@article {doi:10.1002/anie.201709532,
	title = {An Eighteen-Membered Macrocyclic Ligand for Actinium-225 Targeted Alpha Therapy},
	journal = {Angewandte Chemie International Edition},
	volume = {56},
	number = {46},
	year = {2017},
	pages = {14712-14717},
	abstract = {Abstract The 18-membered macrocycle H2macropa was investigated for 225Ac chelation in targeted alpha therapy (TAT). Radiolabeling studies showed that macropa, at submicromolar concentration, complexed all 225Ac (26 kBq) in 5 min at RT. [225Ac(macropa)]+ remained intact over 7 to 8 days when challenged with either excess La3+ ions or human serum, and did not accumulate in any organ after 5 h in healthy mice. A bifunctional analogue, macropa-NCS, was conjugated to trastuzumab as well as to the prostate-specific membrane antigen-targeting compound RPS-070. Both constructs rapidly radiolabeled 225Ac in just minutes at RT, and macropa-Tmab retained >99 \% of its 225Ac in human serum after 7 days. In LNCaP xenograft mice, 225Ac-macropa-RPS-070 was selectively targeted to tumors and did not release free 225Ac over 96 h. These findings establish macropa to be a highly promising ligand for 225Ac chelation that will facilitate the clinical development of 225Ac TAT for the treatment of soft-tissue metastases.},
	keywords = {actinium, CANCER, Chelates, macrocycles, RADIOPHARMACEUTICALS},
	doi = {10.1002/anie.201709532},
	url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/anie.201709532},
	author = {Thiele, Nikki A. and Brown, Victoria and Kelly, James M. and Amor-Coarasa, Alejandro and Jermilova, Una and MacMillan, Samantha N. and Nikolopoulou, Anastasia and Ponnala, Shashikanth and Ramogida, Caterina F. and Robertson, Andrew K. H. and Rodr{\'\i}guez-Rodr{\'\i}guez, Cristina and Schaffer, Paul and Williams Jr., Clarence and Babich, John W. and Radchenko, Valery and Wilson, Justin J.}
}
@article {CNCR:CNCR28811,
	title = {Electronic cigarette use among patients with cancer: Characteristics of electronic cigarette users and their smoking cessation outcomes},
	journal = {Cancer},
	volume = {120},
	number = {22},
	year = {2014},
	pages = {3527{\textendash}3535},
	abstract = {BACKGROUND Given that continued smoking after a cancer diagnosis increases the risk of adverse health outcomes, patients with cancer are strongly advised to quit. Despite a current lack of evidence regarding their safety and effectiveness as a cessation tool, electronic cigarettes (E-cigarettes) are becoming increasingly popular. To guide oncologists{\textquoteright} communication with their patients about E-cigarette use, this article provides what to the authors{\textquoteright} knowledge is the first published clinical data regarding E-cigarette use and cessation outcomes among patients with cancer. METHODS A total of 1074 participants included smokers (patients with cancer) who recently enrolled in a tobacco treatment program at a comprehensive cancer center. Standard demographic, tobacco use history, and follow-up cessation outcomes were assessed. RESULTS A 3-fold increase in E-cigarette use was observed from 2012 to 2013 (10.6\% vs 38.5\%). E-cigarette users were more nicotine dependent than nonusers, had more prior quit attempts, and were more likely to be diagnosed with thoracic and head or neck cancers. Using a complete case analysis, E-cigarette users were as likely to be smoking at the time of follow-up as nonusers (odds ratio, 1.0; 95\% confidence interval, 0.5-1.7). Using an intention-to-treat analysis, E-cigarette users were twice as likely to be smoking at the time of follow-up as nonusers (odds ratio, 2.0; 95\% confidence interval, 1.2-3.3). CONCLUSIONS The high rate of E-cigarette use observed is consistent with recent articles highlighting increased E-cigarette use in the general population. The current longitudinal findings raise doubts concerning the usefulness of E-cigarettes for facilitating smoking cessation among patients with cancer. Further research is needed to evaluate the safety and efficacy of E-cigarettes as a cessation treatment for patients with cancer. Cancer 2014;120:3527{\textendash}3535. {\textcopyright} 2014 American Cancer Society.},
	keywords = {CANCER, electronic cigarettes (E-cigarettes), smoking cessation, tobacco},
	issn = {1097-0142},
	doi = {10.1002/cncr.28811},
	url = {http://dx.doi.org/10.1002/cncr.28811},
	author = {Borderud, Sarah P. and Li, Yuelin and Burkhalter, Jack E. and Sheffer, Christine E. and Ostroff, Jamie S.}
}
@article {2376,
