Toward a unified nomenclature for mammalian ADP-ribosyltransferases.
暂无分享,去创建一个
Bernhard Lüscher | Herwig Schüler | F. Koch-Nolte | B. Lüscher | H. Schüler | M. Hottiger | P. Hassa | Friedrich Koch-Nolte | Michael O Hottiger | Paul O Hassa
[1] E. Phizicky,et al. Analysis of 2'-phosphotransferase (Tpt1p) from Saccharomyces cerevisiae: evidence for a conserved two-step reaction mechanism. , 2005, RNA.
[2] K. Mcmahon,et al. Evidence of endogenous mono-ADP-ribosylation of cardiac proteins via anti-ADP-ribosylarginine immunoreactivity. , 2000, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine.
[3] T. Sugimura,et al. Distribution of cytotoxic and DNA ADP-ribosylating activity in crude extracts from butterflies among the family Pieridae , 2008, Proceedings of the National Academy of Sciences.
[4] T. Sugimura,et al. Polymerization of the adenosine 5'-diphosphate ribose moiety of NAD by rat liver nuclear enzyme. , 1967, Biochimica et biophysica acta.
[5] Daniela Corda,et al. Functional aspects of protein mono‐ADP‐ribosylation , 2003, The EMBO journal.
[6] L. Guarente,et al. Mouse Sir2 Homolog SIRT6 Is a Nuclear ADP-ribosyltransferase* , 2005, Journal of Biological Chemistry.
[7] A. Pautsch,et al. C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins , 2007, Naunyn-Schmiedeberg's Archives of Pharmacology.
[8] F. Schuber,et al. Structure and enzymology of ADP-ribosyl cyclases: conserved enzymes that produce multiple calcium mobilizing metabolites. , 2004, Current molecular medicine.
[9] T. Sugimura,et al. Monoclonal antibodies to poly(adenosine diphosphate ribose) recognize different structures. , 1984, Biochemistry.
[10] A. Schnapp,et al. Functional characterization of the poly(ADP-ribose) polymerase activity of tankyrase 1, a potential regulator of telomere length. , 2002, Journal of molecular biology.
[11] J. Sadoff,et al. Pseudomonas aeruginosa exoenzyme S: an adenosine diphosphate ribosyltransferase distinct from toxin A. , 1978, Proceedings of the National Academy of Sciences of the United States of America.
[12] J. Tainer,et al. Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex , 1999, Nature Structural Biology.
[13] Katharina Dittmar,et al. In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs) , 2005, BMC Genomics.
[14] T. Meyer,et al. Production of anti-(ADP-ribose) antibodies with the aid of a dinucleotide-pyrophosphatase-resistant hapten and their application for the detection of mono(ADP-ribosyl)ated polypeptides. , 1986, European journal of biochemistry.
[15] G. R. Andersen,et al. Stealth and mimicry by deadly bacterial toxins. , 2006, Trends in biochemical sciences.
[16] C. Mueller-Dieckmann,et al. Mammalian ADP-ribosyltransferases and ADP-ribosylhydrolases. , 2008, Frontiers in bioscience : a journal and virtual library.
[17] F. Alt,et al. SIRT4 Inhibits Glutamate Dehydrogenase and Opposes the Effects of Calorie Restriction in Pancreatic β Cells , 2006, Cell.
[18] K. Aktories,et al. Exchange of glutamine-217 to glutamate of Clostridium limosum exoenzyme C3 turns the asparagine-specific ADP-ribosyltransferase into an arginine-modifying enzyme. , 2006, Biochemistry.
[19] D. Nolan,et al. A chromosomal SIR2 homologue with both histone NAD‐dependent ADP‐ribosyltransferase and deacetylase activities is involved in DNA repair in Trypanosoma brucei , 2003, The EMBO journal.
[20] R. Kastelein,et al. Mouse T Cell Membrane Proteins Rt61 and Rt62 Are Arginine/Protein Mono(ADPribosyl)transferases and Share Secondary Structure Motifs with ADP-ribosylating Bacterial Toxins (*) , 1996, The Journal of Biological Chemistry.
[21] M. Ziegler,et al. The power to reduce: pyridine nucleotides--small molecules with a multitude of functions. , 2007, The Biochemical journal.
[22] T. Sugimura,et al. [45] Overview of poly(ADP-ribosyl)ation , 1984 .
[23] Yan Ma,et al. Role of the Dinitrogenase Reductase Arginine 101 Residue in Dinitrogenase Reductase ADP-Ribosyltransferase Binding, NAD Binding, and Cleavage , 2001, Journal of bacteriology.
