@article {2401,
	title = {Arabidopsis LTPG Is a Glycosylphosphatidylinositol-Anchored Lipid Transfer Protein Required for Export of Lipids to the Plant Surface},
	journal = {Plant Cell},
	volume = {21},
	number = {4},
	year = {2009},
	note = {ISI Document Delivery No.: 448XRTimes Cited: 13Cited Reference Count: 42DeBono, Allan Yeats, Trevor H. Rose, Jocelyn K. C. Bird, David Jetter, Reinhard Kunst, Ljerka Samuelsa, Lacey},
	month = {Apr},
	pages = {1230-1238},
	type = {Article},
	abstract = {Plant epidermal cells dedicate more than half of their lipid metabolism to the synthesis of cuticular lipids, which seal and protect the plant shoot. The cuticle is made up of a cutin polymer and waxes, diverse hydrophobic compounds including very-long-chain fatty acids and their derivatives. How such hydrophobic compounds are exported to the cuticle, especially through the hydrophilic plant cell wall, is not known. By performing a reverse genetic screen, we have identified LTPG, a glycosylphosphatidylinositol-anchored lipid transfer protein that is highly expressed in the epidermis during cuticle biosynthesis in Arabidopsis thaliana inflorescence stems. Mutant plant lines with decreased LTPG expression had reduced wax load on the stem surface, showing that LTPG is involved either directly or indirectly in cuticular lipid deposition. In vitro 2-p-toluidinonaphthalene-6-sulfonate assays showed that recombinant LTPG has the capacity to bind to this lipid probe. LTPG was primarily localized to the plasma membrane on all faces of stem epidermal cells in the growing regions of inflorescence stems where wax is actively secreted. These data suggest that LTPG may function as a component of the cuticular lipid export machinery.},
	keywords = {ABC TRANSPORTER, BINDING, CELLS, CUTICULAR WAX, GENE, GENOME-WIDE, MEMBRANE-PROTEINS, PHOSPHOLIPASE-D, PREDICTION SERVER, SEQUENCE TAGS},
	isbn = {1040-4651},
	url = {<Go to ISI>://000266295800020},
	author = {DeBono, A. and Yeats, T. H. and Rose, J. K. C. and Bird, D. and Jetter, R. and Kunst, L. and Samuelsa, L.}
}
@article {2343,
	title = {Fruit-Surface Flavonoid Accumulation in Tomato Is Controlled by a SIMYB12-Regulated Transcriptional Network},
	journal = {Plos Genetics},
	volume = {5},
	number = {12},
	year = {2009},
	note = {ISI Document Delivery No.: 542CTTimes Cited: 3Cited Reference Count: 58Adato, Avital Mandel, Tali Mintz-Oron, Shira Venger, Ilya Levy, Dorit Yativ, Merav Dominguez, Eva Wang, Zhonghua De Vos, Ric C. H. Jetter, Reinhard Schreiber, Lukas Heredia, Antonio Rogachev, Ilana Aharoni, Asaph},
	month = {Dec},
	pages = {23},
	type = {Article},
	abstract = {The cuticle covering plants{\textquoteright} aerial surfaces is a unique structure that plays a key role in organ development and protection against diverse stress conditions. A detailed analysis of the tomato colorless-peel y mutant was carried out in the framework of studying the outer surface of reproductive organs. The y mutant peel lacks the yellow flavonoid pigment naringenin chalcone, which has been suggested to influence the characteristics and function of the cuticular layer. Large-scale metabolic and transcript profiling revealed broad effects on both primary and secondary metabolism, related mostly to the biosynthesis of phenylpropanoids, particularly flavonoids. These were not restricted to the fruit or to a specific stage of its development and indicated that the y mutant phenotype is due to a mutation in a regulatory gene. Indeed, expression analyses specified three R2R3-MYB-type transcription factors that were significantly down-regulated in the y mutant fruit peel. One of these, SIMYB12, was mapped to the genomic region on tomato chromosome 1 previously shown to harbor the y mutation. Identification of an additional mutant allele that co-segregates with the colorless-peel trait, specific down-regulation of SlMYB12 and rescue of the y phenotype by overexpression of SlMYB12 on the mutant background, confirmed that a lesion in this regulator underlies the y phenotype. Hence, this work provides novel insight to the study of fleshy fruit cuticular structure and paves the way for the elucidation of the regulatory network that controls flavonoid accumulation in tomato fruit cuticle.},
