@article {2121,
	title = {Making connections for life: an in vivo map of the yeast interactome},
	journal = {Hfsp Journal},
	volume = {2},
	number = {5},
	year = {2008},
	note = {ISI Document Delivery No.: 355VHTimes Cited: 1Cited Reference Count: 28Kast, Juergen},
	month = {Oct},
	pages = {244-250},
	type = {Article},
	abstract = {Proteins are the true workhorses of any cell. To carry out specific tasks, they frequently bind other molecules in their surroundings. Due to their structural complexity and flexibility, the most diverse array of interactions is seen with other proteins. The different geometries and affinities available for such interactions typically bestow specific functions on proteins. Having available a map of protein - protein interactions is therefore of enormous importance for any researcher interested in gaining insight into biological systems at the level of cells and organisms. In a recent report, a novel approach has been employed that relies on the spontaneous folding of complementary enzyme fragments fused to two different proteins to test whether these interact in their actual cellular context [Tarassov et al., Science 320, 1465-1470 (2008)]. Genome- wide application of this protein- fragment complementation assay has resulted in the first map of the in vivo interactome of Saccharomyces cerevisiae. The current data show striking similarities but also significant differences to those obtained using other large- scale approaches for the same task. This warrants a general discussion of the current state of affairs of protein - protein interaction studies and foreseeable future trends, highlighting their significance for a variety of applications and their potential to revolutionize our understanding of the architecture and dynamics of biological systems.},
	keywords = {AMINO-ACIDS, CELL-CULTURE, COMPLEXES, CROSS-LINKING, IDENTIFICATION, MASS-SPECTROMETRY, PROTEIN-PROTEIN INTERACTIONS, QUANTIFICATION, QUANTITATION, SACCHAROMYCES-CEREVISIAE},
	isbn = {1955-2068},
	url = {<Go to ISI>://000259736700002},
	author = {Kast, J.}
}
@article {2113,
	title = {Plant surface lipid biosynthetic pathways and their utility for metabolic engineering of waxes and hydrocarbon biofuels},
	journal = {Plant Journal},
	volume = {54},
	number = {4},
	year = {2008},
	note = {ISI Document Delivery No.: 299KRTimes Cited: 12Cited Reference Count: 122Jetter, Reinhard Kunst, Ljerka},
	month = {May},
	pages = {670-683},
	type = {Review},
	abstract = {Due to their unique physical properties, waxes are high-value materials that are used in a variety of industrial applications. They are generated by chemical synthesis, extracted from fossil sources, or harvested from a small number of plant and animal species. As a result, the diversity of chemical structures in commercial waxes is low and so are their yields. These limitations can be overcome by engineering of wax biosynthetic pathways in the seeds of high-yielding oil crops to produce designer waxes for specific industrial end uses. In this review, we first summarize the current knowledge regarding the genes and enzymes generating the chemical diversity of cuticular waxes that accumulate at the surfaces of primary plant organs. We then consider the potential of cuticle biosynthetic genes for biotechnological wax production, focusing on selected examples of wax ester chain lengths and isomers. Finally, we discuss the genes/enzymes of cuticular alkane biosynthesis and their potential in future metabolic engineering of plants for the production of renewable hydrocarbon fuels.},
	keywords = {ARABIDOPSIS-THALIANA, BRASSICA-OLERACEA, chain lengths, CONDENSING ENZYME, CUTICULAR WAX, cuticular waxes, ECERIFERUM MUTANTS, EPICUTICULAR WAX, ESTERS, fatty acid elongation, FATTY ACYL-COENZYME, HYDROCARBONS, industrial products, LEAVES PISUM-SATIVUM, MOLECULAR CHARACTERIZATION, SACCHAROMYCES-CEREVISIAE},
