Gotowa bibliografia na temat „Phosphoproteins”
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Artykuły w czasopismach na temat "Phosphoproteins"
Qiao, Yuting, Xianrong Liu, Zhi Jia, Peng Zhang, Li Gao, Bingxin Liu, Lijuan Qiao i Lei Zhang. "In Situ Growth Intercalation Structure MXene@Anatase/Rutile TiO2 Ternary Heterojunction with Excellent Phosphoprotein Detection in Sweat". Biosensors 12, nr 10 (12.10.2022): 865. http://dx.doi.org/10.3390/bios12100865.
Pełny tekst źródłaRodríguez-Vázquez, Raquel, Daniel Mouzo i Carlos Zapata. "Phosphoproteome Analysis Using Two-Dimensional Electrophoresis Coupled with Chemical Dephosphorylation". Foods 11, nr 19 (7.10.2022): 3119. http://dx.doi.org/10.3390/foods11193119.
Pełny tekst źródłaRodriguez Galvan, Joaquin, Brianna Donner, Cat Hoang Veseley, Patrick Reardon, Heather M. Forsythe, Jesse Howe, Gretchen Fujimura i Elisar Barbar. "Human Parainfluenza Virus 3 Phosphoprotein Is a Tetramer and Shares Structural and Interaction Features with Ebola Phosphoprotein VP35". Biomolecules 11, nr 11 (29.10.2021): 1603. http://dx.doi.org/10.3390/biom11111603.
Pełny tekst źródłaQiao, Yuting, Lijuan Qiao, Peize Zhao, Peng Zhang, Fanbin Wu, Jiahui Zhang, Li Gao, Bingxin Liu i Lei Zhang. "Phosphoprotein Detection in Sweat Realized by Intercalation Structure 2D@3D g-C3N4@Fe3O4 Wearable Sensitive Motif". Biosensors 12, nr 6 (24.05.2022): 361. http://dx.doi.org/10.3390/bios12060361.
Pełny tekst źródłaLi, Qing, Jiong Zhang, Yi Fang, Yan Dai, Ping Jia, Ziyan Shen, Sujuan Xu, Xiaoqiang Ding i Feng Zhou. "Phosphoproteome Profiling of uEVs Reveals p-AQP2 and p-GSK3β as Potential Markers for Diabetic Nephropathy". Molecules 28, nr 14 (24.07.2023): 5605. http://dx.doi.org/10.3390/molecules28145605.
Pełny tekst źródłaSkubitz, K. M., J. R. Mendiola i M. S. Collett. "CD15 monoclonal antibodies react with a phosphotyrosine-containing protein on the surface of human neutrophils." Journal of Immunology 141, nr 12 (15.12.1988): 4318–23. http://dx.doi.org/10.4049/jimmunol.141.12.4318.
Pełny tekst źródłaMoradi, Atieh, Shuaijian Dai, Emily Oi Ying Wong, Guang Zhu, Fengchao Yu, Hon-Ming Lam, Zhiyong Wang i in. "Isotopically Dimethyl Labeling-Based Quantitative Proteomic Analysis of Phosphoproteomes of Soybean Cultivars". Biomolecules 11, nr 8 (16.08.2021): 1218. http://dx.doi.org/10.3390/biom11081218.
Pełny tekst źródłaPongprayoon, Wasinee, Atikorn Panya, Janthima Jaresitthikunchai, Narumon Phaonakrop i Sittiruk Roytrakul. "Phosphoprotein Profile of Rice (Oryza sativa L.) Seedlings under Osmotic Stress after Pretreatment with Chitosan". Plants 11, nr 20 (15.10.2022): 2729. http://dx.doi.org/10.3390/plants11202729.
Pełny tekst źródłaGanju, RK, RG Shpektor, DG Brenner i MA Shipp. "CD10/neutral endopeptidase 24.11 is phosphorylated by casein kinase II and coassociates with other phosphoproteins including the lyn src- related kinase". Blood 88, nr 11 (1.12.1996): 4159–65. http://dx.doi.org/10.1182/blood.v88.11.4159.4159.
