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Статті в журналах з теми "HMGA proteins"
Meireles Da Costa, Nathalia, Luis Felipe Ribeiro Pinto, Luiz Eurico Nasciutti, and Antonio Palumbo Jr. "The Prominent Role of HMGA Proteins in the Early Management of Gastrointestinal Cancers." BioMed Research International 2019 (October 13, 2019): 1–7. http://dx.doi.org/10.1155/2019/2059516.
Повний текст джерелаParisi, Silvia, Silvia Piscitelli, Fabiana Passaro, and Tommaso Russo. "HMGA Proteins in Stemness and Differentiation of Embryonic and Adult Stem Cells." International Journal of Molecular Sciences 21, no. 1 (January 6, 2020): 362. http://dx.doi.org/10.3390/ijms21010362.
Повний текст джерелаVignali, Robert, and Silvia Marracci. "HMGA Genes and Proteins in Development and Evolution." International Journal of Molecular Sciences 21, no. 2 (January 19, 2020): 654. http://dx.doi.org/10.3390/ijms21020654.
Повний текст джерелаPIERANTONI, Giovanna Maria, Valter AGOSTI, Monica FEDELE, Heather BOND, Irene CALIENDO, Gennaro CHIAPPETTA, Francesco LO COCO, et al. "High-mobility group A1 proteins are overexpressed in human leukaemias." Biochemical Journal 372, no. 1 (May 15, 2003): 145–50. http://dx.doi.org/10.1042/bj20021493.
Повний текст джерелаLichota, J., and K. D. Grasser. "Interaction of Maize Chromatin-Associated HMG Proteins with Mononucleosomes: Role of Core and Linker Histones." Biological Chemistry 384, no. 7 (July 15, 2003): 1019–27. http://dx.doi.org/10.1515/bc.2003.114.
Повний текст джерелаBalachandran, Akilandeswari, Ajit Zambre, Jagjot Singh Kainth, Lakshmi Dhevi Nagarajha Selvan, Sowmya Parameswaran, Zahra Afrasiabi, Subramanian Krishnakumar, Raghuraman Kannan, and Anandhi Upendran. "Targeting HMGA protein inhibits retinoblastoma cell proliferation." RSC Advances 8, no. 55 (2018): 31510–14. http://dx.doi.org/10.1039/c8ra06026f.
Повний текст джерелаLi, Liping, Wenyan Lu, Alison R. Moliterno, Lingling Xian, Joseph Kim, Ophelia Rogers, Jerry L. Spivak, and Linda Resar. "High Mobility Group A1 Chromatin Regulators: Key Epigenetic Switches and Therapeutic Targets Required for Leukemic Transformation in JAK2 Mutant MPN." Blood 134, Supplement_1 (November 13, 2019): 1680. http://dx.doi.org/10.1182/blood-2019-130262.
Повний текст джерелаIsmail, A. A., S. Wagner, H. Murua Escobar, S. Willenbrock, K. A. Sterenczak, M. T. Samy, A. M. Abd El-Aal, I. Nolte, and P. Wefstaedt. "Effects of High-Mobility Group A Protein Application on Canine Adipose-Derived Mesenchymal Stem CellsIn Vitro." Veterinary Medicine International 2012 (2012): 1–10. http://dx.doi.org/10.1155/2012/752083.
Повний текст джерелаFedele, Monica, Giovanna Maria Pierantoni, Pierlorenzo Pallante, and Alfredo Fusco. "High mobility group A-interacting proteins in cancer: focus on chromobox protein homolog 7, homeodomain interacting protein kinase 2 and PATZ." Journal of Nucleic Acids Investigation 3, no. 1 (March 16, 2012): 1. http://dx.doi.org/10.4081/jnai.2012.3988.
Повний текст джерелаResar, Linda, Donna Marie Williams, Zhizhuang Joe Zhao, Ophelia Rogers, Lingling Xian, Jerry L. Spivak, and Alison R. Moliterno. "High Mobility Group A1/2 Chromatin Remodeling Proteins Associate with Polycythemia Vera Transformation to Acute Leukemia in Humans and a JAK2 V617F Transgenic Mouse Model." Blood 128, no. 22 (December 2, 2016): 1958. http://dx.doi.org/10.1182/blood.v128.22.1958.1958.