	title = {Plectosphaeroic Acids A, B, and C, Indoleamine 2,3-Dioxygenase Inhibitors Produced in Culture by a Marine Isolate of the Fungus Plectosphaerella cucumerina},
	journal = {Organic Letters},
	volume = {11},
	number = {14},
	year = {2009},
	note = {ISI Document Delivery No.: 472NMTimes Cited: 1Cited Reference Count: 29Carr, Gavin Tay, Wendy Bottriell, Helen Andersen, Sarah K. Mauk, A. Grant Andersen, Raymond J.},
	month = {Jul},
	pages = {2996-2999},
	type = {Article},
	abstract = {Laboratory cultures of the fungus Plectosphaerella cucumerina obtained from marine sediments collected in Barkley Sound, British Columbia, yielded the novel alkaloids plectosphaeroic acids A (1) to C (3). The alkaloids 1-3 are inhibitors of indoleamine 2,3-dioxygenase (IDO).},
	keywords = {CANCER, CELLS, chemotherapy, EXIGUAMINE-A, EXPRESSION, IDO, MECHANISM, METABOLITES, SUPPRESSION, TRYPTOPHAN DEGRADATION},
	isbn = {1523-7060},
	url = {<Go to ISI>://000268138800011},
	author = {Carr, G. and Tay, W. and Bottriell, H. and Andersen, S. K. and Mauk, A. G. and Andersen, R. J.}
}
@article {2298,
	title = {Biomimetic synthesis of the IDO inhibitors exiguamine A and B},
	journal = {Nature Chemical Biology},
	volume = {4},
	number = {9},
	year = {2008},
	note = {ISI Document Delivery No.: 339SNTimes Cited: 7Cited Reference Count: 19Volgraf, Matthew Lumb, Jean-Philip Brastianos, Harry C. Carr, Gavin Chung, Marco K. W. Muenzel, Martin Mauk, A. Grant Andersen, Raymond J. Trauner, Dirk},
	month = {Sep},
	pages = {535-537},
	type = {Article},
	abstract = {Biomimetic synthesis is an attempt to assemble natural products along biosynthetic lines without recourse to the full enzymatic machinery of nature. We exemplify this with a total synthesis of exiguamine A and the newly isolated natural product exiguamine B. The most noteworthy feature of this work is an oxidative endgame drawing from the complex chemistry of catecholamines, which allows for ready access to a new class of nanomolar indoleamine-2,3-dioxygenase inhibitors.},
	keywords = {3-DIOXYGENASE, ANALOGS, CANCER, CASCADE, CELLS, ELECTROCYCLIZATIONS, EXPRESSION, INDOLEAMINE 2},
	isbn = {1552-4450},
	url = {<Go to ISI>://000258597700011},
	author = {Volgraf, M. and Lumb, J. P. and Brastianos, H. C. and Carr, G. and Chung, M. K. W. and Munzel, M. and Mauk, A. G. and Andersen, R. J. and Trauner, D.}
}
@article {2037,
	title = {Synthesis of indoleamine 2,3-dioxygenase inhibitory analogues of the sponge alkaloid exiguamine A},
	journal = {Journal of Medicinal Chemistry},
	volume = {51},
	number = {9},
	year = {2008},
	note = {ISI Document Delivery No.: 295USTimes Cited: 17Cited Reference Count: 20Carr, Gavin Chung, Marco K. W. Mauk, A. Grant Andersen, Raymond J.},
	month = {May},
	pages = {2634-2637},
	type = {Article},
	abstract = {Synthetic analogues of the sponge natural product exiguamine A (3) have been prepared and evaluated for their ability to inhibit indoleamine 2,3-dioxygenase in vitro.},
	keywords = {CANCER, CATABOLISM, CELLS, chemotherapy, EXPRESSION, IDO, IMMUNE TOLERANCE, MECHANISM, SMALL-MOLECULE INHIBITORS, TRYPTOPHAN DEGRADATION},
	isbn = {0022-2623},
	url = {<Go to ISI>://000255500000008},
	author = {Carr, G. and Chung, M. K. W. and Mauk, A. G. and Andersen, R. J.}
}
@article {2287,
	title = {Toward [F-18]-labeled aryltrifluoroborate radiotracers: In vivo positron emission tomography imaging of stable aryltrifluoroborate clearance in mice},
	journal = {Journal of the American Chemical Society},
	volume = {130},
	number = {36},
	year = {2008},
	note = {ISI Document Delivery No.: 344TPTimes Cited: 15Cited Reference Count: 35Ting, Richard Harwig, Curtis auf dem Keller, Ulrich McCormick, Siobhan Austin, Pamela Overall, Christopher M. Adam, Michael J. Ruth, Thomas J. Perrin, David M.},
	month = {Sep},
	pages = {12045-12055},
	type = {Article},
	abstract = {The use of a boronic ester as a captor of aqueous [F-18]-fluoride has been previously suggested as a means of labeling biomolecules in one step for positron emission tomography (PET) imaging. For this approach to be seriously considered, the [F-18]-labeled trifluoroborate should be humorally stable such that it neither leaches free [F-18]-fluoride to the bone nor accumulates therein. Herein, we have synthesized a biotinylated boronic ester that is converted to the corresponding trifluoroborate salt in the presence of aqueous [F-18]-fluoride. In keeping with its in vitro aqueous kinetic stability at pH 7.5, the trifluoroborate appears to clear in vivo quite rapidly to the bladder as the stable trifluoroborate salt with no detectable leaching of free [F-18]-fluoride to the bone. When this labeled biotin is preincubated with avidin, the pharmacokinetic clearance of the resulting complex is visibly altered. This work validates initial claims that boronic esters are potentially useful as readily labeled precursors to [F-18]-PET reagents.},
