@article {2147,
	title = {Identification of the wax ester synthase/acyl-coenzyme A: Diacylglycerol acyltransferase WSD1 required for stem wax ester biosynthesis in Arabidopsis},
	journal = {Plant Physiology},
	volume = {148},
	number = {1},
	year = {2008},
	note = {ISI Document Delivery No.: 344SMTimes Cited: 16Cited Reference Count: 52Li, Fengling Wu, Xuemin Lam, Patricia Bird, David Zheng, Huanquan Samuels, Lacey Jetter, Reinhard Kunst, Ljerka},
	month = {Sep},
	pages = {97-107},
	type = {Article},
	abstract = {Wax esters are neutral lipids composed of aliphatic alcohols and acids, with both moieties usually long-chain (C-16 and C-18) or very-long-chain (C-20 and longer) carbon structures. They have diverse biological functions in bacteria, insects, mammals, and terrestrial plants and are also important substrates for a variety of industrial applications. In plants, wax esters are mostly found in the cuticles coating the primary shoot surfaces, but they also accumulate to high concentrations in the seed oils of a few plant species, including jojoba (Simmondsia chinensis), a desert shrub that is the major commercial source of these compounds. Here, we report the identification and characterization of WSD1, a member of the bifunctional wax ester synthase/diacylglycerol acyltransferase gene family, which plays a key role in wax ester synthesis in Arabidopsis (Arabidopsis thaliana) stems, as first evidenced by severely reduced wax ester levels of in the stem wax of wsd1 mutants. In vitro assays using protein extracts from Escherichia coli expressing WSD1 showed that this enzyme has a high level of wax synthase activity and approximately 10-fold lower level of diacylglycerol acyltransferase activity. Expression of the WSD1 gene in Saccharomyces cerevisiae resulted in the accumulation of wax esters, but not triacylglycerol, indicating that WSD1 predominantly functions as a wax synthase. Analyses of WSD1 expression revealed that this gene is transcribed in flowers, top parts of stems, and leaves. Fully functional yellow fluorescent protein-tagged WSD1 protein was localized to the endoplasmic reticulum, demonstrating that biosynthesis of wax esters, the final products of the alcohol-forming pathway, occurs in this subcellular compartment.},
	keywords = {ABC, CLONING, CONDENSING ENZYME, ELONGATION, GENE-EXPRESSION, PLANT CUTICULAR WAXES, SURFACES, THALIANA, TRANSFORMATION, TRANSGENIC ARABIDOPSIS, TRANSPORTER},
	isbn = {0032-0889},
	url = {<Go to ISI>://000258947600010},
	author = {Li, F. and Wu, X. and Lam, P. and Bird, D. and Zheng, H. and Samuels, L. and Jetter, R. and Kunst, L.}
}
@article {441,
	title = {Sequential anaerobic-aerobic treatment of soil contaminated with weathered aroclor 1260},
	journal = {Environmental Science \& Technology},
	volume = {36},
	number = {1},
	year = {2002},
	note = {ISI Document Delivery No.: 509RCTimes Cited: 25Cited Reference Count: 36},
	month = {Jan},
	pages = {100-103},
	type = {Article},
	abstract = {Soil contaminated with weathered Aroclor 1260 was bioremediated by sequential anaerobic and aerobic laboratory-scale treatment The initial concentration was 59 mug of PCBs/g of soil. Following 4 months of anaerobic treatment with an enrichment culture, all of the major components in Aroclor 1260 were completely or partially transformed to less chlorinated PCB congeners. The major products of reductive dechlorination were 24-24-tetrachlorobiphenyl and 24-26-tetrachlorobiphenyl, and the average chlorine substituents per PCB molecule decreased from 6.4 to 5.2. The molar concentration of PCBs did not decrease during the anaerobic treatment. All of the major products formed during the anaerobic treatment were degraded in the subsequent aerobic treatment using Burkholderia sp. strain LB400. After 28 days of the aerobic treatment, the concentration of PCBs was reduced to 20 mug/g of soil. PCBs were not significantly removed in aerobic treatments unless they were bioaugmented with LB400. Also, PCB degradation was not detected in soil bioaugmented with LB400 without prior anaerobic treatment. These results confirm the potential for extensive biological destruction of highly chlorinated, weathered PCB congeners in soil.},
	keywords = {BACTERIA, BIODEGRADATION, CLONING, ENCODING BIPHENYL, EXPRESSION, GENE-CLUSTER, PCBS, POLYCHLORINATED BIPHENYL-DEGRADATION, PSEUDOMONAS STRAIN LB400, REDUCTIVE DECHLORINATION},
	isbn = {0013-936X},
	url = {<Go to ISI>://000173162600031},