Повний текст джерелаДисертації з теми "HMGA proteins"
Beitzel, Brett F. "The role of HMGA proteins in retroviral integration /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2003. http://wwwlib.umi.com/cr/ucsd/fullcit?p3099924.
Повний текст джерелаPellarin, Ilenia. "HMGA PROTEINS IN EPITHELIAL-MESENCHYMAL TRANSITION AND TUMOUR PROGRESSION." Doctoral thesis, Università degli studi di Trieste, 2014. http://hdl.handle.net/10077/10117.
Повний текст джерелаHigh Mobility Group A (HMGA1a, HMGA1b and HMGA2) proteins are architectural nuclear factors, physiological expressed during embryonic development and re-expressed at high levels following neoplastic transformation, playing essential functions in both these processes thanks to their particular plasticity and consequently multifunctionality. HMGA are involved in a wide number of cellular processes, including Epithelial-Mesenchymal transition (EMT), a biologic developmental process characterized by the conversion of epithelial cells to motile mesenchymal ones, with increased capacity of migration and invasion. EMT plays a key role during the progression of different tumours, including breast cancer and also HMGA have been linked to these processes in the acquisition of tumourigenic features. Consequently taking advantage of different breast cancer cell lines to recreate an "EMT model" we have investigated the role of HMGA proteins in EMT and breast carcinoma. We have developed a cellular model, stable for the overexpression of HMGA1 using the human breast cancer cell line MCF7. We have explored different aspects of tumourigenesis, performing transwell migration and invasion assays, demonstrating that cells with high levels of HMGA1 migrate and invade at a higher and significant level in comparison to control cells. Moreover this data was also confirmed with the development of an inducible cell line for HMGA1 overexpression. Therefore we have examined the expression status of different genes, including several specific EMT markers at mRNA level with Real Time PCR, observing a pre-malignant change towards mesenchymal status. We have investigated the response after DNA damage induced by doxorubicin drug, by colony formation assay, demonstrating that HMGA1 overexpressing cells confer a survival advantage to the cells, being able to survive and form a significant higher number of colonies in respect to control cells. Therefore to study deeper the role of HMGA in EMT, we have developed other two cellular systems, a human cellular model of EMT in MDA-MB-468 human breast carcinoma cells treated with Epidermal Growth Factor (EGF) and the well known EMT model, elicited by Transforming Growth Factor-β (TGF-β) in murine mammary epithelial NMuMG cells, in which HMGA2 is functionally determinant. We have demonstrated by Real Time PCR of EMT markers, Western Blot analyses and immunofluorescence the effective reliability of these cellular models, confirmed also by a dramatic change in morphology of treated cells, towards a mesenchymal phenotype. Concluding we have interestingly observed that overexpression of HMGA1 could confer some tumourigenic features (i.e. migration, invasion) and survival advantage to the cells in the MCF7 model after a cellular DNA damage induction; therefore we have different suggestions that HMGA are involved in EMT in other different cellular models.
