Bibliografie tematiche / HMG-box proteins

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Letteratura scientifica selezionata sul tema "HMG-box proteins"

Autore: Grafiati
Pubblicato: 19 ottobre 2022

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Articoli di riviste sul tema "HMG-box proteins"

1

Bianchi, Marco E., e Monica Beltrame. "Flexing DNA: HMG-Box Proteins and Their Partners". American Journal of Human Genetics 63, n. 6 (dicembre 1998): 1573–77. http://dx.doi.org/10.1086/302170.

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Xin, H. "DNA binding by single HMG box model proteins". Nucleic Acids Research 28, n. 20 (15 ottobre 2000): 4044–50. http://dx.doi.org/10.1093/nar/28.20.4044.

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3

Schulman, I. G., T. Wang, M. Wu, J. Bowen, R. G. Cook, M. A. Gorovsky e C. D. Allis. "Macronuclei and micronuclei in Tetrahymena thermophila contain high-mobility-group-like chromosomal proteins containing a highly conserved eleven-amino-acid putative DNA-binding sequence." Molecular and Cellular Biology 11, n. 1 (gennaio 1991): 166–74. http://dx.doi.org/10.1128/mcb.11.1.166.

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HMG (high-mobility-group protein) B and HMG C are abundant nonhistone chromosomal proteins isolated from Tetrahymena thermophila macronuclei with solubilities, molecular weights, and amino acid compositions like those of vertebrate HMG proteins. Genomic clones encoding each of these proteins have been sequenced. Both are single-copy genes that encode single polyadenylated messages whose amounts are 10 to 15 times greater in growing cells than in starved, nongrowing cells. The derived amino acid sequences of HMG B and HMG C contain a highly conserved sequence, the HMG 1 box, found in vertebrate HMGs 1 and 2, and we speculate that this sequence may represent a novel, previously unrecognized DNA-binding motif in this class of chromosomal proteins. Like HMGs 1 and 2, HMGs B and C contain a high percentage of aromatic amino acids. However, the Tetrahymena HMGs are small, are associated with nucleosome core particles, and can be specifically extracted from macronuclei by elutive intercalation, properties associated with vertebrate HMGs 14 and 17, not HMGs 1 and 2. Thus, it appears that these Tetrahymena proteins have features in common with both of the major subgroups of higher eucaryotic HMG proteins. Surprisingly, a linker histone found exclusively in transcriptionally inactive micronuclei also has several HMG-like characteristics, including the ability to be specifically extracted from nuclei by elutive intercalation and the presence of the HMG 1 box. This finding suggests that at least in T. thermophila, proteins with HMG-like properties are not restricted to regions of transcriptionally active chromatin.
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Schulman, I. G., T. Wang, M. Wu, J. Bowen, R. G. Cook, M. A. Gorovsky e C. D. Allis. "Macronuclei and micronuclei in Tetrahymena thermophila contain high-mobility-group-like chromosomal proteins containing a highly conserved eleven-amino-acid putative DNA-binding sequence". Molecular and Cellular Biology 11, n. 1 (gennaio 1991): 166–74. http://dx.doi.org/10.1128/mcb.11.1.166-174.1991.