Pełny tekst źródłaGanju, RK, RG Shpektor, DG Brenner i MA Shipp. "CD10/neutral endopeptidase 24.11 is phosphorylated by casein kinase II and coassociates with other phosphoproteins including the lyn src- related kinase". Blood 88, nr 11 (1.12.1996): 4159–65. http://dx.doi.org/10.1182/blood.v88.11.4159.bloodjournal88114159.
Pełny tekst źródłaRozprawy doktorskie na temat "Phosphoproteins"
Marciniak, Stefan John. "Phosphoproteins of the zymogen granule membrane". Thesis, University of Cambridge, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.243154.
Pełny tekst źródłaPoulain, Fabienne. "Stathmin family phosphoproteins and neuronal morphogenesis". Paris 6, 2007. http://www.theses.fr/2007PA066492.
Pełny tekst źródłaSheppard, Vonda Chantal. "Identification and characterization of diatom kinases catalyzing the phosphorylation of biomineral forming proteins". Diss., Georgia Institute of Technology, 2010. http://hdl.handle.net/1853/37227.
Pełny tekst źródłaLei, Xia. "Identification and characterization of endosomal specific phosphoproteins". Thesis, McGill University, 1994. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=28483.
Pełny tekst źródłaStaubli, Justin Charles. "Development of a phosphoprotein enrichment method to identify and characterize phosphoproteins within leukemia following treatment with the PP2A activator, FTY720". The Ohio State University, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=osu1338269265.
Pełny tekst źródłaChen, Zhaoyuan. "Development of Methods for the Study of Phosphoproteins". Diss., CLICK HERE for online access, 2006. http://contentdm.lib.byu.edu/ETD/image/etd1629.pdf.
Pełny tekst źródłaGoswami, Suranjana. "IDENTIFICATION OF PHOSPHOPROTEINS INVOLVED IN SPERM MATURATION AND FERTILITY". Kent State University / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=kent1532952768427828.
Pełny tekst źródłaSheehan, M. A. "Phosphoproteins in malignant and non-malignant human-human cell hybrids". Thesis, University of Oxford, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.355800.
Pełny tekst źródłaRothman, Deborah Maria. "Caged phosphopeptides and phosphoproteins : agents in unraveling complex biological pathways". Thesis, Massachusetts Institute of Technology, 2005. http://hdl.handle.net/1721.1/32429.
Pełny tekst źródłaVita.
Includes bibliographical references.
Within cellular signaling, protein phosphorylation is the post-translational modification most frequently used to regulate protein activity. Protein kinases and phosphoprotein phosphatases generate and terminate these phosphoryl signals, respectively. Chemical approaches for studying protein phosphorylation and the roles of phosphoproteins include photolabile caged analogs of bioactive species. Caged compounds are ideal chemical probes for studying cellular signaling because they afford researchers spatial and temporal control over the release of targeted effector molecules. Ligands or proteins involved in signal transduction can be chemically caged and subsequently irradiated to release a concentration burst of a specific species, allowing the downstream effects to be monitored without disrupting other aspects of the system. The syntheses and applications of caged phosphopeptides and phosphoproteins have been developed and detailed within this thesis. Two methods to synthesize 1-(2-nitrophenyl)ethyl caged phosphopeptides were developed. These peptides demonstrated good quantum yields of uncaging as compared to literature values of other ortho-nitrobenzyl derived caged compounds. A study in which these caged phosphopeptide tools yielded seminal information about the 14-3-3 protein family's involvement in cell cycle control successfully demonstrated the unique utility of these probes. Furthermore, the synthesis that allowed the extension of the nonsense codon suppression methodology to include caged phosphoproteins was developed.
