Journal articles on the topic 'Hox proteins'
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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 textGalant, Ron, Christopher M. Walsh, and Sean B. Carroll. "Hox repression of a target gene: extradenticle-independent, additive action through multiple monomer binding sites." Development 129, no. 13 (July 1, 2002): 3115–26. http://dx.doi.org/10.1242/dev.129.13.3115.
Full textBeuchle, D., G. Struhl, and J. Muller. "Polycomb group proteins and heritable silencing of Drosophila Hox genes." Development 128, no. 6 (March 15, 2001): 993–1004. http://dx.doi.org/10.1242/dev.128.6.993.
Full textPaço, Ana, Simone Aparecida de Bessa Garcia, Joana Leitão Castro, Ana Rita Costa-Pinto, and Renata Freitas. "Roles of the HOX Proteins in Cancer Invasion and Metastasis." Cancers 13, no. 1 (December 22, 2020): 10. http://dx.doi.org/10.3390/cancers13010010.
Full textBridoux, Laure, Françoise Gofflot, and René Rezsohazy. "HOX Protein Activity Regulation by Cellular Localization." Journal of Developmental Biology 9, no. 4 (December 7, 2021): 56. http://dx.doi.org/10.3390/jdb9040056.
Full textChang, C. P., L. Brocchieri, W. F. Shen, C. Largman, and M. L. Cleary. "Pbx modulation of Hox homeodomain amino-terminal arms establishes different DNA-binding specificities across the Hox locus." Molecular and Cellular Biology 16, no. 4 (April 1996): 1734–45. http://dx.doi.org/10.1128/mcb.16.4.1734.
Full textLu, Q., P. S. Knoepfler, J. Scheele, D. D. Wright, and M. P. Kamps. "Both Pbx1 and E2A-Pbx1 bind the DNA motif ATCAATCAA cooperatively with the products of multiple murine Hox genes, some of which are themselves oncogenes." Molecular and Cellular Biology 15, no. 7 (July 1995): 3786–95. http://dx.doi.org/10.1128/mcb.15.7.3786.
Full textCarnesecchi, Julie, Pedro B. Pinto, and Ingrid Lohmann. "Hox transcription factors: an overview of multi-step regulators of gene expression." International Journal of Developmental Biology 62, no. 11-12 (2018): 723–32. http://dx.doi.org/10.1387/ijdb.180294il.
Full textDraime, Amandine, Laure Bridoux, Yacine Graba, and René Rezsohazy. "Post-translational modifications of HOX proteins, an underestimated issue." International Journal of Developmental Biology 62, no. 11-12 (2018): 733–44. http://dx.doi.org/10.1387/ijdb.180178rr.
Full textKnoepfler, P. S., and M. P. Kamps. "The pentapeptide motif of Hox proteins is required for cooperative DNA binding with Pbx1, physically contacts Pbx1, and enhances DNA binding by Pbx1." Molecular and Cellular Biology 15, no. 10 (October 1995): 5811–19. http://dx.doi.org/10.1128/mcb.15.10.5811.
Full textGofflot, Françoise, and Benoit Lizen. "Emerging roles for HOX proteins in synaptogenesis." International Journal of Developmental Biology 62, no. 11-12 (2018): 807–18. http://dx.doi.org/10.1387/ijdb.180299fg.
Full textRyoo, H. D., T. Marty, F. Casares, M. Affolter, and R. S. Mann. "Regulation of Hox target genes by a DNA bound Homothorax/Hox/Extradenticle complex." Development 126, no. 22 (November 15, 1999): 5137–48. http://dx.doi.org/10.1242/dev.126.22.5137.
Full textChan, S. K., H. D. Ryoo, A. Gould, R. Krumlauf, and R. S. Mann. "Switching the in vivo specificity of a minimal Hox-responsive element." Development 124, no. 10 (May 15, 1997): 2007–14. http://dx.doi.org/10.1242/dev.124.10.2007.
Full textLaurent, Audrey, Rejane Bihan, Francis Omilli, Stephane Deschamps, and Isabelle Pellerin. "PBX proteins: much more than Hox cofactors." International Journal of Developmental Biology 52, no. 1 (2008): 9–20. http://dx.doi.org/10.1387/ijdb.072304al.
Full textPavlopoulos, Anastasios, and Michalis Averof. "Developmental Evolution: Hox Proteins Ring the Changes." Current Biology 12, no. 8 (April 2002): R291—R293. http://dx.doi.org/10.1016/s0960-9822(02)00804-7.