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HMG (high-mobility-group protein) B and HMG C are abundant nonhistone chromosomal proteins isolated from Tetrahymena thermophila macronuclei with solubilities, molecular weights, and amino acid compositions like those of vertebrate HMG proteins. Genomic clones encoding each of these proteins have been sequenced. Both are single-copy genes that encode single polyadenylated messages whose amounts are 10 to 15 times greater in growing cells than in starved, nongrowing cells. The derived amino acid sequences of HMG B and HMG C contain a highly conserved sequence, the HMG 1 box, found in vertebrate HMGs 1 and 2, and we speculate that this sequence may represent a novel, previously unrecognized DNA-binding motif in this class of chromosomal proteins. Like HMGs 1 and 2, HMGs B and C contain a high percentage of aromatic amino acids. However, the Tetrahymena HMGs are small, are associated with nucleosome core particles, and can be specifically extracted from macronuclei by elutive intercalation, properties associated with vertebrate HMGs 14 and 17, not HMGs 1 and 2. Thus, it appears that these Tetrahymena proteins have features in common with both of the major subgroups of higher eucaryotic HMG proteins. Surprisingly, a linker histone found exclusively in transcriptionally inactive micronuclei also has several HMG-like characteristics, including the ability to be specifically extracted from nuclei by elutive intercalation and the presence of the HMG 1 box. This finding suggests that at least in T. thermophila, proteins with HMG-like properties are not restricted to regions of transcriptionally active chromatin.
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Veilleux, Stéphane, e Guylain Boissonneault. "Dynamics of Reporter Gene Stimulation by HMG Box Proteins". DNA and Cell Biology 21, n. 3 (marzo 2002): 199–212. http://dx.doi.org/10.1089/10445490252925440.

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Briquet, Sylvie, Charlotte Boschet, Mathieu Gissot, Emilie Tissandié, Elisa Sevilla, Jean-François Franetich, Isabelle Thiery, Zuhal Hamid, Catherine Bourgouin e Catherine Vaquero. "High-Mobility-Group Box Nuclear Factors of Plasmodium falciparum". Eukaryotic Cell 5, n. 4 (aprile 2006): 672–82. http://dx.doi.org/10.1128/ec.5.4.672-682.2006.

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ABSTRACT In eukaryotes, the high-mobility-group (HMG) nuclear factors are highly conserved throughout evolution and are divided into three families, including HGMB, characterized by an HMG box domain. Some HMGB factors are DNA structure specific and preferentially interact with distorted DNA sequences, trigger DNA bending, and hence facilitate the binding of nucleoprotein complexes that in turn activate or repress transcription. In Plasmodium falciparum, two HMGB factors were predicted: PfHMGB1 and PfHMGB2. They are small proteins, under 100 amino acids long, encompassing a characteristic HMG box domain closely related to box B of metazoan factors, which comprises two HMG box domains, A and B, in tandem. Computational analyses supported the conclusion that the Plasmodium proteins were genuine architectural HMGB factors, and in vitro analyses performed with both recombinant proteins established that they were able to interact with distorted DNA structures and bend linear DNA with different affinities. These proteins were detected in both asexual- and gametocyte-stage cells in Western blotting experiments and mainly in the parasite nuclei. PfHMGB1 is preferentially expressed in asexual erythrocytic stages and PfHMGB2 in gametocytes, in good correlation with transcript levels of expression. Finally, immunofluorescence studies revealed differential subcellular localizations: both factors were observed in the nucleus of asexual- and sexual-stage cells, and PfHMGB2 was also detected in the cytoplasm of gametocytes. In conclusion, in light of differences in their levels of expression, subcellular localizations, and capacities for binding and bending DNA, these factors are likely to play nonredundant roles in transcriptional regulation of Plasmodium development in erythrocytes.
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Kalinowska-Herok, Magdalena, e Piotr Widłak. "High mobility group proteins stimulate DNA cleavage by apoptotic endonuclease DFF40/CAD due to HMG-box interactions with DNA." Acta Biochimica Polonica 55, n. 1 (1 febbraio 2008): 21–26. http://dx.doi.org/10.18388/abp.2008_3196.