	keywords = {apoptosis, BIODISTRIBUTION, CANCER, DESIGN, F-18, MICROPET, NO-CARRIER, PEPTIDES, PET, STABILITY},
	isbn = {0002-7863},
	url = {<Go to ISI>://000258950500044},
	author = {Ting, R. and Harwig, C. and auf dem Keller, U. and McCormick, S. and Austin, P. and Overall, C. M. and Adam,Michael J. and Ruth, T. J. and Perrin,David M.}
}
@article {2287,
	title = {Toward [F-18]-labeled aryltrifluoroborate radiotracers: In vivo positron emission tomography imaging of stable aryltrifluoroborate clearance in mice},
	journal = {Journal of the American Chemical Society},
	volume = {130},
	number = {36},
	year = {2008},
	note = {ISI Document Delivery No.: 344TPTimes Cited: 15Cited Reference Count: 35Ting, Richard Harwig, Curtis auf dem Keller, Ulrich McCormick, Siobhan Austin, Pamela Overall, Christopher M. Adam, Michael J. Ruth, Thomas J. Perrin, David M.},
	month = {Sep},
	pages = {12045-12055},
	type = {Article},
	abstract = {The use of a boronic ester as a captor of aqueous [F-18]-fluoride has been previously suggested as a means of labeling biomolecules in one step for positron emission tomography (PET) imaging. For this approach to be seriously considered, the [F-18]-labeled trifluoroborate should be humorally stable such that it neither leaches free [F-18]-fluoride to the bone nor accumulates therein. Herein, we have synthesized a biotinylated boronic ester that is converted to the corresponding trifluoroborate salt in the presence of aqueous [F-18]-fluoride. In keeping with its in vitro aqueous kinetic stability at pH 7.5, the trifluoroborate appears to clear in vivo quite rapidly to the bladder as the stable trifluoroborate salt with no detectable leaching of free [F-18]-fluoride to the bone. When this labeled biotin is preincubated with avidin, the pharmacokinetic clearance of the resulting complex is visibly altered. This work validates initial claims that boronic esters are potentially useful as readily labeled precursors to [F-18]-PET reagents.},
	keywords = {apoptosis, BIODISTRIBUTION, CANCER, DESIGN, F-18, MICROPET, NO-CARRIER, PEPTIDES, PET, STABILITY},
	isbn = {0002-7863},
	url = {<Go to ISI>://000258950500044},
	author = {Ting, R. and Harwig, C. and auf dem Keller, U. and McCormick, S. and Austin, P. and Overall, C. M. and Adam,Michael J. and Ruth, T. J. and Perrin,David M.}
}
@article {1577,
	title = {Design of targeting ligands in medicinal inorganic chemistry},
	journal = {Chemical Society Reviews},
	volume = {35},
	number = {6},
	year = {2006},
	note = {ISI Document Delivery No.: 047UHTimes Cited: 58Cited Reference Count: 51},
	pages = {534-544},
	type = {Review},
	abstract = {This tutorial review will highlight recent advances in medicinal inorganic chemistry pertaining to the use of multifunctional ligands for enhanced effect. Ligands that adequately bind metal ions and also include specific targeting features are gaining in popularity due to their ability to enhance the efficacy of less complicated metal-based agents. Moving beyond the traditional view of ligands modifying reactivity, stabilizing specific oxidation states, and contributing to substitution inertness, we will discuss recent work involving metal complexes with multifunctional ligands that target specific tissues, membrane receptors, or endogenous molecules, including enzymes.},
	keywords = {CANCER, COMPLEXES, FLUORESCENCE, GADOLINIUM, IN-VITRO, PARACEST AGENTS, PROTEINS, RECEPTOR, therapy, TRANSPORT},
	isbn = {0306-0012},
	url = {<Go to ISI>://000237903700005},
	author = {Storr, T. and Thompson, K. H. and Orvig, Chris}
}
@article {1522,
	title = {Indoleamine 2,3-dioxygenase inhibitors from the Northeastern Pacific marine hydroid Garveia annulata},
	journal = {Journal of Natural Products},
	volume = {69},
	number = {10},
	year = {2006},
	note = {ISI Document Delivery No.: 098ZQTimes Cited: 17Cited Reference Count: 20Pereira, Alban Vottero, Eduardo Roberge, Michel Mauk, A. Grant Andersen, Raymond J.},
	month = {Oct},
	pages = {1496-1499},
	type = {Article},
	abstract = {Crude extracts of the marine hydroid Garveia annulata show potent inhibition of indoleamine 2,3-dioxygenase (IDO). Fractionation of the extract led to the identification of the new polyketides annulin C (1), 2-hydroxygarveatin E (4), garveatin E (5), and garvin C (9). Annulins A (2), B (3), and C (1) were found to be submicromolar inhibitors of IDO.},
