171,698 research outputs found
Ernest C. Turley
No full textErnest C. Turley was a teacher at the Duchesne High School is Roosevelt for a short time
Letter from George W. Turley to Hagan
No full textTypescript letter signed George W. Turley, The Presbytery, 47 Westland Row, Dublin, to (Hagan). Arranging meeting him the next day; asking advice for their notes for their pilgrims. A certain 'C' will come [on pilgrimage] with his wife and secretary but will not tell 'McS' until the last moment
[Juanita Marcus Turley]
No full textBlack & white photograph of Taos Pueblo woman Juanita Marcus Turley wearing traditional jewelry
Anthon Turley
No full textAnthon Turley played basketball for the Duchesne High Schoolin Roosevelt, Utah. He is the son of Ernest C. Turley
Developing a trial monitoring strategy for pH in UK marine waters. A report to Defra for contract ME2109
No full textReligion in world history : the persistence of imperial communion /
No full textIndividuals and groups have long found identity and meaning through religion and its collective expression. In' Religion in World History', John C. Super and Briane K. Turley examine the value of religion for interpreting the human experience in the past and present. Through this they explore those elements of religion that best connect it with cultural and political dynamics that have influenced history. Working within this general framework, Super and Turley bring out three unifying themes: The relationship between formal and informal religious beliefs, how these change through time, and how they are reflected in different cultures The relationship between church and state, from theocracies to the repression of religion The ongoing search for spiritual certainty, and the consequent splintering of core religious beliefs and the development of new onesIncludes bibliographical referencesIndividuals and groups have long found identity and meaning through religion and its collective expression. In' Religion in World History', John C. Super and Briane K. Turley examine the value of religion for interpreting the human experience in the past and present. Through this they explore those elements of religion that best connect it with cultural and political dynamics that have influenced history. Working within this general framework, Super and Turley bring out three unifying themes: The relationship between formal and informal religious beliefs, how these change through time, and how they are reflected in different cultures The relationship between church and state, from theocracies to the repression of religion The ongoing search for spiritual certainty, and the consequent splintering of core religious beliefs and the development of new one
The hyaluronan receptor RHAMM regulates extracellular-regulated kinase
No full textThis article is hosted on a website external to the CBCRA Open Access Archive. Selecting “View/Open” below will launch the full-text article in another browser window.We have identified two RHAMM (receptor for hyaluronan-mediated motility) isoforms that encode an alternatively spliced exon 4 (Hall, C. L., Yang, B., Yang, X., Zhang, S., Turley, M., Samuel, S., Lange, L. A., Wang, C., Curpen, G. D., Savani, R. C., Greenberg, A. H., and Turley, E. A. (1995) Cell 82, 19-26 and Wang, C., Entwistle, J., Hou, G., Li, Q., and Turley, E. A. (1996) Gene 174, 299-306). One of these, RHAMM variant 4 (RHAMMv4), is transforming when overexpressed and regulates Ras signaling (Hall et al.). Here we note using flow cytometry and confocal analysis that RHAMM isoforms encoding exon 4 occur both on the cell surface and in the cytoplasm. Epitope-tagging experiments indicate that RHAMMv4 occurs only in the cytoplasm. Several observations suggest that both cell surface RHAMM isoforms and RHAMMv4 are involved in regulating extracellular-regulated kinase (ERK) activity. Affinity-purified anti-RHAMM exon 4 antibodies block the ability of platelet-derived growth factor to activate ERK, and these reagents modify the protein tyrosine phosphorylation profile of proteins resulting from treatment with platelet-derived growth factor. A dominant negative form of RHAMMv4 inhibits mutant active Ras activation of ERK and coimmunoprecipitates with both mitogen-activated protein kinase kinase and ERK, suggesting that the intracellular RHAMMv4 acts downstream of Ras, possibly at the level of mitogen-activated protein kinase kinase-ERK interactions. Consistent with this, overexpression of RHAMMv4 constitutively activates ERK. These results identify a novel mechanism for the regulation of the Ras-ERK signaling pathway and suggest that RHAMM plays multiple roles in this regulation
TGF-beta 1 stimulation of cell locomotion utilizes the hyaluronan receptor RHAMM and hyaluronan.
