., Z. Shen, D., L. Xue, Z., B. Yuan, H., H. Chang, Y., E. Chen, A., Go, A., Lin, W., Chang, P., W. S. Hou, G., Ueno, K., Godinovic, N., Milin, M., Puljak, I., Soric, I., Stipcevic, M., Tudoric-Ghemo, J., Antunovic, Z., Dzelalija, M., Marasovic, K., Hasan, A., A. Razis, P., Vorvolakos, A., Hall, Alexander, Lippmaa, E., Lippmaa, J., Raidal, M., Subbi, J., A. Aarnio, Pertti, Banzuzi, K., M. Heikkinen, A., V. Heinonen, J., Honkanen, A., Karimäki, Veikko, M. Katajisto, H., Kinnunen, Ritva, M. Lassila-Perini, K., Lefébure, V., Pietarinen, E., Tuominen, E., Tuominiemi, J., Ungaro, D., P. Vanhala, T., Williams, C., Lehti, S., Lindén, T., Äystö, Juha, Julin, R., V. Ruuskanen, P., Kallijarvi, S., Keränen, A., Palmu, L., Remes, K., Suhonen, E., Tuuva, T., Niittylahti, J., Vainio, O., Baek, Y.W., Boget, D., Ditta, J., Drobychev, G., Guillaud, J.P., Maire, M., Mendiburu, J.P., Nédélec, P., Peigneux, J.P., Schneegans, M., Sillou, D., Anfreville, M., Bonamy, P., Bouchand, C., Chipaux, R., Dejardin, M., Denegri, D., X. Gentit, F., Givernaud, A., Kircher, F., Lemoigne, Y., Locci, E., P. Lottin, J., C. Nguyen, M., P. Pansart, J., Payn, A., Rander, J., M. Reymond, J., Rondeaux, F., Rosowsky, A., Roth, P., Verrecchia, P., Badier, J., Bercher, M., Bourotte, J., Busson, Pierre, Chamont, D., Charlot, C., Dobrzynski, L., Gilly, J., Haguenauer, M., Karar, A., B. Kim, G., Kluberg, L., Lecouturier, D., Matricon, P., Milleret, G., Miné, P., Morano, R., Paganini, P., Poilleux, P., Romanteau, T., Albert, A., Berst, J.D., Blaes, R., Brom, J.M., Charles, F., Coffin, J., Didierjean, F., Drouhin, F., Ernenwein, J.-P., Fontaine, J.C., Geist, W., Goerlach, U., Helleboid, J.M., Huss, D., Illinger, C., Juillot, P., Lounis, A., Maazouzi, C., Moreau, S., Riahi, Y., Ripp-Baudot, I., Todorov, T., Vintache, D., Zghiche, A., Ageron, M., Bedjidian, M., Chabanat, E., Combaret, C., Contardo, D., Depasse, P., Drapier, O., Dupanloup, M., El-Mamouni, H., Fay, J., Gascon-Shotkin, S., Giraud, N., Girerd, C., Goyot, M., Haroutunian, R., Ille, B., Lebrun, P., Lethuillier, M., Martin, J.-P., Mathez, H., Mirabito, L., Muanza, G.-S., Perriès, S., Sahuc, P., Smadja, G., Tissot, S., Walder, J.-P., Zach, F., S. Amaglobeli, N., S. Bagaturia, Yu, Glonti, L., G. Kartvelishvili, V., A. Kvatadze, R., Mzhavia, D.A., M. Sakhelashvili, T., G. Shanidze, R., B. Tsamalaidze, Z., Djaoshvili, N., Iashvili, I., I. Kharchilava, A., N. Roinishvili, N., N. Roinishvili, V., Berger, C., Braunschweig, W., Breibach, J., H. Gu, W., Heister, A., Karpinski, W., Kirn, T., König, S., Kukulies, C., Ya Ostapchuk, A., Pandoulas, D., Pierschel, G., Raupach, F., Schael, S., Schmitz, D., Dratzig A. Schultz, Von, Siedling, R., Wallraff, W., Wittmer, B., Banicz, K., Bechstein, S., Böhm, A., Bosseler, K., Faissner, H., S. Fesefeldt, H., Hermann, S., Ivannikov, A., Rein, D., Reithler, H., Szczesny, H., Tonutti, M., Wegner, M., Axer, M., Beissel, F., Commichau, V., Flügge, G., Hangarter, K., Macke, D., Mnich, J., Nowak, A., Petertill, M., Schmitz, P., Schulte, R., Sonnenschein, L., Zander, A., W. Grünewald, M., Hebbeker, T., Höpfner, K., Rosca, A., Bartsch, V., P. Blüm, H., W. De, Boer, Dierlamm, A., Dirkes, G., Drollinger, V., Erdmann, M., Feindt, M., Grigoriev, E., Hartmann, F., Hauler, F., Heiss, A., Müller, T., Roederer, F., J. Simonis, H., Skiba, A., Theel, A., H. Thümmel, W., Weiler, T.J., Weseler, S., K. Resvanis, L., Adzic, P., Barone, M., Bozovic-Jelisavcic, I., K. Fanourakis, G., Geralis, T., Harissopoulos, S., Kokkinias, P., Kyriakis, A., Loukas, D., Markou, A., Markou, C., Mastroyiannopoulos, N., Mousa, J., Siotis, I., Spyropoulou-Stassinaki, M., Staveris-Polykalas, A., G. Tsirigotis, A., Tzamarias, S., Vayaki, A., Zachariadou, K., Zupan, M., Asimidis, A., Evangelou, I., Kokkas, P., Manthos, N., Mitropoulos, O., Prouskas, K., A. Triantis, F., Tzoulis, N., Bagoly, Z., L. Bencze, G., Csilling, Akos, Hajdu, C., Hidas, P., Horváth, Dragos, Ódor, G., Ster, A., Urbàn, L., Vesztergombi, G., Zálán, P., Zsenei, M., Dajkó, G., Fenyvesi, A., Molnár, J., Pálinkás, J., Sohler, D., László Trócsányi, Zoltán, Vamosi, J., Végh, J., Baksay, L., Bondar, T., Juhász, S., Marian, G., Nagy, S., Raics, P., Szabo, J., Szabó, Z., Szegedi, S., Szillási, Z., Sztaricskai, T., Tarjan, P., Zilizi, G., B. Bala, S., Bhatnagar, V., Kaur, M., M. Kohli, J., Singh, J., Borkar, S., Chandratre, V., K. Chaudhury, R., Y. Dixit, M., Ghodgaonkar, M., John, B., K. Kataria, S., K. Mohanty, A., Topkar, A., Aziz, T., Banerjee, S., R. Chendvankar, S., V. Deshpande, P., N. Ganguli, S., Gurtu, A., Katta, S., Maity, M., Mazumdar, K., R. Patil, M., C. Tonwar, S., S. Acharya, B., Bheesette, S., Dugad, S., D. Kalmani, S., R. Krishnaswamy, M., R. Lakkireddi, V., K. Mondal, N., Panyam, N., Vemuri, N., Verma, P., I. Bhardwaj, A., K. Shivpuri, R., K. Verma, V., Abbrescia, M., Colaleo, A., Creanza, D., M. De, Palma, Fiore, L., Iaselli, G., Loddo, F., Maggi, G., Marangelli, B., Menegotto, M., My, S., Natali, S., Nuzzo, S., Pugliese, G., Radicci, V., Ranieri, A., Romano, F., Ruggieri, F., Selvaggi, G., Silvestris, L., Tempesta, P., Zito, G., Benvenuti, A.C., Capiluppi, P., R. Cavallo, F., Cuffiani, M., d'Antone, I., M. 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Smith, R., Spiegel, L., Stuart, D., Suzuki, I., M. Tkaczyk, S., S. Tschirhart, R., Vidal, Roland, Wands, R., Wenzel, H., Whitmore, J., J. Womersley, W., Min Wu, Wei, Yagil, A., A. Yarba, V., R. Adams, M., E. Gerber, C., Papageorgiou, K., Solomon, J., Gobbi, B., Malik, S., Tilden, R., Baumbaugh, B., M. Bishop, J., M. Cason, N., Hildreth, M., J. Karmgard, D., C. Ruchti, R., Warchol, J., Wayne, M., E. Barnes, Virgil, Bolla, G., Bortoletto, Daniela, T. Bujak, A., F. Garfinkel, A., J. Gutay, L., Kopal, M., T. Laasanen, A., Medved, S.A., Pal, I., Rott, C., Roy, Arnaud, Sedov, A., W. Anderson, E., Chakir, H., M. Hauptman, J., Krane, J., Akgun, U., S. Ayan, A., Cooper, A., Fountain, M., Mccliment, E., P. Merlo, J., J. Miller, M., M. Önel, Y., Schmidt, I., A. Barnett, B., Y. Chien, C., Sung Cho, Hyo, Liang, G., Swartz, M., Xie, X., Abdullin, S., Arcelli, S., Baden, D., L. Bard, R., Eno, S., Fong, D., Grassi, T., J. Hadley, N., G. Kellogg, R., Kunori, S., Sharma, A., Skuja, A., Carey, R., S. Hazen, E., T. Kearns, E., Machado, E., Miller, J., Osborne, D., L. Roberts, B., Rohlf, J., Sulak, L.R., D. Sullivan, J., Wu, S., Alverson, G., C. Fenker, H., A. Gaponenko, I., H. Moromisato, J., V. Musienko, Yu, Nicol, S., Paul, T., Reucroft, S., D. Swain, J., Taylor, L., E. Von, Goeler, Yasuda, T., Bauer, G., Friedman, J., Paus, C., Pavlon, S., Rosenson, L., Sumorok, S., Tether, S., Tseng, J., B. Cushman, P., H. Heering, A., J. Kronkvist, I., W. Rusack, R., V. Singovsky, A., Vikas, P., Bhatt, K., Booke, M., M. Cremaldi, L., Kroeger, R.A., Reidy, J., Sanders, D., Summers, D., B. Campbell, W., R. Claes, D., Lundstedt, C., R. Snow, G., Bartz, E., Conway, J., Devlin, T., Doroshenko, J., F. Jacques, P., S. Kalelkar, M., W. Koeth, T., Lath, A., P. Perera, L., Schnetzer, S., V. Somalwar, S., Stone, R., Thomson, G., L. Watts, T., M. Bussat, J., Denes, P., Gupta, V., Mans, J., Marlow, D., A. Piroué, P., P. Stickland, D., Tully, C., Wildish, T., R. Blusk, S., Bodek, A., Budd, H., P. De, Barbaro, Dyshkant, A., Ginther, G., Kruse, M., Ruggiero, D., Sakumoto, W., Slattery, P., Tipton, P., Bylsma, B., S. Durkin, L., Gilmore, J., Gu, J., Herman, D., Kim, C., Larsen, D., Y. Ling, T., J. Rush, C., Sehgal, V., Ferguson, T., Russ, J., K. Terentyev, N., Vogel, H., Vorobev, I., Adams, N., Corcoran, M., Eppley, G., Lamas-Valverde, J., Matveev, M., Miettinen, H., Nussbaum, T., Padley, P., D. Platner, E., Roberts, J., Yepes, P., Akchurin, N., Cranshaw, J., Nagaslaev, V., Papadimitriou, V., F. Sill, A., Wigmans, R., C. Chaney, R., J. Fenyves, Ervin, D. Hammack, H., R. O'Malley, M., J. Suson, D., Vasilev, A., Meyer, H., Mo, L., Nunamaker, T.A., Carlsmith, D., Chumney, P., Dasu, S., Feyzi, F., Jaworski, M., Lackey, J., Loveless, R., Lusin, S., Reeder, D., H. Smith, W., Avezov, A., Belov, M., T. Bisenov, N., A. Gafarov, A., Gasanov, E., Ibragimova, E., Kim, G., N. Koblik, Yu, Rakhmatov, N., Rustamov, I., Shukrullo, I., R. Urkinbaev, A., S. Yuldashev, B., Laboratoire d'Annecy de Physique des Particules (LAPP/Laboratoire d'Annecy-le-Vieux de Physique des Particules), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry])-Centre National de la Recherche Scientifique (CNRS), Laboratoire Leprince-Ringuet (LLR), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-École polytechnique (X)-Centre National de la Recherche Scientifique (CNRS), Institut de Recherches Subatomiques (IReS), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Cancéropôle du Grand Est-Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Institut de Physique Nucléaire de Lyon (IPNL), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), CMS, Laboratoire d'Annecy de Physique des Particules (LAPP), Centre National de la Recherche Scientifique (CNRS)-École polytechnique (X)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3), Centre National de la Recherche Scientifique (CNRS)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry])-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3), and Flores, Sylvie
- Subjects
[PHYS.HEXP] Physics [physics]/High Energy Physics - Experiment [hep-ex] ,[PHYS.PHYS.PHYS-INS-DET] Physics [physics]/Physics [physics]/Instrumentation and Detectors [physics.ins-det] ,[PHYS.HEXP]Physics [physics]/High Energy Physics - Experiment [hep-ex] ,[PHYS.PHYS.PHYS-INS-DET]Physics [physics]/Physics [physics]/Instrumentation and Detectors [physics.ins-det] - Abstract
CMS
- Published
- 2000
24. N6-Substituted AMPs Inhibit Mammalian Deoxynucleotide N-Hydrolase DNPH1
- Author
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Amiable, Claire, primary, Pochet, Sylvie, additional, Padilla, André, additional, Labesse, Gilles, additional, and Kaminski, Pierre Alexandre, additional