	keywords = {CANCER, chemotherapy, ENZYME, HUMAN LENS, MECHANISM, METABOLITES, NUCLEAR CATARACT, REJECTION, TOLERANCE, TRYPTOPHAN DEGRADATION},
	isbn = {0163-3864},
	url = {<Go to ISI>://000241562700025},
	author = {Pereira, A. and Vottero, E. and Roberge, M. and Mauk, A. G. and Andersen, R. J.}
}
@article {1271,
	title = {Modulation of the G(2) cell cycle checkpoint by sesquiterpene lactones psilostachyins A and C isolated from the common ragweed Ambrosia artemisiifolia},
	journal = {Planta Medica},
	volume = {71},
	number = {10},
	year = {2005},
	note = {ISI Document Delivery No.: 985TLTimes Cited: 8Cited Reference Count: 30},
	month = {Oct},
	pages = {938-943},
	type = {Article},
	abstract = {A phenotypic cell-based assay for inhibitors of the G(2) DNA damage checkpoint was used to screen plant extracts from the US National Cancer Institute Natural Products Repository. It revealed activity in a methanol extract from the common ragweed Ambrosia artemisiifolia. Assay-guided fractionation led to the identification of the sesquiterpene lactones psilostachyins A and C as novel checkpoint inhibitors. Elimination of their alpha,beta-unsaturated carbonyl group caused a loss of activity, suggesting that the compounds can bind covalently to target proteins through Michael addition. Psilostachyins A and C also blocked cells in mitosis and caused the formation of aberrant microtubule spindles. However, the compounds did not interfere with microtubule polymerization in vitro. The related sesquiterpene lactones psilostachyin 13, paulitin and isopaulitin were also isolated from the same extract but showed no checkpoint inhibition. The identification of the target(s) of psilostachyins A and C may provide further insight into the signalling pathways involved in cell cycle arrest and mitotic progression.},
	keywords = {Ambrosia artemisiffolia, CAFFEINE, CANCER, cell cycle, checkpoint, CHK1, DILACTONE, DNA-DAMAGE CHECKPOINT, G(2) phase, INHIBITION, KINASE, MCF-7 CELLS, mitosis, P53, PROTEIN, UCN-01},
	isbn = {0032-0943},
	url = {<Go to ISI>://000233401400009},
	author = {Sturgeon, C. M. and Craig, K. and Brown, C. and Rundle, N. T. and Andersen, R. J. and Roberge, M.}
}
@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 {1052,
	title = {Radiohalogens for imaging and therapy},
	journal = {Chemical Society Reviews},
	volume = {34},
	number = {2},
	year = {2005},
	note = {ISI Document Delivery No.: 890PETimes Cited: 34Cited Reference Count: 41},
	pages = {153-163},
	type = {Review},
	abstract = {Radiohalogens play a very important role in radiopharmaceuticals used for medical imaging ( now referred to as molecular imaging) and therapy applications. Development of new radiopharmaceuticals that have radiohalogens incorporated requires an understanding of parameters that are unique to chemistry involving these radionuclides. Those parameters include requirement for production and purification of the halogen radionuclides, as well as development of reaction conditions for use with high specific activity short-lived radionuclides. In this tutorial review, several radiohalogens, their radiolabeling chemistry and their application to medical imaging and therapy are discussed.},
	keywords = {BRAIN, CANCER, F-18, LIGAND, MONOCLONAL-ANTIBODIES, PET, POSITRON-EMISSION-TOMOGRAPHY, RADIOIODINATION, RADIOTHERAPY, SPECT},
	isbn = {0306-0012},
	url = {<Go to ISI>://000226522500005},
	author = {Adam,Michael J. and Wilbur, D. S.}
}
@article {896,
	title = {Inhibition of Chk1 by the G(2) DNA damage checkpoint inhibitor isogranulatimide},
	journal = {Molecular Cancer Therapeutics},
	volume = {3},
	number = {10},
	year = {2004},
	note = {ISI Document Delivery No.: 862KBTimes Cited: 40Cited Reference Count: 40},
	month = {Oct},
	pages = {1221-1227},
	type = {Article},