Le proteine HMGA (HMGA1a, HMGA1b e HMGA2), definite come fattori architetturali della cromatina, sono fisiologicamente espresse ad alti livelli nel corso dello sviluppo embrionale diminuendo gradualmente la loro espressione nel corso del differenziamento. Sono coinvolte, oltre all'aspetto fisiologico, anche in diverse condizioni patologiche, essendo ad esempio ri-espresse ad alti livelli nel corso della trasformazione neoplastica, esercitando funzioni essenziali grazie alla loro alta plasticità, alle peculiari caratteristiche biochimiche e conseguente multifunzionalità. Le proteine HMGA utilizzano diversi meccanismi per esercitare la loro funzione nell'acquisire capacità trasformanti, inclusa la transizione epitelio-mesenchimale. Questo processo biologico, primariamente identificato come fattore chiave dello sviluppo embrionale, è risultato di essere di fondamentale importanza anche nella trasformazione tumorale. Mediante questo meccanismo una cellula epiteliale, mediante molteplici cambiamenti genetici e biochimici acquisisce caratteristiche tipiche di uno "stato mesenchimale", caratterizzato ad esempio da un'aumentata capacità invasiva e migratoria. La transizione epitelio-mesenchimale esercita un ruolo chiave nel corso della progressione di diverse tipologie tumorali, incluso il cancro al seno, a cui in particolare anche le proteine HMGA sono state associate. L'obiettivo della Tesi è quindi quello di studiare il ruolo delle proteine HMGA nella transizione epitelio-mesenchimale e in particolare nel cancro al seno. A questo scopo abbiamo sviluppato diversi modelli cellulari di transizione epitelio-mesenchimale. Il primo modello ha previsto la creazione di un sistema stabile di over-espressione della proteina HMGA1 nella linea epiteliale di tumore al seno MCF7. Abbiamo analizzato diversi aspetti della tumorigenesi mediante saggi di migrazione ed invasione in transwell, dimostrando come alti livelli della proteina HMGA1 inducano un aumento di entrambi i processi rispetto ad una condizione di controllo. Inoltre i dati di migrazione sono stati confermati in un sistema inducibile per la over-espressione di HMGA1 nella stessa linea cellulare MCF7 e da saggi condotti in condizione di deplezione di HMGA1 attraverso strategie di silenziamento, dimostrando ulteriormente come la migrazione sia un fenomeno HMGA1 dipendente. Abbiamo inoltre esaminato lo stato di espressione di diversi geni, inclusi specifici marker di transizione epitelio-mesenchimale, mediante analisi di Real Time PCR, osservando un cambiamento verso una condizione di tipo pre-maligno e di parziale transizione ad uno stato mesenchimale. Inoltre è stata verificata la risposta al danno indotto da doxorubicina mediante saggio di colony formation, dimostrando come cellule over-esprimenti HMGA1 possiedano un vantaggio in termini di sopravvivenza e di numero di colonie formate, rispetto alle cellule di controllo. Per approfondire ulteriormente il ruolo esercitato dalle HMGA nella transizione epitelio-mesenchimale, sono stati sviluppati altri due modelli cellulari, uno nella linea epiteliale umana di cancro al seno MDA-MB-468 trattata con EGF (Epidermal Growth Factor), l'altro nella linea cellulare murina mammaria di tipo epiteliale NMuMG, trattata con TGF-β (Transforming Growth Factor-β), in cui l'azione di HMGA2 è stato dimostrato avere un ruolo determinante. Mediante analisi di Real Time PCR di marker di transizione epitelio-mesenchimale, di Western Blot e di immunofluorescenza abbiamo dimostrato l'effettiva solidità di questi modelli cellulari, confermato anche dal fatto che è possibile apprezzare un consistente cambio morfologico verso un fenotipo mesenchimale e una concomitante over-espressione delle proteine HMGA. Da questi modelli è stato quindi possibile evincere come le HMGA siano coinvolte nell'acquisizione di caratteristiche di tipo tumorale anche mediante processi di transizione epitelio-mesenchimale e come questi modelli siano utili al fine di semplificare network molecolari.
XXV Ciclo
1984
Jakimovska, Frosina. "Characterization of the interaction between nucleophosmin (NPM) and highmobility group a (HMGA) proteins." Doctoral thesis, Università degli studi di Trieste, 2008. http://hdl.handle.net/10077/2760.
