To use all functions of this page, please activate cookies in your browser.
my.chemeurope.com
With an accout for my.chemeurope.com you can always see everything at a glance – and you can configure your own website and individual newsletter.
- My watch list
- My saved searches
- My saved topics
- My newsletter
86 Newest Publications in bmc biochemistry
rss24-08-2010 | Anthony Levasseur; Markku Saloheimo; David Navarro; Martina Andberg; Pierre Pontarotti; Kristiina Kruus; Eric Record, BMC Biochemistry, 2010
Background: The diversity and function of ligninolytic genes in soil-inhabiting ascomycetes has not yet been elucidated, despite their possible role in plant litter decay processes. Among ascomycetes, Trichoderma reesei is a model organism of cellulose and hemicellulose degradation, used for ...
24-08-2010 | Ludmila Roze; Anindya Chanda; Maris Laivenieks; Randolph Beaudry; Katherine Artymovich; Anna Koptina; Deena Awad; Di ..., BMC Biochemistry, 2010
Background: Filamentous fungi in the genus Aspergillus produce a variety of natural products, including aflatoxin, the most potent naturally occurring carcinogen known. Aflatoxin biosynthesis, one of the most highly characterized secondary metabolic pathways, offers a model system to study ...
20-08-2010 | Greta Faccio; Kristiina Kruus; Johanna Buchert; Markku Saloheimo, BMC Biochemistry, 2010
Background: Sulfhydryl oxidases are flavin-dependent enzymes that catalyse the formation of de novo disulfide bonds from the free thiol groups of small compounds, with the reduction of a molecule of oxygen to hydrogen peroxide. Sulfhydryl oxidases have been investigated in the food industry ...
07-08-2010 | Kanteera Soontharapirakkul; Aran Incharoensakdi, BMC Biochemistry, 2010
Background: When cells are exposed to high salinity conditions, they develop a mechanism to extrude excess Na+ from cells to maintain the cytoplasmic Na+ concentration. Until now, the ATPase involved in Na+ transport in cyanobacteria has not been characterized. Here, the characterization of ...
04-08-2010 | John Zaborske; Xiaochen Wu; Ronald Wek; Tao Pan, BMC Biochemistry, 2010
Background: When eukaryotic cells are deprived of amino acids, uncharged tRNAs accumulate and activate the conserved GCN2 protein kinase. Activated Gcn2p up-regulates the general amino acid control pathway through phosphorylation of the translational initiation factor eIF2. In Saccharomyces ...
26-07-2010 | Leo Syrjanen; Martti Tolvanen; Mika Hilvo; Ayodeji Olatubosun; Alessio Innocenti; Andrea Scozzafava; Jenni Leppiniem ..., BMC Biochemistry, 2010
Background: The beta-carbonic anhydrase (CA, EC 4.2.1.1) enzymes have been reported in a variety of organisms, but their existence in animals has been unclear. The purpose of the present study was to perform extensive sequence analysis to show that the beta-CAs are present in invertebrates ...
24-07-2010 | Toshifumi Tomoyasu; Atsushi Tabata; Hideaki Nagamune, BMC Biochemistry, 2010
Background: A small heat shock protein AgsA was originally isolated from Salmonella enterica serovar Typhimurium. We previously demonstrated that AgsA was an effective chaperone that could reduce the amount of heat-aggregated proteins in an Escherichia coli rpoH mutant. AgsA appeared to ...
09-07-2010 | Valerie Barnes; Bethany Strunk; Icksoo Lee; Maik Huttemann; Lori Pile, BMC Biochemistry, 2010
Background: SIN3 is a transcriptional repressor protein known to regulate many genes, including a number of those that encode mitochondrial components. Results: By monitoring RNA levels, we find that loss of SIN3 in Drosophila cultured cells results in up-regulation of not only nuclear ...
01-07-2010 | Douglas Rehder; Chad Borges, BMC Biochemistry, 2010
Background: Cysteine sulfenic acid (Cys-SOH) plays important roles in the redox regulation of numerous proteins. As a relatively unstable posttranslational protein modification it is difficult to quantify the degree to which any particular protein is modified by Cys-SOH within a complex ...
29-06-2010 | Terry Meyer; John Kyndt; Michael Cusanovich, BMC Biochemistry, 2010
Background: Sphaeroides Heme Protein (SHP) was discovered in the purple photosynthetic bacterium, Rhodobacter sphaeroides, and is the only known c-type heme protein that binds oxygen. Although initially not believed to be widespread among the photosynthetic bacteria, the gene has now been ...
