Zobrazeno 1 - 10
of 155
pro vyhledávání: '"Gerhard, Hübner"'
Publikováno v:
Taschenbuch der Technischen Akustik ISBN: 9783662439661
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b2375210b6d711537e769308a13dff8f
https://doi.org/10.1007/978-3-662-43966-1_6-1
https://doi.org/10.1007/978-3-662-43966-1_6-1
Autor:
Christian, Magaña Vergara, Christina Jana Louisa, Kallenberg, Miriam, Rogasch, Christian Gerhard, Hübner, Young-Hwa, Song
Publikováno v:
Protein science : a publication of the Protein Society. 26(11)
Recombinant protein expression is a prerequisite for diverse investigations of proteins at the molecular level. For targets from Mycobacterium tuberculosis it is favorable to use M. smegmatis as an expression host, a species from the same genus. In t
Publikováno v:
Head & Neck. 32:1479-1484
Background. Opinions differ regarding the use- fulness of accurate, but costly, frozen sections. Most physi- cians believe that negative margins are essential for the prognosis of patients with oral and pharyngeal cancer. We examined whether immediat
Publikováno v:
Biochemistry (Moscow). 74:293-300
In this work, we investigated the rate of formation of the central intermediate of the transketolase reaction with thiamine diphosphate (ThDP) or 4'-methylamino-ThDP as cofactors and its stability using stopped-flow spectroscopy and circular dichrois
Autor:
Stephan König, Michael Spinka, Gerhard Hübner, Kai Tittmann, Ralph Golbik, Tobias Werther, Anja Schütz, Carmen Mrestani-Klaus
Publikováno v:
Journal of Biological Chemistry. 283:5344-5354
The gene rv0853c from Mycobacterium tuberculosis strain H37Rv codes for a thiamine diphosphate-dependent alpha-keto acid decarboxylase (MtKDC), an enzyme involved in the amino acid degradation via the Ehrlich pathway. Steady state kinetic experiments
Autor:
Gerhard Hübner, German A. Kochetov, Johanna Brauer, L. E. Meshalkina, Olga Esakova, Ralph Golbik
Publikováno v:
IUBMB Life. 59:104-109
The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically ac
Publikováno v:
Biochemistry. 44:13291-13303
The thiamin diphosphate (ThDP)- and flavin adenine dinucleotide (FAD)-dependent pyruvate oxidase from Lactobacillus plantarum catalyses the conversion of pyruvate, inorganic phosphate, and oxygen to acetyl-phosphate, carbon dioxide, and hydrogen pero
Autor:
E. A. Khanova, L. E. Meshalkina, Gerhard Hübner, Olga Esakova, German A. Kochetov, Ralph Golbik
Publikováno v:
Biochemistry (Moscow). 70:770-776
The influence of transketolase substrates on the interaction of apotransketolase with its coenzyme thiamine diphosphate (TDP) and on the stability of the reconstituted holoenzyme was studied. Donor substrates increased the affinity of the coenzyme fo
Autor:
Gerhard Hübner, Natalia S. Nemeria, Michelle B. Vazquez-Coll, Ebenezer Joseph, Palaniappa Arjunan, William Furey, Frank Jordan, Leon Zhou, Kai Tittmann
Publikováno v:
Journal of Biological Chemistry. 280:21473-21482
The residue Glu636 is located near the thiamine diphosphate (ThDP) binding site of the Escherichia coli pyruvate dehydrogenase complex E1 subunit (PDHc-E1), and to probe its function two variants, E636A and E636Q were created with specific activities
Autor:
Ralph Golbik, Ronald Kluger, Stephan König, Erik Fiedler, Gerhard Hübner, German A. Kochetov, Kai Tittmann, L. E. Meshalkina, Holger Neef, Tatjana Sandalova, Gunter Schneider
Publikováno v:
FEBS Journal. 272:1326-1342
Transketolase from baker's yeast is a thiamin diphosphate-dependent enzyme in sugar metabolism that reconstitutes with various analogues of the coenzyme. The methylated analogues (4′-methylamino-thiamin diphosphate and N1′-methylated thiamin diph