Academic literature on the topic 'DNase I'

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Journal articles on the topic "DNase I"

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Counis, M. F., and A. Torriglia. "DNases and apoptosis." Biochemistry and Cell Biology 78, no. 4 (2000): 405–14. http://dx.doi.org/10.1139/o00-051.

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Here we review the different apoptotic DNases. From a functional point of view, DNases implicated in apoptosis may be classified into three groups: the Ca2+/Mg2+endonucleases, the Mg2+-endonucleases, and the cation-independent endonucleases. The first group includes DNase I which has no specificity for the linker region, DNase gamma which has some homology with DNase I, and other DNases which cleave DNA in the linker region. Both DNase I and DNase gamma have been cloned. The other nucleases of this category have dispersed molecular weights. Their sequences are unknown and it is difficult to de
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SHIOKAWA, Daisuke, Yukari SHIKA та Sei-ichi TANUMA. "Identification of two functional nuclear localization signals in DNase γ and their roles in its apoptotic DNase activity". Biochemical Journal 376, № 2 (2003): 377–81. http://dx.doi.org/10.1042/bj20030820.

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Among DNase I family members, only DNase γ causes DNA fragmentation during apoptosis. However, the molecular basis for this functional feature of DNase γ is poorly understood. Here we describe the identification of functional NLSs (nuclear localization signals) in DNase γ and their roles in its apoptotic function. DNase γ contains two NLSs: a classical bipartite-type NLS (NLS1) located in the N-terminal half, and a short basic domain (NLS2) at the C-terminus. No potential NLSs are found in the primary structures of other DNase I family DNases. Inactivation of either NLS1 or NLS2 causes reduced
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Lauková, Lucia, Barbora Konečná, Ľubica Janovičová, Barbora Vlková, and Peter Celec. "Deoxyribonucleases and Their Applications in Biomedicine." Biomolecules 10, no. 7 (2020): 1036. http://dx.doi.org/10.3390/biom10071036.

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Extracellular DNA, also called cell-free DNA, released from dying cells or activated immune cells can be recognized by the immune system as a danger signal causing or enhancing inflammation. The cleavage of extracellular DNA is crucial for limiting the inflammatory response and maintaining homeostasis. Deoxyribonucleases (DNases) as enzymes that degrade DNA are hypothesized to play a key role in this process as a determinant of the variable concentration of extracellular DNA. DNases are divided into two families—DNase I and DNase II, according to their biochemical and biological properties as
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Reitz, Manfred, Günter Löber, Peter Kleemann, and Wolfgang Dick. "Secretion of Neutral and Acid DNases in Cultivated Human Lymphocytes after Incubation with DNA; Possible Consequences for Inhalation Anesthesia." Zeitschrift für Naturforschung C 50, no. 5-6 (1995): 419–24. http://dx.doi.org/10.1515/znc-1995-5-613.

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Abstract After incubation with DNA human lymphocytes release neutral and acid DNase activities into the culture medium; the release depends on DNA concentration and time of cultivation. The electrophoretic mobility of the released neutral DNase activity is in accordance with DNase I and the electrophoretic mobility of the released acid DNase activity with DNase II. The released DNase activities do not originate from dead cells and are not influenced by blast cell formation. The anesthetic halothane can inhibit the released neutral and acid DNase activities. Inhalation anesthesia can possibly d
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Yun, S. H., M. G. Seo, B. Y. Jung, et al. "Characteristics of DNase activities in excretory/secretory products of infective larvae ofHaemonchus contortus." Journal of Helminthology 86, no. 3 (2011): 363–67. http://dx.doi.org/10.1017/s0022149x11000496.