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The DFF40/CAD endonuclease is primarily responsible for internucleosomal DNA cleavage during the terminal stages of apoptosis. It has been previously demonstrated that the major HMG-box-containing chromatin proteins HMGB1 and HMGB2 stimulate naked DNA cleavage by DFF40/CAD. Here we investigate the mechanism of this stimulation and show that HMGB1 neither binds to DFF40/CAD nor enhances its ability for stable binding to DNA. Comparison of the stimulatory activities of different truncated forms of HMGB1 protein indicates that a structural array of two HMG-boxes is required for such stimulation. HMG-boxes are known to confer specific local distortions of DNA structure upon binding. Interestingly, the presence of DNA strand cross-links formed by cisplatin or transplatin, which may somehow mimic distortions induced by HMG-boxes, also affects DNA cleavage by the nuclease. The data presented suggest that changes induced in DNA conformation upon HMG-box binding makes the substrate more accessible to cleavage by DFF40/CAD nuclease and thus may contribute to preferential linker DNA cleavage during apoptosis.
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Landsman, David, e Michael Bustin. "A signature for the HMG-1 box DNA-binding proteins". BioEssays 15, n. 8 (agosto 1993): 539–46. http://dx.doi.org/10.1002/bies.950150807.

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9

Takusagawa, Mari, Yusuke Kobayashi, Yoichiro Fukao, Kumi Hidaka, Masayuki Endo, Hiroshi Sugiyama, Takashi Hamaji et al. "HBD1 protein with a tandem repeat of two HMG-box domains is a DNA clip to organize chloroplast nucleoids in Chlamydomonas reinhardtii". Proceedings of the National Academy of Sciences 118, n. 20 (11 maggio 2021): e2021053118. http://dx.doi.org/10.1073/pnas.2021053118.

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Compaction of bulky DNA is a universal issue for all DNA-based life forms. Chloroplast nucleoids (chloroplast DNA–protein complexes) are critical for chloroplast DNA maintenance and transcription, thereby supporting photosynthesis, but their detailed structure remains enigmatic. Our proteomic analysis of chloroplast nucleoids of the green alga Chlamydomonas reinhardtii identified a protein (HBD1) with a tandem repeat of two DNA-binding high mobility group box (HMG-box) domains, which is structurally similar to major mitochondrial nucleoid proteins transcription factor A, mitochondrial (TFAM), and ARS binding factor 2 protein (Abf2p). Disruption of the HBD1 gene by CRISPR-Cas9–mediated genome editing resulted in the scattering of chloroplast nucleoids. This phenotype was complemented when intact HBD1 was reintroduced, whereas a truncated HBD1 with a single HMG-box domain failed to complement the phenotype. Furthermore, ectopic expression of HBD1 in the mitochondria of yeast Δabf2 mutant successfully complemented the defects, suggesting functional similarity between HBD1 and Abf2p. Furthermore, in vitro assays of HBD1, including the electrophoretic mobility shift assay and DNA origami/atomic force microscopy, showed that HBD1 is capable of introducing U-turns and cross-strand bridges, indicating that proteins with two HMG-box domains would function as DNA clips to compact DNA in both chloroplast and mitochondrial nucleoids.
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de Froidmont, D., C. Lejour, P. Stoeva e J. M. Jacquemin. "Endosperm Box Binding Proteins: cDNA Cloning of a Wheat HMG Protein". Biotechnology & Biotechnological Equipment 10, n. 1 (gennaio 1996): 15–26. http://dx.doi.org/10.1080/13102818.1996.10818875.

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Più fonti

Tesi sul tema "HMG-box proteins"

1

Bharath, M. M. Srinivas. "Towards The Understanding Of The Structural Biology Of Histone H1". Thesis, Indian Institute of Science, 2000. http://hdl.handle.net/2005/167.

