Academic literature on the topic 'ZNF92'
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Journal articles on the topic "ZNF92"
Bhattacharya, Udayan, Mohammad Kamran, Maroua Manai, Massimo Cristofanilli, and Tan A. Ince. "Cell-of-Origin Targeted Drug Repurposing for Triple-Negative and Inflammatory Breast Carcinoma with HDAC and HSP90 Inhibitors Combined with Niclosamide." Cancers 15, no. 2 (January 4, 2023): 332. http://dx.doi.org/10.3390/cancers15020332.
Full textWang, Luqun, Qiong Liu, Hao Li, Li Lizhen, and Xin Wang. "The Establishment of Bortezomib Resistant Myeloma Cell Line KM3/BTZ and Explore the Resistance Mechanism." Blood 124, no. 21 (December 6, 2014): 5226. http://dx.doi.org/10.1182/blood.v124.21.5226.5226.
Full textLee, Il-Kwon, Jeong-Hwa Choi, Yu Ra Lee, Yeo-Kyeoung Kim, Hee Nam Kim, Kyeong-Soo Park, Je-Jung Lee, et al. "A Single Nucleotide Polymorphism and Its Haplotype of ZNF42 Transcriptional Modulator Gene Predisposes Individuals to High-Risk Acute Myelogenous Leukemia (AML)." Blood 106, no. 11 (November 16, 2005): 4248. http://dx.doi.org/10.1182/blood.v106.11.4248.4248.
Full textHou, Zhao Xia, Zhao Lu Xue, Shao Hong Wang, Xiao Dan Hu, Hao Ran Lu, Chang Lei Niu, Hao Wang, Cai Wang, and Yin Zhou. "Thermal Stability and Structure of Tellurite Glass." Key Engineering Materials 512-515 (June 2012): 994–97. http://dx.doi.org/10.4028/www.scientific.net/kem.512-515.994.
Full textElsayed, E. Mostafa, Mohamed M. Rashad, H. F. Y. Khalil, M. R. Hussein, M. M. B. El-Sabbah, and I. A. Ibrahim. "Electrochemical Performance of Nanocrystalline Zinc Ferrite Films Synthesized Using Electrodeposition." Key Engineering Materials 835 (March 2020): 1–6. http://dx.doi.org/10.4028/www.scientific.net/kem.835.1.
Full textZhang, Ye, and Hong Bing Ji. "Preparation of ZnF2 Nano-Particles by Electrochemical Anodization Method." Advanced Materials Research 476-478 (February 2012): 1616–20. http://dx.doi.org/10.4028/www.scientific.net/amr.476-478.1616.
Full textMaletin, M., E. G. Moshopoulou, and V. V. Srdic. "Magnetic properties of ZnFe2 O4 and In-doped ZnFe2 O4 nanoparticles." physica status solidi (a) 205, no. 8 (May 26, 2008): 1831–34. http://dx.doi.org/10.1002/pssa.200723633.
Full textRichter, Theresia M. M., Sylvain LeTonquesse, Nicolas S. A. Alt, Eberhard Schlücker, and Rainer Niewa. "Trigonal-Bipyramidal Coordination in First Ammoniates of ZnF2: ZnF2(NH3)3 and ZnF2(NH3)2." Inorganic Chemistry 55, no. 5 (February 19, 2016): 2488–98. http://dx.doi.org/10.1021/acs.inorgchem.5b02837.
Full textAsseid, Fathi M., Jack M. Miller, and James H. Clark. "FT-IR and 29Si, 27Al, and 19F MAS NMR studies of the adsorption of CdF2, ZnF2, and CuF2 onto montmorillonite K10; activity towards Friedel–Crafts alkylation." Canadian Journal of Chemistry 70, no. 9 (September 1, 1992): 2398–404. http://dx.doi.org/10.1139/v92-304.
Full textLv, Hao, Yao Ming Ding, Ai Mei Liu, Ju Fang Tong, Xu Nong Yi, and Qian Guang Li. "Nucleation Agent Choice of Li2O–Al2O3–SiO2 Glass Ceramic Having Ideal Micro Spherical Crystal Grains." Advanced Materials Research 311-313 (August 2011): 1332–35. http://dx.doi.org/10.4028/www.scientific.net/amr.311-313.1332.
Full textDissertations / Theses on the topic "ZNF92"
Trusso, Maria Allegra. "THE GENETICS OF BIPOLAR DISORDER AND THE ROLE OF HETEROZYGOSITY FOR NEURONAL CEROID LIPOFUSCINOSIS." Doctoral thesis, Università di Siena, 2022. http://hdl.handle.net/11365/1214195.