- Published
- 2013
- Full Text
- View/download PDF
25. Reversal of the Substrate Specificity of CMP N-Glycosidase to dCMP
- Author
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Sikowitz, Megan D., primary, Cooper, Lisa E., additional, Begley, Tadhg P., additional, Kaminski, Pierre Alexandre, additional, and Ealick, Steven E., additional
- Published
- 2013
- Full Text
- View/download PDF
26. Phosphodeoxyribosyltransferases, Designed Enzymes for Deoxyribonucleotides Synthesis
- Author
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Kaminski, Pierre Alexandre, primary and Labesse, Gilles, additional
- Published
- 2013
- Full Text
- View/download PDF
27. Structure of the oncoprotein Rcl bound to three nucleotide analogues
- Author
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Padilla, André, primary, Amiable, Claire, additional, Pochet, Sylvie, additional, Kaminski, Pierre-Alexandre, additional, and Labesse, Gilles, additional
- Published
- 2013
- Full Text
- View/download PDF
28. Probing the Active Site of the Deoxynucleotide N-Hydrolase Rcl Encoded by the Rat Gene c6orf108
- Author
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Dupouy, Christelle, primary, Zhang, Chi, additional, Padilla, André, additional, Pochet, Sylvie, additional, and Kaminski, Pierre Alexandre, additional
- Published
- 2010
- Full Text
- View/download PDF
29. Phosphorylation of dGMP analogs by vaccinia virus TMP kinase and human GMP kinase
- Author
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Auvynet, Constance, primary, Topalis, Dimitri, additional, Caillat, Christophe, additional, Munier-Lehmann, Hélène, additional, Seclaman, Edward, additional, Balzarini, Jan, additional, Agrofoglio, Luigi André, additional, Kaminski, Pierre Alexandre, additional, Meyer, Philippe, additional, Deville-Bonne, Dominique, additional, and El Amri, Chahrazade, additional
- Published
- 2009
- Full Text
- View/download PDF
30. In Vivo Reshaping the Catalytic Site of Nucleoside 2′-Deoxyribosyltransferase for Dideoxy- and Didehydronucleosides via a Single Amino Acid Substitution
- Author
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Kaminski, Pierre Alexandre, primary, Dacher, Priscilla, additional, Dugué, Laurence, additional, and Pochet, Sylvie, additional
- Published
- 2008
- Full Text
- View/download PDF
31. Structures of Purine 2‘-Deoxyribosyltransferase, Substrate Complexes, and the Ribosylated Enzyme Intermediate at 2.0 Å Resolution,
- Author
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Anand, Ruchi, primary, Kaminski, Pierre Alexandre, additional, and Ealick, Steven E., additional
- Published
- 2004
- Full Text
- View/download PDF
32. Functional Cloning, Heterologous Expression, and Purification of Two Different N-Deoxyribosyltransferases fromLactobacillus helveticus
- Author
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Kaminski, Pierre Alexandre, primary
- Published
- 2002
- Full Text
- View/download PDF
33. Detection of lectin-related sequences in the genome of Sesbania rostrata
- Author
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Kaminski, Pierre Alexandre, primary, Buffard, Dominique, additional, and Strosberg, A.Donny, additional