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AbstractWhile multiple DNase activities occur in the excretory/secretory products (ESPs) of the adultHaemonchus contortus, the DNase activities in ESPs of the infective larvae (L3) have not been studied. Thus, the DNase activities in ESPs ofH. contortusL3 were investigated and compared to those of adults for developmental stage-specific analysis. The DNase activities had relative molecular masses (Mrs) of 34 and 36 kDa upon zymographic analysis at pH 5.0 and 7.0 when the larvae were incubated for over 48 h. The 34 and 36 kDa DNases of L3 ESPs were also detected in adult ESPs with similar chara
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Alekseeva, Ludmila, Aleksandra Sen’kova, Innokenty Savin, Marina Zenkova, and Nadezhda Mironova. "Human Recombinant DNase I (Pulmozyme®) Inhibits Lung Metastases in Murine Metastatic B16 Melanoma Model That Correlates with Restoration of the DNase Activity and the Decrease SINE/LINE and c-Myc Fragments in Blood Cell-Free DNA." International Journal of Molecular Sciences 22, no. 21 (2021): 12074. http://dx.doi.org/10.3390/ijms222112074.

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Tumor-associated cell-free DNAs (cfDNA) play an important role in the promotion of metastases. Previous studies proved the high antimetastatic potential of bovine pancreatic DNase I and identified short interspersed nuclear elements (SINEs) and long interspersed nuclear elements (LINEs)and fragments of oncogenes in cfDNA as the main molecular targets of enzyme in the bloodstream. Here, recombinant human DNase I (commercial name Pulmozyme®), which is used for the treatment of cystic fibrosis in humans, was repurposed for the inhibition of lung metastases in the B16 melanoma model in mice. We fo
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YASUDA, Toshihiro, Haruo TAKESHITA, Tamiko NAKAJIMA, Osamu HOSOMI, Yoshimitsu NAKASHIMA, and Koichiro KISHI. "Rabbit DNase I: purification from urine, immunological and proteochemical characterization, nucleotide sequence, expression in tissues, relationships with other mammalian DNases I and phylogenetic analysis." Biochemical Journal 325, no. 2 (1997): 465–73. http://dx.doi.org/10.1042/bj3250465.

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DNase I from rabbit urine was purified approx. 3600-fold to apparent homogeneity with a 41% yield by affinity chromatography utilizing DNA–cellulose; the purity of the final preparation was assessed by SDS/PAGE, lack of contamination by other nucleases and production of a monospecific antibody against the enzyme. Although the proteochemical and enzymological properties of the purified enzyme resembled those of other mammalian DNases I, the enzymic activity of rabbit DNase I was less efficiently inhibited by monomeric actin than was that of human DNase I, probably due to substitution of an amin
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TAKESHITA, Haruo, Toshihiro YASUDA, Reiko IIDA, et al. "Amphibian DNases I are characterized by a C-terminal end with a unique, cysteine-rich stretch and by the insertion of a serine residue into the Ca2+-binding site." Biochemical Journal 357, no. 2 (2001): 473–80. http://dx.doi.org/10.1042/bj3570473.

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We purified four amphibian deoxyribonucleases I from the pancreases of one toad, two frog and one newt species, by using three different column chromatography methods in sequence. Each of the purified enzymes had a molecular mass of approx. 40kDa and an optimal pH for activity of approx. 8.0. These values were significantly greater than those for other vertebrate DNases I. The full-length cDNA encoding each amphibian DNase I was constructed from the total RNA of the pancreas by using rapid amplification of cDNA ends. Nucleotide sequence analyses revealed two structural characteristics unique t
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Napirei, Markus, Swantje Wulf, Dirk Eulitz, Hans Georg Mannherz, and Thomas Kloeckl. "Comparative characterization of rat deoxyribonuclease 1 (Dnase1) and murine deoxyribonuclease 1-like 3 (Dnase1l3)." Biochemical Journal 389, no. 2 (2005): 355–64. http://dx.doi.org/10.1042/bj20042124.

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Deoxyribonuclease 1 (DNASE1, DNase I) and deoxyribonuclease 1-like 3 (DNASE1L3, DNase γ, DNase Y, LS-DNase) are members of a DNASE1 protein family that is defined by similar biochemical properties such as Ca2+/Mg2+-dependency and an optimal pH of about 7.0 as well as by a high similarity in their nucleic acid and amino acid sequences. In the present study we describe the recombinant expression of rat Dnase1 and murine Dnase1l3 as fusion proteins tagged by their C-terminus to green fluorescent protein in NIH-3T3 fibroblasts and bovine lens epithelial cells. Both enzymes were translocated into t
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Janovičová, Ľubica, Katarína Kmeťová, Nikola Pribulová, et al. "Endogenous DNase Activity in an Animal Model of Acute Liver Failure." International Journal of Molecular Sciences 24, no. 3 (2023): 2984. http://dx.doi.org/10.3390/ijms24032984.