(cont.) The three most commonly phosphorylated amino acids (serine, threonine, and tyrosine) were each incorporated into a test protein in their caged phosphorylated form. Toward studying cell motility, caged phosphoserine was incorporated into position 153 of mVASP for use in live cell assays.
by Deborah Maria Rothman.
Ph.D.
Neubauer, Gitte Jackie. "Microcharacterisation of multi-protein complexes and phosphoproteins by nanoelectrospray mass spectrometry". Thesis, University of London, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.299339.
Pełny tekst źródłaKsiążki na temat "Phosphoproteins"
L, Khandelwal R., i Wang Jerry H, red. Reversible protein phosphorylation in cell regulation. Dordrecht: Kluwer Academic Publishers, 1993.
Znajdź pełny tekst źródłaM, Sefton Bartholomew, i Hunter Tony 1943-, red. Protein phosphorylation. San Diego, Calif: Academic Press, 1998.
Znajdź pełny tekst źródłaInternational Conference on Second Messengers and Phosphoproteins (12th 2004 Montréal, Québec). Second messengers and phosphoprotein signaling: Proceedings of the 12th International Conference on Second Messengers and Phosphoproteins : Montreal, Canada, August 3-7, 2004. Redaktorzy Anand-Srivastava Madhu B, Tremblay Michel i Srivastava Ashok K. Bologna: Medimond International Proceedings, 2004.
Znajdź pełny tekst źródłaN, Kochetkova M., i Engelʹgardt, V. A. b. 1894., red. Rolʹ fosforilirovanii͡a︡ v reguli͡a︡t͡s︡ii kletochnoĭ aktivnosti. Moskva: "Nauka", 1985.
Znajdź pełny tekst źródłaAnnamaria, Torriani-Gorini, Yagil Ezra i Silver S. (Simon), red. Phosphate in microorganisms: Cellular and molecular biology. Washington, D.C: ASM Press, 1994.
Znajdź pełny tekst źródłaSteven, Sikes C., Wheeler A. P, American Chemical Society. Division of Industrial and Engineering Chemistry. i American Chemical Society Meeting, red. Surface reactive peptides and polymers: Discovery and commercialization : developed from a symposium sponsored by the Division of Industrial and Engineering Chemistry at the 197th National Meeting of the American Chemical Society, Dallas, Texas, April 12-13, 1989. Washington, DC: The Society, 1991.
Znajdź pełny tekst źródłaJ, Fielding Christopher, red. Lipid rafts and caveolae: From membrane biophysics to cell biology. Weinheim: Wiley-VCH, 2006.
Znajdź pełny tekst źródłaG, Hardie D., red. Protein phosphorylation: A practical approach. Oxford: Oxford University Press, 1993.
Znajdź pełny tekst źródłaJohn, Solaro R., red. Protein phosphorylation in heart muscle. Boca Raton, Fla: CRC Press, 1986.
Znajdź pełny tekst źródłaNam, Yesi. Partial purification and characterization of human sublingual gland protein kinase(s) responsible for phosphorylating secreted salivary phosphoproteins. Ottawa: National Library of Canada, 1996.
Znajdź pełny tekst źródłaCzęści książek na temat "Phosphoproteins"
Greengard, Paul. "Neuronal Phosphoproteins". W Molecular Neurobiology, 81–119. Totowa, NJ: Humana Press, 1988. http://dx.doi.org/10.1007/978-1-4612-4604-6_5.
Pełny tekst źródłaPuente, Lawrence G., i Lynn A. Megeney. "Isolation of Phosphoproteins". W Methods in Molecular Biology™, 365–72. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-60327-064-9_28.
Pełny tekst źródłaSanz Ressel, Berenice L., i Alfredo A. Molinolo. "Immunohistochemical Techniques for Phosphoproteins". W Methods in Molecular Biology, 259–64. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2811-9_17.
Pełny tekst źródłaVeis, Arthur. "Phosphoproteins From Teeth and Bone". W Ciba Foundation Symposium 136 - Cell and Molecular Biology of Vertebrate Hard Tissues, 161–77. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470513637.ch11.