Full textPANICO, MARIA BEATRICE. "Espressione e localizzazione subcellulare della Zinc Finger Protein 9, prodotto del gene della distrofia miotonica tipo 2." Doctoral thesis, Università degli Studi di Roma "Tor Vergata", 2008. http://hdl.handle.net/2108/413.
Full textExpression and subcellular localization of myotonic dystrophy type 2 protein ZNF9 Dr. M.B.Panico The genetic defect underlying myotonic dystrophy type 2 (DM2) is a CCTG expansion located in intron 1 of the zinc finger protein 9 (ZNF9) gene in chromosome 3q21. ZNF9 is a 19kDa highly conserved protein expressed in various tissues, but its cellular localization and function are still unclear. We have therefore used a previously characterized polyclonal antibody to detect by immunofluorescence (IF) the subcellular localization of ZNF9 in normal human and rat skeletal muscle. In longitudinally sectioned myofibers, IF reactivity for ZNF9 appeared as regular transverse bands 1-1.2 μm thick, throughout the fiber width. In double IF experiments observed by confocal microscopy, ZNF9 showed co-localization with proteins localized at the I-Z band junction such as the sarcoplasmic reticulum Ca/Mg ATPase, the T12 region of titin and desmin. Moreover, in DM2 muscle the ZNF9 intracellular distribution was comparable to that of control. These data indicate that ZNF9 is highly expressed in normal myofibers and its cellular distribution is apparently not disrupted in DM2.
Torre, Eliana do Nascimento. "Metaloproteinases da matriz extracelular e cárie dentária: avaliação dos fluoretos TiF4, SnF2, ZnF2 e NaF na expressão das MMP-2 e MMP-9 salivares humanas." Universidade Federal de Pelotas, 2014. http://repositorio.ufpel.edu.br:8080/handle/prefix/3468.
Full textMade available in DSpace on 2017-05-31T14:54:06Z (GMT). No. of bitstreams: 2 license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5) Metaloproteinases da Matriz Extracelular e Cárie Dentária avaliação dos fluoretos.pdf: 2642976 bytes, checksum: df000dd8b06813ee9a1d22831f7a71a0 (MD5) Previous issue date: 2014-12-20
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior - CAPES
Enzimas bacterianas foram consideradas as principais responsáveis pela degradação da matriz dentinária durante o processo de lesão de cárie dentária. No entanto, a literatura emergente sugere que enzimas derivadas do hospedeiro, e, em particular, as metaloproteinases da matriz (MMPs) contidas na dentina e na saliva podem desempenhar um papel importante neste processo, pela sua capacidade em degradar a matriz orgânica dentinária. Estes fatos possibilitam o estudo de novas opções terapêuticas para a prevenção e tratamento da lesão de cárie dentária. Uma revisão de literatura foi feita, como primeira parte desta tese, para elucidar a presença, localização e o nível de atividade das principais MMPs encontradas no tecido cariado humano, abordando temas relevantes, sobre o papel local das MMPs em relação a este tecido. A seleção dos trabalhos foi feita na base de dados Pubmed, em artigos com idioma inglês, até novembro de 2014. De 411 artigos elegíveis, 14 foram selecionados para o estudo completo, e 08 foram incluídos nesta revisão. A partir desta análise, respeitando os critérios de inclusão/exclusão propostos, pode-se concluir que a literatura possui poucos dados sobre a presença, localização, e nível de atividade enzimática no tecido cariado humano. Além disto, foi encontrada também uma heterogeneidade grande, a respeito das metodologias utilizadas para alcançar os objetivos de cada trabalho, e em relação à classificação do tipo de tecido dentinário cariado estudado. As MMPs mais frequentemente estudadas na dentina cariada humana foram, a MMP-2 e a MMP-9, seguidas pelas MMP-8 e MMP-20. Contudo pode-se sugerir que a MMP-2 parece ser, dentre as metaloproteinases estudadas, a que existe em maior quantidade no tecido dentinário cariado, localizada principalmente nos túbulos dentinários da dentina afetada (interna), próximo ao tecido pulpar. Como segunda parte, foi avaliada a possibilidade de utilização de alguns fluoretos como inibidores de MMPs salivares humanas, para interferir na prevenção ou progressão de lesões de cárie. Os fluoretos de estanho (SnF2), fluoreto de zinco (ZnF2) e o tetrafluoreto de titânio (TiF4), foram testados em comparação com o fluoreto de sódio (NaF), para a inibição de MMPs salivares. Saliva de doadores saudáveis foi usada em ensaio por zimografia e testadas as soluções em concentrações clínicas relevantes. A zimografia mostrou inibição das MMP-2 e MMP-9 em ordem decrescente para os fluoretos ZnF2e TiF4> NaF e SnF2. Com as limitações de um estudo in vitro, pode-se sugerir que devido aos fluoretos testados terem mostrado capacidade de inibição de MMP-2 e -9 salivares,uma nova visão e perspectiva se abre, para o estudo destes materiais, na prevenção das lesões de cárie dentária.