Повний текст джерелаABSTRACT HMGA proteins are members of the high mobility group (HMG) non-histone, architectural chromosomal proteins. The HMGA family consists of: A1a, A1b and A2, the first two being isoforms produced by alternative splicing. These are small proteins, about 100aa residues long, characterized by three basic stretches of AT-hooks which bind to the AT-rich sequences on the DNA minor groove. They are normally present in rapidly proliferating cells (embryo) whereas upon differentiation the levels of these proteins decrease until they are nearly absent from adult cells. Overexpression of these proteins has been correlated with various types of neoplastic transformations. The interaction network of HMGA has been an object of study for years in our laboratory and one of the most intriguing protein-protein interactions studied is the one between HMGA and nucleophosmin. Nucleophosmin (NPM, B23, numatrin or NO38) is one of the most abundant phosphoproteins, mainly localized in the nucleoli but it also shuttles between the nucleus and the cytoplasm. This versatile protein has been proven to be involved in various cellular functions and related to both proliferative and growth-suppressive roles in the cell. The first evidence of the interaction HMGA2-NPM in our lab has been obtained by in vitro assays (affinity chromatography). The step ahead was to see if this interaction occurs in vivo and if it does, to try to find ts functional significance. Thus,immunoprecipitation (IP) experiments were performed.The first one gave the proof thet interaction between HMGA2 protein and NPM (transfected and endogenous) occurs. The second IP gave the evidence that interaction occurs between HMGA1a and NPM too. This in vivo protein-protein interaction was to be given a functional significance. We tested by siRNA HMGA1a treatment if downregulation of HMGA1a expression influences the expression of the SOD2 gene (regulated by NPM). The effect of the HMGA1a silencing has proven to be very slight on the SOD2 gene (a 14% of expression reduction). EMSA experiments have been performed in order to test the effect of NPM on the DNA binding properties of the HMGA2 protein with the DNA probes E3 and HCRII. In both cases it has been observed that NPM increases the DNA binding affinity of the HMGA2 protein.
1979
Zammitti, Salvina. "Post-translational modifications of high mobility group a (HMGA) proteins in neoplastic transformation." Doctoral thesis, Università degli studi di Trieste, 2010. http://hdl.handle.net/10077/3614.
Повний текст джерелаLe proteine HMG (High Mobility Group) sono la famiglia più ampiamente e meglio caratterizata fra le proteine cromosomiche non istoniche. Esse sono raggruppate in tre sottofamiglie: HMGA, HMGB ed HMGN. Ciascuna sottofamiglia è caraterizzata da una sequenza o motivo funzionale attraverso il quale sono capaci di legarsi a specifiche strutture sul DNA o sulla cromatina. La famiglia HMGA di mammifero consiste di due geni funzionali: HMGA1 and HMGA2. Lo splicing alternativo del trascritto del gene HMGA1 dà origine alle proteine HMGA1a ed HMGA1b. La proteina HMGA2 è codificata dall’altro gene. Le proteine HMGA partecipano a specifiche interazioni proteina-DNA e proteina-proteina inducendo sia cambiamenti strutturali della cromatina che la formazione di complessi macromolecolari su regioni promotrici//enhancer di diversi geni. Pertanto esse sono descritte come fattori archietturali della trascrizione. Grazie alla loro multifunzionalità, ese partecipano a diversi processi biologici quali l’integrazione virale, l’embriogenesi e la differenziazione, l’apoptosi, la senescenza, la trasformazione neoplastica ed il riparo del DNA. La caratteristica di proteine oncofetali attribuita alle HMGA prende origine dal fatto che esse sono (i) altamente espresse durante l’embriogenesi, (ii) assenti o espresse a bassi livelli nei tessuti adulti e (iii) altamente riespresse nelle cellule trasformate. Queste proteine sono, tra le proteine nucleari, quelle più soggette a modificazioni post-traduzionali e le loro attività sono modulate da una ampia varietà di modificazioni post-traduzionali. In questo lavoro di tesi, grazie all’uso di linee cellulari di cancro mammario in cui è stata indotta la reversione del fenotipo neoplastico tramite trattamento farmacologico e successive analisi di spettrometria di massa, si è ricercata una connessione tra le modificazioni post-traduzionali delle HMGA ed il processo di trasformazione neoplastica. Inoltre, grazie ad una nuova strategia in vitro sviluppata nel nostro laboratorio per l’identificazione di partner molecolari delle proteine HMGA, si è dimostrato che la proteina HMGA1a si associa con la proteina Ku70, che è un fattore chiave coinvolto nel riparo delle rotture al doppio filamento di DNA attraverso il “non-homologous end joining”. Numerose evidenze sperimentali suggeriscono che l’inibizione del riparo del DNA da parte delle HMGA posa contribuire alle instabilità genetiche e cromosomiche comunemente ritrovate nelle celle cancerose. Perciò, si è ricercata una relazione funzionale tra le proteine HMGA e le proteine chiave nel meccanismo di riparo del DNA attraverso “non-homologous end joining”, focalizzando l’attenzione in particolare sulla proteina DNA-PK (DNA-dependent protein kinase), che ha una funzione regolatrice chiave in questo processo.