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In the eukaryotic nucleus, an immense length of DNA is compactly packaged to generate an ordered three-dimensional hierarchical structure called chromatin (van Holde, 1988; Wolffe, A.P, 1998). This organization forms a template for various DNA transaction processes like replication, transcription, recombination etc. The different stages of organization of the chromatin finally results in the 10,000-fold compaction observed in the metaphase chromosome. The problem of how the fibres of chromatin are folded has interested biologists and biochemists for decades. It has long been recognized that the Histones play a major part in this folding. However, the distinctly different roles of the Histones H2A, H2B, H3 and H4 on one hand and the lysine rich Histones such as Histone H1 and its cognates on the other, were not understood until after the discovery of the nucleosomes in the early 1970s. Some of the early insights into the structure of chromatin came through the digestion of nuclear chromatin with calcium-dependent endonucleases like micrococcal nuclease. A repeating kinetic intermediate of about 200 bp of DNA with Histones was obtained (Simpson, 1978). Based on repeating pattern of micrococcal nuclease digested chromatin and structural studies, Kornberg (1974) proposed that chromatin is composed of a flexible chain of repeating units of 100 A0 diameter. These units were termed as "nucleosomes" (Oudet et al, 1975). It then became clear that the Histones H2A, H2B, H3 and H4 were constituents of the nucleosome core particle whereas the lysine rich Histone H1 was somehow associated with the linker DNA between core particles. Hence, the formers are called core Histones and the latter as linker Histones. On further digestion of nucleosome, a nucleosome core was obtained in which wrapping of 146 bp of DNA about the Histone octamer to form the core particle provided the first level of folding. Electron microscopy and X-ray diffraction techniques suggested that this particle is a disk, 57 A0 thick and 110 A0 in diameter, and that the DNA is wound around the Histone core (Finch et al, 1977), But this cannot account for the many thousand-fold condensation of the DNA in the eukaryotic nucleus. The "string of beads" structure observed obviously could not satisfy the compaction requirement. It soon became evident that there exists some level of higher order folding of the chromatin fiber. In a classical paper, Finch and Klug (1976), showed that the extended nucleosomal filaments condense into irregular fibers of about 30 nm diameter in the presence of low concentrations of Mg 2+. Based on the data from earlier structural studies, these authors proposed a solenoid model in which nucleosomes were wrapped into a regular helix with a pitch of about 11nm. Later, it was observed that the formation of well defined fibers requires the presence of lysine rich Histones such as Histone H1.
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Bounaix, Morand du Puch Christophe. "Analyse des interactions ADN lésé / protéines : Optimisations méthodologiques et applications aux dommages de l’ADN engendrés par les dérivés du platine". Grenoble, 2010. https://theses.hal.science/tel-00549987.