Bacterial enzymes were considered the main responsible factor for the degradation of the dentine matrix during the carious lesion. However, the emerging literature suggests that host derived enzymes, and, specially, the matrix metalloproteinases (MMPs) found in the dentine and in the saliva may play an important role in this process, due to their capacity to contribute to degradation of the dentine organic matrix. These facts are important as they enable the study of new therapeutic options for the dental caries lesions prevention and treatment. A literature review was carried out, as the first part of this thesis, to clarify the presence, location and the activity level of the main MMPs found in the human carious tissues,approaching relevant issues, on the local role of the MMPs in regard to this tissue. The selection of the papersdone based on the Pubmed database, in the English language, until November 2014. From 411 eligible papers, 14 were selected for the full study, and 8 were included in this review. From this analysis, respecting the inclusion/exclusion criteria proposed, it can be concluded that the literature has little data on the presence, location and enzymatic activity level in the human carious tissue. Besides this, great differences were found concerning the methodologies used to reach the purposes of their work, and in regard to the classificationof the type of carious dentinal tissue studied. The MMPs more often studied in the carious lesions inhuman dentine were the MMP-2, andMMP-9, followed by MMP-8 and MMP-20. Besides this, it can be suggested that the MMP-2 seems to be, among the studied metalloproteinases, the one in larger quantity in the carious dentinal tissue, mainly in the dentinal tubulesof the affected dentine (internal), proximitywith the pulp tissue. As a second part, the possibility of some fluoride usage as inhibitors of MMPs human salivary has been studied, to interferein the prevention or progressionof carious lesions. The tin fluoride (SnF2), the zinc fluoride (ZnF2) and the titanium tetrafluoride (TiF4), were tested in comparison to the sodium fluoride (NaF), for the inhibition of salivary MMPs. Saliva of healthy donors was used in Zymography, and the solutions were tested in relevant clinical concentrations. The Zymography showed inhibition of the MMP-2 and MMP-9 in decreasing order for the fluorides ZnF2 and TiF4> NaF and SnF2.With the limitations of an in vitro study, it can be suggested that due to the fact, the fluorides tested have shown the capacity of inhibiting the salivary MMP-2 and MMP-9, a new view and perspective arises for the study of these materials in the prevention of dental caries lesion.
Maguer, Jean-Jacques. "Synthèse, étude structurale et magnétique d'halogénures engageant des éléments 3d ou 4f, dans les systèmes : LiF-ZnF2-InF3, BaF2-BaCl2-MF2 et AF-YbF3(A=H3O+)." Le Mans, 1995. http://www.theses.fr/1995LEMA1001.
Full textChen, Chieh-Ming, and 陳傑明. "Electronic and Atomic Structure Study of ZnFe2-yCryO4 (y=0~2) Electrode for the Electrochemical Reactivity." Thesis, 2015. http://ndltd.ncl.edu.tw/handle/21668291126207762017.
Full text淡江大學
物理學系碩士班
103
In the report, while the Cyclic-Voltage (CV) result of ZnFe2-yCryO4 (y=0~2) showed that the different ratio y have the same oxidation potential but the different reduction potential. Therefore, it is important to explore the connection between electronic and atomic structure by Synchrotron radiation technologies. Extended x-ray absorption fine structure (EXAFS) showed the normal spinel structure, and the EXAFS fitting showed the bond length of Fe-O and Cr-O. X-ray absorption near edge structure (XANES) showed the unoccupied state electronic structure, and X-ray emission spectroscopy (XES) showed the occupied state information. Compared with electronic structure and electrochemical performance, Find out the relationship between the occupied/unoccupied state and charge/discharge potential.
Datu, Andrea-Kaye. "Regulation of Poly (A)-Binding Protein Expression in Response to Heat Shock and Recovery." Thesis, 2012. http://hdl.handle.net/10214/4056.
Full textHuan-Hsuan and 胡桓軒. "Arginine methylation of ZNF9 and putative differential recognition by anti-Sm autoantibody from SLE patients." Thesis, 2007. http://ndltd.ncl.edu.tw/handle/04454469045144720266.
