Academic literature on the topic 'Hox proteins'
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Journal articles on the topic "Hox proteins"
Shen, W. F., J. C. Montgomery, S. Rozenfeld, J. J. Moskow, H. J. Lawrence, A. M. Buchberg, and C. Largman. "AbdB-like Hox proteins stabilize DNA binding by the Meis1 homeodomain proteins." Molecular and Cellular Biology 17, no. 11 (November 1997): 6448–58. http://dx.doi.org/10.1128/mcb.17.11.6448.
Full textMann, Richard S., and Markus Affolter. "Hox proteins meet more partners." Current Opinion in Genetics & Development 8, no. 4 (August 1998): 423–29. http://dx.doi.org/10.1016/s0959-437x(98)80113-5.
Full textZhang, Jianxuan, Jae-Hung Shieh, Liren Liu, Magdalena Plasilova, Yue Zhang, Gianni Morrone, Malcolm A. S. Moore, and Pengbo Zhou. "Ubiquitin-Proteolytic Control of HOX Homeodomain Proteins." Blood 108, no. 11 (November 16, 2006): 1121. http://dx.doi.org/10.1182/blood.v108.11.1121.1121.
Full textShen, Wei-fang, Keerthi Krishnan, H. J. Lawrence, and Corey Largman. "The HOX Homeodomain Proteins Block CBP Histone Acetyltransferase Activity." Molecular and Cellular Biology 21, no. 21 (November 1, 2001): 7509–22. http://dx.doi.org/10.1128/mcb.21.21.7509-7522.2001.
Full textMartinou, Eirini, Giulia Falgari, Izhar Bagwan, and Angeliki M. Angelidi. "A Systematic Review on HOX Genes as Potential Biomarkers in Colorectal Cancer: An Emerging Role of HOXB9." International Journal of Molecular Sciences 22, no. 24 (December 14, 2021): 13429. http://dx.doi.org/10.3390/ijms222413429.
Full textPellerin, I., C. Schnabel, K. M. Catron, and C. Abate. "Hox proteins have different affinities for a consensus DNA site that correlate with the positions of their genes on the hox cluster." Molecular and Cellular Biology 14, no. 7 (July 1994): 4532–45. http://dx.doi.org/10.1128/mcb.14.7.4532-4545.1994.
Full textPellerin, I., C. Schnabel, K. M. Catron, and C. Abate. "Hox proteins have different affinities for a consensus DNA site that correlate with the positions of their genes on the hox cluster." Molecular and Cellular Biology 14, no. 7 (July 1994): 4532–45. http://dx.doi.org/10.1128/mcb.14.7.4532.
Full textScott, Matthew P. "Hox proteins reach out round DNA." Nature 397, no. 6721 (February 1999): 649–51. http://dx.doi.org/10.1038/17685.
Full textKyba, Michael. "Modulating the malignancy of Hox proteins." Blood 129, no. 3 (January 19, 2017): 269–70. http://dx.doi.org/10.1182/blood-2016-11-751909.
Full textRinaldi, Lucrezia, Andrew J. Saurin, and Yacine Graba. "Fattening the perspective of Hox protein specificity through SLiMming." International Journal of Developmental Biology 62, no. 11-12 (2018): 755–66. http://dx.doi.org/10.1387/ijdb.180306yg.
Full textDissertations / Theses on the topic "Hox proteins"
Goh, Siew-Lee. "Functional studies of MEIS1, a HOX co-factor." Thesis, McGill University, 2007. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=103200.
Full textSvingen, Terje, and n/a. "Hox Transcription Factors: Their Involvement in Human Cancer Cells and In Vitro Functional Specificity." Griffith University. School of Biomolecular and Biomedical Science, 2005. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20050830.135356.
Full textSvingen, Terje. "Hox Transcription Factors: Their Involvement in Human Cancer Cells and In Vitro Functional Specificity." Thesis, Griffith University, 2005. http://hdl.handle.net/10072/365774.
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Doctor of Philosophy (PhD)
School of Biomolecular and Physical Sciences
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Phelan, Michael Leo. "A molecular analysis of functional differences between hox proteins." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/tape16/PQDD_0026/NQ37012.pdf.