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La présence de lésions sur l'ADN contribue à déstabiliser sa structure, bloquant certains processus vitaux pour la cellule. Ces altérations peuvent cependant avoir un intérêt thérapeutique, par exemple dans le cas de l'utilisation d'anticancéreux tels que les dérivés du platine. Les adduits volumineux qu'ils génèrent, s'ils ne sont pas réparés, entraînent la cellule vers l'apoptose. La compréhension de la réponse à ces anticancéreux passe par l'étude des protéines qui interagissent directement avec les dommages, et dont l'ensemble constitue l'interactome des lésions de l'ADN. Ce travail de thèse présente le développement d'outils destinés à compléter la liste des protéines associées aux adduits du platine. Dans un premier temps, nous avons utilisé un piège à protéines (ligand fishing) constitué de plasmides lésés fixés sur des billes magnétiques. Trois dérivés du platine ont été sélectionnés pour générer les lésions : le cisplatine (molécule princeps), l'oxaliplatine, et le satraplatine. Ce piège a permis d'obtenir, à partir d'extraits nucléaires issus de cellules cancéreuses HeLa et grâce à une identification par protéomique, une liste de candidats comprenant des protéines déjà connues (HMGB1, hUBF, complexe FACT), mais aussi 29 nouveaux membres de l'interactome. Parmi ceux-ci, nous avons relevé PNUTS, TOX4 et WDR82, qui constituent les sous-unités du complexe PTW/PP, très récemment découvert. La présence de ce complexe a été également validée sur un modèle d'adénocarcinome mammaire MDA MB 231, et les conséquences biologiques de son interaction avec les adduits du platine devront maintenant être précisées. Dans un second temps, nous avons mis au point une biopuce permettant d'étudier les interactions ADN lésé/protéine par SPRi. Les affinités respectives d'HMGB1 et du nouveau candidat TOX4 pour les adduits des trois dérivés du platine ont pu être ainsi confirmées. Dans un dernier temps, nous avons étudié le rôle de DDB2 (acteur de la reconnaissance des photoproduits UV) dans la prise en charge des adduits platinés. Les expérimentations menées sur les cellules MDA MB 231 exprimant DDB2 de façon différentielle nous ont permis de vérifier que cette protéine ne participe pas à la réparation des adduits du cisplatine, contribuant plutôt à potentialiser l'action cytotoxique de cet agent. Dans le futur, nos microsystèmes pourront être adaptés à l'étude de l'interactome d'autres lésions de l'ADN
DNA lesions contribute to the alteration of DNA structure, thereby inhibiting essential cellular processes. Such alterations may be beneficial for chemotherapies, for example in the case of platinum anticancer agents. They generate bulky adducts that, if not repaired, ultimately cause apoptosis. A better understanding of the biological response to such molecules can be obtained through the study of proteins that directly interact with the damages. These proteins constitute the DNA lesions interactome. This thesis presents the development of tools aiming at increasing the list of platinum adduct-associated proteins. Firstly, we designed a ligand fishing system made of damaged plasmids immobilized onto magnetic beads. Three platinum drugs were selected for our study: cisplatin, oxaliplatin and satraplatin. Following exposure of the trap to nuclear extracts from HeLa cancer cells and identification of retained proteins by proteomics, we obtained already known candidates (HMGB1, hUBF, FACT complex) but also 29 new members of the platinated-DNA interactome. Among them, we noted the presence of PNUTS, TOX4 and WDR82, which associate to form the recently-discovered PTW/PP complex. Their capture was then confirmed with a second model, namely breast cancer cell line MDA MB 231, and the biological consequences of such an interaction now need to be elucidated. Secondly, we adapted a SPRi biochip to the study of platinum-damaged DNA/proteins interactions. Affinity of HMGB1 and newly characterized TOX4 for adducts generated by our three platinum drugs could be validated thanks to the biochip. Finally, we used our tools, as well as analytical chemistry and biochemistry methods, to evaluate the role of DDB2 (a factor involved in the recognition of UV-induced lesions) in the repair of cisplatin adducts. Our experiments using MDA MB 231 cells differentially expressing DDB2 showed that this protein is not responsible for the repair of platinum damages. Instead, it appears to act as a positive mediator of their cytotoxicity. In the near future, the abovementioned microsystems will be adapted to the study of the interactome of other DNA lesions
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Sparkes, Andrew Charles. "The isolation and characterisation of Sry-related HMG box gene from Droposhila melanogaster". Thesis, University of Portsmouth, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.310391.

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Roemer, Sarah Clark. "Structural and functional analysis of progesterone receptor-DNA interaction /". Connect to full text via ProQuest. IP filtered, 2005.

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Thesis (Ph.D. in Molecular Biology) -- University of Colorado at Denver and Health Sciences Center, 2005.
Typescript. Includes bibliographical references (leaves 165-185). Free to UCDHSC affiliates. Online version available via ProQuest Digital Dissertations;
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Rittenhouse, Kimberley Rochelle. "Bullwinkle, an HMG box protein, is required for proper development during oogenesis, embryogenesis and metamorphosis in Drosophila melanogaster /". Thesis, Connect to this title online; UW restricted, 1996. http://hdl.handle.net/1773/10267.

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Chan, Chien-Yi, e 詹前毅. "The Suppressive Role of Transcription Factor HMG box-Containing Protein 1 (HBP1) in Oral Cancer Malignancy". Thesis, 2017. http://ndltd.ncl.edu.tw/handle/ff8a7s.

