@article {2127,
	title = {Autophagy-modulating aminosteroids isolated from the sponge Cliona celata},
	journal = {Organic Letters},
	volume = {10},
	number = {14},
	year = {2008},
	note = {ISI Document Delivery No.: 326ABTimes Cited: 4Cited Reference Count: 18Keyzers, Robert A. Daoust, Julie Davies-Coleman, Michael T. Van Soest, Rob Balgi, Aruna Donohue, Elizabeth Roberge, Michel Andersen, Raymond J.},
	month = {Jul},
	pages = {2959-2962},
	type = {Article},
	abstract = {Clionamines A-D (1-4), new aminosteroids that modulate autophagy, have been isolated from South African specimens of the sponge Cliona celata. Clionamine D (4) has an unprecedented spiro bislactone side chain.},
	keywords = {2 STEROIDAL ALKALOIDS, CORTICIUM SP, marine sponge, YEAST},
	isbn = {1523-7060},
	url = {<Go to ISI>://000257629200011},
	author = {Keyzers, R. A. and Daoust, J. and Davies-Coleman, M. T. and Van Soest, R. and Balgi, A. and Donohue, E. and Roberge, M. and Andersen, R. J.}
}
@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 {480,
	title = {Oligomerization-dependent association of the SAM domains from Schizosaccharomyces pombe Byr2 and Ste4},
	journal = {Journal of Biological Chemistry},
	volume = {277},
	number = {42},
	year = {2002},
	note = {ISI Document Delivery No.: 605EATimes Cited: 21Cited Reference Count: 46},
	month = {Oct},
	pages = {39585-39593},
	type = {Article},
	abstract = {SAM (sterile alpha motif) domains are protein-protein interaction modules found in a large number of regulatory proteins. Byr2 and Ste4 are two SAM domain-containing proteins in the mating pheromone response pathway of the fission yeast, Schizosaccharomyces pombe. Byr2 is a mitogen-activated protein kinase kinase kinase that is regulated by Ste4. Tu et al (Tu, H., Barr, M., Dong, D. L., and Wigler, M. (1997) Mol. Cell. Biol. 17, 5876-5887) showed that the isolated SAM domain of Byr2 binds a fragment of Ste4 that contains both a leucine zipper (Ste4-LZ) domain as well as a SAM domain, suggesting that Byr2-SAM and Ste4-SAM may form a hetero-oligomer. Here, we show that the individual SAM domains of Ste4 and Byr2 are monomeric at low concentrations and bind to each other in a 1:1 stoichiometry with a relatively weak dissociation constant of 56 +/- 3 mum. Inclusion of the Ste4-LZ domain, which determines the oligomeric state of Ste4, has a dramatic effect on binding affinity, however. We find that the Ste4-LZ domain is trimeric and, when included with the Ste4-SAM domain, yields a 3:1 Ste4-LZ-SAM:Byr2-SAM complex with a tight dissociation constant of 19 +/- 4 nm. These results suggest that the Ste4-LZ-SAM protein may recognize multiple binding sites on Byr2-SAM, indicating a new mode of oligomeric organization for SAM domains. The fact that high affinity binding occurs only with the addition of an oligomerization domain suggests that it may be necessary to include ancillary oligomerization modules when searching for binding partners of SAM domains.},
	keywords = {CRYSTAL-STRUCTURE, HUMAN LEUKEMIA, IDENTIFICATION, KINASE, LAC REPRESSOR, PROTEIN-KINASE, RECEPTOR, TEL, TRANSCRIPTION FACTOR, TYROSINE, YEAST},
	isbn = {0021-9258},
	url = {<Go to ISI>://000178662500069},
	author = {Ramachander, R. and Kim, C. A. and Phillips, M. L. and Mackereth, C. D. and Thanos, C. D. and McIntosh, L. P. and Bowie, J. U.}
}
@article {3984,
	title = {On-line monitoring and control of methanol concentration in shake-flask cultures of Pichia pastoris},
	journal = {Biotechnology and Bioengineering},
	volume = {56},
	number = {3},
	year = {1997},
	note = {ISI Document Delivery No.: XZ728Times Cited: 48Cited Reference Count: 19},
	month = {Nov},
	pages = {279-286},
	type = {Article},
	abstract = {The methylotrophic yeast Pichia pastoris can be used to express recombinant genes at high levels under the control of the methanol-inducible alcohol oxidase 1 (AOX1) promoter. Accurate regulation of the methanol concentration in P. pastoris cultures is necessary to maintain induction, while preventing accumulation of methanol to cytotoxic levels. We developed an inexpensive methanol sensor that uses a gas-permeable silicone rubber tube immersed in the culture medium and an organic solvent vapor detector. The sensor was used to monitor methanol concentration continuously throughout a fed-batch shake-flask culture of a P. pastoris clone producing the N-lobe of human transferrin. The sensor calibration was stable for the duration of the culture and the output signal accurately reflected the methanol concentration determined off-line by HPLC. A closed-loop control system utilizing this sensor was developed and used to maintain a 0.3\% (v/v) methanol concentration in the culture. Use of this system resulted in a fivefold increase in volumetric protein productivity over levels obtained using the conventional fed-batch protocol. (C) 1997 John Wiley \& Sons, Inc.},
	keywords = {fermentation, GENE-EXPRESSION, methanol monitoring and control, methanol sensor, methylotrophic yeast, Pichia pastoris, PROTEINS, SEMICONDUCTOR GAS SENSORS, shake-flask cultures, TRANSFERRIN, YEAST},
	isbn = {0006-3592},
	url = {<Go to ISI>://A1997XZ72800005},
	author = {Guarna, M. M. and Lesnicki, G. J. and Tam, B. M. and Robinson, J. and Radziminski, C. Z. and Hasenwinkle, D. and Boraston, A. and Jervis, E. and MacGillivray, R. T. A. and Turner, R. F. B. and Kilburn, D. G.}
}