- Published
- 1986
- Full Text
- View/download PDF
34. N6-Substituted AMPs Inhibit Mammalian Deoxynucleotide N-Hydrolase DNPH1.
- Author
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Amiable, Claire, Pochet, Sylvie, Padilla, André, Labesse, Gilles, and Kaminski, Pierre Alexandre
- Subjects
NUCLEOTIDE sequence ,HYDROLASES ,ANTINEOPLASTIC agents ,CYTOKININS ,BASE pairs ,GROWTH factors - Abstract
The gene dnph1 (or rcl) encodes a hydrolase that cleaves the 2’-deoxyribonucleoside 5’-monophosphate (dNMP) N-glycosidic bond to yield a free nucleobase and 2-deoxyribose 5-phosphate. Recently, the crystal structure of rat DNPH1, a potential target for anti-cancer therapies, suggested that various analogs of AMP may inhibit this enzyme. From this result, we asked whether N
6 -substituted AMPs, and among them, cytotoxic cytokinin riboside 5’-monophosphates, may inhibit DNPH1. Here, we characterized the structural and thermodynamic aspects of the interactions of these various analogs with DNPH1. Our results indicate that DNPH1 is inhibited by cytotoxic cytokinins at concentrations that inhibit cell growth. [ABSTRACT FROM AUTHOR]- Published
- 2013
- Full Text
- View/download PDF
35. Expanding substrate specificity of nucleoside 2-deoxyribosyltransferase
- Author
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Kaminski, Pierre Alexandre, Dugué, Laurence, and Pochet, Sylvie
- Abstract
Nucleoside 2′-deoxyribosyltransferase (NDT) is usedto synthesize unnatural 2′-deoxyribonucleosides, modified mostly on the heterocyclic base. Here we describe a strategy for improving 2,3-dideoxyribosyl(ddR) transfer activity of NDT by combining mutagenesis and in vivo selection in E. coli.
- Published
- 2008
- Full Text
- View/download PDF
36. [A family of bacteriophages uses an expanded genetic alphabet].
- Author
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Kaminski PA
- Subjects
- Base Pairing, DNA chemistry, Humans, Hydrogen Bonding, Thymine, Bacteriophages genetics
- Abstract
Bacteriophage genomes are the richest source of modified nucleobases of any life form. Of these, 2,6-diaminopurine (2-aminoadénine) that pairs with thymine by forming three hydrogen bonds is the only one violating Watson and Crick's base pairing. 2,6-diaminopurine (2-aminoadénine), initially found in the cyanophage S-2L, is more widespread than expected and has also been detected in bacteriophage infecting Gram-negative and Gram-positive bacteria. The biosynthetic pathway for aminoadenine containing DNA as well as the exclusion of adenine are now elucidated. This example of a natural deviation from the DNA canonical nucleotides represents only one of the possibilities explored by nature and provides a proof of concept for the synthetic biology of non-canonical nucleic acids., (© 2022 médecine/sciences – Inserm.)
- Published
- 2022
- Full Text
- View/download PDF
37. PbsP, a cell wall-anchored protein that binds plasminogen to promote hematogenous dissemination of group B Streptococcus.
- Author
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Buscetta M, Firon A, Pietrocola G, Biondo C, Mancuso G, Midiri A, Romeo L, Galbo R, Venza M, Venza I, Kaminski PA, Gominet M, Teti G, Speziale P, Trieu-Cuot P, and Beninati C
- Subjects
- Amino Acid Sequence, Animals, Bacterial Adhesion physiology, Cell Wall metabolism, Endothelial Cells metabolism, Fibrinolysin metabolism, Humans, Mice, Protein Binding, Streptococcal Infections microbiology, Streptococcus metabolism, Streptococcus agalactiae genetics, Streptococcus agalactiae pathogenicity, Virulence, Adhesins, Bacterial metabolism, Plasminogen metabolism, Streptococcus agalactiae metabolism
- Abstract
Streptococcus agalactiae (Group B Streptococcus or GBS) is a leading cause of invasive infections in neonates whose virulence is dependent on its ability to interact with cells and host components. We here characterized a surface protein with a critical function in GBS pathophysiology. This adhesin, designated PbsP, possesses two Streptococcal Surface Repeat domains, a methionine and lysine-rich region, and a LPXTG cell wall-anchoring motif. PbsP mediates plasminogen (Plg) binding both in vitro and in vivo and we showed that cell surface-bound Plg can be activated into plasmin by tissue plasminogen activator to increase the bacterial extracellular proteolytic activity. Absence of PbsP results in a decreased bacterial transmigration across brain endothelial cells and impaired virulence in a murine model of infection. PbsP is conserved among the main GBS lineages and is a major plasminogen adhesin in non-CC17 GBS strains. Importantly, immunization of mice with recombinant PbsP confers protective immunity. Our results indicate that GBS have evolved different strategies to recruit Plg which indicates that the ability to acquire cell surface proteolytic activity is essential for the invasiveness of this bacterium., (© 2016 John Wiley & Sons Ltd.)