Full textChoo, Siew Woh. "The in vivo specificity of HOX proteins in Drosophila." Thesis, University of Cambridge, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.609425.
Full textIaroshenko, V. (Vladislav). "Role of human HOX-proteins in different cancer types." Bachelor's thesis, University of Oulu, 2019. http://jultika.oulu.fi/Record/nbnfioulu-201905221901.
Full textLitim-Mecheri, Isma. "Spécificité des protéines Hox : Rôle des motifs connus et découverte de nouveaux motifs." Thesis, Aix-Marseille 2, 2011. http://www.theses.fr/2011AIX22096.
Full textHox genes are responsible for the identity of segments along the antero-posterior axis. They are evolutionarily conserved and encode transcription factors. In vitro, all Hox proteins bind to a similar nucleotide sequence via a highly conserved DNA binding domain, the homeodomain (HD). This low specificity of DNA binding in vitro contrasts with their specificity in vivo. One way to explain this paradaox is that Hox protein function with protein cofactors, best represented by Extradenticle (Exd) in Drosophila, Pbx in mammals (collectivaly refered as PBC). Hox-PBC interaction relies on a motif located upstream of the HD, conserved in most Hox proteins, the Hexapeptide (HX). Recent work in our group identified a novel mode of Hox-PBC interaction, non-generic, specific to a subset only of Hox paralog groups, and relying on a motif located C-terminal to the HD. This highlight plasticity in Hox-PBC interaction.My PhD work aimed at investigating the mode of action of Hox protein, by studying the function of three protein motifs, with known or putative role in Exd recruitment by the Drosophila Hox protein AbdominalA (AbdA). The approach taken aimed at analyzing, using a large functional window, how these motifs, taken in isolation or collectively, define AbdA protein activity. Conclusions highlight the absence of pleitropy and a high degree of functional interaction for these protein motifs. The second part of my PhD work has been to initiate the search for novel functionally important protein motifs within Hox proteins. This was approached by selecting phylogenetically conserved motifs, and addressing their function in vitro and in vivo following motif mutations. At least one functional domain was isolated, that contributes predominantly to Dfd protein function
Weicksel, Steven E. "hox Gene Regulation and Function During Zebrafish Embryogenesis: A Dissertation." eScholarship@UMMS, 2013. https://escholarship.umassmed.edu/gsbs_diss/692.
Full textWeicksel, Steven E. "hox Gene Regulation and Function During Zebrafish Embryogenesis: A Dissertation." eScholarship@UMMS, 2010. http://escholarship.umassmed.edu/gsbs_diss/692.
Full textRinaldi, Lucrezia. "Novel functions for Hox proteins in the development of the spinal cord." Thesis, Aix-Marseille, 2018. http://www.theses.fr/2018AIXM0261/document.
Full textHox genes encode conserved homeodomain transcription factors that coordinate the specification of regional body identity during the development of bilaterian animals. There are 39 Hox genes in higher vertebrates, organized into four complexes (named A to D) on the chromosomes. Thirteen groups of paralogue genes occupy similar positions within the complexes and exhibit similar modes of expression and functions. In addition to their specific functions, for which these transcription factors are well known, some recent studies are suggestive of "generic" functions, i.e. functions common outside paralogy groups. The goal of this thesis was to look for generic functions of vertebrate Hox proteins, focusing on the development of the spinal cord in chick and mouse. We identified two such functions, implying B cluster Hox genes. The first regards the potential of Hox proteins to control autophagy, which was previously established for Drosophila Hox proteins in the fat body. My work established the spatio temporal dynamic of autophagy during spinal cord development in chick and mouse embryos. This dynamic identified complementary autophagy and Hox patterns, suggesting a generic role for Hox proteins in the repression of autophagy, which could be confirmed by gain of function in chick embryo. The second Hox generic function regards the control of spinal cord neurogenesis. The study of Hox expression highlighted a predominant expression of B cluster Hox genes in the neural tube Intermediate Zone (IZ), where they activate the expression of the Lzts1 gene, the product of which modulates AKT signaling to ultimately control neuronal differentiation
Books on the topic "Hox proteins"
Graba, Yacine. Hox genes: Methods and protocols. New York: Humana Press, 2014.
