Littérature scientifique sur le sujet « Transforming growth factor β receptor II »
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Articles de revues sur le sujet "Transforming growth factor β receptor II"
Anders, Robert A., Sandra L. Arline, Jules J. E. Doré et Edward B. Leof. « Distinct Endocytic Responses of Heteromeric and Homomeric Transforming Growth Factor β Receptors ». Molecular Biology of the Cell 8, no 11 (novembre 1997) : 2133–43. http://dx.doi.org/10.1091/mbc.8.11.2133.
Texte intégralZhang, Wei, Yaxin Jiang, Qiang Wang, Xinyong Ma, Zeyu Xiao, Wei Zuo, Xiaohong Fang et Ye-Guang Chen. « Single-molecule imaging reveals transforming growth factor-β-induced type II receptor dimerization ». Proceedings of the National Academy of Sciences 106, no 37 (31 août 2009) : 15679–83. http://dx.doi.org/10.1073/pnas.0908279106.
Texte intégralWicks, Stephen J., Stephen Lui, Nadia Abdel-Wahab, Roger M. Mason et Andrew Chantry. « Inactivation of Smad-Transforming Growth Factor β Signaling by Ca2+-Calmodulin-Dependent Protein Kinase II ». Molecular and Cellular Biology 20, no 21 (1 novembre 2000) : 8103–11. http://dx.doi.org/10.1128/mcb.20.21.8103-8111.2000.
Texte intégralClarke, David C., Meredith L. Brown, Richard A. Erickson, Yigong Shi et Xuedong Liu. « Transforming Growth Factor β Depletion Is the Primary Determinant of Smad Signaling Kinetics ». Molecular and Cellular Biology 29, no 9 (17 février 2009) : 2443–55. http://dx.doi.org/10.1128/mcb.01443-08.
Texte intégralJacko, A. M., L. Nan, S. Li, J. Tan, J. Zhao, D. J. Kass et Y. Zhao. « De-ubiquitinating enzyme, USP11, promotes transforming growth factor β-1 signaling through stabilization of transforming growth factor β receptor II ». Cell Death & ; Disease 7, no 11 (novembre 2016) : e2474-e2474. http://dx.doi.org/10.1038/cddis.2016.371.
Texte intégralHALL, Frederick L., Paul D. BENYA, Silvia R. PADILLA, Denise CARBONARO-HALL, Richard WILLIAMS, Sue BUCKLEY et David WARBURTON. « Transforming growth factor-β type-II receptor signalling : intrinsic/associated casein kinase activity, receptor interactions and functional effects of blocking antibodies ». Biochemical Journal 316, no 1 (15 mai 1996) : 303–10. http://dx.doi.org/10.1042/bj3160303.
Texte intégralBhowmick, Neil A., Roy Zent, Mayshan Ghiassi, Maureen McDonnell et Harold L. Moses. « Integrin β1Signaling Is Necessary for Transforming Growth Factor-β Activation of p38MAPK and Epithelial Plasticity ». Journal of Biological Chemistry 276, no 50 (5 octobre 2001) : 46707–13. http://dx.doi.org/10.1074/jbc.m106176200.
Texte intégralTsuchida, K., K. A. Lewis, L. S. Mathews et W. W. Vale. « Molecular Characterization of Rat Transforming Growth Factor-β Type II Receptor ». Biochemical and Biophysical Research Communications 191, no 3 (mars 1993) : 790–95. http://dx.doi.org/10.1006/bbrc.1993.1286.
Texte intégralDatta, Pran K., et Harold L. Moses. « STRAP and Smad7 Synergize in the Inhibition of Transforming Growth Factor β Signaling ». Molecular and Cellular Biology 20, no 9 (1 mai 2000) : 3157–67. http://dx.doi.org/10.1128/mcb.20.9.3157-3167.2000.
Texte intégralFernandez, Tania, Stephanie Amoroso, Shellyann Sharpe, Gary M. Jones, Valery Bliskovski, Alexander Kovalchuk, Lalage M. Wakefield, Seong-Jin Kim, Michael Potter et John J. Letterio. « Disruption of Transforming Growth Factor β Signaling by a Novel Ligand-dependent Mechanism ». Journal of Experimental Medicine 195, no 10 (13 mai 2002) : 1247–55. http://dx.doi.org/10.1084/jem.20011521.
