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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
MeSH Review

Prokaryotic Cells

 
 
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Disease relevance of Prokaryotic Cells

 

High impact information on Prokaryotic Cells

  • Membrane adenosine triphosphatases of prokaryotic cells [6].
  • The structural elucidation of clear but distant homologs of actin and tubulin in bacteria and GFP labeling of these proteins promises to reinvigorate the field of prokaryotic cell biology [7].
  • This points to an evolutionary parallel between DNA segregation and cytokinesis in prokaryotic cells, and reveals a potential molecular mechanism for plasmid and chromosome segregation mediated by the ubiquitous ParA-type proteins [8].
  • Still unclear, however, is exactly why most eukaryotic cells, in contrast to prokaryotic cells, express a novel form of hsp 70 (i.e., hsp 72) after experiencing stress [9].
  • Studies of deeply buried, sedimentary microbial communities and associated biogeochemical processes during Ocean Drilling Program Leg 201 showed elevated prokaryotic cell numbers in sediment layers where methane is consumed anaerobically at the expense of sulfate [10].
 

Chemical compound and disease context of Prokaryotic Cells

 

Biological context of Prokaryotic Cells

 

Anatomical context of Prokaryotic Cells

 

Associations of Prokaryotic Cells with chemical compounds

  • Fumarate reductases and succinate dehydrogenases play central roles in the metabolism of eukaryotic and prokaryotic cells [17].
  • In addition to Pi, it is also shown in this report that the synthesis of both PLC-H and PLC-N is induced by compounds which are not only derived from the substrate product of both enzymes, i.e. phosphorylcholine, but are also known osmoprotectants in eukaryotic and prokaryotic cells [18].
  • These results suggest that it may be possible to use an arginine decarboxylase inhibitor in conjunction with known inhibitors of ornithine decarboxylase to block all putrescine biosynthesis in prokaryotic cells and thus to study the effects of such inhibition in these organisms [19].
  • L-Carnitine (R-[-]-3-hydroxy-4-trimethylaminobutyrate) is found in both eukaryotic and prokaryotic cells and participates in diverse processes including long-chain fatty-acid transport and osmoprotection [20].
  • Our results support the hypothesis [Williams, R.J.P. (1982) FEBS Lett. 140, 3-10] that prokaryotic cells may contain a standing pool of free or loosely bound Fe(II) that is capable of acting in a regulatory capacity [21].
 

Gene context of Prokaryotic Cells

References

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  2. Molecular characterization of a family of choline-binding proteins of Clostridium beijerinckii NCIB 8052. Evolution and gene redundancy in prokaryotic cell. Sánchez-Beato, A.R., García, J.L. Gene (1996) [Pubmed]
  3. Diversity of retron elements in a population of rhizobia and other gram-negative bacteria. Rice, S.A., Bieber, J., Chun, J.Y., Stacey, G., Lampson, B.C. J. Bacteriol. (1993) [Pubmed]
  4. Facets of heat shock protein 70 show immunotherapeutic potential. Todryk, S.M., Gough, M.J., Pockley, A.G. Immunology (2003) [Pubmed]
  5. Characterization of the glycoprotein D gene products of equine herpesvirus 1 using a prokaryotic cell expression vector. Love, D.N., Bell, C.W., Whalley, J.M. Vet. Microbiol. (1992) [Pubmed]
  6. Membrane adenosine triphosphatases of prokaryotic cells. Downie, J.A., Gibson, F., Cox, G.B. Annu. Rev. Biochem. (1979) [Pubmed]
  7. Molecules of the bacterial cytoskeleton. Löwe, J., van den Ent, F., Amos, L.A. Annual review of biophysics and biomolecular structure. (2004) [Pubmed]
  8. Bacterial DNA segregation dynamics mediated by the polymerizing protein ParF. Barillà, D., Rosenberg, M.F., Nobbmann, U., Hayes, F. EMBO J. (2005) [Pubmed]
  9. The constitutive and stress inducible forms of hsp 70 exhibit functional similarities and interact with one another in an ATP-dependent fashion. Brown, C.R., Martin, R.L., Hansen, W.J., Beckmann, R.P., Welch, W.J. J. Cell Biol. (1993) [Pubmed]
  10. Heterotrophic Archaea dominate sedimentary subsurface ecosystems off Peru. Biddle, J.F., Lipp, J.S., Lever, M.A., Lloyd, K.G., Sørensen, K.B., Anderson, R., Fredricks, H.F., Elvert, M., Kelly, T.J., Schrag, D.P., Sogin, M.L., Brenchley, J.E., Teske, A., House, C.H., Hinrichs, K.U. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
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  14. Characterization of a conserved alpha-helical, coiled-coil motif at the C-terminal domain of the ATP-dependent FtsH (HflB) protease of Escherichia coli. Shotland, Y., Teff, D., Koby, S., Kobiler, O., Oppenheim, A.B. J. Mol. Biol. (2000) [Pubmed]
  15. Occurrence of an ascamycin dealanylating enzyme, Xc-aminopeptidase, in mammalian cell membranes and susceptibility to ascamycin. Osada, H., Isono, K. J. Antibiot. (1986) [Pubmed]
  16. HSP90--news from the front. Jakob, U. Front. Biosci. (1996) [Pubmed]
  17. Open conformation of a flavocytochrome c3 fumarate reductase. Bamford, V., Dobbin, P.S., Richardson, D.J., Hemmings, A.M. Nat. Struct. Biol. (1999) [Pubmed]
  18. Osmoprotectants and phosphate regulate expression of phospholipase C in Pseudomonas aeruginosa. Shortridge, V.D., Lazdunski, A., Vasil, M.L. Mol. Microbiol. (1992) [Pubmed]
  19. DL-alpha-(Difluoromethyl)arginine: a potent enzyme-activated irreversible inhibitor of bacterial decarboxylases. Kallio, A., McCann, P.P., Bey, P. Biochemistry (1981) [Pubmed]
  20. Crystal structure of Escherichia coli crotonobetainyl-CoA: carnitine CoA-transferase (CaiB) and its complexes with CoA and carnitinyl-CoA. Rangarajan, E.S., Li, Y., Iannuzzi, P., Cygler, M., Matte, A. Biochemistry (2005) [Pubmed]
  21. Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli. Bagg, A., Neilands, J.B. Biochemistry (1987) [Pubmed]
  22. Cell and chloroplast division requires ARTEMIS. Fulgosi, H., Gerdes, L., Westphal, S., Glockmann, C., Soll, J. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  23. Subcellular localization and biological activity of M(r) 18,000 basic fibroblast growth factor: site-directed mutagenesis of a putative nuclear translocation sequence. Presta, M., Gualandris, A., Urbinati, C., Rusnati, M., Coltrini, D., Isacchi, A., Caccia, P., Bergonzoni, L. Growth Factors (1993) [Pubmed]
  24. Inhibition of prokaryotic cell growth by HIV1 Vpr. Bodéus, M., Margottin, F., Durand, H., Rouer, E., Benarous, R. Res. Virol. (1997) [Pubmed]
  25. Cloning of cDNA coding for human tissue-type plasminogen activator and its expression in Escherichia coli. Harris, T.J., Patel, T., Marston, F.A., Little, S., Emtage, J.S., Opdenakker, G., Volckaert, G., Rombauts, W., Billiau, A., De Somer, P. Mol. Biol. Med. (1986) [Pubmed]
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