Full textVervoort, Michel. "Functional evolution of Hox proteins in arthropods." BioEssays 24, no. 9 (August 22, 2002): 775–79. http://dx.doi.org/10.1002/bies.10146.
Full textHess, Jay L., Zhaohai Yang, Haoren Wang, Ya-Xiong Chen, Thomas A. Milne, Mary Ellen Martin, Robert K. Slany, and Xianxin Hua. "Interaction of MLL Amino Terminal Sequences with Menin Is Required for Transformation." Blood 106, no. 11 (November 16, 2005): 664. http://dx.doi.org/10.1182/blood.v106.11.664.664.
Full textLu, Q., and M. P. Kamps. "Structural determinants within Pbx1 that mediate cooperative DNA binding with pentapeptide-containing Hox proteins: proposal for a model of a Pbx1-Hox-DNA complex." Molecular and Cellular Biology 16, no. 4 (April 1996): 1632–40. http://dx.doi.org/10.1128/mcb.16.4.1632.
Full textViganò, Maria Alessandra, Giuliana Di Rocco, Vincenzo Zappavigna, and Fulvio Mavilio. "Definition of the Transcriptional Activation Domains of Three Human HOX Proteins Depends on the DNA-Binding Context." Molecular and Cellular Biology 18, no. 11 (November 1, 1998): 6201–12. http://dx.doi.org/10.1128/mcb.18.11.6201.
Full textSalsi, Valentina, Silvia Ferrari, Roberta Ferraresi, Andrea Cossarizza, Alexis Grande, and Vincenzo Zappavigna. "HOXD13 Binds DNA Replication Origins To Promote Origin Licensing and Is Inhibited by Geminin." Molecular and Cellular Biology 29, no. 21 (August 24, 2009): 5775–88. http://dx.doi.org/10.1128/mcb.00509-09.
Full textChang, C. P., Y. Jacobs, T. Nakamura, N. A. Jenkins, N. G. Copeland, and M. L. Cleary. "Meis proteins are major in vivo DNA binding partners for wild-type but not chimeric Pbx proteins." Molecular and Cellular Biology 17, no. 10 (October 1997): 5679–87. http://dx.doi.org/10.1128/mcb.17.10.5679.
Full textMilne, Thomas A., Mary Ellen Martin, Robert K. Slany, and Jay L. Hess. "Leukemogenic MLL Fusion Proteins Promote MLL Association with HOX Loci Resulting in Persistent Expression." Blood 104, no. 11 (November 16, 2004): 386. http://dx.doi.org/10.1182/blood.v104.11.386.386.
Full textLi, X., A. Veraksa, and W. McGinnis. "A sequence motif distinct from Hox binding sites controls the specificity of a Hox response element." Development 126, no. 24 (December 15, 1999): 5581–89. http://dx.doi.org/10.1242/dev.126.24.5581.
Full textSánchez, M., P. A. Jennings, and C. Murre. "Conformational changes induced in Hoxb-8/Pbx-1 heterodimers in solution and upon interaction with specific DNA." Molecular and Cellular Biology 17, no. 9 (September 1997): 5369–76. http://dx.doi.org/10.1128/mcb.17.9.5369.
Full textPrimon, Monika, Keith D. Hunter, Hardev S. Pandha, and Richard Morgan. "Kinase Regulation of HOX Transcription Factors." Cancers 11, no. 4 (April 10, 2019): 508. http://dx.doi.org/10.3390/cancers11040508.
Full textJacobs, Yakop, Catherine A. Schnabel, and Michael L. Cleary. "Trimeric Association of Hox and TALE Homeodomain Proteins Mediates Hoxb2 Hindbrain Enhancer Activity." Molecular and Cellular Biology 19, no. 7 (July 1, 1999): 5134–42. http://dx.doi.org/10.1128/mcb.19.7.5134.
Full textPineault, Nicolas, Carolina Abramovich, Hideaki Ohta, and R. Keith Humphries. "Differential and Common Leukemogenic Potentials of Multiple NUP98-Hox Fusion Proteins Alone or with Meis1." Molecular and Cellular Biology 24, no. 5 (March 1, 2004): 1907–17. http://dx.doi.org/10.1128/mcb.24.5.1907-1917.2004.
