Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Eukaryotes, proteome analysis

Fig. 8. Principal component analysis of the distribution of the predicted folds in bacterial, archaeal, and eukaryotic proteomes. (a) First and second principal components (b) third and fourth principal components. Aae, Aquifex aeolicus Mge, Mycoplasm genitalium Mpn, Mycoplasma pneumoniae Rpr, Rickettsia prowazekii Bbu, Borrelia burgdorferi Bsu, Bacillus subtilis, Hin, Haemophilus influenzae, Hpy, Helicobacter pylori Tma, Thermotoga mari-... Fig. 8. Principal component analysis of the distribution of the predicted folds in bacterial, archaeal, and eukaryotic proteomes. (a) First and second principal components (b) third and fourth principal components. Aae, Aquifex aeolicus Mge, Mycoplasm genitalium Mpn, Mycoplasma pneumoniae Rpr, Rickettsia prowazekii Bbu, Borrelia burgdorferi Bsu, Bacillus subtilis, Hin, Haemophilus influenzae, Hpy, Helicobacter pylori Tma, Thermotoga mari-...
One-step characterization of a eukaryotic cell pro-teome is difficult if not impossible to achieve. There is a growing trend in eukaryotes proteomics toward characterization of subcellular structures. The reason for this shift from global proteomics to subcellular proteomics is the complexity of eukaryotic cells and subcellular organelles. Therefore the proteomic analysis of subcellular organelles will be an important aspect of toxicoproteomics. [Pg.871]

Recent proteomic analysis indicated that the cilia of mammalian photoreceptor cells are significantly more complex than other eukaryotic cilium (Liu et al. 2006). Over 1200 different polypeptides have been identified by the quantitative analysis of the proteome of photoreceptor outer segment compared with the proteome of the axoneme/ciliary fraction of mouse photoreceptor cells. This data set contains all previously identified protein components of the photoreceptor cilium (e.g. Schmitt and Wolfrum 2001). An understanding how the identified proteins function in their native environment of the diverse compartments of the photoreceptor cilia will require increased knowledge of their molecular interaction and networking. Insights into the organization and composition of diverse protein complexes may also provide novel information on how functional modules of the cell, recently proposed by Hofmann et al. 2006, are connected. [Pg.214]

Recall Has proteomic analysis heen done on multicellular eukaryotes ... [Pg.403]

Eicosanoid Protocols, Q itQdhy Elias A. Lianas, 1999 119. Chromatin Protocols, edited by. 8. Becker, 1999 118. RNA CProtein Interaction Protocols, edited by Susan R. Haynes, 1999 117. Electron Microscopy Methods and Protocols, edited by M A. Nasser Hajibagheri, 1999 116. Protein Lipidation Protocols, edited by Michael H. Gelb, 1999 115. Immunocytochemical Methods and Protocols (2nd ed.), edited by Lorette C. Javois, 1999 114. Calcium Signaling Protocols, edited by David G. Lambert, 1999 113. DNA Repair Protocols Eukaryotic Systems, edited by Daryl S. Henderson, 1999 112. 2-D Proteome Analysis Protocols, edited by Andrew J. Link, 1999 111. Plant Cell Culture Protocols, edited by Robert D. Hall, 1999 110. Lipoprotein Protocols, edited by M Ordovas, 1998 109. Lipase and Phospholipase Protocols, edited by Mark H Doolittle and Karen Reue, 1999 108. Free Radical and Antioxidant Protocols, edited by Donald Armstrong, 1998... [Pg.435]

Holder T, Basquin C, Ebert J, Randel N, Jollivet D, Conti E, Jekely G, Bono F. Deep-transcriptome-sequencing and proteome analysis of the hydrothermal vent annelid Alvinella pompejana identifies the CvP-bias as a robust measure of eukaryotic thermostability. Biok tr. 2013 8 2. doi 10.1186/1745-6150-6-2. [Pg.755]

The analysis of adenylylation requires preparatively adenylylated proteins in order to determine the site of the PTM, to determine the structure of the modified proteins, and to establish the functional consequences for Rabl-activity. Also, the systematic investigation of adenylylation in live cells and their distribution among different prokaryotic and eukaryotic proteomes requires specific tools... [Pg.143]

Before we describe the chemistry of the compartments involved, note that like prokaryotes, a number of oxidative enzymes are found in the cytoplasm but they do not release damaging chemicals (see Section 6.10). We also observed that such kinds of kinetic compartments are not enclosed by physical limitations such as membranes. We have also mentioned that increased size itself makes for kinetic compartments if diffusion is restricted. In this section, we see many additional advantages of eukaryotes from those given in Section 7.4. How deceptive it can be to use just the DNA, the all-embracing proteome, metabolome or metallome in discussing evolution without the recognition of the thermodynamic importance of compartments and their concentrations These data could be useful both here and in simpler studies of single-compartment bacteria even in the analysis of species but not much information is available. [Pg.290]

Haresh K, Suresh K, Khairul Anus A, Saminathan S (1999) Isolate resistance of Blastocystis hominis to metronidazole. Trop Med Int Health 4 274-277 Inui H, Ono K, Miyatake K, Nakano Y, Kitaoka S (1987) Purification and characterization of pyruvate NADP+ oxidoreductase in Euglena gracilis. J Biol Chem 262 9130-9135 Keithly JS, Langreth SG, Buttle KF, Mannella CA (2005) Electron tomographic and ultra-structural analysis of the Cryptosporidium parvum relict mitochondrion, its associated membranes, and organelles. J Eukaryot Microbiol 52 132-140 Kurland CG, Andersson SGE (2000) Origin and evolution of the mitochondrial proteome. Micro Mol Biol Rev 64 786-820... [Pg.263]

Consortium for the Functional Genomics of Microbial Eukaryotes. University of Manchester, U.K URL http //www. cogeme.man.ac.uk. Analysis of the transcriptome and proteome of Saccharomyces cerevisiae (yeast) and a ntunber of plant and human fungal pathogens together with a bioinformatics centre. [Pg.54]

The relatively new field termed proteomics deals with the assignment of molecular and cellular functions to the tens of thousands of protein products encoded by prokaryotic and eukaryotic genomes. In addition, it seeks to develop and apply new methods for the global analysis of protein expression and protein function. These methods must fulfill distinct requirements ranging from the analysis of many proteins in parallel and in samples of high complexity up to the characterization of proteins in a dynamic cellular environment, in which these biomolecules are subject to a myriad of post-translational modifications and actions ofvarious activators and inhibitors [250,251]. [Pg.67]


See other pages where Eukaryotes, proteome analysis is mentioned: [Pg.15]    [Pg.315]    [Pg.166]    [Pg.61]    [Pg.304]    [Pg.24]    [Pg.24]    [Pg.411]    [Pg.68]    [Pg.18]    [Pg.152]    [Pg.422]    [Pg.210]    [Pg.1353]    [Pg.262]    [Pg.268]    [Pg.23]    [Pg.212]    [Pg.4]    [Pg.137]    [Pg.222]    [Pg.220]    [Pg.209]    [Pg.218]    [Pg.59]    [Pg.1045]    [Pg.2116]    [Pg.630]    [Pg.109]    [Pg.124]    [Pg.558]    [Pg.404]    [Pg.507]    [Pg.289]    [Pg.629]    [Pg.109]    [Pg.263]    [Pg.565]   
See also in sourсe #XX -- [ Pg.22 ]




SEARCH



Eukaryotes analysis

Proteome analysis

Proteome/Proteomic analysis

Proteomic analysis

© 2024 chempedia.info