Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Jason A. Kuchar"'
Autor:
Sinisa Dovat, Christoph W. Turk, Kimberly J. Payne, Zafer Gurel, Tapani Ronni, Sam Ho, Jason A. Kuchar
Publikováno v:
Journal of Biological Chemistry. 283:8291-8300
Ikaros encodes a zinc finger protein that is involved in heritable gene silencing. In hematopoietic cells, Ikaros localizes to pericentromeric heterochromatin (PC-HC) where it recruits its target genes, resulting in their activation or repression via
Autor:
Erik J. Soderblom, Steven C. Huber, Jia Li, Xiaofeng Wang, Jason A. Kuchar, Tadao Asami, Michael B. Goshe, Brett S. Phinney, Steven D. Clouse, Shigeo Yoshida
Publikováno v:
The Plant Cell. 17:1685-1703
Brassinosteroids (BRs) regulate multiple aspects of plant growth and development and require an active BRASSINOSTEROID-INSENSITIVE1 (BRI1) and BRI1-ASSOCIATED RECEPTOR KINASE1 (BAK1) for hormone perception and signal transduction. Many animal recepto
Autor:
Lawrence M. Sayre, David M. Dooley, Jason A. Kuchar, Bradley O. Elmore, Jennifer Smith, Eric M. Shepard
Publikováno v:
European Journal of Biochemistry. 269:3645-3658
Four substrate analogs, 4-(2-naphthyloxy)-2-butyn-1-amine (1), 1,4-diamino-2-chloro-2-butene (2), 1,6-diamino-2,4-hexadiyne (3), and 2-chloro-5-phthalimidopentylamine (4) have been tested as inhibitors against mammalian, plant, bacterial, and fungal
Autor:
David M. Dooley, Jason A. Kuchar
Publikováno v:
Journal of Inorganic Biochemistry. 83:193-204
Lysyl oxidase from Pichia pastoris has been successfully overexpressed. EPR and resonance Raman experiments have shown that copper and TPQ are present, respectively. Lysyl oxidase from P. pastoris has a similar substrate specificity to the mammalian
Autor:
Mihwa Lee, David B. Langley, Paul J. Ellis, Katrina Willingham, J. Mitchell Guss, Aina E. Cohen, David M. Dooley, Jason A. Kuchar, Megan J. Maher, Hans C. Freeman
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 58:2177-2179
A copper-containing amine oxidase (PPLO) from the yeast Pichia pastoris has been purified and crystallized in two forms. PPLO is a glycoprotein. The molecular mass from SDS-polyacrylamide gels is 112 kDa, consistent with 20% glycosylation by weight (
The plant hormone jasmonic acid (JA) activates host defense responses against a broad spectrum of herbivores. Although it is well established that JA controls the expression of a large set of target genes in response to tissue damage, very few gene p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7372210a852df9b1e942ab529bfe23ab
https://europepmc.org/articles/PMC1323180/
https://europepmc.org/articles/PMC1323180/
Autor:
Robert P. Hausinger, Jason A. Kuchar
Publikováno v:
Chemical reviews. 104(2)
Publikováno v:
The Journal of biological chemistry. 279(15)
Synthesis of active Klebsiella aerogenes urease requires four accessory proteins to generate, in a GTP-dependent process, a dinuclear nickel active site with the metal ions bridged by a carbamylated lysine residue. The UreD and UreF accessory protein
Autor:
P.J. Ellis, Aina E. Cohen, Anthony P. Duff, David B. Langley, J.M. Guss, Jason A. Kuchar, Eric M. Shepard, Hans C. Freeman, David M. Dooley
Publikováno v:
Biochemistry. 42(51)
Pichia pastoris lysyl oxidase (PPLO) is unique among the structurally characterized copper amine oxidases in being able to oxidize the side chain of lysine residues in polypeptides. Remarkably, the yeast PPLO is nearly as effective in oxidizing a mam
Autor:
David M. Dooley, Jason A. Kuchar, Alan Jay Smith, Joanne E. Dove, Judith P. Klinman, Doreen E. Brown
Publikováno v:
FEBS letters. 398(2-3)
A copper amine oxidase from Pichia pastoris is the only known non-mammalian lysyl oxidase [Tur, S.S. and Lerch, K. (1988) FEBS Lett. 238, 74–76]. Recently, the cofactor in mammalian lysyl oxidase has been identified as a novel lysine tyrosylquinone