Full textPeltenburg, L. T., and C. Murre. "Specific residues in the Pbx homeodomain differentially modulate the DNA-binding activity of Hox and Engrailed proteins." Development 124, no. 5 (March 1, 1997): 1089–98. http://dx.doi.org/10.1242/dev.124.5.1089.
Full textTaniguchi, Yasushi. "Hox Transcription Factors: Modulators of Cell-Cell and Cell-Extracellular Matrix Adhesion." BioMed Research International 2014 (2014): 1–12. http://dx.doi.org/10.1155/2014/591374.
Full textGhosh, Priyanjali, and Charles G. Sagerström. "Developing roles for Hox proteins in hindbrain gene regulatory networks." International Journal of Developmental Biology 62, no. 11-12 (2018): 767–74. http://dx.doi.org/10.1387/ijdb.180141cs.
Full textShanmugam, Kandavel, Nancy C. Green, Isabel Rambaldi, H. Uri Saragovi, and Mark S. Featherstone. "PBX and MEIS as Non-DNA-Binding Partners in Trimeric Complexes with HOX Proteins." Molecular and Cellular Biology 19, no. 11 (November 1, 1999): 7577–88. http://dx.doi.org/10.1128/mcb.19.11.7577.
Full textJoshi, R., L. Sun, and R. Mann. "Dissecting the functional specificities of two Hox proteins." Genes & Development 24, no. 14 (July 15, 2010): 1533–45. http://dx.doi.org/10.1101/gad.1936910.
Full textAnsari, Aseem Z., and Kimberly J. Peterson-Kaufman. "A Partner Evokes Latent Differences between Hox Proteins." Cell 147, no. 6 (December 2011): 1220–21. http://dx.doi.org/10.1016/j.cell.2011.11.046.
Full textRossi, Alessandra, Karin J. Ferrari, Andrea Piunti, SriGanesh Jammula, Fulvio Chiacchiera, Luca Mazzarella, Andrea Scelfo, Pier Giuseppe Pelicci, and Diego Pasini. "Maintenance of leukemic cell identity by the activity of the Polycomb complex PRC1 in mice." Science Advances 2, no. 10 (October 2016): e1600972. http://dx.doi.org/10.1126/sciadv.1600972.
Full textChoe, Seong-Kyu, Nikolaos Vlachakis, and Charles G. Sagerström. "Meis family proteins are required for hindbrain development in the zebrafish." Development 129, no. 3 (February 1, 2002): 585–95. http://dx.doi.org/10.1242/dev.129.3.585.
Full textCastelli-Gair, J. "The lines gene of Drosophila is required for specific functions of the Abdominal-B HOX protein." Development 125, no. 7 (April 1, 1998): 1269–74. http://dx.doi.org/10.1242/dev.125.7.1269.
Full textOzernyuk, Nikolay, and Dimitry Schepetov. "HOX-Gene Cluster Organization and Genome Duplications in Fishes and Mammals: Transcript Variant Distribution along the Anterior–Posterior Axis." International Journal of Molecular Sciences 23, no. 17 (September 1, 2022): 9990. http://dx.doi.org/10.3390/ijms23179990.
Full textAlper, Scott, and Cynthia Kenyon. "The zinc finger protein REF-2 functions with the Hox genes to inhibit cell fusion in the ventral epidermis of C. elegans." Development 129, no. 14 (July 15, 2002): 3335–48. http://dx.doi.org/10.1242/dev.129.14.3335.
Full textRemacle, Sophie, Leïla Abbas, Olivier De Backer, Nathalie Pacico, Anthony Gavalas, Françoise Gofflot, Jacques J. Picard, and René Rezsöhazy. "Loss of Function but No Gain of Function Caused by Amino Acid Substitutions in the Hexapeptide of Hoxa1 In Vivo." Molecular and Cellular Biology 24, no. 19 (October 1, 2004): 8567–75. http://dx.doi.org/10.1128/mcb.24.19.8567-8575.2004.
Full textCh'ng, Q., and C. Kenyon. "egl-27 generates anteroposterior patterns of cell fusion in C. elegans by regulating Hox gene expression and Hox protein function." Development 126, no. 15 (August 1, 1999): 3303–12. http://dx.doi.org/10.1242/dev.126.15.3303.
Full textDe Kumar, Bony, and Diane C. Darland. "The Hox protein conundrum: The “specifics” of DNA binding for Hox proteins and their partners." Developmental Biology 477 (September 2021): 284–92. http://dx.doi.org/10.1016/j.ydbio.2021.06.002.
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