Full text中山醫學大學
生物醫學科學學系碩士班
95
Anti-Sm is one type of autoantibodies from systemic lupus erythematosus (SLE) patients. Methylation status of specific arginine residues on SmD-1 has been reported to cause differential recognition by anti-Sm. Previous studies in our laboratory used Anti-Sm autosera from three different local SLE patients to analyze AdOx-treated (proteins presumably at hypomethylation state) and untreated (proteins at normal methylation state) HeLa cell extracts by western blots. There were no significant differences between the signals corresponding to SmD1 in samples of different methylation status. However, a few weaker signals were consistently detected from cell extracts treated with AdOx than the ones without. One interesting protein identified by mass spectrometry is ZNF9, which has the GAR domain, a common feature in substrates of protein arginine methyltransferases. We observed that recombinant GST-ZNF9 expressed in Escherichia coli could be methylated by recombinant RMT1 and PRMT1 in vitro. However, no significant differences could be detected between the signals corresponding to GST-ZNF9 of different methylation status after a non-radiation in vitro methylation experiment by western blot with a methylarginine specific antibody 7E6. Therefore, the E. coli expressed recombinant ZNF9 protein could not be used to investigate whether the arginine methylation status affect the recognition of anti-Sm. Nevertheless, FLAG-ZNF9 expressed in HeLa cells could be detected by 7E6 and anti-Sm, while the ones expressed in AdOx-treated HeLa cells has much weaker signals. Furthermore, wild-type FLAG-ZNF9 could be recognized by SYM10 (symmetric dimethylarginine specific antibody) and ASYM24 (asymmetric dimethylarginine specific antibody) but GAR-domain deleted mutant ZNF9 could not. We also observed that FLAG-ZNF9 may interact with two different protein arginine methyltransferase PRMT1 and PRMT5 by an co-immunoprecipitation experiment. In summery, in this study we demonstrate that ZNF9 has both symmetric and asymmetric dimethylarginine modifications and can be differentially recognized by anti-Sm due to the methylation status.
Δρακόπουλος, Βασίλειος. "Μελέτη της δομής με χρήση της φασματοσκοπίας Raman των υγρών φθοριούχων μιγμάτων : LnF3 - KF (Ln: La, Ce, Nd, Sm, Dy, Yb, Y) και ZnF2 - AF (A:K,Cs)." Thesis, 2000. http://nemertes.lis.upatras.gr/jspui/handle/10889/2297.
Full textBook chapters on the topic "ZNF92"
Morrison, Clyde Arthur. "ZnF2." In Crystal Fields for Transition-Metal Ions in Laser Host Materials, 48–50. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-95686-7_9.
Full text"Relationship between the structural modifications and luminescence efficiencies of ZnF2-MO-TeO2 glasses doped with Ho3+ and Er3+ ions." In Current Trends on Lanthanide Glasses and Materials, 136–58. Materials Research Forum LLC, 2017. http://dx.doi.org/10.21741/9781945291159-6.
Full textWinblad, Stefan, and Anne-Berit Ekström. "Myotonic Dystrophy." In Cognitive and Behavioral Abnormalities of Pediatric Diseases. Oxford University Press, 2010. http://dx.doi.org/10.1093/oso/9780195342680.003.0057.
Full textConference papers on the topic "ZNF92"
de Souza Antero, Giulia, Jaqueline V. Gunha, Aloisi Somer, and Andressa Novatski. "EFEITO DA ADIÇÃO DE ZNF2 EM VIDROS TELURETOS." In XXI Semana da Física. Ponta Grossa, Paraná: Even3, 2018. http://dx.doi.org/10.29327/xxifisica.128783.
Full textBanshchikov, A. G., N. F. Kartenko, A. K. Kaveev, M. M. Moisseeva, and Nikolai S. Sokolov. "Growth and structural characterization of ZnF2 epitaxial layers on Si." In SPIE Proceedings, edited by Zhores I. Alferov and Leo Esaki. SPIE, 2002. http://dx.doi.org/10.1117/12.510497.
Full textNaresh, V., and S. Buddhudu. "VIS-NIR emission analysis of Tm3+ doped LiF-ZnF2-AlF3-B2O3-SiO2 glasses." In NANOFORUM 2014. AIP Publishing LLC, 2015. http://dx.doi.org/10.1063/1.4917890.
Full textKochanowicz, Marcin, and Dominik Dorosz. "Thermal and optical properties of SiO2-Al2O3-PbF2-ZnF2-ZnO-LaF3-Nd2O3 glasses." In Optical Fibers and Their Applications 2008. SPIE, 2008. http://dx.doi.org/10.1117/12.804518.
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