[24] J. Weigelt,et al. Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3. , 2009, Journal of medicinal chemistry.
[25] James E. Evans,et al. ART2, a T Cell Surface Mono-ADP-ribosyltransferase, Generates Extracellular Poly(ADP-ribose)* , 2006, Journal of Biological Chemistry.
[26] M. Hottiger,et al. Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going? , 2006, Microbiology and Molecular Biology Reviews.
[27] E. Phizicky,et al. A functional homolog of a yeast tRNA splicing enzyme is conserved in higher eukaryotes and in Escherichia coli. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[28] D. Litchfield,et al. Substrate-assisted catalysis by PARP10 limits its activity to mono-ADP-ribosylation. , 2008, Molecular cell.
[29] Robert J Fieldhouse,et al. Needle in the haystack: structure-based toxin discovery. , 2008, Trends in biochemical sciences.
[30] R. Depping,et al. The mono-ADP-ribosyltransferases Alt and ModB of bacteriophage T4: target proteins identified. , 2005, Biochemical and biophysical research communications.
[31] R. Collier,et al. Understanding the mode of action of diphtheria toxin: a perspective on progress during the 20th century. , 2001, Toxicon : official journal of the International Society on Toxinology.
[32] T. Lange,et al. Tankyrase, a poly(ADP-ribose) polymerase at human telomeres. , 1998, Science.
[33] D. Corda,et al. Physiological relevance of the endogenous mono(ADP‐ribosyl)ation of cellular proteins , 2005, The FEBS journal.
[34] C. Brenner,et al. NAD+ metabolism in health and disease. , 2007, Trends in biochemical sciences.
[35] J. Denu. The Sir 2 family of protein deacetylases. , 2005, Current opinion in chemical biology.
[36] M. Malanga,et al. Poly(ADP-ribose) molecules formed during DNA repair in vivo. , 1994, The Journal of biological chemistry.
[37] F. Bazan,et al. ADP-ribosyltransferases: plastic tools for inactivating protein and small molecular weight targets. , 2001, Journal of biotechnology.
[38] A. R. Merrill,et al. The nature and character of the transition state for the ADP‐ribosyltransferase reaction , 2008, EMBO reports.
[39] M. Duraisingh,et al. Plasmodium falciparum Sir2: an Unusual Sirtuin with Dual Histone Deacetylase and ADP-Ribosyltransferase Activity , 2007, Eukaryotic Cell.
[40] Antje Chang,et al. BRENDA, AMENDA and FRENDA the enzyme information system: new content and tools in 2009 , 2008, Nucleic Acids Res..
[41] G. Poirier,et al. Immunodot blot method for the detection of poly(ADP-ribose) synthesized in vitro and in vivo. , 1998, Analytical biochemistry.
[42] V. Kickhoefer,et al. The 193-Kd Vault Protein, Vparp, Is a Novel Poly(Adp-Ribose) Polymerase , 1999, The Journal of cell biology.
[43] K. Acharya,et al. A family of killer toxins , 2006, The FEBS journal.
[44] G. de Murcia,et al. The PARP superfamily , 2004, BioEssays : news and reviews in molecular, cellular and developmental biology.
[45] H. Tsuge,et al. Structural basis of actin recognition and arginine ADP-ribosylation by Clostridium perfringens ι-toxin , 2008, Proceedings of the National Academy of Sciences.
[46] R. Fieldhouse,et al. Cholix Toxin, a Novel ADP-ribosylating Factor from Vibrio cholerae* , 2008, Journal of Biological Chemistry.
[47] Jianjun Sun,et al. How bacterial ADP-ribosylating toxins recognize substrates , 2004, Nature Structural &Molecular Biology.
[48] G. Schulz,et al. The mechanism of the elongation and branching reaction of poly(ADP-ribose) polymerase as derived from crystal structures and mutagenesis. , 1998, Journal of molecular biology.
[49] I. Pastan,et al. The crystal structure of Pseudomonas aeruginosa exotoxin domain III with nicotinamide and AMP: conformational differences with the intact exotoxin. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[50] S. Hoshino,et al. Increase in ADP‐ribosyltransferase activity of rat T lymphocyte alloantigen RT6.1 by a single amino acid mutation , 1996, FEBS letters.
[51] Simon Messner,et al. Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites , 2009, Nucleic acids research.
[52] D. Cassel,et al. Mechanism of cholera toxin action: covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase system. , 1978, Proceedings of the National Academy of Sciences of the United States of America.