	author = {Master, E. R. and Lai, V. W. M. and Kuipers, B. and Cullen, W. R. and Mohn, W. W.}
}
@article {4312,
	title = {Equus caballus gelsolin - cDNA sequence and protein structural implications},
	journal = {European Journal of Biochemistry},
	volume = {251},
	number = {3},
	year = {1998},
	note = {ISI Document Delivery No.: YV719Times Cited: 4Cited Reference Count: 48},
	month = {Feb},
	pages = {613-621},
	type = {Article},
	abstract = {We have generated and characterized the cDNA from equine smooth muscle that Encodes gelsolin, an actin-modulating protein. Overlapping cDNA clones synthesized by the reverse transcriptaseoplymerase chain reaction and clones isolated from a horse genomic library provided the complete primary structure for the intracellular isoform of gelsolin, while cDNA complemented with protein sequence data produced the full-length primary transcript of the gelsolin isoform found circulating in equine plasma. The deduced amino acid sequences of the intracellular and secreted versions of equine gelsolin infer polypeptides of 731 and 755 residues with apparent molecular masses of 80.7 kDa and 83.2 kDa, respectively. Multiple sequence alignment analysis of equine, human, porcine, and murine orthologs of gelsolin demonstrates prominent similarities among all of these proteins, with the horse and human molecules exhibiting the largest degree of likeness with respect to polypeptide length and overall sequence composition. Both horse and human plasma gelsolins are comprised of 755 amino acids with 94\% of the residues identical, while the degree of sequence identity in the shorter (731 residues) cytoplasmic gelsolins is 95 \%. Analysis of the sequences and structures of the six related domains that comprise gelsolin emphasizes the strong correlation that exists between primary structural conservation among mammalian gelsolins and maintenance of the three-dimensional domain fold characteristic of members of this protein family.},
	keywords = {actin-binding protein, ACTIN-SEVERING PROTEINS, amino acid sequence, AMPLIFICATION, BINDING DOMAIN, cDNA sequence, CLONING, CYTOPLASMIC FORMS, DNA, END, extraction, gelsolin, HORSE PLASMA GELSOLIN, MUSCLE, protein structure},
	isbn = {0014-2956},
	url = {<Go to ISI>://000071855900009},
	author = {Koepf, E. K. and Hewitt, J. and Vo, H. and MacGillivray, R. T. A. and Burtnick, L. D.}
}
@article {3983,
	title = {The inhibition of glutamate racemase by D-N-hydroxyglutamate},
	journal = {Bioorganic \& Medicinal Chemistry Letters},
	volume = {7},
	number = {17},
	year = {1997},
	note = {ISI Document Delivery No.: XX507Times Cited: 20Cited Reference Count: 30},
	month = {Sep},
	pages = {2265-2270},
	type = {Article},
	abstract = {We report that D-N-hydroxyglutamate is ii competitive inhibitor of glutamate racemase (K-I=56 mu M). The compound acts as an alternate substrate and is converted into a-ketoglutarate and ammonia (K-M=57 mu M, k(cat)/K-M=3.2x10(3) M(-1)sec(-1)), An imine intermediate is likely the species causing the inhibition. L-N-hydroxyglutamate is a weak inhibitor and is slowly converted to alpha-ketoglutarate (k(cat)/K-M=30 M(-1)sec(-1)). (C) 1997 Elsevier Science Ltd.},
	keywords = {CLONING, DIAMINOPIMELIC ACID, EPIMERASE, ESCHERICHIA-COLI, GENE, L-ALANINE, LACTOBACILLUS, MURI, PEDIOCOCCUS-PENTOSACEUS, resistance},
	isbn = {0960-894X},
	url = {<Go to ISI>://A1997XX50700025},
	author = {Glavas, S. and Tanner, M. E.}
}
@article {3437,
	title = {AQUEOUS 2-PHASE POLYMER SYSTEMS AS TOOLS FOR THE STUDY OF A RECOMBINANT SURFACE-EXPRESSED ESCHERICHIA-COLI HEMAGGLUTININ},
	journal = {Applied and Environmental Microbiology},
	volume = {61},
	number = {9},
	year = {1995},
	note = {ISI Document Delivery No.: RT798Times Cited: 5Cited Reference Count: 15},
	month = {Sep},
	pages = {3251-3255},
	type = {Article},