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Deoxyribonucleases (DNases) cleave extracellular DNA (ecDNA) and are under intense research as interventions for diseases associated with high ecDNA, such as acute live injury. DNase I treatment decreases morbidity and mortality in this animal model. Endogenous DNase activity has high interindividual variability. In this study, we tested the hypothesis that high endogenous DNase activity is beneficial in an animal model of acute liver failure. DNase activity was measured in the plasma of adult male mice taken before i.p. injection of thioacetamide to induce acute liver failure. The survival of
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Dissertations / Theses on the topic "DNase I"

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Hosseini, Mona. "Genome-wide DNaseI hypersensitive sites profiles in laboratory mouse strains by DNase-seq." Thesis, University of Oxford, 2013. http://ora.ox.ac.uk/objects/uuid:c76109fc-93b5-4e0b-b7df-0277cbf527a9.

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Variation at regulatory elements, identified through hypersensitivity to digestion by Deoxyribonuclease I (DNase I), is believed to contribute to variation in complex traits, but the extent and consequences of this variation are poorly characterized. To investigate the relationship between sequence variation, and the functional consequences of variation in chromatin accessibility, genome-wide DNase I hypersensitive sites (DHS) of terminally differentiated erythroblasts were studied in eight inbred strains of mice studied (A/J, AKR/J, BALBc/J, C3H/HeJ, C57BL/6J, CBA/J, DBA/2J, and LP/J). These
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Focareta, Tony. "The extracellular DNase(s) of vibrio cholerae /." Title page, abstract and table of contents only, 1989. http://web4.library.adelaide.edu.au/theses/09PH/09phf652.pdf.

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Nascimento, Juliana Minardi. "Caracterização da DNase da peçonha da serpente Bothrops alternatus : comparação com a DNase acida de mamiferos envolvida em apoptose." [s.n.], 2008. http://repositorio.unicamp.br/jspui/handle/REPOSIP/314698.

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Orientadores: Stephen Hyslop, Carla Beatriz Collares-Buzato<br>Tese (doutorado) - Universidade Estadual de Campinas, Instituto de Biologia<br>Made available in DSpace on 2018-08-10T23:21:13Z (GMT). No. of bitstreams: 1 Nascimento_JulianaMinardi_D.pdf: 8097756 bytes, checksum: 5350a8b542e9015bd5486f4418b36285 (MD5) Previous issue date: 2008<br>Resumo: As peçonhas de serpentes Bothrops são responsáveis por diversos danos locais (na região da mordida) e sistêmicos durante o envenenamento. Dentre as manifestações sistêmicas, a insuficiência renal aguda e um dos mais importantes efeitos tóxicos c
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Mejia, Lara Adrian Alberto. "Generation and isolation of recombinant DNase II enzyme." To access this resource online via ProQuest Dissertations and Theses @ UTEP, 2007. http://0-proquest.umi.com.lib.utep.edu/login?COPT=REJTPTU0YmImSU5UPTAmVkVSPTI=&clientId=2515.

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Pommer, Ansgar J. "Mechanistic studies on the DNase domain of colicin E9." Thesis, University of East Anglia, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.361425.

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Hashimoto, Tatsunori B. (Tatsunori Benjamin). "Computation identification of transcription factor binding using DNase-seq." Thesis, Massachusetts Institute of Technology, 2014. http://hdl.handle.net/1721.1/87945.