Texte intégralThèses sur le sujet "Transforming growth factor β receptor II"
Abe, Hideharu. « A Vitamin D Analog Regulates Mesangial Cell Smooth Muscle Phenotypes in a Transforming Growth Factor-β Type II Receptor-mediated Manner ». Kyoto University, 2001. http://hdl.handle.net/2433/150576.
Texte intégral本文データは平成22年度国立国会図書館の学位論文(博士)のデジタル化実施により作成された画像ファイルを基にpdf変換したものである
Kyoto University (京都大学)
0048
新制・課程博士
博士(医学)
甲第8877号
医博第2380号
新制||医||771(附属図書館)
UT51-2001-F207
京都大学大学院医学研究科内科系専攻
(主査)教授 中尾 一和, 教授 小川 修, 教授 北 徹
学位規則第4条第1項該当
Sharmin, Nahid. « Therapeutic Targeting of BMP and TGF-β Signalling Pathways for the Resolution of Pulmonary Arterial Hypertension ». Thesis, University of Bradford, 2018. http://hdl.handle.net/10454/17177.
Texte intégralCommonwealth Scholarship Commission in the UK
The full text will be available at the end of the embargo period, 31st July 2024.
Alyahya, Linda. « Expression of ADAM metalloproteases during transforming growth factor β-induced senescence in breast cancer cells ». Thesis, Kansas State University, 2017. http://hdl.handle.net/2097/35375.
Texte intégralBiochemistry and Molecular Biophysics Interdepartmental Program
Anna Zolkiewska
Cellular senescence is a state of irreversible cell cycle arrest in response to non-lethal stress. In cancer cells, senescence can be induced by chemotherapy, radiation, or signals from the tumor microenvironment, such as transforming growth factor β (TGFβ). Senescent cells are metabolically active and have altered gene expression compared to their non-senescent counterparts. Senescent cells release a wide variety of factors, including extracellular domains of transmembrane proteins that require proteolytic cleavage by specific proteases. ADAMs (A Disintegrin and Metalloprotease domain-containing proteins) are enzymes that cleave many transmembrane proteins, such as growth factor precursors or adhesion molecules, and thus may act as sheddases in senescent cells. Here, we investigate ADAM expression levels during TGFβ- induced cellular senescence. SUM149PT and SUM102PT breast cancer cells were incubated with TGFβ, followed by treatment with high doses of paclitaxel to remove actively proliferating, non-senescent cells. Induction of cellular senescence was examined by evaluating changes in cell size and granularity, and by β-galactosidase staining. ADAM mRNA levels were measured by quantitative reverse transcription polymerase chain reaction (qRT-PCR). Among several ADAMs tested, ADAM12 mRNA was significantly upregulated in senescent cells. In addition, we demonstrated that ADAM12 knock-down leads to decreased activation of epidermal growth factor receptor (EGFR), an important modulator of cancer cell growth, survival, and metastasis. This effect of ADAM12 knock-down was likely due to a diminished release of soluble EGF or EGF-like ligands from cells. Since senescent cells often release increased amounts of these ligands, ADAM12 may modulate the senescence secretome in senescent breast cancer cells.
Holásková, Ida. « I. Distribution of transforming growth factor beta 1, TGF receptor II and decorin in the sheep uterus shortly after breeding ». Morgantown, W. Va. : [West Virginia University Libraries], 2007. https://eidr.wvu.edu/etd/documentdata.eTD?documentid=5373.
Texte intégralTitle from document title page. Document formatted into pages; contains ix, 144 p. : ill. (some col.). Includes abstract. Includes bibliographical references (p. 126-144).
Mohan, D. Saravana. « Xenopus Laevis TGF-ß : Cloning And Characterization Of The Signaling Receptors ». Thesis, Indian Institute of Science, 2000. http://hdl.handle.net/2005/228.
Texte intégralDavies, R. J. « Dysfunctional response to transforming growth factor-beta contribute to the development of familial pulmonary arterial hypertension due to mutations in bone morphogenetic protein type II receptor ». Thesis, University of Cambridge, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.598337.
Texte intégralSACCOMANI, Gianmaria. « Expression, purification and crystallization attempts of a functional domain of human transforming growth factor beta receptor II - structural characterization of bile acid-binding proteins (Doctoral Thesis) ». Doctoral thesis, 2009. http://hdl.handle.net/11562/337422.