XXII Ciclo
1973
ALTAMURA, SANDRO. "IDENTIFICAZIONE E CARATTERIZZAZIONE DI PARTNERS MOLECOLARI DELLE PROTEINE HMGA." Doctoral thesis, Università degli studi di Trieste, 2007. http://thesis2.sba.units.it/store/handle/item/12290.
Повний текст джерелаUesugi, Hiroko. "Prevalence and characterization of novel P-ANCA, antibodies to the high mobility group non-histone chromosomal proteins HMG1 and HMG2, in systemic rheumatic diseases." Kyoto University, 2000. http://hdl.handle.net/2433/151400.
Повний текст джерелаRagab, Anan. "Genetic and functional studies on abundant Drosophila HMGB proteins." Thesis, University of Cambridge, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.615068.
Повний текст джерелаZayed, Hatem. "Improvement of the sleeping beauty transposon system." [S.l. : s.n.], 2003. http://www.diss.fu-berlin.de/2003/243/index.html.
Повний текст джерелаAdair, Jennifer Eileen. "Molecular and genetic influence of HMGA1 proteins on nucleotide excision repair." Online access for everyone, 2005. http://www.dissertations.wsu.edu/Dissertations/Fall2005/j%5Fadair%5F120605.pdf.
Повний текст джерелаArnoldo, Laura. "HMGA1 proteins regulate gene expression by modulating histone H3 phosphorylation." Doctoral thesis, Università degli studi di Trieste, 2014. http://hdl.handle.net/10077/10112.
Повний текст джерелаHMGA1 is an oncogene encoding for an architectural transcription factor that affects fundamental cell processes, leading to neoplastic transformation. The two main mechanisms by which HMGA1 protein is known to be involved in cancer concern the regulation of gene expression by altering DNA structure and interacting with a conspicuous number of transcription factors. Here we provide evidence of an additional level of gene expression regulation exploited by HMGA1 to exert its oncogenic activity. Starting from protein-protein interaction data showing that HMGA1 interacts with histones, we show that HMGA1 regulates gene expression by affecting the epigenetic status of cancer cells. In particular, it modulates the signalling cascade mediated by the RAS/RAF/MEKK/ERK/RSK2 pathway regulating the levels of histone H3 phosphorylation at Serine 10 and Serine 28. We demonstrate that the down-regulation of these two H3 post-translational modifications by HMGA1 silencing and by inhibitors of the RAS/RAF/MEKK/ERK pathway is linked to cell migration decrease and morphological changes resembling the mesenchymal to epithelial transition.
HMGA1 è un oncogene codificante per un fattore trascrizionale architetturale che influenza fondamentali processi cellulari, portando alla trasformazione neoplastica. I due principali meccanismi tramite cui la proteina HMGA1 è nota essere coinvolta nel cancro riguardano la regolazione dell’espressione genica tramite l’alterazione della struttura del DNA e l’interazione con un cospicuo numero di fattori di trascrizione. Qui forniamo la prova di un addizionale livello di regolazione dell’espressione genica sfruttato da HMGA1 per esercitare la sua attività oncogenica. Partendo da dati d’interazione proteina-proteina che mostrano che HMGA1 interagisce con gli istoni, mostriamo che HMGA1 regola l’espressione genica influenzando lo stato epigenetico delle cellule cancerose. In particolare, essa modula la cascata di segnalazione mediata dalla via di RAS/RAF/MEKK/ERK/RSK2 regolando i livelli di fosforilazione dell’istone H3 sulla Serina 10 e sulla Serina 28. Noi dimostriamo che la down-regolazione di queste due modificazioni post-traduzionali di H3 tramite il silenziamento di HMGA1 e l’utilizzo di inibitori della via di RAS/RAF/MEKK/ERK/RSK2 è correlata alla diminuzione della migrazione cellulare e a cambiamenti morfologici che ricordano la transizione mesenchimo-epiteliale.
