The Experts below are selected from a list of 142356 Experts worldwide ranked by ideXlab platform
Zigang Dong - One of the best experts on this subject based on the ideXlab platform.
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resveratrol induces apoptosis by directly targeting ras gtpase activating Protein sh3 domain binding Protein 1
Oncogene, 2015Co-Authors: Naomi Oi, Margarita Malakhova, Ann M Bode, Yan Li, Lizhi Zhang, Z. Xu, Jian Yuan, Zigang DongAbstract:Resveratrol induces apoptosis by directly targeting Ras-GTPase-activating Protein SH3 domain-binding Protein 1
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epigallocatechin gallate suppresses lung cancer cell growth through ras gtpase activating Protein sh3 domain binding Protein 1
Cancer Prevention Research, 2010Co-Authors: Junghyun Shim, Ann M Bode, Zhengyuan Su, Jungil Chae, Chung S Yang, Zigang DongAbstract:Green tea is a highly popular beverage globally. Green tea contains a number of polyphenol compounds referred to as catechins, and (−)-epigallocatechin gallate (EGCG) is believed to be the major biologically active compound found in green tea. EGCG has been reported to suppress lung cancer, but the molecular mechanisms of the inhibitory effects of EGCG are not clear. We found that EGCG interacted with the Ras–GTPase-activating Protein SH3 domain-binding Protein 1 (G3BP1) with high binding affinity ( K d = 0.4 μmol/L). We also showed that EGCG suppressed anchorage-independent growth of H1299 and CL13 lung cancer cells, which contain an abundance of the G3BP1 Protein. EGCG was much less effective in suppressing anchorage-independent growth of H460 lung cancer cells, which express much lower levels of G3BP1. Knockdown shG3BP1-transfected H1299 cells exhibited substantially decreased proliferation and anchorage-independent growth. shG3BP1 H1299 cells were resistant to the inhibitory effects of EGCG on growth and colony formation compared with shMock-transfected H1299 cells. EGCG interfered with the interaction of G3BP1 and the Ras–GTPase-activating Protein and further suppressed the activation of Ras. Additional results revealed that EGCG effectively attenuated G3BP1 downstream signaling, including extracellular signal-regulated kinase and mitogen-activated Protein kinase/extracellular signal-regulated kinase kinase, in wild-type H1299 and shMock H1299 cells but had little effect on H460 or shG3BP1 H1299 cells. Overall, these results strongly indicate that EGCG suppresses lung tumorigenesis through its binding with G3BP1. Cancer Prev Res; 3(5); 670–9. ©2010 AACR.
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Epigallocatechin Gallate Suppresses Lung Cancer Cell Growth through Ras–GTPase-activating Protein SH3 Domain-Binding Protein 1
Cancer prevention research (Philadelphia Pa.), 2010Co-Authors: Junghyun Shim, Ann M Bode, Jungil Chae, Chung S Yang, Dong Joon Kim, Feng Zhu, Zigang DongAbstract:Green tea is a highly popular beverage globally. Green tea contains a number of polyphenol compounds referred to as catechins, and (−)-epigallocatechin gallate (EGCG) is believed to be the major biologically active compound found in green tea. EGCG has been reported to suppress lung cancer, but the molecular mechanisms of the inhibitory effects of EGCG are not clear. We found that EGCG interacted with the Ras–GTPase-activating Protein SH3 domain-binding Protein 1 (G3BP1) with high binding affinity ( K d = 0.4 μmol/L). We also showed that EGCG suppressed anchorage-independent growth of H1299 and CL13 lung cancer cells, which contain an abundance of the G3BP1 Protein. EGCG was much less effective in suppressing anchorage-independent growth of H460 lung cancer cells, which express much lower levels of G3BP1. Knockdown shG3BP1-transfected H1299 cells exhibited substantially decreased proliferation and anchorage-independent growth. shG3BP1 H1299 cells were resistant to the inhibitory effects of EGCG on growth and colony formation compared with shMock-transfected H1299 cells. EGCG interfered with the interaction of G3BP1 and the Ras–GTPase-activating Protein and further suppressed the activation of Ras. Additional results revealed that EGCG effectively attenuated G3BP1 downstream signaling, including extracellular signal-regulated kinase and mitogen-activated Protein kinase/extracellular signal-regulated kinase kinase, in wild-type H1299 and shMock H1299 cells but had little effect on H460 or shG3BP1 H1299 cells. Overall, these results strongly indicate that EGCG suppresses lung tumorigenesis through its binding with G3BP1. Cancer Prev Res; 3(5); 670–9. ©2010 AACR.