Texte intégralThe aim of this thesis work was to determine the three-dimensional structure of the cytoplasmatic domain of the transforming growth factor β receptor II, and of zebrafish and human ileal bile acid-binding proteins using the X-ray diffraction technique. The expression of TGFBR2 was attempted using different expression systems (E. coli, Pichia pastoris, insect cells transfected with recombinant baculovirus and Nicotiana benthamiana) but only a low amount of soluble recombinant protein was obtained. A refolding method was used to obtain the soluble protein from inclusion bodies and using the refolded protein two microcrystals were found in the preliminary crystallization trials, but they were not suitable for X-ray diffraction experiments. The optimization trials did not produce better samples than microcrystals. Human ileal bile acid-binding protein (HiBABP) and zebrafish ileal bile acid-binding protein (ZiBABP) were expressed in E. coli and purified by immobilized metal ion affinity chromatography, using the hexa-histidine tag added to the C-terminus of the proteins. The three dimensional structure of ZiBABP was determinated both in its apo-form and bound to cholic acid by the molecular replacement method. The resolution was 1.6 Ǻ for the apo-form and 2.2 Ǻ for the two different crystal forms of the complex with cholate. This is the first crystallographic structure of an Ileal bile acid-binding protein. In the case of HiBABP, crystals were obtained in two different crystallization conditions, but their size and quality did not allow to proceed with the structure determination. Optimization experiments of the crystallization conditions are currently being carried out to improve the quality of those crystals. A recent study has shown the presence of a new variant of HiBABP called Human Ileal bile acid-binding protein long (HiBABP-L) and therefore another goal of this thesis work was to determine the three-dimensional structure of this protein. HiBABP-L was expressed in E. coli and attempts to purify the protein of interest are still in progress.
Lin, Ching-Yi, et 林靜宜. « Helicobacter pylori Heat Shock Protein 60 Trigger SMAD Signal Pathway by Interacting with Transforming Growth Factor-β receptor II ». Thesis, 2008. http://ndltd.ncl.edu.tw/handle/18092904893492487352.
Texte intégral國立交通大學
生物科技系所
97
Helicobacter pylori have explored multiple mechanisms to evade host immune surveillance for chronic infection. But either of them is restricted by certain bacterial strains containing potential virulent factors, or those immune-restrained functions only limit to some specific immunocytes. However, the long-term persistence of H. pylori suggests a more comprehensive and powerful factor(s) hinds behind to regulate host immune system. Helicobacter pylori heat shock protein 60 (HpHsp60) was previous identified as an adhesion molecule or a potent immunogen. This study aims to study the structure of HpHsp60s and evaluates their functions on host immune responses. Analyzing the structure of HpHsp60 via amino acid blast, circular dichroism and electrophoresis indicated most recombinant HpHsp60s form dimers or tetramers that are quite different than E. coli Hsp60 protein structure. Moreover, a novel property of HpHsp60 was found, which is, by mimicking TGF-β1, HpHsp60 could exert immune regulatory effects. With structural homology to the receptor binding site of TGF-β1, HpHsp60 could interact with TGF-β receptor II, trigger SMAD pathway, and inhibiting the immune functions of THP-1 monocytic cells and peripheral mononuclear cells (PBMCs). Our study provides a new hint that H. pylori may employ Hsp60 to surrender host immunity.
Kohli, Gurneet. « Investigations of transforming growth factor -ß1 action during zebrafish oocyte maturation and cloning of its type II receptor / ». 2005.
Trouver le texte intégralTypescript. Includes bibliographical references (leaves 56-62). Also available on the Internet. MODE OF ACCESS via web browser by entering the following URL: http://gateway.proquest.com/openurl?url%5Fver=Z39.88-2004&res%5Fdat=xri:pqdiss &rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&rft_dat=xri:pqdiss:MR11827
Lin, Yi-Fan, et 林逸凡. « Extract of Reishi Polysaccharides Regulates Epithelial-Mesenchymal Transitions via the Lipid Rafts-dependent Ubiquitination of Transforming Growth Factor-β Receptor in MDA-MB-231 Breast Cancer Cells ». Thesis, 2012. http://ndltd.ncl.edu.tw/handle/59452972963242012772.