XXV Ciclo
1983
Книги з теми "HMGA proteins"
Mumford, Katherine Laura. Genomic cloning and gene organisation of the Drosophila HMG box protein DSox14. Portsmouth: University of Portsmouth, School of Biological Sciences, 1999.
Знайти повний текст джерелаGelder, Wiebke. Identifizierung von mit HMGA2 interagierenden Proteinen. GRIN Verlag GmbH, 2011.
Знайти повний текст джерелаAn, Woojin. Interaction of linker proteins, H1 and HMG1, with nucleosome reconstituted on positioning sequences. 1998.
Знайти повний текст джерелаSiino, Joseph S. Replacement of conserved threonines by alanine residues: Effect on the dissociation constant of recombinant human HMG-I. 1992.
Знайти повний текст джерелаLehn, Donald Andrew. The non-histone chromosomal protein HMG-I(Y) and its interactions with nucleic acids. 1989.
Знайти повний текст джерелаWiklund, Olov, and Jan Borén. Pathogenesis of atherosclerosis: lipid metabolism. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780198755777.003.0011.
Повний текст джерелаЧастини книг з теми "HMGA proteins"
Fedele, Monica, and Alfredo Fusco. "Pituitary Adenoma: Role of HMGA Proteins." In Tumors of the Central Nervous System, Volume 10, 161–68. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-5681-6_18.
Повний текст джерелаTravers, Andrew A. "Gene Regulation by HMGA and HMGB Chromosomal Proteins and Related Architectural DNA-Binding Proteins." In DNA Conformation and Transcription, 147–58. Boston, MA: Springer US, 2005. http://dx.doi.org/10.1007/0-387-29148-2_11.
Повний текст джерелаKotzka, Jörg, Wilhelm Krone, and Dirk Müller-Wieland. "Sterol-regulatory element binding proteins (SREBPs): gene-regulatory target of statin action." In HMG-CoA Reductase Inhibitors, 35–54. Basel: Birkhäuser Basel, 2002. http://dx.doi.org/10.1007/978-3-0348-8135-7_3.
Повний текст джерелаMaher, L. James. "Studies of Sequence-Nonspecific HMGB DNA-Binding Proteins." In Biological and Medical Physics, Biomedical Engineering, 143–62. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-0-387-92808-1_7.
Повний текст джерелаGoodwin, G. H., R. H. Nicolas, C. A. Wright, and S. Zavou. "The Structures and Functions of the Low Molecular Weight HMG Proteins." In Chromosomal Proteins and Gene Expression, 221–38. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-7615-6_15.
Повний текст джерелаLaland, S. G., T. Lund, and J. Holtlund. "Post-Translational Modification of the Low Molecular Weight HMG Chromosomal Proteins." In Chromosomal Proteins and Gene Expression, 239–47. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-7615-6_16.
Повний текст джерелаPuigdomènech, Pere, and Matilde Jose. "Structure and Function in the HMG-1 Family of Chromosomal Proteins." In Chromosomal Proteins and Gene Expression, 249–61. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-7615-6_17.
Повний текст джерелаWittemann, B., F. A. Bautz, H. Michels, and H. Truckenbrodt. "Autoantibodies to Nonhistone Chromosomal Proteins HMG-1 and HMG-2 in Subsets of Juvenile Chronic Arthritis (JCA)." In Molecular and Cell Biology of Autoantibodies and Autoimmunity. Abstracts, 105–6. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-46681-6_89.
Повний текст джерелаMcA’Nulty, M. M., and S. J. Lippard. "Consequences of HMG-Domain Protein Binding to Cisplatin-Modified DNA." In Nucleic Acids and Molecular Biology, 264–84. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79488-9_13.
Повний текст джерелаBillings, Paul C., and Edward N. Hughes. "Role of HMG and Other Proteins in Recognition of Cisplatin DNA Damage." In DNA Damage and Repair, 133–41. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1007/978-1-59259-455-9_9.