	keywords = {AFFECTS VEGETATIVE DEVELOPMENT, ARABIDOPSIS-THALIANA, EVOLUTION, EXPRESSION, GENE, IDENTIFICATION, LIQUID-CHROMATOGRAPHY, METABOLISM, PHENYLPROPANOID BIOSYNTHESIS, REGULATOR},
	isbn = {1553-7390},
	url = {<Go to ISI>://000273469700027},
	author = {Adato, A. and Mandel, T. and Mintz-Oron, S. and Venger, I. and Levy, D. and Yativ, M. and Dominguez, E. and Wang, Z. H. and De Vos, R. C. H. and Jetter, R. and Schreiber, L. and Heredia, A. and Rogachev, I. and Aharoni, A.}
}
@article {2303,
	title = {The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {105},
	number = {39},
	year = {2008},
	note = {ISI Document Delivery No.: 386WWTimes Cited: 15Cited Reference Count: 41Wilke, Mark S. Heller, Markus Creagh, A. Louise Haynes, Charles A. McIntosh, Lawrence P. Poole, Keith Strynadka, Natalie C. J.},
	month = {Sep},
	pages = {14832-14837},
	type = {Article},
	abstract = {The intrinsic antimicrobial resistance of the opportunistic human pathogen Pseudomonas aeruginosa is compounded in mutant strains that overexpress multidrug efflux pumps such as the prominent drug-proton antiporter, MexAB-OprM. The primary regulator of the mexAB-oprM operon is the MarR family repressor, MexR. An additional repressor, NalC, also regulates mexAB-oprM by controlling expression of ArmR, an antirepressor peptide that is hypothesized to prevent the binding of MexR to its cognate DNA operator via an allosteric protein-peptide interaction. To better understand how ArmR modulates MexR, we determined the MexR-binding region of ArmR as its C-terminal 25 residues and solved the crystal structure of MexR in a 2: 1 complex with this ArmR fragment at 1.8 angstrom resolution. This structure reveals that the C-terminal residues of ArmR form a kinked alpha-helix, which occupies a pseudo-symmetrical and largely hydrophobic binding cavity located at the centre of the MexR dimer. Although the ArmR-binding cavity partially overlaps with the small molecule effector-binding sites of other MarR family members, it possesses a larger and more complex binding surface to accommodate the greater size and specific physicochemical properties of a peptide effector. Comparison with the structure of apo-MexR reveals that ArmR stabilizes a dramatic conformational change that is incompatible with DNA-binding. Thus, this work defines the structural mechanism by which ArmR allosterically derepresses MexR-controlled gene expression in P. aeruginosa and reveals important insights into the regulation of multidrug resistance.},
	keywords = {DEINOCOCCUS-RADIODURANS, DNA-BINDING, EXPRESSION, GENE, gene regulation, MarR, MARR FAMILY, MECHANISM, mexAB-oprM, MULTIDRUG EFFLUX OPERON, OPRM, PA3719, protein peptide, REPRESSOR, TRANSCRIPTIONAL REGULATOR HUCR},
	isbn = {0027-8424},
	url = {<Go to ISI>://000261914300004},
	author = {Wilke, M. S. and Heller, M. and Creagh, A. L. and Haynes, C. A. and McIntosh, L. P. and Poole, K. and Strynadka, N. C. J.}
}
@article {1149,
	title = {Quantitative proteomic analysis of sokotrasterol sulfate-stimulated primary human endothelial cells},
	journal = {Molecular \& Cellular Proteomics},
	volume = {4},
	number = {2},
	year = {2005},
	note = {ISI Document Delivery No.: 902UFTimes Cited: 9Cited Reference Count: 40},
	month = {Feb},
	pages = {191-204},
	type = {Article},