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Abstract 4509: Epigallocatechin gallate suppresses tumorigenesis of lung cancer cells by targeting Ras-GTPase-activating Protein SH3-domain binding Protein 1
Experimental and Molecular Therapeutics, 2010Co-Authors: Junghyun Shim, Ann M Bode, Chung S Yang, Dong Joon Kim, Feng Zhu, Jung-ii Chae, Nam-pyo Cho, Zigang DongAbstract:(−)-Epigallocatechin gallate (EGCG) is one of the major green tea catechins that is suggested to have a role as a preventive agent in cancer, obesity, diabetes, and cardiovascular disease. Here we identified Ras-GTPase-activating Protein SH3-domain binding Protein 1 (G3BP1) as an important and novel molecular target of EGCG in lung cancer. EGCG interacted with the G3BP1 with high binding affinity (K d = 0.4 μmol/liter). We also showed that EGCG suppressed anchorage-independent growth of H1299 and CL13 lung cancer cells, which contain an abundance of the G3BP1 Protein. EGCG was much less effective in suppressing anchorage-independent growth of H460 lung cancer cells in which G3BP1 levels are low. Knockdown shG3BP1-transfected H1299 cells exhibited substantially decreased proliferation and anchorage-independent growth. shG3BP1-H1299 cells were resistant to the inhibitory effect of EGCG on growth and colony formation compared to shMock-transfected H1299 cells. EGCG interfered with the interaction between G3BP1 and Ras-GTPase-activating Protein (Ras-GAP) and further suppressed the activation of Ras. Additional results revealed that EGCG effectively attenuated G3BP1-downstream signaling, including extracellular signaling-regulated kinases, and MAPK kinase in wildtype H1299 and shMock-H1299 cells, but had little effect on H460 or shG3BP1- H1299 cells. Overall, these results strongly indicate that EGCG suppresses lung tumorigenesis through its binding with G3BP1. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr 4509.
Dieter Gallwitz - One of the best experts on this subject based on the ideXlab platform.
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A yeast GTPase-activating Protein that interacts specifically with a member of the Ypt/Rab family.
Nature, 1993Co-Authors: Molly Strom, Petra Vollmer, Tjie J. Tan, Dieter GallwitzAbstract:Members of the Ras superfamily of GTP-binding Proteins are involved in a variety of cellular processes, including signal transduction, cytoskeletal organization and Protein transport. GTP-binding Proteins of the Ypt/Rab family direct vesicular Protein transport in the secretory and endocytic pathways in the yeast Saccharomyces cerevisiae (Ypt Proteins) and in mammalian systems (Rab Proteins). The cellular activity of monomeric GTP-binding Proteins is influenced by Proteins that regulate GDP/GTP exchange and GTP hydrolysis. GTPase-activating Proteins (GAPs) can increase the slow intrinsic GTPase activity of GTP-binding Proteins by several orders of magnitude. As GAPs modulate the activity of GTP-binding Proteins, they are thought to give a biochemical handle on the functioning of Ypt/Rab Proteins in transport vesicle budding and docking or fusion at donor and acceptor membranes. We report here the first cloned GTPase-activating Protein for the Ypt/Rab Protein family. The gene, GYP6 (GAP of Ypt6 Protein), encodes a Protein of 458 amino acids which is highly specific for the Ypt6 Protein and shows little or no cross-reactivity with other Ypt/Rab family members or with H-Ras p21.
