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D O Toft

Showing results (91-100 of 109) with videos related to

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Journal of Cellular Biochemistry|October 1, 1995
Estrogen response in the hFOB 1.19 human fetal osteoblastic cell line stably transfected with the human estrogen receptor geneS A Harris, K R Tau, R J Enger, et al.
Cancer Research|July 1, 1992
Response of human breast cancer cells to heat shock and chemotherapeutic drugsD R Ciocca, S A Fuqua, S Lock-Lim, et al.
Endocrinology|February 1, 1990
Progesterone-induced avidin as a marker of cytodifferentiation in the oviduct: comparison to ovalbuminT K Joensuu, T J Ylikomi, D O Toft, et al.
Biochemistry|November 5, 1985
Immunological evidence that the nonhormone binding component of avian steroid receptors exists in a wide range of tissues and speciesR M Riehl, W P Sullivan, B T Vroman, et al.
The Journal of Biological Chemistry|October 5, 2001
Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complexY Guo, T Guettouche, M Fenna, et al.
Molecular and Cellular Biology|February 1, 1993
Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70D F Smith, W P Sullivan, T N Marion, et al.
European Journal of Cell Biology|October 1, 1989
Immunofluorescence colocalization of the 90-kDa heat-shock protein and microtubules in interphase and mitotic mammalian cellsT Redmond, E R Sanchez, E H Bresnick, et al.
The Journal of Biological Chemistry|August 11, 1995
The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90K A Hutchison, L F Stancato, J K Owens-Grillo, et al.
The Journal of Biological Chemistry|November 5, 1991
Characterization of progesterone receptor binding to the 90- and 70-kDa heat shock proteinsD B Schowalter, W P Sullivan, N J Maihle, et al.
Biochemistry|September 22, 1987
Immunologic analysis of human breast cancer progesterone receptors. 2. Structure, phosphorylation, and processingL L Wei, P L Sheridan, N L Krett, et al.
Pageof 11

Showing results (91-100 of 109) with videos related to

Sort By:
Pageof 11
Journal of Cellular Biochemistry|October 1, 1995
Estrogen response in the hFOB 1.19 human fetal osteoblastic cell line stably transfected with the human estrogen receptor geneS A Harris, K R Tau, R J Enger, et al.
Cancer Research|July 1, 1992
Response of human breast cancer cells to heat shock and chemotherapeutic drugsD R Ciocca, S A Fuqua, S Lock-Lim, et al.
Endocrinology|February 1, 1990
Progesterone-induced avidin as a marker of cytodifferentiation in the oviduct: comparison to ovalbuminT K Joensuu, T J Ylikomi, D O Toft, et al.
Biochemistry|November 5, 1985
Immunological evidence that the nonhormone binding component of avian steroid receptors exists in a wide range of tissues and speciesR M Riehl, W P Sullivan, B T Vroman, et al.
The Journal of Biological Chemistry|October 5, 2001
Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complexY Guo, T Guettouche, M Fenna, et al.
Molecular and Cellular Biology|February 1, 1993
Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70D F Smith, W P Sullivan, T N Marion, et al.
European Journal of Cell Biology|October 1, 1989
Immunofluorescence colocalization of the 90-kDa heat-shock protein and microtubules in interphase and mitotic mammalian cellsT Redmond, E R Sanchez, E H Bresnick, et al.
The Journal of Biological Chemistry|August 11, 1995
The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90K A Hutchison, L F Stancato, J K Owens-Grillo, et al.
The Journal of Biological Chemistry|November 5, 1991
Characterization of progesterone receptor binding to the 90- and 70-kDa heat shock proteinsD B Schowalter, W P Sullivan, N J Maihle, et al.
Biochemistry|September 22, 1987
Immunologic analysis of human breast cancer progesterone receptors. 2. Structure, phosphorylation, and processingL L Wei, P L Sheridan, N L Krett, et al.
Pageof 11