	abstract = {The endothelium forms a continuous monolayer at the interface between blood and tissue and contributes significantly to the sensing and transducing of signals between blood and tissue. New blood vessel formation, or angiogenesis, is initiated by the activation of endothelial cells and is an important process required for various pathological and physiological situations. This study used cleavable isotope-coded affinity tag reagents combined with mass spectrometry to investigate the molecular basis of a recently discovered angiogenesis-promoting steroid, sokotrasterol sulfate. Changes in the relative abundances of over 1000 proteins within human endothelial cells treated with sokotrasterol sulfate and vehicle-treated cells were identified and quantitated using this technique. A method that examines the entire ensemble of quantitative measurements was developed to identify proteins that showed a statistically significant change in relative abundance resulting from treatment with sokotrasterol sulfate. A total of 93 proteins was significantly up-regulated, and 37 were down-regulated in response to sokotrasterol sulfate stimulation of endothelial cells. Among the up-regulated proteins, several were identified that are novel to endothelial cells and are likely involved in cell communication and morphogenesis. These findings are consistent with a role for sokotrasterol sulfate in endothelial sprouting.},
	keywords = {CANCER, DIFFERENTIATION, EXPRESSION, GENE, GROWTH-FACTOR, ISCHEMIC-HEART-DISEASE, MASS-SPECTROMETRY, MOLECULE, THERAPEUTIC ANGIOGENESIS, VEGF},
	isbn = {1535-9476},
	url = {<Go to ISI>://000227381300008},
	author = {Karsan, A. and Pollet, I. and Yu, L. R. and Chan, K. C. and Conrads, T. P. and Lucas, D. A. and Andersen, R. J. and Veenstra, T.}
}
@article {1301,
	title = {RS1, a discoidin domain-containing retinal cell adhesion protein associated with X-linked retinoschisis, exists as a novel disulfide-linked octamer},
	journal = {Journal of Biological Chemistry},
	volume = {280},
	number = {11},
	year = {2005},
	note = {ISI Document Delivery No.: 905HQTimes Cited: 33Cited Reference Count: 25},
	month = {Mar},
	pages = {10721-10730},
	type = {Article},
	abstract = {RS1, also known as retinoschisin, is an extracellular protein that plays a crucial role in the cellular organization of the retina. Mutations in RS1 are responsible for X-linked retinoschisis, a common, early-onset macular degeneration in males that results in a splitting of the inner layers of the retina and severe loss in vision. RS1 is assembled and secreted from photoreceptors and bipolar cells as a homo-oligomeric protein complex. Each subunit consists of a 157-amino acid discoidin domain flanked by two small segments of 39 and 5 amino acids. To begin to understand how the structure of RS1 relates to its role in retinal cell adhesion and X-linked retinoschisis, we have determined the subunit organization and disulfide bonding pattern of RS1 by SDS gel electrophoresis, velocity sedimentation, and mass spectrometry. Our results indicate that RS1 exists as a novel octamer in which the eight subunits are joined together by Cys(59)-Cys(223) intermolecular disulfide bonds. Subunits within the octamer are further organized into dimers mediated by Cys(40)-Cys(40) bonds. These cysteines lie just outside the discoidin domain indicating that these flanking segments primarily function in the octamerization of RS1. Within the discoidin domain, two cysteine pairs (Cys(63)-Cys(219) and Cys(110)-Cys(142)) form intramolecular disulfide bonds that are important in protein folding, and one cysteine (Cys(83)) exists in its reduced state. Because mutations that disrupt subunit assembly cause X-linked retinoschisis, the assembly of RS1 into a disulfide-linked homo-octamer appears to be critical for its function as a retinal cell adhesion protein.},
	keywords = {C2 DOMAIN, COAGULATION-FACTOR-V, CRYSTAL-STRUCTURES, EXPRESSION, FACTOR-VIII, GENE, JUVENILE RETINOSCHISIS, MUTATIONS, PHOTORECEPTOR, RESOLUTION},
	isbn = {0021-9258},
	url = {<Go to ISI>://000227559600118},
	author = {Wu, W. W. H. and Wong, J. P. and Kast, J. and Molday, R. S.}
}
@article {934,
	title = {Diversity in structure and function of the Ets family PNT domains},
	journal = {Journal of Molecular Biology},
	volume = {342},
	number = {4},
	year = {2004},