Find full textHow proteins work. New York: Garland Science, 2012.
Find full text1946-, Liepa George U., ed. Dietary proteins: How they alleviate disease and promote better health. Champaign, Ill: American Oil Chemistsʼ Society, 1992.
Find full textAllen, John F. How does protein phosphorylation regulate photosynthesis?. Amsterdam: Elsevier, 1992.
Find full textGelderloos, Peter. How nonviolence protects the state. Cambridge, Mass: South End Press, 2007.
Find full textGelderloos, Peter. How nonviolence protects the state. Harrisonburg, VA: Signalfire Press, 2005.
Find full textGelderloos, Peter. How nonviolence protects the state. Cambridge, MA: South End Press, 2006.
Find full textSusanne, Brakmann, and Johnsson Kai, eds. Directed molecular evolution of proteins: Or how to improve enzymes for biocatalysis. Weinheim: Wiley-VCH, 2002.
Find full textEzrin, Calvin. The endocrine control diet: How to beat the metabolic trap and lose weight permanently. New York: Harper & Row, 1990.
Find full textChurch discipline: How the church protects the name of Jesus. Wheaton, Ill: Crossway, 2012.
Find full textBook chapters on the topic "Hox proteins"
Agrawal, Pavan, and L. S. Shashidhara. "ChIP for Hox Proteins from Drosophila Imaginal Discs." In Methods in Molecular Biology, 241–53. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1242-1_15.
Full textGrawenhoff, Julia, Sebastian Baumann, and Sebastian P. Maurer. "In Vitro Reconstitution of Kinesin-Based, Axonal mRNA Transport." In Methods in Molecular Biology, 547–68. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-1990-2_29.
Full textSljoka, Adnan. "Structural and Functional Analysis of Proteins Using Rigidity Theory." In Sublinear Computation Paradigm, 337–67. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-4095-7_14.
Full textYoung, V. R., and P. L. Pellett. "How to Evaluate Dietary Protein." In Milk Proteins, 7–36. Heidelberg: Steinkopff, 1989. http://dx.doi.org/10.1007/978-3-642-85373-9_3.
Full textJencks, W. P. "How Does ATP Make Work?" In Protein Structure and Protein Engineering, 1–5. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-74173-9_1.
Full textKangueane, Pandjassarame, and Christina Nilofer. "Hot Spots at the Protein-Protein Interface." In Protein-Protein and Domain-Domain Interactions, 87–92. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-10-7347-2_7.
Full textLamichhane, Rajan. "How Proteins Recognize RNA." In Biophysics of RNA-Protein Interactions, 3–21. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9726-8_1.
Full textWhite, Stephen H., Gunnar von Heijne, and Donald M. Engelman. "How Proteins Shape Membranes." In Cell Boundaries, 235–64. New York: Garland Science, 2021. http://dx.doi.org/10.1201/9780429341328-8.
Full textGoodsell, David S. "How Evolution Shapes Proteins." In Atomic Evidence, 51–58. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-32510-1_8.
Full textBill, Roslyn M., Leigh Revers, and Iain B. H. Wilson. "Sugars And Proteins: How They Get It Together." In Protein Glycosylation, 85–145. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-4939-0_3.
Full textConference papers on the topic "Hox proteins"
Zhou, Pengbo, Jennifer Lee, Jianxuan Zhang, Liren Liu, Jae-Hung Shieh, and Malcolm A. S. Moore. "Abstract 1157: Ubiquitin-proteolytic control of HOX homeodomain proteins in normal and malignant hematopoiesis." In 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.am10-1157.
Full textMunch, Katharina, Claire Berton-Carabin, Karin Schroen, and Simeon Stoyanov. "Plant protein-stabilized emulsions: Implications of protein and non-protein components for lipid oxidation." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/zznf4565.