Повний текст джерелаТези доповідей конференцій з теми "HMGA proteins"
Fatchiyah, Fatchiyah, and Shella Clarista Natasia. "Inhibition potency of HMGR enzyme against hypercholesterolemia by bioactive peptides of CSN1S2 protein from caprine milk." In THE 8TH ANNUAL BASIC SCIENCE INTERNATIONAL CONFERENCE: Coverage of Basic Sciences toward the World’s Sustainability Challanges. Author(s), 2018. http://dx.doi.org/10.1063/1.5062812.
Повний текст джерелаSa’adah, Noor Nailis, Elshinta Riantica, Awik Puji Dyah Nurhayati, Nova Maulidina Ashuri та Dewi Hidayati. "Molecular Docking of Anthocyanin Compound as Anti-Hyperlipidemia Against PPARα, HMG-CoA Reductase and ACAT Proteins". У 7th International Conference on Biological Science (ICBS 2021). Paris, France: Atlantis Press, 2022. http://dx.doi.org/10.2991/absr.k.220406.033.
Повний текст джерелаEsposito, Francesco, Mara Tornincasa, Eleonora Borbone, and Giovanna Maria Pierantoni. "Abstract 206: High mobility group A1(HMGA1) proteins localize at the mitochondria and inhibit the p53-mediated intrinsic-apoptotic pathway." In 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.am2011-206.
Повний текст джерелаTakaha, Natsuki, Ichiro Takeuchi, Yoshihiro Sowa, Yasunori Kimura, Terukazu Nakamura, Fumiya Hongo, Kazuya Mikami, Akihiro Kawauchi, and Tsuneharu Miki. "Abstract 606: Expression and role of high mobility group protein AT-hook 1 (HMGA1) in human renal cell carcinoma." In 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.am2011-606.
Повний текст джерелаBatista, Keila Zaniboni Siqueira, Andressa Karine Boehringer, Marina Schndeider, Vinicius Vialle Ferreira, and Mercedes Gabriela Ratto Reiter. "DOSAGEM DE IMUNOGLOBULINA A E PROTEÍNAS TOTAIS EM AMOSTRAS DO BANCO DE LEITE HUMANO DE BLUMENAU/SC." In I Congresso Brasileiro de Imunologia On-line. Revista Multidisciplinar em Saúde, 2021. http://dx.doi.org/10.51161/rems/959.
Повний текст джерелаLobbardi, 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.
Повний текст джерелаLobbardi, 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.
Повний текст джерелаChia, Lionel, Lingling Xian, Guangjing Zhu, Mohammad Heydarian, William B. Issacs, Karen Reddy, and Linda Smith Resar. "Abstract 3352: HMGA1 chromatin remodeling protein induces HOXB13 to drive cancer stem cell properties and tumor progression in prostate cancer models." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3352.
Повний текст джерелаScott, 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.
Повний текст джерелаRajan, Neena, Nate Stetson, Robert Maidhof, Mitchell Levine, and Nadeen Chahine. "In Vivo Administration of an Inflammatory Stimulant can Trigger Loss of Biomechanical and Biochemical Properties of the Intervertebral Disc." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80495.
Повний текст джерелаЗвіти організацій з теми "HMGA proteins"
Boonyaratanakornkit, Viroj. Chromatin HMG-I (Y) as a Co-regulatory Protein for Estrogen Receptor Action in Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, May 1999. http://dx.doi.org/10.21236/ada368525.
Повний текст джерелаBoonyaratanakornkit, Viroj. Chromatin HMG-I(Y) as a Co-Regulatory Protein for Estrogen Receptor Action in Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, April 2000. http://dx.doi.org/10.21236/ada391523.
Повний текст джерелаAly, Radi, James H. Westwood, and Carole L. Cramer. Novel Approach to Parasitic Weed Control Based on Inducible Expression of Cecropin in Transgenic Plants. United States Department of Agriculture, May 2003. http://dx.doi.org/10.32747/2003.7586467.bard.
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