	abstract = {Inhibitors of the G(2) DNA damage checkpoint can selectively sensitize cancer cells with mutated p53 to killing by DNA-damaging agents. Isogranulatimide is a G2 checkpoint inhibitor containing a unique indole/maleimide/ imidazole skeleton identified in a phenotypic cell-based screen; however, the mechanism of action of isogranulatimide is unknown. Using natural and synthetic isogranulatimide analogues, we show that the imide nitrogen and a basic nitrogen at position 14 or 15 in the imidazole ring are important for checkpoint inhibition. Isogranulatimide shows structural resemblance to the aglycon of UCN-01, a potent bisindolemaleimide inhibitor of protein kinase Cbeta (IC50, 0.001 mumol/L) and of the checkpoint kinase Chk1 (IC50, 0.007 mumol/L). In vitro kinase assays show that isogranulatimide inhibits Chk1 (IC50, 0.1 mumol/L) but not protein kinase Cbeta. Of 13 additional protein kinases tested, isogranulatimide significantly inhibits only glycogen synthase kinase-3beta (IC50, 0.5 mumol/L). We determined the crystal structure of the Chk1 catalytic domain complexed with isogranulatimicle. Like UCN-01, isogranulatimide binds in the ATP-binding pocket of Chk1 and hydrogen bonds with the backbone carbonyl oxygen of Glu(85) and the amide nitrogen Of Cys(87). Unlike UCN-01, the basic N15 of isogranulatimide interacts with Glu(17), causing a conformation change in the kinase glycine-rich loop that may contribute importantly to inhibition. The mechanism by which isogranulatimide inhibits Chk1 and its favorable kinase selectivity profile make it a promising candidate for modulating checkpoint responses in tumors for therapeutic benefit.},
	keywords = {7-HYDROXYSTAUROSPORINE UCN-01, ACTIVATION, CANCER, CELL-CYCLE, DEPENDENT PROTEIN-KINASE, IDENTIFICATION, MECHANISMS, PHOSPHORYLATION, SPECIFICITY, SUBSTRATE},
	isbn = {1535-7163},
	url = {<Go to ISI>://000224488400006},
	author = {Jiang, X. X. and Zhao, B. G. and Britton, R. and Lim, L. Y. and Leong, D. and Sanghera, J. S. and Zhou, B. B. S. and Piers, E. and Andersen, R. J. and Roberge, M.}
}
@article {941,
	title = {The tumor invasion inhibitor dihydromotuporamine C activates RHO, remodels stress fibers and focal adhesions, and stimulates sodium-proton exchange},
	journal = {Cancer Research},
	volume = {64},
	number = {4},
	year = {2004},
	note = {ISI Document Delivery No.: 778MKTimes Cited: 23Cited Reference Count: 45},
	month = {Feb},
	pages = {1468-1474},
	type = {Article},
	abstract = {The motuporamines are macrocyclic alkaloids that inhibit tumor cell invasion by an, as yet, unknown mechanism. A structure-activity study recently identified dihydromotuporamine C (dhMotC) as a highly active and readily synthesized analogue. Here, we show that dhMotC causes subtle cytoskeletal alterations in highly invasive MDA231 breast tumor cells that include an increase in the thickness and number of cytoplasmic actin stress fibers. Experiments with serum-starved Swiss 3T3 fibroblasts showed that micromolar concentrations of dhMotC that inhibit tumor cell invasion induce the formation of new stress fibers and large focal adhesion complexes that are dispersed around the entire cell periphery. dhMotC treatment of Swiss 3T3 cells also initiates a strong, long-lived activation of the small GTP-binding protein Rho, and it stimulates Rho kinase-dependent sodium-proton exchanger activity. Liposome-mediated cell loading of C3 exoenzyme prevents dhMotC-mediated Rho activation and stress fiber formation in 3T3 cells. C3 exoenzyme loading also reestablishes elongated MDA231 breast tumor cell invasion in the presence of dhMotC. Taken together, these results indicate that the ability to activate Rho is one important determinant of the anti-invasive activity of dhMotC.},
	keywords = {ANGIOGENESIS, CANCER, CELL-MIGRATION, FARNESYLTRANSFERASE INHIBITORS, GROWTH, GTP-BINDING PROTEIN, GTPASES, KINASE, MEMBRANE PROTRUSION, PROGRESSION},
	isbn = {0008-5472},
	url = {<Go to ISI>://000189245200037},
	author = {McHardy, L. M. and Sinotte, R. and Troussard, A. and Sheldon, C. and Church, J. and Williams, D. E. and Andersen, R. J. and Dedhar, S. and Roberge, M. and Roskelley, C. D.}
}
@article {671,
	title = {HTI-286, a synthetic analogue of the tripeptide hemiasterlin, is a potent antimicrotubule agent that circumvents P-glycoprotein-mediated resistance in vitro and in vivo},
	journal = {Cancer Research},
	volume = {63},
	number = {8},
	year = {2003},
	note = {ISI Document Delivery No.: 668TETimes Cited: 57Cited Reference Count: 32},
	month = {Apr},
	pages = {1838-1845},
	type = {Article},