Full textTruskett, Thomas M. "How Concentration and Crowding Impact Protein Stability: Insights From a Coarse-Grained Model." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192239.
Full textRao, Jiajia. "Tuning plant protein for improved functionality and flavor profile: From field to application." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/xqxj4886.
Full textShahbazi, Zahra, Horea T. Ilies¸, and Kazem Kazerounian. "Protein Molecules as Natural Nano Bio Devices: Mobility Analysis." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13021.
Full textKirkpatrick, Emma, and Mac Marshall. "Spotlight on sustainability: How growing consumer preferences are changing the plant-based protein industry." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/gggk2278.
Full textGear, LR A., D. Freas, and J. D. Carty. "EARLY (< 5 SEC) PHOSPHORYLATIONS OF PLATELET PROTEINS FOLLOWING ACTIVATION BY ADP AND ADRENALIN, SEPARATELY AND IN COMBINATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643640.
Full textDevaki, Neksha. "Utilization of mildly fractionated pea proteins for the development of heat-stable beverage emulsions." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/ivne6416.
Full textHojilla-Evangelista, Milagros, and Roque Evangelista. "Green' Production of Protein Isolate from Novel Golden Pennycress Seeds." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/trho6904.
Full textBuehler, Markus J., and Sebastien Uzel. "Deformation and Failure of Collagenous Tissues: A Multi-Scale Study." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-205480.
Full textReports on the topic "Hox proteins"
Daddario, Sunshine. The Role of HOX Proteins in Androgen-Independent Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, November 2008. http://dx.doi.org/10.21236/ada494966.
Full textDaddario, Sunshine. The Role of HOX Proteins in Androgen-Independent Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, November 2006. http://dx.doi.org/10.21236/ada470623.
Full textHerman, Eliot D., Gad Galili, and Alan Bennett. Recognition and Disposal of Misfolded Seed Proteins. United States Department of Agriculture, August 1994. http://dx.doi.org/10.32747/1994.7568791.bard.
Full textEpel, Bernard L., Roger N. Beachy, A. Katz, G. Kotlinzky, M. Erlanger, A. Yahalom, M. Erlanger, and J. Szecsi. Isolation and Characterization of Plasmodesmata Components by Association with Tobacco Mosaic Virus Movement Proteins Fused with the Green Fluorescent Protein from Aequorea victoria. United States Department of Agriculture, September 1999. http://dx.doi.org/10.32747/1999.7573996.bard.
Full textMorrison, Mark, and Joshuah Miron. Molecular-Based Analysis of Cellulose Binding Proteins Involved with Adherence to Cellulose by Ruminococcus albus. United States Department of Agriculture, November 2000. http://dx.doi.org/10.32747/2000.7695844.bard.
Full textYalovsky, Shaul, and Julian Schroeder. The function of protein farnesylation in early events of ABA signal transduction in stomatal guard cells of Arabidopsis. United States Department of Agriculture, January 2002. http://dx.doi.org/10.32747/2002.7695873.bard.
Full textAsenath-Smith, Emily, Emily Jeng, Emma Ambrogi, Garrett Hoch, and Jason Olivier. Investigations into the ice crystallization and freezing properties of the antifreeze protein ApAFP752. Engineer Research and Development Center (U.S.), September 2022. http://dx.doi.org/10.21079/11681/45620.
Full textOhad, Nir, and Robert Fischer. Regulation of Fertilization-Independent Endosperm Development by Polycomb Proteins. United States Department of Agriculture, January 2004. http://dx.doi.org/10.32747/2004.7695869.bard.
Full textAvni, Adi, and Gitta L. Coaker. Proteomic investigation of a tomato receptor like protein recognizing fungal pathogens. United States Department of Agriculture, January 2015. http://dx.doi.org/10.32747/2015.7600030.bard.
Full textCoplin, David L., Shulamit Manulis, and Isaac Barash. roles Hrp-dependent effector proteins and hrp gene regulation as determinants of virulence and host-specificity in Erwinia stewartii and E. herbicola pvs. gypsophilae and betae. United States Department of Agriculture, June 2005. http://dx.doi.org/10.32747/2005.7587216.bard.
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