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Thesis: S.M., Massachusetts Institute of Technology, Department of Electrical Engineering and Computer Science, 2014.<br>Cataloged from PDF version of thesis.<br>Includes bibliographical references (pages 41-43).<br>Here we describe Protein Interaction Quantitation (PIQ), a computational method that models the magnitude and shape of genome-wide DNase profiles to facilitate the identification of transcription factor (TF) binding sites. Through the use of machine learning techniques, PIQ identified binding sites for >700 TFs from one DNase-seq experiment with accuracy comparable to ChIP-seq for
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Foerster, Amei Barbara. "Die DNase X als prädiktiver Marker in malignen gynäkologischen Tumoren? /." Freiburg i.Br, 2008. http://opac.nebis.ch/cgi-bin/showAbstract.pl?sys=000256414.

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Nuthall, Hugh. "Analysis of DNase I hypersensitive sites in the CFTR gene." Thesis, University of Oxford, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.298724.

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Li, Wei. "Protein-protein interaction specificity of immunity proteins for DNase colicins." Thesis, University of East Anglia, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.302033.

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Shah, Pallav Lalji. "Recombinant human DNase I in the treatment of cystic fibrosis." Thesis, King's College London (University of London), 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.297271.

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Books on the topic "DNase I"

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N, Payne J., and Trent Institute for Health Services Research. Working Group on Acute Purchasing., eds. The Use of DNase in cystic fibrosis. Trent Institute for Health ServicesResearch, 1996.

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Weston, Simon Alan. An X-ray crystallographic analysis of the DNase I - d(GGTATACC)2 complex. University of Portsmouth, 1992.

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Huang, Weei-Yuarn. Nucleosomal structure and functions: Characterization of the hamster cardiac myosin heavy chain genes DNase I hypersensitive sites. National Library of Canada = Bibliothèque nationale du Canada, 1997.

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Chan, Jonathan Ka Lok. Association of DNAse hypersensitive chromatin domains with the nuclear envelope and with nuclear pore complexes in 3T3 fibroblasts. National Library of Canada, 1999.

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Ugarković, Ðurðica, ed. Satellite DNAs in Physiology and Evolution. Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-74889-0.

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Association of Community Health Councils for England and Wales., ed. Outpatient appointments: 'did not attends' (DNAs). Associationof Community Health Councils for England and Wales, 1994.

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Ðurðica Ugarković. Satellite DNAs in Physiology and Evolution. Springer International Publishing AG, 2022.

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Ugarković, Ðurðica. Satellite DNAs in Physiology and Evolution. Springer International Publishing AG, 2021.

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Chou, Ping-Jung. Base inclinations in natural and synthetic DNAs. 1993.

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Expresión génica durante la embriogénesis del maíz (Zea mays L.), clonaje de c-DNAs correspondientes a genes inducidos por la Hormona ABA. 1987.

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Book chapters on the topic "DNase I"

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Cumming, Jeffrey M., Bradley J. Sinclair, Charles A. Triplehorn, et al. "DNAse." In Encyclopedia of Entomology. Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6359-6_960.

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Leblanc, Benoît, and Tom Moss. "DNase I Footprinting." In Methods in Molecular Biology™. Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60327-015-1_3.

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Cardew, Antonia S., and Keith R. Fox. "DNase I Footprinting." In Methods in Molecular Biology. Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60327-418-0_10.

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Shibata, Yoichiro, and Gregory E. Crawford. "Mapping Regulatory Elements by DNaseI Hypersensitivity Chip (DNase-Chip)." In Microarray Analysis of the Physical Genome. Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60327-192-9_13.

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Lahm, A., S. A. Weston, and D. Suck. "Structure of DNase I." In Nucleic Acids and Molecular Biology. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-84292-4_11.

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Dotti, Isabella, and Serena Bonin. "DNase Treatment of RNA." In Guidelines for Molecular Analysis in Archive Tissues. Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-17890-0_18.

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Duan, Zhijun. "Targeted DNase Hi-C." In Methods in Molecular Biology. Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0664-3_5.

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Chaudhari, Archana, Ruma Raghuvanshi, and Mitesh Kumar Dwivedi. "Determination of DNAse Activity." In Methods and Protocols in Food Science. Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2509-5_7.