	abstract = {Hemiasterlin is a natural product derived from marine sponges that, like other structurally diverse peptide-like molecules, binds to the Vincapeptide site in tubulin, disrupts normal microtubule dynamics, and, at stoichiometric amounts, depolymerizes microtubules. Total synthesis of hemiasterlin and its analogues has been accomplished, and optimal pharmacological features of the series have been explored. The biological profile of one analogue, HTI-286, was studied here. HTI-286 inhibited the polymerization of purified tubulin, disrupted microtubule organization in cells, and induced mitotic arrest, as well as apoptosis. HTI-286 was a potent inhibitor of proliferation (mean IC50 = 2.5 +/- 2.1 nm in 18 human tumor cell lines) and had substantially less interaction with multidrug resistance protein (P-glycoprotein) than currently used antimicrotubule agents, including paclitaxel, docetaxel, vinorelbine, or vinblastine. Resistance to HTI-286 was not detected in cells overexpressing the drug transporters MRP1 or MXR. In athymic mice implanted with human tumor xenografts, HTI-286 administered i.v. in saline inhibited the growth of numerous human tumors derived from carcinoma of the skin, breast, prostate, brain, and colon. Marked tumor regression was observed when used on established tumors that were >1 gram in size. Moreover, HTI-286 inhibited the growth of human tumor xenografts (e.g., HCT-15, DLD-1, MX-1W, and KB-8-5) where paclitaxel and vincristine were ineffective because of inherent or acquired resistance associated with P-glycoprotein. Efficacy was also achieved with p.o. administration of HTI-286. These data suggest that HTI-286 has excellent preclinical properties that may translate into superior clinical activity, as well as provide a useful synthetic reagent to probe the drug contact sites of peptide-like molecules that interact with tubulin.},
	keywords = {ADRIAMYCIN, BETA-TUBULIN, CANCER, CARCINOMA-CELLS, CYTOTOXIC PEPTIDES, DOLASTATIN ANALOG, DRUG-RESISTANCE, EXPRESSION, MECHANISMS, MULTIDRUG-RESISTANCE},
	isbn = {0008-5472},
	url = {<Go to ISI>://000182308600021},
	author = {Loganzo, F. and Discafani, C. M. and Annable, T. and Beyer, C. and Musto, S. and Hari, M. and Tan, X. Z. and Hardy, C. and Hernandez, R. and Baxter, M. and Singanallore, T. and Khafizova, G. and Poruchynsky, M. S. and Fojo, T. and Nieman, J. A. and Ayral-Kaloustian, S. and Zask, A. and Andersen, R. J. and Greenberger, L. M.}
}
@article {775,
	title = {Ruthenium(II) acetylacetonato-sulfoxide complexes},
	journal = {Inorganic Chemistry Communications},
	volume = {6},
	number = {8},
	year = {2003},
	note = {ISI Document Delivery No.: 707PBTimes Cited: 9Cited Reference Count: 35},
	month = {Aug},
	pages = {996-1000},
	type = {Article},
	abstract = {The water-soluble Ru-II acetylacetonato-sulfoxide complexes, cis-Ru(acac)(2)(DMSO)(2) (1) and Ru(acac)(2)(meso-BESE) (2), were synthesized (BESE = 1,2-bis(ethylsulfinyl)ethane = EtS(O)(CH2)(2)S(O)Et). Both complexes were characterized by H-1 and C-13{H-1} NMR, UV-Vis, and IR spectroscopies, as well as MS, elemental analysis, solution conductivity, and cyclic voltammetry, while the molecular structure of 2 was determined also by X-ray crystallography. All sulfoxide ligands are S-bonded. The complexes were tested against human breast cancer cells (MDA-MB-435S) using an in vitro MTT assay, a colorimetric determination of cell viability; IC50 values of >2000 and 1500 +/- 100 muM were determined for 1 and 2, respectively, while cisplatin exhibits an IC50 value of 30 +/- 5 muM. (C) 2003 Elsevier Science B.V. All rights reserved.},
	keywords = {2D NMR spectroscopy, acetylacetonato, ANTITUMOR-ACTIVITY, CANCER, CHEMISTRY, COLORIMETRIC ASSAY, COORDINATION, INVITRO, PRECURSOR, ruthenium, STRUCTURAL-CHARACTERIZATION, sulfoxides, TUMOR CELL-LINES},
	isbn = {1387-7003},
	url = {<Go to ISI>://000184518100004},
	author = {Wu, A. and Kennedy, David C and Patrick, B. O. and James, Brian R.}
}
@article {641,
	title = {The synthesis, structural characterization, and in vitro anti-cancer activity of chloro(p-cymene) complexes of ruthenium(II) containing a disulfoxide ligand},
	journal = {Inorganica Chimica Acta},
	volume = {352},
	year = {2003},
	note = {ISI Document Delivery No.: 711FATimes Cited: 39Cited Reference Count: 47},
	month = {Aug},
	pages = {238-246},
	type = {Article},
	abstract = {Two diruthenium(II) complexes [RuCl2(p-cymene)](2)(mu-BESE) (1), [RuCl2(p-cymene)](2)(mu-BESP) (2), and the mononuclear salt [RuCl(p-cymene)(BESE)]PF6 (3), containing the disulfoxides BESE and BESP, were synthesized and characterized by elemental analysis, and NMR and IR spectroscopies, and were shown to contain S-bound sulfoxide groups; the disulfoxides are EtS(O)(CH2)(n) S(O)Et, where n = 2 (BESE) or 3 (BESP). Complexes 1 and 3 were also characterized by X-ray crystallography. Preliminary in vitro tests of I and 3 were conducted using the MTT assay, which measures mitochondrial dehydrogenase activity as an indication of cell viability; these complexes showed in vitro anti-cancer activity against a human mammary cancer cell line (MDA-MB-435s) with IC50 values of 360 and 55 muM, respectively. (C) 2003 Elsevier B.V. All rights reserved.},
