Zobrazeno 1 - 10
of 63
pro vyhledávání: '"Paul V. Viitanen"'
Autor:
Celeste Weiss, Adina Niv, Galit Levy-Rimler, Paul V. Viitanen, Abdussalam Azem, Rajach Sharkia
Publikováno v:
Annual Plant Reviews
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3eb129df4a35e2a040b8df5ebc8e2501
https://doi.org/10.1002/9781119312994.apr0062
https://doi.org/10.1002/9781119312994.apr0062
Autor:
Paul V. Viitanen, R. B. McQualter, Michael G. O'Shea, Nicholas J. Walton, Stevens M. Brumbley, Knut Meyer, Barrie Fong Chong, Drew E. Van Dyk
Publikováno v:
Plant Biotechnology Journal. 3:29-41
Sugarcane (Saccharum hybrids) was evaluated as a production platform for p-hydroxybenzoic acid using two different bacterial proteins (a chloroplast-targeted version of Escherichia coli chorismate pyruvate-lyase and 4-hydroxycinnamoyl-CoA hydratase/l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8c9e9b6993aab966f0ea165771a83dfa
https://doi.org/10.1111/j.1467-7652.2004.00095.x
https://doi.org/10.1111/j.1467-7652.2004.00095.x
Autor:
Daniel P. O'Keefe, Philip A. Rea, Drew E. Van Dyk, Dolores M. Bartholomew, Sze-Mei Cindy Lau, Paul V. Viitanen
Publikováno v:
Plant Physiology. 130:1562-1572
Through the development and application of a liquid chromatography-mass spectrometry-based procedure for measuring the transport of complex organic molecules by vacuolar membrane vesicles in vitro, it is shown that the mechanism of uptake of sulfonyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd085e5a4e7f2b62ee0fd259cef4d57e
https://doi.org/10.1104/pp.008334
https://doi.org/10.1104/pp.008334
Publikováno v:
Planta. 215:26-32
The serine carboxypeptidase-like protein 1- O-sinapoylglucose:malate sinapoyltransferase (SMT) catalyzes the transfer of the sinapoyl moiety of 1- O-sinapoylglucose to malate in the formation of sinapoylmalate in some members of the Brassicaceae. Rab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::443bd300f5b6c803fbff535345278685
https://doi.org/10.1007/s00425-001-0716-y
https://doi.org/10.1007/s00425-001-0716-y
Publikováno v:
Biochemistry. 41:1795-1806
X-ray crystal structures of L-3,4-dihydroxy-2-butanone-4-phosphate synthase from Magnaporthe grisea are reported for the E-SO{sub 4}{sup 2-}, E-{sub 4}{sup 2-}-Mg{sup 2+}, E-SO{sub 4}{sup 2-}-Mn{sup 2+}, E-SO{sub 4}{sup 2-}-Mn{sup 2+}-glycerol, and E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::503de53e74795b29508c29b1f6d010a9
https://doi.org/10.1021/bi015652u
https://doi.org/10.1021/bi015652u
Autor:
Yacov Delarea, Adina Niv, Paul V. Viitanen, Abdussalam Azem, Anat Greenberg, Celeste Weiss, Rajach Sharkia, Galit Levy-Rimler, Ariel Lustig
Publikováno v:
European Journal of Biochemistry. 268:3465-3472
Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. The goal of this study was to investigate the structure and function of the mammalian mitochondrial chaperonin system. We present e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3ca8b05bf1df6abe46953a025cc6816e
https://doi.org/10.1046/j.1432-1327.2001.02243.x
https://doi.org/10.1046/j.1432-1327.2001.02243.x
Publikováno v:
Structure. 9(5):399-408
Background: Riboflavin synthase catalyzes the dismutation of two molecules of 6,7-dimethyl-8-(1′-D-ribityl)-lumazine to yield riboflavin and 4-ribitylamino-5-amino-2,6-dihydroxypyrimidine. The homotrimer of 23 kDa subunits has no cofactor requireme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d520684d4f8d383c0f2578ac14abf885
Publikováno v:
Protein & Peptide Letters. 8:69-73
Escherichia coli riboflavin synthase crystallizes at 22 C in the presence of 7-10percent by volume diglyme, 20-50 mM MgCl2 and pH 7.0. In this medium diffraction quality crystals are routinely obtained within 5 h and they are stable for 10 weeks. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::12ad8ad08ce7975625a05585beb76816
https://doi.org/10.2174/0929866013409698
https://doi.org/10.2174/0929866013409698
Publikováno v:
Structure. 9:11-18
Background: 3,4-Dihydroxy-2-butanone-4-phosphate synthase catalyzes a commitment step in the biosynthesis of riboflavin. On the enzyme, ribulose 5-phosphate is converted to 3,4-dihydroxy-2-butanone 4-phosphate and formate in steps involving enolizati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::805572fecd1e04dfbed26ecd33b9cfd0
https://doi.org/10.1016/s0969-2126(00)00550-5
https://doi.org/10.1016/s0969-2126(00)00550-5
Autor:
Joanne C. Cusumano, Dieter Strack, Knut Meyer, Clint Chapple, Amber M. Shirley, Paul V. Viitanen, Max O. Ruegger, Claus Lehfeldt
Publikováno v:
The Plant Cell. 12:1295-1306
Serine carboxypeptidases contain a conserved catalytic triad of serine, histidine, and aspartic acid active-site residues. These enzymes cleave the peptide bond between the penultimate and C-terminal amino acid residues of their protein or peptide su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ad3ee1d5a36006f6276da49fb427ddff
https://doi.org/10.1105/tpc.12.8.1295
https://doi.org/10.1105/tpc.12.8.1295