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a yeast gtpase activating Protein that interacts specifically with a member of the ypt rab family
Nature, 1993Co-Authors: Molly Strom, Petra Vollmer, Tjie J. Tan, Dieter GallwitzAbstract:Members of the Ras superfamily of GTP-binding Proteins are involved in a variety of cellular processes, including signal transduction, cytoskeletal organization and Protein transport. GTP-binding Proteins of the Ypt/Rab family direct vesicular Protein transport in the secretory and endocytic pathways in the yeast Saccharomyces cerevisiae (Ypt Proteins) and in mammalian systems (Rab Proteins). The cellular activity of monomeric GTP-binding Proteins is influenced by Proteins that regulate GDP/GTP exchange and GTP hydrolysis. GTPase-activating Proteins (GAPs) can increase the slow intrinsic GTPase activity of GTP-binding Proteins by several orders of magnitude. As GAPs modulate the activity of GTP-binding Proteins, they are thought to give a biochemical handle on the functioning of Ypt/Rab Proteins in transport vesicle budding and docking or fusion at donor and acceptor membranes. We report here the first cloned GTPase-activating Protein for the Ypt/Rab Protein family. The gene, GYP6 (GAP of Ypt6 Protein), encodes a Protein of 458 amino acids which is highly specific for the Ypt6 Protein and shows little or no cross-reactivity with other Ypt/Rab family members or with H-Ras p21.
Molly Strom - One of the best experts on this subject based on the ideXlab platform.
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A yeast GTPase-activating Protein that interacts specifically with a member of the Ypt/Rab family.
Nature, 1993Co-Authors: Molly Strom, Petra Vollmer, Tjie J. Tan, Dieter GallwitzAbstract:Members of the Ras superfamily of GTP-binding Proteins are involved in a variety of cellular processes, including signal transduction, cytoskeletal organization and Protein transport. GTP-binding Proteins of the Ypt/Rab family direct vesicular Protein transport in the secretory and endocytic pathways in the yeast Saccharomyces cerevisiae (Ypt Proteins) and in mammalian systems (Rab Proteins). The cellular activity of monomeric GTP-binding Proteins is influenced by Proteins that regulate GDP/GTP exchange and GTP hydrolysis. GTPase-activating Proteins (GAPs) can increase the slow intrinsic GTPase activity of GTP-binding Proteins by several orders of magnitude. As GAPs modulate the activity of GTP-binding Proteins, they are thought to give a biochemical handle on the functioning of Ypt/Rab Proteins in transport vesicle budding and docking or fusion at donor and acceptor membranes. We report here the first cloned GTPase-activating Protein for the Ypt/Rab Protein family. The gene, GYP6 (GAP of Ypt6 Protein), encodes a Protein of 458 amino acids which is highly specific for the Ypt6 Protein and shows little or no cross-reactivity with other Ypt/Rab family members or with H-Ras p21.
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a yeast gtpase activating Protein that interacts specifically with a member of the ypt rab family
Nature, 1993Co-Authors: Molly Strom, Petra Vollmer, Tjie J. Tan, Dieter GallwitzAbstract:Members of the Ras superfamily of GTP-binding Proteins are involved in a variety of cellular processes, including signal transduction, cytoskeletal organization and Protein transport. GTP-binding Proteins of the Ypt/Rab family direct vesicular Protein transport in the secretory and endocytic pathways in the yeast Saccharomyces cerevisiae (Ypt Proteins) and in mammalian systems (Rab Proteins). The cellular activity of monomeric GTP-binding Proteins is influenced by Proteins that regulate GDP/GTP exchange and GTP hydrolysis. GTPase-activating Proteins (GAPs) can increase the slow intrinsic GTPase activity of GTP-binding Proteins by several orders of magnitude. As GAPs modulate the activity of GTP-binding Proteins, they are thought to give a biochemical handle on the functioning of Ypt/Rab Proteins in transport vesicle budding and docking or fusion at donor and acceptor membranes. We report here the first cloned GTPase-activating Protein for the Ypt/Rab Protein family. The gene, GYP6 (GAP of Ypt6 Protein), encodes a Protein of 458 amino acids which is highly specific for the Ypt6 Protein and shows little or no cross-reactivity with other Ypt/Rab family members or with H-Ras p21.