	keywords = {anti-cancer activity, arene complexes, CANCER, cell, COMPLEX, COORDINATION, crystal structures, CRYSTAL-STRUCTURE, DIMETHYL-SULFOXIDE LIGAND, DIRUTHENIUM(II), disulfoxide ligands, INHIBITION, p-Cymene complexes, RADIOSENSITIZING ACTIVITY, ruthenium complexes, SOLUTION CHEMISTRY},
	isbn = {0020-1693},
	url = {<Go to ISI>://000184727900029},
	author = {Huxham, L. A. and Cheu, E. L. S. and Patrick, B. O. and James, Brian R.}
}
@article {543,
	title = {Motuporamines, anti-invasion and anti-angiogenic alkaloids from the marine sponge Xestospongia exigua (Kirkpatrick): Isolation, structure elucidation, analogue synthesis, and conformational analysis},
	journal = {Journal of Organic Chemistry},
	volume = {67},
	number = {1},
	year = {2002},
	note = {ISI Document Delivery No.: 509MHTimes Cited: 32Cited Reference Count: 28},
	month = {Jan},
	pages = {245-258},
	type = {Article},
	abstract = {Extracts of the sponge Xestospongia exigua collected in Papua New Guinea were positive in a new assay for anti-invasion activity. Bioassay-guided fractionation led to the identification of the three known motuporamines A (1), B (2), and C (3) along with the new motuporamines D (4), E (5), and F (6) and a mixture of G, H, and 1 (15). Motuporamines A (1), B (2), and C (3) and the mixture of G, H, and 1 (15) were responsible for the anti-invasion activity of the crude extract. Motuporamine C (3) has also been found to be anti-angiogenic. A series of analogues of the motuporamines have been synthesized and evaluated for anti-invasive activity. These SAR results revealed that a saturated 15-membered cyclic amine fused to the natural motuporamine diamine side chain (13) represented the optimal structure for anti-invasive activity in this family. Single-crystal X-ray diffraction analysis of one of the analogues 20 showed that in the solid state its 16-membered macrocyclic amine fragment adopted the [4444] quadrangular conformation predicted by calculations to be the lowest energy conformation for the corresponding cycloalkane, cyclobexadecane. These data along with literature X-ray data and conformational analysis for derivatives of azacyclotridecane have been used as precedents for predicting the lowest energy ring conformations of other motuporamines. The SAR data from the natural and synthetic motuporamines have been combined with the conformational analyses to provide an outline of the functionality and shape required for activity in this family of alkaloids and to design a new analogue 49 that showed good anti-invasion activity.},
	keywords = {A-C, CANCER, INHIBITOR, METASTASIS, METATHESIS, TUMOR-GROWTH},
	isbn = {0022-3263},
	url = {<Go to ISI>://000173151200039},
	author = {Williams, D. E. and Craig, K. S. and Patrick, B. and McHardy, L. M. and Van Soest, R. and Roberge, M. and Andersen, R. J.}
}
@article {5209,
	title = {Coordination chemistry of vanadium in metallopharmaceutical candidate compounds},
	journal = {Coordination Chemistry Reviews},
	volume = {219},
	year = {2001},
	note = {ISI Document Delivery No.: 478JQTimes Cited: 138Cited Reference Count: 119},
	month = {Sep-Oct},
	pages = {1033-1053},
	type = {Review},
	abstract = {The discovery of vanadium{\textquoteright}s insulin-like behaviour in vitro, and later of the orally available glucose- and lipid-lowering capability of these same compounds in vivo, has stimulated renewed interest in vanadium coordination chemistry. Besides the anti-diabetic effects for which it is now so well known, vanadium also exhibits a number of other therapeutic effects including anti-tumour and anti-inflammatory activities. In this review, emphasis will be on the most recent developments in the coordination chemistry of vanadium(III), (IV) and (V), as related to development of these compounds for pharmaceutical use. How best to measure bioactivity and the pharmaceutical relevance of accompanying increased oxidative stress will also be considered. (C) 2001 Elsevier Science B.V. All rights reserved.},
	keywords = {bioactivity, BIOLOGICAL-ACTIVITY, CANCER, CRYSTAL-STRUCTURE, Diabetes mellitus, DIABETES-MELLITUS, ESEEM, INSULIN-LIKE ACTIVITIES, OXIDATIVE STRESS, OXOVANADIUM(IV) COMPLEXES, OXYGEN-BRIDGED DIMER, PEROXO HETEROLIGAND VANADATES(V), pharmaceutical agents, RAY, SPECTROSCOPIC PROPERTIES, structure-activity relationships, TYROSINE PHOSPHORYLATION, vanadium complexes},
	isbn = {0010-8545},