Pełny tekst źródłaVeis, Arthur, Boris Sabsay i Chou Bing Wu. "Phosphoproteins as Mediators of Biomineralization". W ACS Symposium Series, 1–12. Washington, DC: American Chemical Society, 1991. http://dx.doi.org/10.1021/bk-1991-0444.ch001.
Pełny tekst źródłaRokka, Anne, Eva-Mari Aro i Alexander V. Vener. "Thylakoid Phosphoproteins: Identification of Phosphorylation Sites". W Methods in Molecular Biology, 171–86. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-925-3_15.
Pełny tekst źródłaHolt, C., i R. T. Bailey. "Interaction of Phosphoproteins with Calcium Phosphate". W Springer Series in Biophysics, 169–70. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-73925-5_33.
Pełny tekst źródłaVolovik, O. I., T. T. Nosenko i S. K. Sytnik. "Control of Chloroplast Electron Transport by Phosphoproteins". W Photosynthesis: Mechanisms and Effects, 2063–66. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_483.
Pełny tekst źródłaHenjes, Frauke, Frank Götschel, Anika Jöcker i Ulrike Korf. "Quantitative Analysis of Phosphoproteins Using Microspot Immunoassays". W Methods in Molecular Biology, 191–201. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-286-1_13.
Pełny tekst źródłaBank, B., D. L. Chute i J. Gurd. "Vertebrate Memory Models: Alterations in Neuronal Phosphoproteins". W Brain Plasticity, Learning, and Memory, 544. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-5003-3_54.
Pełny tekst źródłaStreszczenia konferencji na temat "Phosphoproteins"
Baldelli, Elisa, Vienna Ludovini, Lucio Crinò, Lance Liotta, Emanuel Petricoin i Mariaelena Pierobon. "Abstract 1994: Impact of laser capture microdissection on cancer signaling proteins and phosphoproteins". W 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.am2015-1994.
Pełny tekst źródłaGao, Ming, Ta-Chen Huang, Chi-Long Chen, Hui-Ching Tu, Wen-Chi Feng, Yen-Shen Lu, Pei-Yen Yeh i in. "Abstract 3761: Tissue processing time affects the expression of phosphoproteins after breast cancer resection". W Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3761.
Pełny tekst źródłaMueller, Claudius, Lorenzo Colarossi, Antonella Chiechi, Rosa I. Gallagher, Amy VanMeter, Kirsten H. Edmiston, Frankie A. Holmes, Yasir Nagarwala, Lance A. Liotta i Virginia A. Espina. "Abstract 1265: Tissue is alive: Preserving phosphoproteins and tissue morphology in clinical trial samples". W Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-1265.
Pełny tekst źródłaSidhanth, C., Manoj Garg, P. Manasa, S. Krishna Priya, S. Bindhya, S. Sneha, R. P. Nagare, S. Shirley, M. Kanchan i Trivadi S. Ganesan. "Abstract 212: Identification by mass spectrometry of unique phosphoproteins subsequent to signaling through c-ErbB2". W Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-212.
Pełny tekst źródłaKilmer, Greg, Krishna Vattem, Eric Hommema, Ken Maas, Atul Deshpande i Brian L. Webb. "Abstract LB-119: Production of functionally active glycoproteins and phosphoproteins based on a novel human in vitro expression system". W Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-lb-119.
Pełny tekst źródłaHofmann, Marco H., i Klaus-Peter Kuenkele. "Abstract 710: Kinetic of phosphoproteins in the PI3K and MAPK pathway reflect responsiveness of Ewing's Sarcoma cells to R1507, a human IgG1 Mab that binds IGF-IR". W Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-710.
Pełny tekst źródłaImaoka, T., i T. Asaji. "FUNCTION OF PLATELET 47K PHOSPHOPROTEIN". W XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644634.