Texte intégral國立陽明大學
生醫光電研究所
100
Ten leading cause of death in Taiwan, cancer is always at the first of placing, and breast cancer mortality has been rising. One reason of that because the cancer cell will metastasis, then cancer metastasis-related mechanisms be paid great attention more and more in recent years. Epithelial-mesenchymal transition (EMT) is a process that cancer cells become aggressive, and it has been marker of tumor metastasis in recent years. Besides, Transforming growth factor beta 1 (TGF-β1) is one of the important factors that cause EMT. Ganoderma Lucidum (Reishi) is treatment of many diseases in Chinese herbal medicine. Ganoderma lucidum polysaccharides is one of many constituents that have bioactivity which are known in Ganoderma Lucidum . MDA-MB-231 is an invasion human breast cancer cell line. In our study, we conjecture that EMT was affected by EORP because the EMT markers (E-cadherin, γ-catenin, N-cadherin and vimentin) change after we used EORP to treatment MDA-MB-231. We also found the production of TGFβ-RI and TGFβ-RII were down after a treatment of EORP. And the TGFβ-RI and TGFβ-RII was ubiquitination in MDA-MB-231 after a treatment of EORP. In addition, EORP also induced lipid rafts expression that with TGFβ-RI or TGFβ-RII expression. These results showed that EORP regulates EMT via the lipid rafts-dependent ubiquitination of TGFβ-R in MDA-MB-231 Breast Cancer Cells.
Livres sur le sujet "Transforming growth factor β receptor II"
Jakowlew, Sonia B., dir. Transforming Growth Factor-β in Cancer Therapy, Volume II. Totowa, NJ : Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9.
Texte intégralChapitres de livres sur le sujet "Transforming growth factor β receptor II"
Naumann, Ulrike, et Michael Weller. « Modulating TGF-β Receptor Signaling : A Novel Approach of Cancer Therapy ». Dans Transforming Growth Factor-β in Cancer Therapy, Volume II, 653–69. Totowa, NJ : Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9_39.
Texte intégralDe Crescenzo, Gregory, Heman Chao, John Zwaagstra, Yves Durocher et Maureen D. O’Connor-McCourt. « Engineering TGF-β Traps : Artificially Dimerized Receptor Ectodomains as High-affinity Blockers of TGF-β Action ». Dans Transforming Growth Factor-β in Cancer Therapy, Volume II, 671–84. Totowa, NJ : Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9_40.
Texte intégralBandyopadhyay, Abhik, et LuZhe Sun. « Soluble TGF-β Type III Receptor Suppresses Malignant Progression of Human Cancer Cells ». Dans Transforming Growth Factor-β in Cancer Therapy, Volume II, 723–35. Totowa, NJ : Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9_44.
Texte intégralWang, Guiying Y., Xiaochua H. Hu, Rongmei M. Zhang, Lindsey J. Leach et Zewei W. Luo. « TGF-β Ligands, TGF-β Receptors, and Lung Cancer ». Dans Transforming Growth Factor-β in Cancer Therapy, Volume II, 79–93. Totowa, NJ : Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9_6.
Texte intégralSuzuki, Eiji, et Steven M. Albelda. « Soluble Type II Transforming Growth Factor-β Receptor Inhibits Tumorigenesis by Augmenting Host Antitumor Immunity ». Dans Transforming Growth Factor-β in Cancer Therapy, Volume II, 697–706. Totowa, NJ : Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9_42.
Texte intégralRuscetti, Francis, Salem Akel, Maria Birchenall-Roberts, Zhouhong Cao et Anita B. Roberts. « Smad Signaling in Leukemic Growth and Differentiation : Crosstalk Between Smad and Multiple Pathways Through Activation of the TGF-β Type I Receptor ». Dans Transforming Growth Factor-β in Cancer Therapy, Volume II, 247–61. Totowa, NJ : Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9_17.
Texte intégralLiu, Wei, Chekhau Chua, Zhen Gao, Xiaoli Wu et Yilin Cao. « Overexpressed Truncated TGF-β Type II Receptor Inhibits Fibrotic Behavior of Keloid Fibroblasts In Vitro and Experimental Scar Formation In Vivo ». Dans Transforming Growth Factor-β in Cancer Therapy, Volume I, 703–21. Totowa, NJ : Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-292-2_45.
Texte intégralLacher, Markus D., W. Michael Korn et Rosemary J. Akhurst. « Reversal of EMT by Small-Molecule Inhibitors of TGF-β Type I and II Receptors : Implications for Carcinoma Treatment ». Dans Transforming Growth Factor-β in Cancer Therapy, Volume II, 707–22. Totowa, NJ : Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9_43.
Texte intégralSalajegheh, Ali. « Transforming Growth Factor Beta-Receptor Type II (TGFβR2) ». Dans Angiogenesis in Health, Disease and Malignancy, 339–43. Cham : Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-28140-7_54.