	isbn = {0960-7412},
	url = {<Go to ISI>://000255755000012},
	author = {Jetter, R. and Kunst, L.}
}
@article {1518,
	title = {Exploring the mode-of-action of bioactive compounds by chemical-genetic profiling in yeast},
	journal = {Cell},
	volume = {126},
	number = {3},
	year = {2006},
	note = {ISI Document Delivery No.: 075KITimes Cited: 111Cited Reference Count: 68Parsons, Ainslie B. Lopez, Andres Givoni, Inmar E. Williams, David E. Gray, Christopher A. Porter, Justin Chua, Gordon Sopko, Richelle Brost, Renee L. Ho, Cheuk-Hei Wang, Jiyi Ketela, Troy Brenner, Charles Brill, Julie A. Fernandez, G. Esteban Lorenz, Todd C. Payne, Grego S. Ishihara, Satoru Ohya, Yoshikazu Andrews, Brenda Hughes, Timothy R. Frey, Brendan J. Graham, Todd R. Andersen, Raymond J. Boone, Charles},
	month = {Aug},
	pages = {611-625},
	type = {Article},
	abstract = {Discovering target and off-target effects of specific compounds is critical to drug discovery and development. We generated a compendium of "chemical-genetic interaction" profiles by testing the collection of viable yeast haploid deletion mutants for hypersensitivity to 82 compounds and natural product extracts. To cluster compounds with a similar mode-of-action and to reveal insights into the cellular pathways and proteins affected, we applied both a hierarchical clustering and a factorgram method, which allows a gene or compound to be associated with more than one group. In particular, tamoxifen, a breast cancer therapeutic, was found to disrupt calcium homeostasis and phosphatidylserine (PS) was recognized as a target for papuamide B, a cytotoxic lipopeptide with anti-HIV activity. Further, the profile of crude extracts resembled that of its constituent purified natural product, enabling detailed classification of extract activity prior to purification. This compendium should serve as a valuable key for interpreting cellular effects of novel compounds with similar activities.},
	keywords = {1, 3-BETA-D-GLUCAN SYNTHASE, BREAST-CANCER CELLS, DELETION MUTANTS, drug, EXPRESSION, GENOME-WIDE ANALYSIS, HAPLOINSUFFICIENCY, INDUCED, SACCHAROMYCES-CEREVISIAE, THEONELLA-SWINHOEI, TRANSCRIPTION FACTOR},
	isbn = {0092-8674},
	url = {<Go to ISI>://000239883400019},
	author = {Parsons, A. B. and Lopez, A. and Givoni, I. E. and Williams, D. E. and Gray, C. A. and Porter, J. and Chua, G. and Sopko, R. and Brost, R. L. and Ho, C. H. and Wang, J. Y. and Ketela, T. and Brenner, C. and Brill, J. A. and Fernandez, G. E. and Lorenz, T. C. and Payne, G. S. and Ishihara, S. and Ohya, Y. and Andrews, B. and Hughes, T. R. and Frey, B. J. and Graham, T. R. and Andersen, R. J. and Boone, C.}
}
@article {1355,
	title = {Roles for the Drs2p-Cdc50p complex in protein transport and phosphatidylserine asymmetry of the yeast plasma membrane},
	journal = {Traffic},
	volume = {7},
	number = {11},
	year = {2006},
	note = {ISI Document Delivery No.: 093GOTimes Cited: 30Cited Reference Count: 76Chen, Sophie Wang, Jiyi Muthusamy, Baby-Periyanayaki Liu, Ke Zare, Sara Andersen, Raymond J. Graham, Todd R.},
	month = {Nov},
	pages = {1503-1517},
	type = {Article},
