Structure and posttranslational modification of lipoyl domain of 2-oxo-acid dehydrogenase multienzyme complexes
Perham, R.N.
Methods in Enzymology 251: 436-448
1995
ISSN/ISBN: 0076-6879 PMID: 7651225 Document Number: 452212
Document emailed within 1 workday
Related Documents
Drozdov-Tikhomirov, L.N.; Buzinier, M.A.; Vompe, A.G.; Skurida, G.I. 1994: Optimal structure of the multienzyme system of the tricarboxylic acid cycle of E. coli during growth on various carbon sources Biokhimiia 59(3): 368-380Gol'dshteĭn, B.N.; Kornilov, V.V.; Smetanich, I.S. 1986: Symmetry of multienzyme complexes Molekuliarnaia Biologiia 20(1): 242-249
Artiukhov, V.G.; Nakvasina, M.A.; Lysenko, I.A.; Agisheva, N.V. 2001: Structure-functional modification of lactate dehydrogenase isoforms under the effect of ultraviolet radiation and active forms of oxygen Ukrains'kyi Biokhimichnyi Zhurnal 73(1): 29-42
Vinogradova, R.P.; Kucherenko, N.E. 1986: High molecular weight multienzyme complexes of aminoacyl-tRNA-synthetases in eukaryotic cells Ukrainskii Biokhimicheskii Zhurnal 58(4): 89-100
Katahira, M.; Knegtel, R.; Schilthius, J.; Boelens, R.; Eib, D.; van der Saag, P.; Kaptein, R. 1992: The structure of the human retinoic acid receptor-beta DNA-binding domain determined by NMR Nucleic Acids Symposium Series 27: 65-66
Adler, G. 2005: The posttranslational modification of thyrotropin receptor and thyroid diseases Endokrynologia Polska 56(1): 72-77
Shima, F.; Kataoka, T. 2005: Critical role of posttranslational modification of Ras proteins in effector activation Seikagaku. Journal of Japanese Biochemical Society 77(6): 519-526
Li, Y-hua.; Bi, H-chang.; Huang, M. 2011: Effects of posttranslational modification on the activity of cytochrome P450: current progress Yao Xue Xue Bao 46(5): 487-492
Hancock, J.F. 1995: Reticulocyte lysate assay for in vitro translation and posttranslational modification of Ras proteins Methods in Enzymology 255: 60-65
Korosteleva, T.A.; Shvaĭdetskii, I.I. 1974: Structure and excretion of the formed in vivo antigenic complexes containing 3-oxyanthranilic acid Voprosy Onkologii 20(12): 72-76
Bressac, C.; Bré, M.H.; Darmanaden-Delorme, J.; Laurent, M.; Levilliers, N.; Fleury, A. 1995: A massive new posttranslational modification occurs on axonemal tubulin at the final step of spermatogenesis in Drosophila European Journal of Cell Biology 67(4): 346-355
Piekiełko-Witkowska, A. 2006: Phosphorylation of serine-arginine rich proteins--pleiotropic effect of one type posttranslational modification Postepy Biochemii 52(4): 383-389
Haworth, J.C.; Perry, T.L.; Blass, J.P.; Hansen, S.; Urquhart, N. 1976: Lactic acidosis in three sibs due to defects in both pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase complexes Pediatrics 58(4): 564-572
Agadzhanian, S.A.; Arutiunian, A.A.; Karabashian, L.V. 1984: Identification of a glutamate dehydrogenase amino acid residue modified by 2,2,6,6-tetramethyl-4-oxopiperidine-1-oxyl. Study of the type of inactivation of a catalytically active enzyme oligomer in modification Bioorganicheskaia Khimiia 10(9): 1171-1176
Gu, K.F.; Chang, T.M. 1990: Conversion of ammonia or urea into essential amino acids, L-leucine, L-valine, and L-isoleucine, using artificial cells containing an immobilized multienzyme system and dextran-NAD+. 2. Yeast alcohol dehydrogenase for coenzyme recycling Biotechnology and Applied Biochemistry 12(3): 227-236
Cieśla, J.; Fraczyk, T.; Zieliński, Z.; Sikora, J.; Rode, W. 2006: Altered mouse leukemia L1210 thymidylate synthase, associated with cell resistance to 5-fluoro-dUrd, is not mutated but rather reflects posttranslational modification Acta Biochimica Polonica 53(1): 189-198
Raznikov, A.V.; Egorov, T.A.; Mirgorodskaia, O.V.; Skliankina, V.A.; Avaeva, S.M. 1992: Functionally important residues of glutamic acid in E. coli pyrophosphatase. I. Chemical modification and localization in the primary structure Biokhimiia 57(12): 1902-1912
Holland, S.K.; Harlos, K.; Blake, C.C. 1987: Deriving the generic structure of the fibronectin type II domain from the prothrombin Kringle 1 crystal structure EMBO Journal 6(7): 1875-1880
Lavrik, O.I.; Nevinskiĭ, G.A.; Riazankin, I.A. 1979: Influence of the structure of photoreactive ATP analogs on the affinity modification of phenylalanyl-tRNA synsthetase. Modification of the enzyme at two types of nucleotide sites Molekuliarnaia Biologiia 13(5): 1001-1011
Silverman, C.; Mascelli, M.A.; Karl, D.W.; Kirby, E.P. 1987: Modification of the platelet-binding domain of von Willebrand factor Journal of Laboratory and Clinical Medicine 110(1): 113-118