The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Chemical Compound Review

AMPPNP     [[[[(2R,3S,4R,5R)-5-(6- aminopurin-9-yl)-3...

Synonyms: AMP-PNP, CHEMBL1230989, CHEBI:40749, CHEBI:47785, AC1L1OZK, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of ADENYLYL IMIDODIPHOSPHATE

 

Psychiatry related information on ADENYLYL IMIDODIPHOSPHATE

 

High impact information on ADENYLYL IMIDODIPHOSPHATE

  • The protein was selectively extracted from microtubules using a combination of GTP and AMP-PNP [8].
  • The ATP analog 5'-adenylyl imidodiphosphate (AMP-PNP) inhibits transcription of specific genes by the RNA polymerase II contained in whole cell extracts, not only with promoters that contain A as the first nucleotide of the transcript, but also with those that initiate transcripts with G or U [9].
  • AMP-PNP and the other imidotriphosphates have little effect on purified HeLa cell RNA polymerase II initiation and elongation of transcription [9].
  • We show here, however, that for the folding of malate dehydrogenase and Rubisco there is also an absolute requirement for ATP in the cis ring, as ADP and AMP-PNP are unable to promote folding [10].
  • We have used negative-stain electron microscopy and image analysis to study the structures of microtubules and tubulin sheets decorated with the motor domain (head) of kinesin in three states: in the presence of an unhydrolysable ATP analogue, 5'-adenylylimidodiphosphate (AMP-PNP); without nucleotides; and with adenosine 5'-diphosphate (ADP) [11].
 

Chemical compound and disease context of ADENYLYL IMIDODIPHOSPHATE

 

Biological context of ADENYLYL IMIDODIPHOSPHATE

  • Common features between the ATPase and fast axonal transport include interaction with the cytoskeleton in the presence of AMP-PNP, ready extractability, no Ca2+ dependence and inhibition by EDTA [16].
  • When ATP in the recording pipette was replaced with AMP-PNP, SP still inhibited IM, but no desensitization was observed, indicating that ATP hydrolysis is required for desensitization [17].
  • The release of EDGF activity from ROS membranes would require a phosphorylation mechanism since AMP-PNP, an ATP analogue, is not efficient [18].
  • The beat frequency of the reactivated sperm varied with ATP concentration according to Michaelis-Menten kinetics ("Km" = 0.24 mM; "Vmax" = 44 Hz) and was competitively inhibited by AMP-PNP (Ki" approximately to 8.1 mM) [19].
  • Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24) [20].
 

Anatomical context of ADENYLYL IMIDODIPHOSPHATE

 

Associations of ADENYLYL IMIDODIPHOSPHATE with other chemical compounds

 

Gene context of ADENYLYL IMIDODIPHOSPHATE

  • Using an in vitro assembly assay, purified Sba1(His6) bound to Hsp90 only in the presence of adenosine 5'-O-(3-thiotriphosphate) or adenyl-imidodiphosphate [28].
  • In addition, Dmc1 catalyzes strand assimilation of ssDNA oligonucleotides into homologous supercoiled duplex DNA in a reaction promoted by ATP or the non-hydrolyzable ATP analogue AMP-PNP [29].
  • The H1069C mutant shows normal phosphorylation in the presence of inorganic phosphate; it binds an ATP analogue, beta,gamma-imidoadenosine 5'-triphosphate (AMP-PNP), and copper and undergoes nucleotide-dependent conformational transitions similar to those of the wild-type WNDP [30].
  • In the presence of 1mM ATP or AMP-PNP, oligomeric Aip2p/Dld2p bound to all substrates so far examined, and modified the conformation of actin, DNase I, the mature form of invertase, prepro-alpha-factor, pro-alpha-factor, and mitochondrial superoxide dismutase, as determined by the trypsin susceptibility assay [31].
  • We found that preparations of 10 mM AMP-PNP opened phosphorylated CFTR Cl- channels [32].
 