	abstract = {The surface expression of an integral membrane hemagglutinin, HRA1, cloned from Escherichia coli O9:H10:K99 in heterologous E. coli strains was studied by utilizing a variety of polyethylene glycol-dextran and dextran-Ficoll aqueous two-phase polymer systems. Bacteria containing plasmids that encoded the hemagglutinin were found to partition differently from both the host bacteria lacking the plasmid and the original hemagglutinating strain in several of these systems. By using molecular biological techniques, the origin of the partition difference was unambiguously correlated to the expression of HRA1, providing evidence independent of the agglutination phenotype that the protein was accessible to the surrounding milieu. It Was demonstrated by using bacterial partition in charge-sensitive systems that the agglutination event was not likely to be due to the presence of a nonspecific positively charged surface protein, as HRA1-expressing clones showed no less affinity for the relatively positive polyethylene glycol-rich upper phase than did control bacteria, This work demonstrates the utility of aqueous polymer two-phase systems for the study of surface-expressed recombinant proteins, due to the sensitivity of the systems and the presence of excellent controls (the host bacteria before plasmid introduction). In cloning and expression studies of surface-associated proteins, two-phase aqueous polymer systems could be used as an alternative to antibody production for the monitoring of surface expression, and these systems may give valuable information on the surface exposure of the protein.},
	keywords = {ANTIGEN, CLONING, PROTEIN, STRAINS},
	isbn = {0099-2240},
	url = {<Go to ISI>://A1995RT79800010},
	author = {Lutwyche, P. and Norrisjones, R. and Brooks, D. E.}
}
@article {3013,
	title = {THE CELLULOSE-BINDING DOMAIN OF ENDOGLUCANASE-A (CENA) FROM CELLULOMONAS-FIMI - EVIDENCE FOR THE INVOLVEMENT OF TRYPTOPHAN RESIDUES IN BINDING},
	journal = {Molecular Microbiology},
	volume = {11},
	number = {4},
	year = {1994},
	note = {ISI Document Delivery No.: MW536Times Cited: 96Cited Reference Count: 46},
	month = {Feb},
	pages = {747-755},
	type = {Article},
	abstract = {Cellulomonas fimi endo-beta-1-4-glucanase A (CenA) contains a discrete N-terminal cellulose-binding domain (CBDCenA). Related CBDs occur in at least 16 bacterial glycanases and are characterized by four highly conserved Trp residues, two of which correspond to W14 and W68 of CBDCenA. The adsorption of CBDCenA to crystalline cellulose was compared with that of two Trp mutants (W14A and W68A). The affinities of the mutant CBDs for cellulose were reduced by approximately 50- and 30-fold, respectively, relative to the wild type. Physical measurements indicated that the mutant CBDs fold normally. Fluorescence data indicated that W14 and W68 were exposed on the CBD, consistent with their participation in binding to cellobiosyl residues on the cellulose surface.},
	keywords = {BACTERIAL CELLULASE, CELLOBIOHYDROLASES, CLONING, DNA, FLUORESCENS SUBSP CELLULOSA, FUNCTIONAL DOMAINS, GENE, PROTEIN, SEQUENCE, THERMOMONOSPORA-FUSCA},
	isbn = {0950-382X},
	url = {<Go to ISI>://A1994MW53600013},
	author = {Din, N. and Forsythe, I. J. and Burtnick, L. D. and Gilkes, N. R. and Miller, R. C. and Warren, R. A. J. and Kilburn, D. G.}
}
@article {3144,
	title = {TECHNOLOGY FOR REGENERABLE BIOSENSOR PROBES BASED ON ENZYME CELLULOSE-BINDING DOMAIN CONJUGATES},
	journal = {Biotechnology Progress},
	volume = {10},
	number = {4},
	year = {1994},
	note = {ISI Document Delivery No.: PC847Times Cited: 9Cited Reference Count: 39},
	month = {Jul-Aug},
	pages = {433-440},
	type = {Article},
	abstract = {The application of enzyme-based biosensors for on-line bioprocess monitoring and control has been slowed by problems relating to the in situ sterilizability of the probe and the stability of the enzyme component. A novel technology with the potential to address both of these difficulties is presented here, The approach is based on the reversible immobilization of enzymes conjugated with the cellulose binding domain (CBD) of cellulases from Cellulomonas fimi. A regenerable biosensor electrode can be configured with a cellulose matrix onto which the enzyme-CBD conjugate can be repeatedly loaded (bound by the CBD) and subsequently eluted by perfusing the cellulose matrix with the appropriate solution. Glucose oxidase (GOx) conjugated to CBD with glutaraldehyde was used in an experimental glucose biosensor to demonstrate the feasibility of multiple cycles of loading and elution of the conjugate. Michaelis-Menten enzyme kinetics provided an empirical model for the calibration of the experimental biosensor. The development of a computer-controlled prototype glucose biosensor and a fermentation monitoring system based on this approach is discussed.},
	keywords = {CLONING, electrode, ESCHERICHIA-COLI, EXOGLUCANASE, FIMI, GENE, GLUCOSE-OXIDASE, IMMOBILIZATION, ONLINE DETERMINATION, SEQUENCE},
	isbn = {8756-7938},
	url = {<Go to ISI>://A1994PC84700014},
	author = {Phelps, M. R. and Hobbs, J. B. and Kilburn, D. G. and Turner, R. F. B.}
}