Pełny tekst źródłaPsallidas, Ioannis, Keparesia Karabela, Davina Simoes, Sophia Magkouta, Charis Roussos, Ioannis Kalomenidis i Georgios T. Stathopoulos. "Secreted Phosphoprotein-1 Enhances Urethane-induced Lung Carcinogenesis". W 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.a2521.
Pełny tekst źródłaMerlin, J.-L., M. Lion, J. Wong, T. Bachelot, F. André, I. Treilleux, D. Loussouarn i in. "Abstract P1-08-27: Quantitative analysis of tumor expression of phosphoproteins from PI3-kinase and MAP-kinase signaling pathways as biomarkers of the biological and clinical activity of trastuzumab and everolimus in breast cancer: Unicancer RADHER phase II trial results". W Abstracts: Thirty-Sixth Annual CTRC-AACR San Antonio Breast Cancer Symposium - Dec 10-14, 2013; San Antonio, TX. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/0008-5472.sabcs13-p1-08-27.
Pełny tekst źródłaSeewaldt, Victoria L., Catherine Ibarra-Drendall, Patrick Pilie, William Barry, Gloria Broadwater i Emanuel Petricoin. "Abstract A108: Phosphoprotein network activation during breast cancer initiation". W Abstracts: AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Nov 7-10, 2010; Philadelphia, PA. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1940-6207.prev-10-a108.
Pełny tekst źródłaRaporty organizacyjne na temat "Phosphoproteins"
Routtenberg, Aryeh. Phosphoprotein Regulation of Behavioral Reactivity. Fort Belvoir, VA: Defense Technical Information Center, kwiecień 1992. http://dx.doi.org/10.21236/ada250400.
Pełny tekst źródłaRouttenberg, Aryeh. Phosphoprotein Regulation of Synaptic Reactivity. Fort Belvoir, VA: Defense Technical Information Center, maj 1991. http://dx.doi.org/10.21236/ada237849.
Pełny tekst źródłaRouttenberg, Aryeh. Phosphoprotein Regulation of Behavioral Reactivity. Fort Belvoir, VA: Defense Technical Information Center, lipiec 1990. http://dx.doi.org/10.21236/ada228751.
Pełny tekst źródłaKristjansdottir, Kolbrun. Differential Phosphoprotein Profiling of Tamoxifen Response. Fort Belvoir, VA: Defense Technical Information Center, sierpień 2008. http://dx.doi.org/10.21236/ada502498.
Pełny tekst źródłaKristjansdottir, Kolbrun, Stephen J. Kron i Geoffrey L. Greene. Differential Phosphoprotein Profiling of Tamoxifen Response. Fort Belvoir, VA: Defense Technical Information Center, sierpień 2009. http://dx.doi.org/10.21236/ada524493.
Pełny tekst źródłaKristjansdottir, Kolbrun. Differential Phosphoprotein Profiling of Tamoxifen Response. Fort Belvoir, VA: Defense Technical Information Center, sierpień 2010. http://dx.doi.org/10.21236/ada549243.
Pełny tekst źródłaRouttenberg, Aryeh. Phosphoprotein Regulation of Synaptic Reactivity: Enhancement and Control of a Molecular Gating Mechanism. Fort Belvoir, VA: Defense Technical Information Center, luty 1987. http://dx.doi.org/10.21236/ada179463.
Pełny tekst źródłaRouttenberg, A. Phosphoprotein Regulation of Synaptic Reactivity: Enhancement and Control of a Molecular Gating Mechanism. Fort Belvoir, VA: Defense Technical Information Center, marzec 1985. http://dx.doi.org/10.21236/ada154511.
Pełny tekst źródłaRouttenberg, Aryeh. Phosphoprotein Regulation of Synaptic Reactivity: Enhancement and Control of a Molecular Gating Mechanism. Fort Belvoir, VA: Defense Technical Information Center, kwiecień 1985. http://dx.doi.org/10.21236/ada217196.
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