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Chen, Zih-Hua, e 陳咨樺. "The role of transcription factor HMG box-containing protein 1 (HBP1) in insulin sensitivity of adipocytes". Thesis, 2018. http://ndltd.ncl.edu.tw/handle/95ne3a.

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Libri sul tema "HMG-box proteins"

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Mumford, Katherine Laura. Genomic cloning and gene organisation of the Drosophila HMG box protein DSox14. Portsmouth: University of Portsmouth, School of Biological Sciences, 1999.

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Capitoli di libri sul tema "HMG-box proteins"

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Travers, Andrew A., e Jean O. Thomas. "Chromosomal HMG-box proteins". In Chromatin Structure and Dynamics: State-of-the-Art, 103–34. Elsevier, 2004. http://dx.doi.org/10.1016/s0167-7306(03)39005-2.

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Banerjee, Arundhati, e Sujay Ray. "An Optimized In Silico Neuroinformatics Approach". In Handbook of Research on Natural Computing for Optimization Problems, 802–20. IGI Global, 2016. http://dx.doi.org/10.4018/978-1-5225-0058-2.ch032.

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A computationally optimized molecular analysis into the cell-fate regulations from embryonic development is one of the unexplored zones in human neurogenic field. It is governed by SOX11 (Sex determining regions-Y bOX-11) protein domain's interaction with DNA. In the present study, 3D monomer of the responsible domain of SOX11 was constructed, simulated and analyzed. Residues indulged with DNA interaction were examined. The observed conserved residue, Arg3 and Arg16 in the wild-type SOX11-DNA interaction were mutated with Ala3 and Ala16. Mutated SOX11-HMG protein sequence was re-modeled and optimized. Residue-level alteration on DNA interaction was examined. On mutation, stability of the proteins (on DNA interaction) and protein-DNA complexes were discerned via energy-calculating parameters, solvent-accessibility area, electrostatic surface-potential and conformational switching, with supportive statistical significance. Therefore, this probe provides an outlook to discern SOX11 to interact firmly with DNA via mutations and thereby perform cell-fate determinations more efficiently.
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Atti di convegni sul tema "HMG-box proteins"

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Lobbardi, Riadh, Jordan Pinder, Barbara Martinez, Jessica Blackburn, Nouran Abdelfattah, Debra Toiber, Manon De Waard et al. "Abstract 3865: Thymocyte selection-associated HMG box protein (TOX) induces genomic instability in T-cell acute lymphoblastic leukemia". In 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.am2015-3865.

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Lobbardi, Riadh, Jordan Pinder, Barbara Martinez-Pastor, Jessica Blackburn, Brian J. Abraham, Marc Mansour, Nouran S. Abdelfattah et al. "Abstract 3583: Thymocyte selection-associated HMG box protein (TOX) induces genomic instability in T-cell acute lymphoblastic leukemia". In 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.am2016-3583.

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Scott, Andrew C., Steven Camara, Peter Lauer, Alexandra Synder, Dmitriy Zamarin, Tyler Walther, Olivier Levy et al. "Abstract A215: Thymocyte selection-associated HMG box protein TOX is a master regulator of tumor-specific T-cell dysfunction". In Abstracts: Fourth CRI-CIMT-EATI-AACR International Cancer Immunotherapy Conference: Translating Science into Survival; September 30 - October 3, 2018; New York, NY. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/2326-6074.cricimteatiaacr18-a215.

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Chou, I.-Tai, Chien-Yi Chan, Ming-Fen Lee e Chun-Yin Huang. "Abstract 2202: HMG box-containing protein 1 (HBP1) is a direct target of transcription factor FOXO1 in invasive oral cancer". In 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.am2012-2202.

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Chan, Chien-Yi, Ming-Fen Lee, I.-Tai Chou, Amy S. Yee e Chun-Yin Huang. "Abstract 5624: HMG box-containing protein 1 (HBP1) participates in the antitumor effect of N-acetylcysteine (NAC) in invasive oral cancer". In 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.am2012-5624.

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