No full textTGF-beta is a potent stimulator of motility in a variety of cell types. It has recently been shown that hyaluronan (HA) can directly promote locomotion of cells through interaction with the HA receptor RHAMM. We have investigated the role of RHAMM and HA in TGF-beta-stimulated locomotion and show that TGF-beta triggers the transcription, synthesis and membrane expression of the RHAMM receptor and the secretion of HA coincident with the induction of the locomotory response. This was demonstrated by both incubating cells with exogenous TGF-beta1 and by stimulating the production of bioactive TGF-beta1 in tumor cells transfected with TGF-beta1 under the control of the metallothionein promoter. TGF-beta1-induced locomotion was suppressed by antibodies that prevented HA/RHAMM interaction, using polyclonal antibodies to either RHAMM fusion protein or RHAMM peptides, or mAbs to purified RHAMM. Peptides corresponding to the HA-binding motif of RHAMM also suppressed TGF-beta1-induced increases in motility rate. Spontaneous locomotion of fibrosarcoma cells was blocked by neutralizing secreted TGF-beta with panspecific TGF-beta antibodies and by inhibition of TGF-beta1 secretion with antisense oligonucleotides. Polyclonal anti-RHAMM fusion protein antibodies and peptide from the RHAMM HA-binding motif also suppressed the spontaneous motility rate of fibrosarcoma cells. These data suggest that fibrosarcoma cell locomotion requires TGF-beta, and the pathway by which TGF-beta stimulates locomotion uses the HA receptor RHAMM and HA.PT: J; CR: ALLEN JB, 1990, J EXP MED, V171, P231 ANZANO MA, 1985, MOL CELL BIOL, V5, P242 BARNARD JA, 1990, BIOCHIM BIOPHYS ACTA, V1032, P79 BASSOLS A, 1988, J BIOL CHEM, V263, P3039 BRAY BA, 1991, AM REV RESPIR DIS, V143, P284 CHAN BM, 1992, CELL, V68, P1051 CHEN JK, 1987, P NATL ACAD SCI USA, V84, P5287 CULTY M, 1990, J CELL BIOL 1, V111, P2765 DALAL BI, 1993, AM J PATHOL, V143, P381 DANIELPOUR D, 1989, J CELL PHYSIOL, V138, P79 DELPECH B, 1981, J NEUROCHEM, V36, P855 DERYNCK R, 1987, CANCER RES, V47, P707 DOEGE K, 1987, J BIOL CHEM, V262, P17757 FASSEN AE, 1992, J CELL BIOL, V116, P521 FAVA RA, 1991, J EXP MED, V173, P1121 GOETINCK PF, 1987, J CELL BIOL, V105, P2403 GOUGH NM, 1988, ANAL BIOCHEM, V173, P93 HARDWICK C, 1992, J CELL BIOL, V117, P1343 HEINE UI, 1987, J CELL BIOL, V105, P286 HEINO J, 1989, J BIOL CHEM, V264, P380 HELDIN P, 1989, BIOCHEM J, V258, P919 HOOK M, 1984, ANNU REV BIOCHEM, V53, P847 HURTA RAR, 1991, J BIOL CHEM, V266, P24097 HYNES RO, 1992, CELL, V69, P11 KAHARI VM, 1991, J BIOL CHEM, V266, P10608 KHALIL N, 1989, J EXP MED, V170, P727 KHALIL N, 1991, CIBA F SYMP, V157, P194 KIMATA K, 1983, CANCER RES, V43, P1347 KLEINSOYER C, 1989, ARTERIOSCLEROSIS, V9, P147 KRUSIUS T, 1987, J BIOL CHEM, V262, P13120 LAEMMLI UK, 1970, NATURE, V227, P680 LIOTTA LA, 1988, CANCER SURV, V7, P631 MADRI JA, 1988, J CELL BIOL, V106, P1375 MASSAGUE J, 1990, ANNU REV CELL BIOL, V6, P597 MCCARTHY JB, 1992, IN PRESS CRC CRIT RE MCCLARTY GA, 1987, BIOCHEM BIOPH RES CO, V145, P1276 MOORADIAN DL, 1992, J NATL CANCER I, V84, P523 NEAME PJ, 1986, J BIOL CHEM, V261, P3519 NETTELBLADT O, 1989, AM REV RESPIR DIS, V139, P759 NUGENT MA, 1992, J BIOL CHEM, V267, P21256 PARTIN AW, 1988, CANCER RES, V48, P6050 PARTIN AW, 1989, P NATL ACAD SCI USA, V86, P1254 PERIDES G, 1989, J BIOL CHEM, V264, P5981 PEROTTI D, 1991, CANCER RES, V51, P5491 PIERCE GF, 1989, P NATL ACAD SCI USA, V86, P2229 