	abstract = {Drs2p, a P-type adenosine triphosphatase required for a phosphatidylserine (PS) flippase activity in the yeast trans Golgi network (TGN), was first implicated in protein trafficking by a screen for mutations synthetically lethal with arf1 (swa). Here, we show that SWA4 is allelic to CDC50, encoding a membrane protein previously shown to chaperone Drs2p from the endoplasmic reticulum to the Golgi complex. We find that cdc50 Delta exhibits the same clathrin-deficient phenotypes as drs2 Delta, including delayed transport of carboxypeptidase Y to the vacuole, mislocalization of resident TGN enzymes and the accumulation of aberrant membrane structures. These trafficking defects precede appearance of cell polarity defects in cdc50 Delta, suggesting that the latter are a secondary consequence of disrupting Golgi function. Involvement of Drs2p-Cdc50p in PS translocation suggests a role in restricting PS to the cytosolic leaflet of the Golgi and plasma membrane. Annexin V binding and papuamide B hypersensitivity indicate that drs2 Delta or cdc50 Delta causes a loss of plasma membrane PS asymmetry. However, clathrin and other endocytosis null mutants also exhibit a comparable loss of PS asymmetry, and studies with drs2-ts and clathrin (chc1-ts) conditional mutants suggest that loss of plasma membrane asymmetry is a secondary consequence of disrupting protein trafficking.},
	keywords = {annexin V, ATPase, B, CARBOXYPEPTIDASE-Y, Cdc50p, clathrin, CLATHRIN-COATED VESICLES, Drs2p, flippase, Golgi complex, GOLGI-COMPLEX, IN-VIVO, INTRAHEPATIC CHOLESTASIS, P-type, P-TYPE ATPASES, papuamide, phosphatidylserine, PHOSPHOLIPID, PUTATIVE AMINOPHOSPHOLIPID, SACCHAROMYCES-CEREVISIAE, TRANSLOCASES, TRANSLOCATION, VACUOLAR PROTEINS},
	isbn = {1398-9219},
	url = {<Go to ISI>://000241156500008},
	author = {Chen, S. and Wang, J. Y. and Muthusamy, B. P. and Liu, K. and Zare, S. and Andersen, R. J. and Graham, T. R.}
}
@article {1103,
	title = {Dissecting the domain structure of Cdc4p, a myosin essential light chain involved in Schizosaccharomyces pombe cytokinesis},
	journal = {Biochemistry},
	volume = {44},
	number = {36},
	year = {2005},
	note = {ISI Document Delivery No.: 962ZGTimes Cited: 3Cited Reference Count: 75},
	month = {Sep},
	pages = {12136-12148},
	type = {Article},
	abstract = {Cytokinesis is the process by which one cell divides into two. Key in the cytokinetic mechanism of Schizosaccharomyces pombe is the contractile ring myosin, which consists of two heavy chains (Myo2p), two essential light chains (Cdc4p), and two regulatory light chains (R1c1p). Cdc4p is a dumbbell-shaped EF-hand protein composed of N- and C-terminal domains separated by a flexible linker. The properties of these two domains are of particular interest because each is hypothesized to have independent functions in binding different components of the cytokinesis machinery. To help define these properties, we used NMR spectroscopy to compare the structure, stability, and dynamics of the isolated N- and C-terminal domains with one another and with native Cdc4p. On the basis of invariant chemical shifts, the N-domain retains the same structure in isolation as in the context of the full-length Cdc4p, whereas the C-domain appears markedly perturbed. This perturbation results from intramolecular binding of the residual linker sequence at the N-terminus of the C-domain in a mode similar to that used by native Cdc4p to associate with target polypeptide sequences. NMR relaxation, thermal denaturation, and amide hydrogen exchange experiments also indicate that the C-domain is less stable and more dynamic than the N-domain, both in isolation and in the full-length protein. We hypothesize that these properties reflect a conformational plasticity of the C-domain, which may allow Cdc4p to interact with several regulatory or contractile ring proteins necessary for cytokinesis.},
	keywords = {CALCIUM-MODULATED PROTEINS, CONFORMATIONAL CHANGE, CONTRACTILE RING, FISSION, GROUP, HYDROGEN-EXCHANGE, MUSCLE TROPONIN-C, N-15 NMR RELAXATION, NUCLEAR MAGNETIC-RESONANCE, SACCHAROMYCES-CEREVISIAE, SKELETAL-MUSCLE, YEAST},
	isbn = {0006-2960},
	url = {<Go to ISI>://000231771500022},
	author = {Escobar-Cabrera, E. and Venkatesan, M. and Desautels, M. and Hemmingsen, S. 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.}
}
