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275 results on '"Whitesell L"'

1. First results from the JWST Early Release Science Program Q3D: Benchmark Comparison of Optical and Mid-IR Tracers of a Dusty, Ionized Red Quasar Wind at z=0.435

Author

Rupke, D. S. N., Wylezalek, D., Zakamska, N. L., Veilleux, S., Bertemes, C., Ishikawa, Y., Liu, W., Sankar, S., Vayner, A., Lim, H. X. G., McCrory, R., Murphree, G., Whitesell, L., Shen, L., Liu, G., Barrera-Ballesteros, J. K., Chen, H. -W., Diachenko, N., Goulding, A. D., Greene, J. E., Hainline, K. N., Hamann, F., Heckman, T., Johnson, S. D., Lutz, D., Lützgendorf, N., Mainieri, V., Nesvadba, N., Ogle, P., and Sturm, E.

Subjects
Astrophysics - Astrophysics of Galaxies
Abstract

The [OIII] 5007 A emission line is the most common tracer of warm, ionized outflows in active galactic nuclei across cosmic time. JWST newly allows us to use mid-infrared spectral features at both high spatial and spectral resolution to probe these same winds. Here we present a comparison of ground-based, seeing-limited [OIII] and space-based, diffraction-limited [SIV] 10.51 micron maps of the powerful, kiloparsec-scale outflow in the Type 1 red quasar SDSS J110648.32+480712.3. The JWST data are from the Mid-InfraRed Instrument (MIRI). There is a close match in resolution between the datasets (0."6), in ionization potential of the O$^{+2}$ and S$^{+3}$ ions (35 eV), and in line sensitivity (1e-17 to 2e-17 erg/s/cm$^2$/arcsec$^2$). The [OIII] and [SIV] line shapes match in velocity and linewidth over much of the 20 kpc outflowing nebula, and [SIV] is the brightest line in the rest-frame 3.5-19.5 micron range, demonstrating its usefulness as a mid-IR probe of quasar outflows. [OIII] is nevertheless intriniscally brighter and provides better contrast with the point-source continuum, which is strong in the mid-IR. There is a strong anticorrelation of [OIII]/[SIV] with average velocity, which is consistent with a scenario of differential obscuration between the approaching (blueshifted) and receding (redshifted) sides of the flow. The dust in the wind may also obscure the central quasar, consistent with models that attribute red quasar extinction to dusty winds., Comment: resubmitted to match published version; minor changes

Published
2023
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5. Screening And Design Of Tumor Necrosis Factor-

Author

Becherer, J, primary, Conway, J, additional, Warner, J, additional, Bickett, D, additional, Leesnitzer, M, additional, Seaton, T, additional, Mitchell, J, additional, McConnell, R, additional, Tippin, T, additional, Whitesell, L, additional, Rizzolio, M, additional, Hedeen, K, additional, Beaudet, E, additional, Andersen, M, additional, Lambert, M, additional, Austin, R, additional, Stanford, J, additional, Bubacz, D, additional, Chan, J, additional, Schaller, L, additional, Gaul, M, additional, Cowan, D, additional, Boncek, V, additional, Rabinowitz, M, additional, Musso, D, additional, McDougald, D, additional, Kaldor, I, additional, Glennon, K, additional, Wiethe, R, additional, Guo, Y, additional, Andrews, R, additional, and Moss, M, additional

Published
2000
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7. Terminal neuroendocrine differentiation of human prostate carcinoma cells in response to increased intracellular cyclic AMP

Author

Bang, Y.-J., Pirnia, F., Fang, W.-G., Kang, W.K., Sartor, O., Whitesell, L., Ha, M.J., Tsokos, M., Sheahan, M.D., Nguyen, P., Niklinski, W.T., Myers, C.E., and Trepel, J.B.

Subjects
Endocrine gland cancer -- Research, Cell differentiation -- Analysis, Science and technology
Abstract

Clinicopathologic studies of focal neuroendocrine differentiation of adrenocarcinomas of the prostrate reveal two human prostatic adrenocarcinoma cell lines which are multipotential neoplasias and exhibit epithelial and neuroendocrine differentiation. The lineage commitment of adrenocarcinoma of the prostrate shows plasticity. Cell-permanent cAMP analogues, which initiate terminal differentiation, suggest that hydrolysis-resistant cyclic nucleotides can be employed in the treatment of advanced prostrate cancer.