- Published
- 2016
- Full Text
- View/download PDF
38. N (6)-substituted AMPs inhibit mammalian deoxynucleotide N-hydrolase DNPH1.
- Author
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Amiable C, Pochet S, Padilla A, Labesse G, and Kaminski PA
- Subjects
- Adenosine Monophosphate analogs & derivatives, Adenosine Monophosphate chemistry, Adenosine Monophosphate metabolism, Amino Acid Sequence, Animals, Catalytic Domain, Enzyme Activation drug effects, Humans, Kinetics, Models, Molecular, Molecular Conformation, Molecular Sequence Data, N-Glycosyl Hydrolases chemistry, N-Glycosyl Hydrolases genetics, Nuclear Proteins chemistry, Nuclear Proteins genetics, Protein Binding, Proto-Oncogene Proteins chemistry, Proto-Oncogene Proteins genetics, Rats, Sequence Alignment, Thermodynamics, Adenosine Monophosphate pharmacology, N-Glycosyl Hydrolases metabolism, Nuclear Proteins metabolism, Proto-Oncogene Proteins metabolism
- Abstract
The gene dnph1 (or rcl) encodes a hydrolase that cleaves the 2'-deoxyribonucleoside 5'-monophosphate (dNMP) N-glycosidic bond to yield a free nucleobase and 2-deoxyribose 5-phosphate. Recently, the crystal structure of rat DNPH1, a potential target for anti-cancer therapies, suggested that various analogs of AMP may inhibit this enzyme. From this result, we asked whether N (6)-substituted AMPs, and among them, cytotoxic cytokinin riboside 5'-monophosphates, may inhibit DNPH1. Here, we characterized the structural and thermodynamic aspects of the interactions of these various analogs with DNPH1. Our results indicate that DNPH1 is inhibited by cytotoxic cytokinins at concentrations that inhibit cell growth.
- Published
- 2013
- Full Text
- View/download PDF
39. Functional cloning, heterologous expression, and purification of two different N-deoxyribosyltransferases from Lactobacillus helveticus.
- Author
-
Kaminski PA
- Subjects
- Cloning, Molecular, Deoxyguanosine metabolism, Electrophoresis, Polyacrylamide Gel, Escherichia coli genetics, Escherichia coli growth & development, Glucosyltransferases chemistry, Glucosyltransferases isolation & purification, Glucosyltransferases metabolism, Lactobacillus genetics, Mass Spectrometry, Pentosyltransferases chemistry, Pentosyltransferases isolation & purification, Pentosyltransferases metabolism, Selection, Genetic, Substrate Specificity, Glucosyltransferases genetics, Lactobacillus enzymology, Pentosyltransferases genetics
- Abstract
Lactobacillus helveticus contains two types of N-deoxyribosyltransferases: DRTase I catalyzes the transfer of 2'-deoxyribose between purine bases exclusively whereas DRTase II is able to transfer the 2'-deoxyribose between two pyrimidine or between pyrimidine and purine bases. An Escherichia coli strain, auxotrophic for guanine and unable to use deoxyguanosine as source of guanine, was constructed to clone the corresponding genes. By screening a genomic bank for the production of guanine, the L. helveticus ptd and ntd genes coding for DRTase I and II, respectively, were isolated. Although the two genes have no sequence similarity, the two deduced polypeptides display 25.6% identity, with most of the residues involved in substrate binding and the active site nucleophile Glu-98 being conserved. Overexpression and purification of the two proteins shows that DRTase I is specific for purines with a preference for deoxyinosine (dI) > deoxyadenosine > deoxyguanosine as donor substrates whereas DRTase II has a strong preference for pyrimidines as donor substrates and purines as base acceptors. Purine analogues were substrates as acceptor bases for both enzymes. Comparison of DRTase I and DRTase II activities with dI as donor or hypoxanthine as acceptor and colocalization of the ptd and add genes suggest a specific role for DRTase I in the metabolism of dI.
- Published
- 2002
- Full Text
- View/download PDF
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