Analytical, diagnostic and therapeutic context of ADENYLYL IMIDODIPHOSPHATE

References

  1. Initiation by RNA polymerase II and formation of runoff transcripts containing unblocked and unmethylated 5' termini. Ernst, H., Filipowicz, W., Shatkin, A.J. Mol. Cell. Biol. (1983) [Pubmed]
  2. Slow interaction of 5'-adenylyl-beta,gamma-imidodiphosphate with Escherichia coli DNA gyrase. Evidence for cooperativity in nucleotide binding. Tamura, J.K., Bates, A.D., Gellert, M. J. Biol. Chem. (1992) [Pubmed]
  3. The role of ATP in in vitro vaccinia virus RNA synthesis effects of AMP-PNP and ATP gamma S. Shuman, S., Spencer, E., Furneaux, H., Hurwitz, J. J. Biol. Chem. (1980) [Pubmed]
  4. ATP dependence of vesicular stomatitis virus transcription initiation and modulation by mutation in the nucleocapsid protein. Perrault, J., McLear, P.W. J. Virol. (1984) [Pubmed]
  5. The identification, purification, and characterization of a pancreatic beta-cell form of the microtubule adenosine triphosphatase kinesin. Balczon, R., Overstreet, K.A., Zinkowski, R.P., Haynes, A., Appel, M. Endocrinology (1992) [Pubmed]
  6. Membrane/microtubule tip attachment complexes (TACs) allow the assembly dynamics of plus ends to push and pull membranes into tubulovesicular networks in interphase Xenopus egg extracts. Waterman-Storer, C.M., Gregory, J., Parsons, S.F., Salmon, E.D. J. Cell Biol. (1995) [Pubmed]
  7. Ligand binding to (Na,K)-ATPase labeled with 5-iodoacetamidofluorescein. Kapakos, J.G., Steinberg, M. J. Biol. Chem. (1986) [Pubmed]
  8. Identification of dynamin, a novel mechanochemical enzyme that mediates interactions between microtubules. Shpetner, H.S., Vallee, R.B. Cell (1989) [Pubmed]
  9. Mechanism of RNA polymerase II--specific initiation of transcription in vitro: ATP requirement and uncapped runoff transcripts. Bunick, D., Zandomeni, R., Ackerman, S., Weinmann, R. Cell (1982) [Pubmed]
  10. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Rye, H.S., Burston, S.G., Fenton, W.A., Beechem, J.M., Xu, Z., Sigler, P.B., Horwich, A.L. Nature (1997) [Pubmed]
  11. Nucleotide-dependent angular change in kinesin motor domain bound to tubulin. Hirose, K., Lockhart, A., Cross, R.A., Amos, L.A. Nature (1995) [Pubmed]
  12. Crystal structures of Escherichia coli topoisomerase IV ParE subunit (24 and 43 kilodaltons): a single residue dictates differences in novobiocin potency against topoisomerase IV and DNA gyrase. Bellon, S., Parsons, J.D., Wei, Y., Hayakawa, K., Swenson, L.L., Charifson, P.S., Lippke, J.A., Aldape, R., Gross, C.H. Antimicrob. Agents Chemother. (2004) [Pubmed]
  13. Thermodynamics of active-site ligand binding to Escherichia coli glutamine synthetase. Ginsburg, A., Gorman, E.G., Neece, S.H., Blackburn, M.B. Biochemistry (1987) [Pubmed]
  14. Endothelin-1 (ET)-induced mobilization of intracellular Ca2+ stores from the smooth muscle facilitates sympathetic cotransmission by potentiation of adenosine 5'-triphosphate (ATP) motor activity: studies in the rat vas deferens. Donoso, M.V., Montes, C.G., Lewin, J., Fournier, A., Calixto, J.B., Huidobro-Toro, J.P. Peptides (1992) [Pubmed]
  15. Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium Thermotoga maritima. Auerbach, G., Jacob, U., Grättinger, M., Schurig, H., Jaenicke, R. Biol. Chem. (1997) [Pubmed]
  16. A novel brain ATPase with properties expected for the fast axonal transport motor. Brady, S.T. Nature (1985) [Pubmed]
  17. Desensitization of the inhibition of the M-current in sympathetic neurons: effects of ATP analogs, polyanions, and multiple agonist applications. Simmons, M.A., Becker, J.B., Mather, R.J. Neuron (1990) [Pubmed]