Published
1994

9. Tight Coordination of Protein Translation and Heat Shock Factor 1 Activation Supports the Anabolic Malignant State

Author

Massachusetts Institute of Technology. Department of Biological Engineering, Massachusetts Institute of Technology. Department of Biology, Koch Institute for Integrative Cancer Research at MIT, Tang, Yun-chi, Koeva, Martina I., Amon, Angelika B., Lindquist, Susan, Santagata, S., Mendillo, Marc L., Subramanian, A., Perley, C. C., Roche, S. P., Wong, B., Narayan, Rajiv, Kwon, H., Golub, Todd R., Porco, J. A., Whitesell, L., Tang, Yun-Chi, Koeva, Martina I, Amon, Angelika B, Massachusetts Institute of Technology. Department of Biological Engineering, Massachusetts Institute of Technology. Department of Biology, Koch Institute for Integrative Cancer Research at MIT, Tang, Yun-chi, Koeva, Martina I., Amon, Angelika B., Lindquist, Susan, Santagata, S., Mendillo, Marc L., Subramanian, A., Perley, C. C., Roche, S. P., Wong, B., Narayan, Rajiv, Kwon, H., Golub, Todd R., Porco, J. A., Whitesell, L., Tang, Yun-Chi, Koeva, Martina I, and Amon, Angelika B

Abstract

The ribosome is centrally situated to sense metabolic states, but whether its activity, in turn, coherently rewires transcriptional responses is unknown. Here, through integrated chemical-genetic analyses, we found that a dominant transcriptional effect of blocking protein translation in cancer cells was inactivation of heat shock factor 1 (HSF1), a multifaceted transcriptional regulator of the heat-shock response and many other cellular processes essential for anabolic metabolism, cellular proliferation, and tumorigenesis. These analyses linked translational flux to the regulation of HSF1 transcriptional activity and to the modulation of energy metabolism. Targeting this link with translation initiation inhibitors such as rocaglates deprived cancer cells of their energy and chaperone armamentarium and selectively impaired the proliferation of both malignant and premalignant cells with early-stage oncogenic lesions., Kathy and Curt Marble Cancer Research Fund

Published
2015

12. Tight Coordination of Protein Translation and HSF1 Activation Supports the Anabolic Malignant State

Author

Santagata, S., Mendillo, Marc L., Subramanian, A., Perley, C. C., Roche, S. P., Wong, B., Narayan, Rajiv, Kwon, H., Golub, Todd R., Porco, J. A., Whitesell, L., Lindquist, Susan, Tang, Yun-Chi, Koeva, Martina I, Amon, Angelika B, Massachusetts Institute of Technology. Department of Biological Engineering, Massachusetts Institute of Technology. Department of Biology, Koch Institute for Integrative Cancer Research at MIT, Tang, Yun-chi, Koeva, Martina I., Amon, Angelika B., and Lindquist, Susan

Abstract

The ribosome is centrally situated to sense metabolic states, but whether its activity, in turn, coherently rewires transcriptional responses is unknown. Here, through integrated chemical-genetic analyses, we found that a dominant transcriptional effect of blocking protein translation in cancer cells was inactivation of heat shock factor 1 (HSF1), a multifaceted transcriptional regulator of the heat-shock response and many other cellular processes essential for anabolic metabolism, cellular proliferation, and tumorigenesis. These analyses linked translational flux to the regulation of HSF1 transcriptional activity and to the modulation of energy metabolism. Targeting this link with translation initiation inhibitors such as rocaglates deprived cancer cells of their energy and chaperone armamentarium and selectively impaired the proliferation of both malignant and premalignant cells with early-stage oncogenic lesions., Kathy and Curt Marble Cancer Research Fund

Published
2013

15. Abstract OT3-2-05: Randomized phase II study of fulvestrant with or without ganetespib in patients (pts) with hormone receptor (HR)-positive metastatic breast cancer

Author

Lin, NU, primary, Whitesell, L, additional, Gelman, R, additional, Mayer, E, additional, Krop, IE, additional, Santagata, S, additional, Lowe, A, additional, Proia, D, additional, Farooq, S, additional, Brown, M, additional, Iannone, M, additional, Lindquist, S, additional, and Winer, EP, additional

Published
2013
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21. Antisense inhibition of oncogene expression