Nicholas C. Popescu - One of the best experts on this subject based on the ideXlab platform.
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Deleted in liver cancer 3 (DLC-3), a novel Rho GTPase-activating Protein, is downregulated in cancer and inhibits tumor cell growth
Oncogene, 2007Co-Authors: Marian E. Durkin, V Ullmannova, M Guan, Nicholas C. PopescuAbstract:Deleted in liver cancer 3 (DLC-3), a novel Rho GTPase-activating Protein, is downregulated in cancer and inhibits tumor cell growth
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DLC-1:a Rho GTPase-activating Protein and tumour suppressor
Journal of cellular and molecular medicine, 2007Co-Authors: Marian E. Durkin, Bao-zhu Yuan, Xiaoling Zhou, Drazen B. Zimonjic, Douglas R. Lowy, Snorri S. Thorgeirsson, Nicholas C. PopescuAbstract:The deleted in liver cancer 1 (DLC-1) gene encodes a GTPase activating Protein that acts as a negative regulator of the Rho family of small GTPases. Rho Proteins transduce signals that influence cell morphology and physiology, and their aberrant up-regulation is a key factor in the neoplastic process, including metastasis. Since its discovery, compelling evidence has accumulated that demonstrates a role for DLC-1 as a bona fide tumour suppressor gene in different types of human cancer. Loss of DLC-1 expression mediated by genetic and epigenetic mechanisms has been associated with the development of many human cancers, and restoration of DLC-1 expression inhibited the growth of tumour cells in vivo and in vitro. Two closely related genes, DLC-2 and DLC-3, may also be tumour suppressors. This review presents the current status of progress in understanding the biological functions of DLC-1 and its relatives and their roles in neoplasia.
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Identification and characterization of a gene encoding a putative mouse Rho GTPase activating Protein gene 8, Arhgap8.
Gene, 2003Co-Authors: Zhihong Shan, Thomas Haaf, Nicholas C. PopescuAbstract:Rho GTPase activating Proteins promote the intrinsic GTP hydrolysis activity of Rho family Proteins. We isolated a putative mouse ortholog of the human Rho GTPase activating Protein 8, ARHGAP8. The open reading frame encodes a peptide of 387 amino acids with high homology to human ARHGAP8 in its N-terminal domain. Both radiation hybrid mapping and fluorescent in situ hybridization localized the gene to mouse chromosome 15E. The 23 kb genomic Arhgap8 sequence consists of eight exons and seven introns. Northern blot and RT-PCR analyses showed that a transcript of approximately 1.9 kb is ubiquitously expressed in various adult mouse tissues with particularly strong expression in kidney.
Kelly Hiatt - One of the best experts on this subject based on the ideXlab platform.
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introduction of neurofibromin 1 gtpase activating Protein related domain grd restores normal growth in nfl murine cells
Pediatric Research, 1999Co-Authors: Kelly Hiatt, Gideon Bollag, Kevin Shannon, Youyan Zhang, Wade D ClappAbstract:Introduction of Neurofibromin 1 GTPase Activating Protein Related Domain (GRD) Restores Normal Growth in Nfl -/- Murine Cells
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Introduction of Neurofibromin 1 GTPase Activating Protein Related Domain (GRD) Restores Normal Growth in Nfl -/- Murine Cells
Pediatric Research, 1999Co-Authors: Kelly Hiatt, Gideon Bollag, Kevin Shannon, Youyan Zhang, D. Wade ClappAbstract:Introduction of Neurofibromin 1 GTPase Activating Protein Related Domain (GRD) Restores Normal Growth in Nfl -/- Murine Cells