	note = {ISI Document Delivery No.: 855WLTimes Cited: 17Cited Reference Count: 86},
	month = {Sep},
	pages = {1249-1264},
	type = {Article},
	abstract = {The PNT (or Pointed) domain, present within a subset of the Ets family of transcription factors, is structurally related to the larger group of SAM domains through a common tertiary arrangement of four alpha-helices. Previous studies have shown that, in contrast to the PNT. domain from Tel, this domain from Ets-1 contains an additional N-terminal helix integral to its folded structure. To further investigate the structural plasticity of the PNT domain, we have used NMR spectroscopy to characterize this domain from two additional Ets proteins, Erg and GABPalpha. These studies both define the conserved and variable features of the PNT domain, and demonstrate that the additional N-terminal helix is also present in GABPa, but not Erg. In contrast to Tel and Yan, which self-associate to form insoluble polymers, we also show that the isolated PNT domains from Ets-1, Ets-2, Erg, Fli-1, GABPalpha, and Pnt-P2 are monomeric in solution. Furthermore, these soluble PNT domains do not associate in any pair-wise combination. Thus these latter Ets family PNT domains likely mediate interactions with additional components of the cellular signaling or transcriptional machinery. (C) 2004 Elsevier Ltd. All rights reserved.},
	keywords = {ALPHA-MOTIF SAM, ASSIGNMENT, AUTOMATED, CHEMICAL-SHIFT, DIPOLAR COUPLINGS, ENDOTHELIAL-CELL DIFFERENTIATION, Erg, GABP, GENE, NMR-SPECTRA, POINTED DOMAIN, protein interactions, PROTEIN-KINASE, SAM domain, TRANSCRIPTION FACTOR},
	isbn = {0022-2836},
	url = {<Go to ISI>://000224005500015},
	author = {Mackereth, C. D. and Scharpf, M. and Gentile, L. N. and Macintosh, S. E. and Slupsky, C. M. and McIntosh, L. P.}
}
@article {800,
	title = {Yeast genome-wide drug-induced haploinsufficiency screen to determine drug mode of action},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {101},
	number = {13},
	year = {2004},
	note = {ISI Document Delivery No.: 809PNTimes Cited: 73Cited Reference Count: 23},
	month = {Mar},
	pages = {4525-4530},
	type = {Article},
	abstract = {Methods to systematically test drugs against all possible proteins in a cell are needed to identify the targets underlying their therapeutic action and unwanted effects. Here, we show that a genome-wide drug-induced haploinsufficiency screen by using yeast can reveal drug mode of action in yeast and can be used to predict drug mode of action in human cells. We demonstrate that dihydromotuporamine C, a compound in preclinical development that inhibits angiogenesis and metastasis by an unknown mechanism, targets sphingolipid metabolism. The systematic, unbiased and genome-wide nature of this technique makes it attractive as a general approach to identify cellular pathways affected by drugs.},
	keywords = {DELETION, GENE, INVASION, MUTANT, PATHWAYS, PDK1, SACCHAROMYCES-CEREVISIAE, SUPPRESSORS},
	isbn = {0027-8424},
	url = {<Go to ISI>://000220648700037},
	author = {Baetz, K. and McHardy, L. and Gable, K. and Tarling, T. and Reberioux, D. and Bryan, J. and Andersen, R. J. and Dunn, T. and Hieter, P. and Roberge, M.}
}
@article {5048,
	title = {Cdc4p, a contractile ring protein essential for cytokinesis in Schizosaccharomyces pombe, interacts with a phosphatidylinositol 4-kinase},
	journal = {Journal of Biological Chemistry},
	volume = {276},
	number = {8},
	year = {2001},
	note = {ISI Document Delivery No.: 404RUTimes Cited: 27Cited Reference Count: 35},
	month = {Feb},
	pages = {5932-5942},
	type = {Article},