Author

Neckers, L, Whitesell, L, Rosolen, Angelo, and Geselowitz, Da

Subjects
Oncogene Proteins, Base Sequence, Receptors, Retinoic Acid, Interleukins, Molecular Sequence Data, Ribonuclease H, Receptors, Cell Surface, Oncogenes, Oligonucleotides, Antisense, DNA, Antisense, ErbB Receptors, Gene Expression Regulation, Neoplastic, Antisense Elements (Genetics), Genes, Animals, Humans, RNA, Antisense, Carrier Proteins, Growth Substances, Protein Kinases
Abstract

To understand the role of individual genes in regulating biological processes, one must be able to interfere specifically with either their expression or function. While monoclonal antibodies have proven very useful in studying cell surface proteins, the specific inhibition of intracellular proteins in viable cells is a much more difficult problem. The goal of antisense technology is to develop small oligonucleotides, plasmids, or retroviral vectors which can be readily introduced into living cells in order to inhibit specific gene expression. In this review, we briefly describe the principles of antisense usage, including problems of cellular uptake and intracellular distribution, mechanism of antisense action, and the properties of various oligonucleotide derivatives. In addition we present several examples of the biological effects of antisense administration used to study the role of specific genes in the regulation of cell growth and differentiation.

Published
1992

49. Cytotoxic Constituents of Aspergillus terreus from the Rhizosphere of Opuntia versicolor of the Sonoran Desert

Author

Wijeratne, E. M. K., Turbyville, T. J., Zhang, Z., Bigelow, D., Pierson, L. S., III, VanEtten, H. D., Whitesell, L., Canfield, L. M., and Gunatilaka, A. A. L.

Abstract

A novel cyclopentenedione, asterredione (1), two new terrecyclic acid A derivatives, (+)-5(6)-dihydro-6-methoxyterrecyclic acid A (2) and (+)-5(6)-dihydro-6-hydroxyterrecyclic acid A (3), and five known compounds, (+)-terrecyclic acid A (4), (−)-quadrone (5), betulinan A (6), asterriquinone D (7), and asterriquinone C-1 (8), were isolated from Aspergillus terreus occurring in the rhizosphere of Opuntia versicolor, using bioassay-guided fractionation. Acid-catalyzed reaction of 2 under mild conditions afforded 4, whereas under harsh conditions 2 yielded 5 and (−)-isoquadrone (9). Catalytic hydrogenation and methylation of 4 afforded 5(6)-dihydro-terrecyclic acid A (10) and (+)-terrecyclic acid A methyl ester (11), respectively. The structures of 1−11 were elucidated by spectroscopic methods. All compounds were evaluated for cytotoxicity in a panel of three sentinel cancer cell lines, NCI-H460 (non-small cell lung cancer), MCF-7 (breast cancer), and SF-268 (CNS glioma), and were found to be moderately active. Cell cycle analysis of 2, 4, and 5 using the NCI-H460 cell line indicated that 4 is capable of disrupting the cell cycle through an apparent arrest to progression at the G1 and G2/M phases in this p53 competent cell line. A pathway for the biosynthetic origin of asterredione (1) from asterriquinone D (7) is proposed.

Published
2003

50. Possible role for serine/threonine phosphorylation in the regulation of the heteroprotein complex between the hsp90 stress protein and the pp60v-src tyrosine kinase.

Author

Mimnaugh, E G, Worland, P J, Whitesell, L, and Neckers, L M

Abstract

The abundant, cytoplasmic 90-kDa heat-shock protein associates transiently with the Rous sarcoma virus oncogenic protein tyrosine kinase, pp60v-src, directs its cellular trafficking and negatively regulates its kinase activity. Here we report that the serine/threonine phosphatase inhibitor, okadaic acid, destabilized the heat-shock protein 90-pp60v-src chaperone complex in v-src-transfected cells. Concomitant with complex destabilization by okadaic acid, phosphoserine was doubled and phosphothreonine was increased 20-fold in the heat-shock protein 90. Although phosphorylation of the total pool of immunoprecipitable pp60v-src was unchanged, okadaic acid slightly increased phosphoserine and phosphothreonine levels specifically in pp60v-src bound to heat-shock protein 90. The low level of tyrosine phosphorylation in the pp60v-src complexed with heat-shock protein 90 was further decreased by okadaic acid. Interestingly, okadaic acid-stabilized hyperphosphorylation of the heat-shock protein 90-pp60v-src complex lowered the level of pp60v-src in cell membranes, the functional location for pp60v-src. We suggest that serine/threonine phosphorylation of heat-shock protein 90 and/or pp60v-src functions as a regulatory molecular trigger to release pp60v-src from the chaperone complex at the inner surface of cell membranes.

Published
1995

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