Texte intégralRowley, David R. « Reactive Stroma and Evolution of Tumors : Integration of Transforming Growth Factor-β, Connective Tissue Growth Factor, and Fibroblast Growth Factor-2 Activities ». Dans Transforming Growth Factor-β in Cancer Therapy, Volume II, 475–505. Totowa, NJ : Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9_30.
Texte intégralActes de conférences sur le sujet "Transforming growth factor β receptor II"
Murari, Catherine, Gillian M. Howell et Michael G. Brattain. « Abstract B60 : Identification of the specific histone deacetylases involved in the silencing of transforming growth factor β receptor II in colon cancer ». Dans Abstracts : AACR Special Conference on Chromatin and Epigenetics in Cancer - June 19-22, 2013 ; Atlanta, GA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.cec13-b60.
Texte intégralSanthekadur, Prasanna K., Rachel Gredler, Maaged Akiel, Paul Dent, Paul B. Fisher et Devanand Sarkar. « Abstract 2628 : The multifunctional protein staphylococcal nuclease domain containing-1 (SND1) promotes migration and invasion of hepatocellular carcinoma (HCC) cells by modulating angiotensin II type 1 receptor (AT1R) and transforming growth factor-β (TGF-β) s ». Dans Proceedings : AACR 104th Annual Meeting 2013 ; Apr 6-10, 2013 ; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-2628.
Texte intégralNg, Evelyn, et John Di Guglielmo. « Abstract 4593 : Analysis of transforming growth factor β receptor trafficking on different signaling transduction pathways ». Dans Proceedings : AACR 107th Annual Meeting 2016 ; April 16-20, 2016 ; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-4593.
Texte intégralRosman, Diana S., Yana Bromberg, Aliyah Weinstein et Michael Reiss. « Abstract 2118 : Phenotypic diversity of disease-associated transforming growth factor-β (TGF-β) type I receptor gene (TGFBR1) mutants ». Dans Proceedings : AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011 ; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2118.
Texte intégralPozarska, Agnieszka, Gero Niess, Werner Seeger et Rory Morty. « A role for the accessory type III transforming growth factor β receptor (Tgfbr3) in lung alveolarisation ». Dans ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.pa4026.
Texte intégralPark, Jin-hong, Seung-Hee Ryu, Jeong-Yoon Oh, Youn-Joo Yang et Sang-wook Lee. « Abstract 2494 : The protective effect of a novel transforming growth factor-β receptor inhibitor against radiation-induced fibrosis ». Dans Proceedings : AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011 ; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2494.
Texte intégralMalkoski, Stephen, Timothy Cleaver, Sarah Haeger, Karen Rodriguez, Jessyka Lighthall, Shi-Long Lu, Daniel Merrick et Xiao-Jing Wang. « Transforming Growth Factor Beta Receptor Type II Deletion Increases The Multiplicity And Growth Of K-RAS Induced Lung Cancers ». Dans American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a4044.
Texte intégralMoshkovich, Nellie, Misako Sato, Binwu Tang, Yu-an Yang, Kathleen C. Flanders, Mitsutaka Kadota, Howard Yang, Maxwell P. Lee et Lalage M. Wakefield. « Abstract 2244 : Functional interactions between estrogen-related-receptor β (ESRRB) and transforming growth factor-beta (TGF-β) in the regulation of breast cancer stem cell dynamics ». Dans Proceedings : AACR 106th Annual Meeting 2015 ; April 18-22, 2015 ; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-2244.
Texte intégralBabiker, Nusaiba A., Ahmed T. Negmeldin et Eman M. El-labbad. « In Silico Fragment-Based Drug Design and Molecular Docking of Tranilast Analogues as Potential Inhibitors of Transforming Growth Factor- β Receptor Type 1 ». Dans ECMC 2022. Basel Switzerland : MDPI, 2022. http://dx.doi.org/10.3390/ecmc2022-13472.
Texte intégralLi, Min, Manda Sai Krishnaveni, Changgong Li, Zea Borok et Parviz Minoo. « Epithelial-Specific Deletion Of Transforming Growth Factor-² (TGF-²) Receptor Type II (T²RII) In The Lung Confers Relative Resistance To Bleomycin Injury ». Dans American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a3525.
Texte intégralRapports d'organisations sur le sujet "Transforming growth factor β receptor II"
Forbes, Digna S., et Roby A. Jensen. Mechanisms of Transforming Growth Factor Beta-Receptor II Loss in Breast Neoplasia. Fort Belvoir, VA : Defense Technical Information Center, décembre 2002. http://dx.doi.org/10.21236/ada420478.
Texte intégral