Zobrazeno 1 - 10
of 110
pro vyhledávání: '"H.-J. Hecht"'
Autor:
H. J. Hecht, C. Erck, Andreas Jeron, R. Roubin, T. P. Arstila, Eliisa Kekäläinen, Siegfried Weiss, K. Wagner, Henk S.P. Garritsen, Darius Moharregh-Khiabani, Hansjörg Hauser, Jan Buer, Robert Geffers, Michael Probst-Kepper, Frank Ocklenburg, Rudi Balling, N. Viegas, Andrea Kröger, H. Lünsdorf
Publikováno v:
Journal of Cellular and Molecular Medicine
Recent evidence suggests that regulatory pathways might control sustained high levels of FOXP3 in regulatory CD4(+)CD25(hi) T (T(reg)) cells. Based on transcriptional profiling of ex vivo activated T(reg) and helper CD4(+)CD25(-) T (T(h)) cells we ha
Publikováno v:
Journal of Molecular Biology. 279:889-900
The structures of cofactor-free haloperoxidases from Streptomyces aureofaciens , Streptomyces lividans , and Pseudomonas fluorescens have been determined at resolutions between 1.9 A and 1.5 A. The structures of two enzymes complexed with benzoate or
Autor:
H.-J. Hecht, Giuseppe Zanotti, Dritan Siliqi, Bryant W. York, J. Gonzalez Platas, Carmelo Giacovazzo
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 52:813-825
The procedure described in the papers I-V of this series [Giacovazzo, Siliqi & Ralph (1994). Acta Cryst. A50, 503-505; Giacovazzo, Siliqi & Spagna (1994). Acta Cryst. A50, 609-621; Giacovazzo, Siliqi & Zanotti (1995). Acta Cryst. A51, 177-188; Giacov
Publikováno v:
Nature Structural Biology. 1:532-537
The crystal structure of the bromoperoxidase A2 from Streptomyces aureofaciens (ATCC 10762) has been determined by isomorphous replacement and refined to 2.05 A resolution with an R-value of 18.4%. The enzyme catalyzes the bromination of organic comp
Publikováno v:
Journal of Chromatography A. 668:153-164
NADH oxidase from Thermus thermophilus HB8 was selected to study the interaction of flavoproteins with structurally defined dye ligands. The fact that the enzyme binds NADH in addition to FAD favours the enzyme as a model for studying the interaction
Publikováno v:
Scopus-Elsevier
2,3-Dihydroxybiphenyl 1,2-dioxygenase, an enzyme of the biphenyl biodegradation pathway that cleaves the first of the aromatic rings, was purified to apparent homogeneity from Pseudomonas sp. strain LB400 that had been engineered to hyperexpress the
Autor:
S A, Guerrero, L, Flohé, H M, Kalisz, M, Montemartini, E, Nogoceke, H J, Hecht, P, Steinert, M, Singh
Publikováno v:
European journal of biochemistry. 259(3)
Tryparedoxin (TXN) has recently been discovered as a constituent of the complex peroxidase system in the trypanosomatid Crithidia fasciculata [Nogoceke et al. (1997) Biol. Chem. 378, 827-836] where it catalyzes the reduction of a peroxiredoxin-type p
Autor:
Josef Altenbuchner, T. Haag, H.-J. Hecht, Harald Sobek, R Bantleon, K H van Pée, O. Pfeifer, I. Pelletier
Publikováno v:
Environment & Chemistry ISBN: 9789401040327
Bacteria synthesize a large number of halogenated organic compounds. Some of these halogenated secondary metabolites show antibiotic activity against bacteria and fungi. 7-chlorotetracycline, chloramphenicol and pyrrolnitrin are amongst these antibio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::28c4d8842c80fe3cbae2199ae8f05167
https://doi.org/10.1007/978-94-011-0061-8_16
https://doi.org/10.1007/978-94-011-0061-8_16
Publikováno v:
Journal of Biomolecular NMR. 22:375-376
Publikováno v:
The Journal of biological chemistry. 268(4)
2,3-Dihydroxybiphenyl 1,2-dioxygenase, an enzyme of the biphenyl biodegradation pathway that cleaves the first of the aromatic rings, was purified to apparent homogeneity from Pseudomonas sp. strain LB400 that had been engineered to hyperexpress the