	url = {<Go to ISI>://000171343600035},
	author = {Thompson, K. H. and Orvig, Chris}
}
@article {5179,
	title = {Inhibition of tumor cell invasion and angiogenesis by motuporamines},
	journal = {Cancer Research},
	volume = {61},
	number = {18},
	year = {2001},
	note = {ISI Document Delivery No.: 474LKTimes Cited: 41Cited Reference Count: 26},
	month = {Sep},
	pages = {6788-6794},
	type = {Article},
	abstract = {Tissue invasion is an important determinant of angiogenesis and metastasis and constitutes an attractive target for cancer therapy. We have developed an assay to identify agents that inhibit invasion by mechanisms other than inhibition of cell attachment or cytotoxicity. A screen of marine sponge extracts identified motuporamines as micromolar inhibitors of invasion of basement membrane gels by MDA-231 breast carcinoma, PC-3 prostate carcinoma, and U-87 and U-251 glioma cells. Motuporamine C inhibits cell migration in monolayer cultures and impairs actin-mediated membrane ruffling at the leading edge of lamellae. Motuporamine C also reduces beta1-integrin activation, raising the possibility that it interferes with "inside-out" signaling to integrins. In addition, motuporamine C inhibits angiogenesis in an in vitro sprouting assay with human endothelial cells and an in vivo chick chorioallantoic membrane assay. The motuporamines show little or no toxicity or inhibition of cell proliferation, and they are structurally simple and easy to synthesize, making them attractive drug candidates.},
	keywords = {CANCER, GTPASES, INTEGRINS, MIGRATION},
	isbn = {0008-5472},
	url = {<Go to ISI>://000171108400030},
	author = {Roskelley, C. D. and Williams, D. E. and McHardy, L. M. and Leong, K. G. and Troussard, A. and Karsan, A. and Andersen, R. J. and Dedhar, S. and Roberge, M.}
}
@article {4903,
	title = {Improved synthesis of isogranulatimide, a G2 checkpoint inhibitor. Syntheses of didemnimide C, isodidemnimide A, neodidemnimide A, 17-methylgranulatimide, and isogranulatimides A-C},
	journal = {Journal of Organic Chemistry},
	volume = {65},
	number = {2},
	year = {2000},
	note = {ISI Document Delivery No.: 276YFTimes Cited: 44Cited Reference Count: 35},
	month = {Jan},
	pages = {530-535},
	type = {Article},
	abstract = {A concise, improved synthesis of isogranulatimide (6), a naturally occurring substance with G2 checkpoint inhibition activity, is described. Also reported are the syntheses of didemnimide C (18), isodidemnimide A (24), neodidemnimide A (36), 17-methylgranulatimide (9), and isogranulatimides A (10), B (11), and C (12). Compounds 9-12, congeners of isogranulatimide (6), are now available for biological evaluation.},
	keywords = {BHK CELLS, CAFFEINE, CANCER, CELL-CYCLE CHECKPOINTS, CISPLATIN, DERIVATIVES, DNA-REPLICATION, ENHANCEMENT, IMIDAZOLES, RADIOSENSITIZATION},
	isbn = {0022-3263},
	url = {<Go to ISI>://000084905400039},
	author = {Piers, E. and Britton, R. and Andersen, R. J.}
}
@article {3876,
	title = {Cytotoxic peptides hemiasterlin, hemiasterlin A and hemiasterlin B induce mitotic arrest and abnormal spindle formation},
	journal = {Cancer Chemotherapy and Pharmacology},
	volume = {39},
	number = {3},
	year = {1997},
	note = {ISI Document Delivery No.: VZ251Times Cited: 66Cited Reference Count: 17},
	month = {Jan},
	pages = {223-226},
	type = {Article},
	abstract = {Purpose: Hemiasterlin, hemiasterlin A and hemiasterlin B are newly isolated cytotoxic tripeptides with potential as antitumor drugs. We wished to determine their mechanism of cytotoxicity. Methods: We studied their effect on cell survival, cell cycle progression, and microtubule morphology in MCF-7 human mammary carcinoma cells. Results: At the nanomolar concentrations at which they were cytotoxic, the peptides induced arrest in mitotic metaphase. Hemiasterlin A produced abnormal mitotic spindles like those produced by the microtubule inhibitors taxol, nocodazole and vinblastine at low concentrations. At high concentrations hemiasterlin A did not cause microtubule bundling like taxol, but caused microtubule depolymerization like nocodazole and vinblastine. Conclusions: The hemiasterlins probably exert their cytotoxic effect by inhibiting spindle microtubule dynamics.},
	keywords = {CANCER, COLCHICINE SITE, FOSTRIECIN, INHIBITION, microtubules, mitosis, NATURAL-PRODUCTS, OKADAIC ACID, PHOSPHATASE-2A, PODOPHYLLOTOXIN, TAXOL, TUBULIN, VINBLASTINE, VINCA DOMAIN},
	isbn = {0344-5704},
	url = {<Go to ISI>://A1997VZ25100008},
	author = {Anderson, H. J. and Coleman, J. E. and Andersen, R. J. and Roberge, M.}
}