POSTLETHWAITE AE, 1987, J EXP MED, V165, P251 REIBMAN J, 1991, P NATL ACAD SCI USA, V88, P6805 ROBERTS AB, 1990, HDB EXPT PHARM, V95, P419 SAMUEL SK, 1992, EMBO J, V11, P1599 SATO Y, 1988, J CELL BIOL, V107, P1199 SCHOR SL, 1989, IN VITRO CELL DEV B, V25, P737 SCHWARZ LC, 1990, GROWTH FACTORS, V3, P115 STAMENKOVIC I, 1991, EMBO J, V10, P343 STOKER M, 1991, BIOCHIM BIOPHYS ACTA, V1072, P81 THOMAS L, 1992, J CELL BIOL, V118, P971 TOOLE BP, 1979, P NATL ACAD SCI USA, V76, P6299 TOOLE BP, 1989, CIBA F SYMP, V143, P138 TOOLE BP, 1990, CURR OPIN CELL BIOL, V2, P839 TURLEY EA, 1985, CANCER RES, V45, P5098 TURLEY EA, 1985, EXP CELL RES, V161, P17 TURLEY EA, 1987, BIOCHEMISTRY-US, V26, P2997 TURLEY EA, 1989, EXP CELL RES, V181, P340 TURLEY EA, 1991, ADV DRUG DELIVER REV, V7, P257 TURLEY EA, 1991, J CELL BIOL, V112, P1041 WAHL SM, 1987, P NATL ACAD SCI USA, V84, P5788 WELSH DR, 1991, P NATL ACAD SCI USA, V87, P7678 YAMADA KM, 1990, CANCER RES, V50, P4485 YAMAGUCHI Y, 1990, NATURE, V346, P281 YANG BH, 1993, J BIOL CHEM, V268, P8617; NR: 69; TC: 73; J9: J CELL BIOL; PG: 10; GA: ME817Source type: Electronic(1
The hyaluronan receptor RHAMM regulates extracellular-regulated kinase
No full textThis article is hosted on a website external to the CBCRA Open Access Archive. Selecting “View/Open” below will launch the full-text article in another browser window.We have identified two RHAMM (receptor for hyaluronan-mediated motility) isoforms that encode an alternatively spliced exon 4 (Hall, C. L., Yang, B., Yang, X., Zhang, S., Turley, M., Samuel, S., Lange, L. A., Wang, C., Curpen, G. D., Savani, R. C., Greenberg, A. H., and Turley, E. A. (1995) Cell 82, 19-26 and Wang, C., Entwistle, J., Hou, G., Li, Q., and Turley, E. A. (1996) Gene 174, 299-306). One of these, RHAMM variant 4 (RHAMMv4), is transforming when overexpressed and regulates Ras signaling (Hall et al.). Here we note using flow cytometry and confocal analysis that RHAMM isoforms encoding exon 4 occur both on the cell surface and in the cytoplasm. Epitope-tagging experiments indicate that RHAMMv4 occurs only in the cytoplasm. Several observations suggest that both cell surface RHAMM isoforms and RHAMMv4 are involved in regulating extracellular-regulated kinase (ERK) activity. Affinity-purified anti-RHAMM exon 4 antibodies block the ability of platelet-derived growth factor to activate ERK, and these reagents modify the protein tyrosine phosphorylation profile of proteins resulting from treatment with platelet-derived growth factor. A dominant negative form of RHAMMv4 inhibits mutant active Ras activation of ERK and coimmunoprecipitates with both mitogen-activated protein kinase kinase and ERK, suggesting that the intracellular RHAMMv4 acts downstream of Ras, possibly at the level of mitogen-activated protein kinase kinase-ERK interactions. Consistent with this, overexpression of RHAMMv4 constitutively activates ERK. These results identify a novel mechanism for the regulation of the Ras-ERK signaling pathway and suggest that RHAMM plays multiple roles in this regulation
Charity Lamb: A Comic
No full textThis short comic depicts Charity Lamb and her decision to kill her husband in order to protect her children. It includes scenes of her husband\u27s abuse and the moments after the killing when she ran away. Illustrations were done by C.J. Turley, and the text was written by Sam Hannigan.https://digitalcommons.linfield.edu/aha_2017/1000/thumbnail.jp
- …