	abstract = {The proposed function of Cdc4p, an essential contractile ring protein in Schizosaccharomyces pombe, is that of a myosin essential light chain. However, five conditionally lethal cdc4 alleles exhibit complementation in diploids. Such interallelic complementation is not readily explained if the sole function of Cde4p is that of a myosin essential light chain. Complementation of cdc4 alleles could occur only if different mutant forms can assemble into an active oligomeric complex or if Cdc4p has more than one essential function. To search for other proteins that may interact with Cdc4p, we performed a two-hybrid screen and identified two such candidates: one similar to Saccharomyces cerevisiae Vps27p and the other a putative phosphatidylinositol (PI) 4-kinase. finding of Cdc4p to the latter and to myosin heavy chain (Myo2p) was confirmed by immunosorbent assays. Deletion studies demonstrated interaction between the Cdc4p C-terminal domain and the PI 4-kinase C-terminal domain. Furthermore, interaction was abolished by the Cdc4p C-terminal domain point mutation, Gly(107) to Ser. This allele also causes failure of cytokinesis. Ectopic expression of the PI 4-kinase C-terminal domain caused cytokinesis defects that were most extreme in cells carrying the G107S allele. We suggest that Cdc4p plays multiple roles in cytokinesis and that interaction with a PI I-kinase may be important for contractile ring assembly and/or function.},
	keywords = {ACTOMYOSIN RING, BINDING, CELL-DIVISION CYCLE, F-ACTIN, FISSION YEAST, GENE, IDENTIFICATION, LIGHT-CHAIN, LOCALIZATION, MYOSIN HEAVY-CHAIN},
	isbn = {0021-9258},
	url = {<Go to ISI>://000167115100071},
	author = {Desautels, M. and Den Haese, J. P. and Slupsky, C. M. and McIntosh, L. P. and Hemmingsen, S. M.}
}
@article {4772,
	title = {Structural proteomics of an archaeon},
	journal = {Nature Structural Biology},
	volume = {7},
	number = {10},
	year = {2000},
	note = {ISI Document Delivery No.: 362LRTimes Cited: 188Cited Reference Count: 29},
	month = {Oct},
	pages = {903-909},
	type = {Article},
	abstract = {A set of 424 nonmembrane proteins from Methanobacterium thermoautotrophicum were cloned, expressed and purified for structural studies. Of these, similar to 20\% were found to be suitable candidates for X-ray crystallographic or NMR spectroscopic analysis without further optimization of conditions, providing an estimate of the number of the most accessible structural targets in the proteome. A retrospective analysis of the experimental behavior of these proteins suggested some simple relations between sequence and solubility. implying that data bases of protein properties will be useful in optimizing high throughput strategies. Of the first 10 structures determined, several provided clues to biochemical functions that were not detectable from sequence analysis, and in many cases these putative functions could be readily confirmed by biochemical methods. This demonstrates that structural proteomics is feasible and can play a central role in functional genomics},
	keywords = {ALIGNMENT, CLASSIFICATION, GENE, genomics, PREDICTION, PROTEIN-STRUCTURE, SCOP},
	isbn = {1072-8368},
	url = {<Go to ISI>://000089779900022},
	author = {Christendat, D. and Yee, A. and Dharamsi, A. and Kluger, Y. and Savchenko, A. and Cort, J. R. and Booth, V. and Mackereth, C. D. and Saridakis, V. and Ekiel, I. and Kozlov, G. and Maxwell, K. L. and Wu, N. and McIntosh, L. P. and Gehring, K. and Kennedy, M. A. and Davidson, A. R. and Pai, E. F. and Gerstein, M. and Edwards, A. M. and Arrowsmith, C. H.}
}
@article {4696,
	title = {The highly conserved beta-hairpin of the paired DNA-binding domain is required for assembly of Pax-Ets ternary complexes},
	journal = {Molecular and Cellular Biology},
	volume = {19},
	number = {3},
	year = {1999},
	note = {ISI Document Delivery No.: 168MYTimes Cited: 37Cited Reference Count: 57},
	month = {Mar},
	pages = {2231-2241},
	type = {Article},
