Search Results - "Lannigan, D A"

The serine/threonine protein kinase, p90 ribosomal s6 kinase, is an important regulator of prostate cancer cell proliferation by CLARK, D. E, ERRINGTON, T. M, SMITH, J. A, FRIERSON, H. F, WEBER, M. J, LANNIGAN, D. A

“…An increase in the activity of mitogen-activated protein kinase (MAPK) has been correlated with the progression of prostate cancer to advanced disease in…”
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Estrogen Receptor Selectively Binds the ``Coding Strand'' of an Estrogen Responsive Element by Lannigan, Deborah A., Notides, Angelo C.

“…An initial step in the transcriptional activation of the prolactin gene by estrogen is the binding of the estrogen-receptor complex to a specific nucleotide…”
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Estradiol-induced Phosphorylation of Serine 118 in the Estrogen Receptor Is Independent of p42/p44 Mitogen-activated Protein Kinase by Joel, Peteranne B., Traish, Abdulmaged M., Lannigan, Deborah A.

“…Phosphorylation of Ser118 of human estrogen receptor α (ER) enhances ER-mediated transcription and is induced by hormone binding and by activation of the…”
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Decreased intracellular Na+ concentration is an early event in murine erythroleukemic cell differentiation by Lannigan, D A, Knauf, P A

“…A decrease in Na+/K+-pump activity is an early event of Friend murine erythroleukemic (MEL) cell differentiation along the erythroid pathway. This decreased…”
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Rsk2 allosterically activates estrogen receptor α by docking to the hormone-binding domain by Clark, David E., Poteet-Smith, Celeste E., Smith, Jeffrey A., Lannigan, Deborah A.

“…We describe a novel mechanism for transcriptional regulation, in which docking of p90 ribosomal S6 kinase 2 (Rsk2) to the hormone‐binding domain (HBD) of…”
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Estradiol and phorbol ester cause phosphorylation of serine 118 in the human estrogen receptor by Joel, P B, Traish, A M, Lannigan, D A

“…Serine 118 is definitively identified as a major site of phosphorylation in the human estrogen receptor expressed in COS-1 cells treated with estradiol or…”
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Generation of constitutively active p90 ribosomal S6 kinase in vivo. Implications for the mitogen-activated protein kinase-activated protein kinase family by Poteet-Smith, C E, Smith, J A, Lannigan, D A, Freed, T A, Sturgill, T W

“…p90 ribosomal S6 kinases (RSKs), containing two distinct kinase catalytic domains, are phosphorylated and activated by extracellular signal-regulated kinase…”
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A novel mechanism for eukaryotic gene expression. The involvement of DNA tertiary structure in estrogen receptor recognition of its target nucleotide sequence by Lannigan, D A, Notides, A C

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Relationship of the decreases in protein synthesis and intracellular Na+ during friend murine erythroleukemic cell differentiation by Lannigan, D A, Knauf, P A, Macara, I G

“…The earliest known ionic event during Friend murine erythroleukemic (MEL) cell differentiation along the erythroid pathway is a 45% drop in intracellular…”
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Estrogen-responsive elements contain non-B DNA by Lannigan, D A, Koszewski, N J, Notides, A C

“…The estrogen receptor, a hormone-regulated transcription factor, regulates gene expression by interacting with a specific nucleotide sequence called the…”
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Analysis of estrogen receptor interaction with tertiary-structured estrogen responsive elements by Lannigan, D A, Tomashek, J J, Obourn, J D, Notides, A C

“…An initial crucial step in estrogen activation of gene expression is the interaction of the estrogen receptor with a specific nucleotide sequence [estrogen…”
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Creation of a stress-activated p90 ribosomal S6 kinase. The carboxyl-terminal tail of the MAPK-activated protein kinases dictates the signal transduction pathway in which they function by Smith, J A, Poteet-Smith, C E, Lannigan, D A, Freed, T A, Zoltoski, A J, Sturgill, T W

“…Mitogen-activated protein kinase-activated protein kinases (MAPKAPKs) lie immediately downstream of the mitogen-activated protein kinases (MAPKs),…”
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Phenamil, an amiloride analogue, inhibits differentiation of Friend murine erythroleukemic cells by Lannigan, D A, Bennington, J B, Cragoe, Jr, E J, Knauf, P A

“…Amiloride has been reported to inhibit Friend murine erythroleukemic (MEL) cell commitment to differentiate by inhibiting the MEL cell plasma membrane Na+-Ca2+…”
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Estrogen regulation of transcription by Lannigan, D A, Notides, A C

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Use of the yeast one-hybrid system to screen for mutations in the ligand-binding domain of the estrogen receptor by Bush, Sara M., Folta, Sara, Lannigan, Deborah A.

“…This report describes a novel yeast one-hybrid system which easily allows for the detection of mutations in the ligand-binding domain of the estrogen receptor…”
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Estrogen receptor phosphorylation by Lannigan, Deborah A

“…Estrogen receptor α (ERα) is phosphorylated on multiple amino acid residues. For example, in response to estradiol binding, human ERα is predominately…”
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Abstract P1-06-05: Breast cancer organoid cultures preserve intra-tumor heterogeneity and reveal intrinsically resistant phenotypes to standard chemotherapies by Sowder, ME, Ludwik, KA, Pasic, L, Brenin, DR, Stricker, TP, Macara, IG, Lannigan, DA

“…Abstract Breast cancer intra-tumor heterogeneity contributes to chemotherapy resistance and decreased patient survival, yet no reliable in vitro models exist…”
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Identification of the first specific inhibitor of p90 ribosomal S6 kinase (RSK) reveals an unexpected role for RSK in cancer cell proliferation by SMITH, Jeffrey A, POTEET-SMITH, Celeste E, YAMING XU, ERRINGTON, Timothy M, HECHT, Sidney M, LANNIGAN, Deborah A

“…p90 ribosomal S6 kinase (RSK) is an important downstream effector of mitogen-activated protein kinase, but its biological functions are not well understood. We…”
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The Function of the p190 Rho GTPase-activating Protein Is Controlled by Its N-terminal GTP Binding Domain by Tatsis, N, Lannigan, D A, Macara, I G

“…p190 is a GTPase-activating protein (GAP) for the Rho family of GTPases. The GAP domain of p190 is at the C terminus of the protein. At its N terminus, p190…”
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Novel biosensors for the detection of estrogen receptor ligands by De, Siddhartha, Macara, Ian G., Lannigan, Deborah A.

“…There exists a significant need for the detection of novel estrogen receptor (ER) ligands for pharmaceutical uses, especially for treating complications…”
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