[53] F. Koch-Nolte,et al. Premature stop codons inactivate the RT6 genes of the human and chimpanzee species. , 1994, Journal of molecular biology.
[54] J. Vonesch,et al. PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression , 2003, Journal of Cell Science.
[55] N. Hara,et al. Glutamic Acid 207 in Rodent T-cell RT6 Antigens Is Essential for Arginine-specific ADP-ribosylation* , 1996, The Journal of Biological Chemistry.
[56] J. Bazan,et al. Sequence and structural links between distant ADP-ribosyltransferase families. , 1997, Advances in experimental medicine and biology.
[57] R. Braren,et al. The family of toxin‐related ecto‐ADP‐ribosyltransferases in humans and the mouse , 2002, Protein science : a publication of the Protein Society.
[58] J. Moss,et al. ADP-Ribosylarginine Hydrolases and ADP-Ribosyltransferases , 1997 .
[59] A. Zolkiewska. Ecto-ADP-ribose transferases: cell-surface response to local tissue injury. , 2005, Physiology.
[60] R. Rappuoli,et al. Three conserved consensus sequences identify the NAD‐binding site of ADP‐ribosylating enzymes, expressed by eukaryotes, bacteria and T‐even bacteriophages , 1996, Molecular microbiology.
[61] R. Aguiar,et al. B-aggressive Lymphoma Family Proteins Have Unique Domains That Modulate Transcription and Exhibit Poly(ADP-ribose) Polymerase Activity* , 2005, Journal of Biological Chemistry.
[62] C. E. Stebbins,et al. A steric antagonism of actin polymerization by a salmonella virulence protein. , 2006, Structure.
[63] J. Moss,et al. Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositol-linked ADP-ribosyltransferases. , 1994, Biochemistry.
[64] T. Katada,et al. ADP ribosylation of the specific membrane protein of C6 cells by islet-activating protein associated with modification of adenylate cyclase activity. , 1982, The Journal of biological chemistry.
[65] J. Ménissier-de murcia,et al. Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching. , 1997, Biochemistry.
[66] Y. Nishizuka,et al. Studies on the polymer of adenosine diphosphate ribose. I. Enzymic formation from nicotinamide adenine dinuclotide in mammalian nuclei. , 1967, The Journal of biological chemistry.
[67] J. Tainer,et al. The ARTT motif and a unified structural understanding of substrate recognition in ADP-ribosylating bacterial toxins and eukaryotic ADP-ribosyltransferases. , 2002, International journal of medical microbiology : IJMM.
[68] G. Marsischky,et al. Role of Glutamic Acid 988 of Human Poly-ADP-ribose Polymerase in Polymer Formation , 1995, The Journal of Biological Chemistry.
[69] P. Chambon,et al. Nicotinamide mononucleotide activation of new DNA-dependent polyadenylic acid synthesizing nuclear enzyme. , 1963, Biochemical and biophysical research communications.
[70] J. Tainer,et al. Crystal structure and novel recognition motif of rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: structural insights for recognition specificity and catalysis. , 2001, Journal of molecular biology.
[71] B. Zabel,et al. Human nuclear NAD+ ADP-ribosyltransferase: localization of the gene on chromosome 1q41-q42 and expression of an active human enzyme in Escherichia coli. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[72] D. Corda,et al. Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome , 2009, Proceedings of the National Academy of Sciences.
[73] Modification of the ADP-ribosyltransferase and NAD Glycohydrolase Activities of a Mammalian Transferase (ADP-ribosyltransferase 5) by Auto-ADP-ribosylation* , 1999, The Journal of Biological Chemistry.
[74] Emma Griffiths,et al. Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr , 2008, Proceedings of the National Academy of Sciences.
[75] K. Aktories,et al. Bacillus sphaericus mosquitocidal toxin (MTX) and pierisin: the enigmatic offspring from the family of ADP‐ribosyltransferases , 2006, Molecular microbiology.
[76] F. Koch-Nolte,et al. Emerging Roles of NAD+ and Its Metabolites in Cell Signaling , 2009, Science Signaling.
[77] F. Malavasi,et al. Flow cytometric and immunoblot assays for cell surface ADP-ribosylation using a monoclonal antibody specific for ethenoadenosine. , 2003, Analytical biochemistry.
[78] M. Hottiger,et al. The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases. , 2008, Frontiers in bioscience : a journal and virtual library.
[79] D Eisenberg,et al. Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide. , 1996, Biochemistry.