@article {2088,
	title = {Reactivity of Cp*Mo(NO)(= CHCMe3) with olefins and dienes: C-H activation reactions of molybdenacyclobutanes},
	journal = {Organometallics},
	volume = {27},
	number = {12},
	year = {2008},
	note = {ISI Document Delivery No.: 312BHTimes Cited: 5Cited Reference Count: 30Graham, Peter A. Buschhaus, Miriam S. A. Pamplin, Craig B. Legzdins, Peter},
	month = {Jun},
	pages = {2840-2851},
	type = {Article},
	abstract = {Reactions of a variety of cyclic and acyclic olefins with the title alkylidene complex (formed spontaneously by loss of neopentane from Cp*Mo(NO)(CH2CMe3)(2) under ambient conditions) result in the initial formation of molybdenacyclobutane complexes (Cp* = C5Me5). These molybdenacyclobutane complexes do not react via olefin metathesis or cyclopropanation pathways, but instead via C-H activation. Thus, when cyclopentene is the olefinic substrate, the direct result of C-H activation at the beta-position of the metallacyclobutane affords a thermally stable allyl hydrido complex that can be isolated. Such an allyl hydride intermediate is not isolable for larger cyclic olefins (cyclohexene, cycloheptene, and cyclooctene) or acyclic olefins (allylbenzene and 1-hexene). Instead, those complexes react further, undergoing a second C-H activation at the allylic position to produce eta(4)-trans-diene complexes concomitant with the loss of dihydrogen. Upon heating, these eta(4)-trans-diene complexes liberate diene, thereby enabling the 14e Cp*Mo(NO) metal fragment to catalyze the oligomerization of cyclic olefins and dienes including cyclohexene and 1,4-cyclohexadiene. In the case of the acyclic olefin allylbenzene, the metal fragment catalyzes a dimerization to (E)-(4-methylpent-1-ene-1,5-diyl)dibenzene under ambient conditions.},
	keywords = {ALPHA-HYDROGEN ABSTRACTION, BONDS, COMPLEXES, CRYSTAL-STRUCTURES, CYCLOHEXENE, METATHESIS, MOLYBDENUM, NEOPENTYLIDENE, OLIGOMERIZATION, TUNGSTEN},
	isbn = {0276-7333},
	url = {<Go to ISI>://000256643600023},
	author = {Graham, P. A. and Buschhaus, M. S. A. and Pamplin, C. B. and Legzdins,Peter}
}
@article {1019,
	title = {Mutations in the SAM domain of the ETV6-NTRK3 chimeric tyrosine kinase block polymerization and transformation activity},
	journal = {Molecular and Cellular Biology},
	volume = {24},
	number = {11},
	year = {2004},
	note = {ISI Document Delivery No.: 822JXTimes Cited: 12Cited Reference Count: 53},
	month = {Jun},
	pages = {4636-4650},
	type = {Article},
	abstract = {The 12p13 ETV6 (TEL) gene is frequently targeted by chromosomal translocations in human malignancies, resulting in the formation of oncogenic ETV6 gene fusions. Many of the known partner genes encode protein tyrosine kinases (PTKs), generating fusion proteins that function as chimeric PTKs. ETV6-NTRK3 (EN), comprised of the ETV6 SAM domain fused to the NTRK3 PTK, is unique among ETV6 chimeric oncoproteins, as it is expressed in cancers of multiple lineages. We initially hypothesized that, similar to other ETV6-PTK chimeras, SAM-mediated dimerization of EN leads to constitutive activation of the PTK and downstream signaling cascades. However, when the EN SAM domain was replaced with an inducible FK506 binding protein (FKBP) dimerization system, resulting FKBP-NTRK3 chimeras failed to transform NIH 3T3 cells even though PTK activation was preserved. It was recently shown that the ETV6 SAM domain has two potential interacting surfaces, raising the possibility that this domain can mediate protein polymerization. We therefore mutated each EN SAM binding interface in a manner shown previously to abolish self-association of wild-type ETV6. Each mutation completely blocked the ability of EN to polymerize, to activate its PTK, and to transform NIH 3T3 cells. Furthermore, EN itself formed large polymeric structures within cells while mutant EN proteins were present only as monomers. Finally, we observed a dominant negative effect on the transformation of isolated SAM domains coexpressed in EN-transformed cells. Taken together, our results suggest that higher-order polymerization may be a critical requirement for the transformation activity of EN and possibly other ETV6-PTK fusion proteins.},
	keywords = {ABL-RELATED GENE, ACUTE LYMPHOBLASTIC-LEUKEMIA, BCR-ABL, CHROMOSOMAL TRANSLOCATION, CHRONIC MYELOMONOCYTIC LEUKEMIA, CONGENITAL FIBROSARCOMA, FUSION PROTEIN, INTERFACE, MYELOID-LEUKEMIA, OLIGOMERIZATION, PROTEIN-KINASE},
	isbn = {0270-7306},
	url = {<Go to ISI>://000221536600004},
	author = {Tognon, C. E. and Mackereth, C. D. and Somasiri, A. M. and McIntosh, L. P. and Sorensen, P. H. B.}
}
@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.}
}