	abstract = {Pax family transcription factors bind DNA through the paired domain. This domain, which is comprised of two helix-turn-helix motifs and a beta-hairpin structure, is a target of mutations in congenital disorders of mice and humans. Previously, we showed that Pax-5 (B-cell-specific activator protein) recruits proteins of the Ets proto-oncogene family to bind a composite DNA site that is essential for efficient transcription of the early-B-cell-specific mb-1 promoter. Here, evidence is provided for specific interactions between Ets-1 and the amino-terminal subdomains of Pax proteins. By tethering deletion fragments of Pax-5 to a heterologous DNA-binding domain, we show that 73 amino acids (amino acids 12 to 84) of its amino-terminal subdomain can recruit the ETS domain of Ets-1 to bind the composite site. Furthermore, an amino acid (Gln22) within the highly conserved beta-hairpin motif of Pax-5 is essential for efficient recruitment of Ets-1. The ability to recruit Ets proteins to bind DNA is a shared property of Pax proteins, as demonstrated by cooperative DNA binding of Ets-1 with sequences derived from the paired domains of Pax-2 and Pax-3. The strict conservation of sequences required for recruitment of Ets proteins suggests that Pax-Ets interactions are important for regulating transcription in diverse tissues during cellular differentiation.},
	keywords = {B-CELL-DEVELOPMENT, BOX, GENE, HMG DOMAIN, MURINE ETS-1, POINT MUTATION, STRUCTURAL BASIS, TRANSCRIPTION FACTORS, V-ETS, WAARDENBURG-SYNDROME},
	isbn = {0270-7306},
	url = {<Go to ISI>://000078697900061},
	author = {Wheat, W. and Fitzsimmons, D. and Lennox, H. and Krautkramer, S. R. and Gentile, L. N. and McIntosh, L. P. and Hagman, J.}
}
@article {4273,
	title = {Covalent adduct formation with a mutated enzyme: Evidence for a thioester intermediate in the reaction catalyzed by UDP-glucose dehydrogenase},
	journal = {Journal of the American Chemical Society},
	volume = {120},
	number = {26},
	year = {1998},
	note = {ISI Document Delivery No.: ZZ420Times Cited: 15Cited Reference Count: 23},
	month = {Jul},
	pages = {6613-6614},
	type = {Article},
	keywords = {ALDEHYDE DEHYDROGENASE, biosynthesis, GENE, GROUP-A, HYALURONIC-ACID SYNTHESIS, INSERTION, MOLECULAR CHARACTERIZATION, MUTATIONS, PNEUMONIAE, STREPTOCOCCI, TYPE-3 CAPSULAR POLYSACCHARIDE},
	isbn = {0002-7863},
	url = {<Go to ISI>://000074727600028},
	author = {Ge, X. and Campbell, R. E. and van de Rijn, I. and Tanner, M. E.}
}
@article {4405,
	title = {Structure of the Ets-1 pointed domain and mitogen-activated protein kinase phosphorylation site},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {95},
	number = {21},
	year = {1998},
	note = {ISI Document Delivery No.: 129DLTimes Cited: 84Cited Reference Count: 37},
	month = {Oct},
	pages = {12129-12134},
	type = {Article},
	abstract = {The Pointed (PNT) domain and an adjacent mitogen-activated protein (MAP) kinase phosphorylation site are defined by sequence conservation among a subset of ets transcription factors and are implicated in two regulatory strategies, protein interactions and posttranslational modifications, respectively. By using NMR, we have determined the structure of a 110-residue fragment of murine Ets-1 that includes the PNT domain and MAP kinase site. The Ets-1 PNT domain forms a monomeric five-helix bundle. The architecture is distinct from that of any known DNA- or protein-binding module, including the helix-loop-helix fold proposed for the PNT domain of the ets protein TEL. The MAP kinase site is in a highly flexible region of both the unphosphorylated and phosphorylated forms of the Ets-1 fragment. Phosphorylation alters neither the structure nor monomeric state of the PNT domain. These results suggest that the Ets-1 PNT domain functions in heterotypic protein interactions and support the possibility that target recognition is coupled to structuring of the MAP kinase site.},
	keywords = {beta, CHRONIC MYELOMONOCYTIC LEUKEMIA, FUSION, GENE, NMR, OLIGOMERIZATION, TEL, TRANSCRIPTION FACTORS, TRANSLOCATION, TROPONIN-C},
	isbn = {0027-8424},
	url = {<Go to ISI>://000076447900013},
	author = {Slupsky, C. M. and Gentile, L. N. and Donaldson, L. W. and Mackereth, C. D. and Seidel, J. J. and Graves, B. J. and McIntosh, L. P.}
}
@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 {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.}
}