  18. Regulation of eye derived growth factor binding to membranes by light, ATP or GTP in photoreceptor outer segments. Plouët, J., Mascarelli, F., Loret, M.D., Faure, J.P., Courtois, Y. EMBO J. (1988) [Pubmed]
  19. Effects of adenylyl imidodiphosphate, a nonhydrolyzable adenosine triphosphate analog, on reactivated and rigor wave sea urchin sperm. Penningroth, S.M., Witman, G.B. J. Cell Biol. (1978) [Pubmed]
  20. Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24). Bossemeyer, D., Engh, R.A., Kinzel, V., Ponstingl, H., Huber, R. EMBO J. (1993) [Pubmed]
  21. Attachment of transported vesicles to microtubules in axoplasm is facilitated by AMP-PNP. Lasek, R.J., Brady, S.T. Nature (1985) [Pubmed]
  22. Pitfalls in the use of lead nitrate for the histochemical demonstration of adenylate cyclase activity. Lemay, A., Jarett, L. J. Cell Biol. (1975) [Pubmed]
  23. Uptake of calcium by the endoplasmic reticulum of the frog photoreceptor. Ungar, F., Piscopo, I., Letizia, J., Holtzman, E. J. Cell Biol. (1984) [Pubmed]
  24. Evidence for a direct, nucleotide-sensitive interaction between actin and liver cell membranes. Tranter, M.P., Sugrue, S.P., Schwartz, M.A. J. Cell Biol. (1989) [Pubmed]
  25. Organelle, bead, and microtubule translocations promoted by soluble factors from the squid giant axon. Vale, R.D., Schnapp, B.J., Reese, T.S., Sheetz, M.P. Cell (1985) [Pubmed]
  26. Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23. Young, J.C., Hartl, F.U. EMBO J. (2000) [Pubmed]
  27. How azide inhibits ATP hydrolysis by the F-ATPases. Bowler, M.W., Montgomery, M.G., Leslie, A.G., Walker, J.E. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  28. SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins. Fang, Y., Fliss, A.E., Rao, J., Caplan, A.J. Mol. Cell. Biol. (1998) [Pubmed]
  29. Saccharomyces cerevisiae Dmc1 protein promotes renaturation of single-strand DNA (ssDNA) and assimilation of ssDNA into homologous super-coiled duplex DNA. Hong, E.L., Shinohara, A., Bishop, D.K. J. Biol. Chem. (2001) [Pubmed]
  30. The role of the invariant His-1069 in folding and function of the Wilson's disease protein, the human copper-transporting ATPase ATP7B. Tsivkovskii, R., Efremov, R.G., Lutsenko, S. J. Biol. Chem. (2003) [Pubmed]
  31. Oligomeric Aip2p/Dld2p modifies the protein conformation of both properly folded and misfolded substrates in vitro. Hachiya, N.S., Sakasegawa, Y., Sasaki, H., Jozuka, A., Tsukita, S., Kaneko, K. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  32. 5'-Adenylylimidodiphosphate does not activate CFTR chloride channels in cell-free patches of membrane. Carson, M.R., Welsh, M.J. Am. J. Physiol. (1993) [Pubmed]
  33. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Roseman, A.M., Chen, S., White, H., Braig, K., Saibil, H.R. Cell (1996) [Pubmed]
  34. The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome. Rohrwild, M., Pfeifer, G., Santarius, U., Müller, S.A., Huang, H.C., Engel, A., Baumeister, W., Goldberg, A.L. Nat. Struct. Biol. (1997) [Pubmed]
  35. Characterization of the microtubule movement produced by sea urchin egg kinesin. Porter, M.E., Scholey, J.M., Stemple, D.L., Vigers, G.P., Vale, R.D., Sheetz, M.P., McIntosh, J.R. J. Biol. Chem. (1987) [Pubmed]
  36. Characterization of mitotic motors by their relative sensitivity to AMP-PNP. Lee, G.M. J. Cell. Sci. (1989) [Pubmed]
  37. Characterization of the ATP-binding domain of the sarco(endo)plasmic reticulum Ca(2+)-ATPase: probing nucleotide binding by multidimensional NMR. Abu-Abed, M., Mal, T.K., Kainosho, M., MacLennan, D.H., Ikura, M. Biochemistry (2002) [Pubmed]
 
WikiGenes - Universities