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Leblanc, Benoît P., and Tom Moss. "In Vitro DNase I Footprinting." In Methods in Molecular Biology. Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2877-4_2.

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Filichkin, Sergei A., and Molly Megraw. "DNase I SIM: A Simplified In-Nucleus Method for DNase I Hypersensitive Site Sequencing." In Methods in Molecular Biology. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7125-1_10.

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Conference papers on the topic "DNase I"

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Assallum, H., L. Miranda, L. J. Delorenzo, and K. N. Harris. "Bronchoscopically DNase Instillation for Refractory Lobar Atelectasis." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a4653.

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West, Abby L., Mark H. Griep, Dan P. Cole, and Shashi P. Karna. "Gold nanocluster-DNase 1 hybrid materials for DNA contamination sensing." In 2014 IEEE 14th International Conference on Nanotechnology (IEEE-NANO). IEEE, 2014. http://dx.doi.org/10.1109/nano.2014.6968066.

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LUO, KAIXUAN, and ALEXANDER J. HARTEMINK. "USING DNASE DIGESTION DATA TO ACCURATELY IDENTIFY TRANSCRIPTION FACTOR BINDING SITES." In Proceedings of the Pacific Symposium. WORLD SCIENTIFIC, 2012. http://dx.doi.org/10.1142/9789814447973_0009.

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Lian, Deyuan, Bo He, Fengfei Song, Meng Li, and Weixing Feng. "Research on preprocessing of DNase signal in DNAprotein binding sites detection." In 2014 IEEE International Conference on Mechatronics and Automation (ICMA). IEEE, 2014. http://dx.doi.org/10.1109/icma.2014.6885942.

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Xu, Siwen, Ying Wang, Huan Liu, Duojiao Chen, Hongyuan Bi, and Weixing Feng. "A new method for alleviating sequence-specific biases in DNase-seq." In 2017 First International Conference on Electronics Instrumentation & Information Systems (EIIS). IEEE, 2017. http://dx.doi.org/10.1109/eiis.2017.8298582.

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Pedersen, HL, KD Horvei, D. Thiyagarajan, et al. "PS1:17 Lupus nephritis: severely reduced urinary dnase i levels reflect loss of renal dnase i, disease progression and may reduce the need for renal biopsies." In 11th European Lupus Meeting, Düsseldorf, Germany, 21–24 March 2018, Abstract presentations. Lupus Foundation of America, 2018. http://dx.doi.org/10.1136/lupus-2018-abstract.65.

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Sang, Peichao, Duojiao Chen, Siwen Xu, and Weixing Feng. "Identification method of transcription factor binding sites based on DNase-Seq signal." In 2015 IEEE International Conference on Mechatronics and Automation (ICMA). IEEE, 2015. http://dx.doi.org/10.1109/icma.2015.7237735.

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Trofimenko, A., M. Mamus, E. Mozgovaya, S. Bedina, and S. Spitsina. "PO.2.34 Anti-DNase i antibodies: an emerging diagnostic marker of SLE." In 13th European Lupus Meeting, Stockholm (October 5–8, 2022). Lupus Foundation of America, 2022. http://dx.doi.org/10.1136/lupus-2022-elm2022.64.

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Gunnarsson, I., F. Guo-Zhong, HG Mannherz, M. Napirei, A. Gültekin, and J. Frostegård. "FRI0132 Decreased serum dnase 1 activity levels in sle patients with active disease." In Annual European Congress of Rheumatology, Annals of the rheumatic diseases ARD July 2001. BMJ Publishing Group Ltd and European League Against Rheumatism, 2001. http://dx.doi.org/10.1136/annrheumdis-2001.167.

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Shetty, Prashanth, Alex Francioni, and Adeel Jafri. "Intrapleural use of tissue plasminogen activator and DNase in management of pleural infection." In ERS International Congress 2023 abstracts. European Respiratory Society, 2023. http://dx.doi.org/10.1183/13993003.congress-2023.pa3858.

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Reports on the topic "DNase I"

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West, Abby L., Mark H. Griep, Dan P. Cole, and Shashi P. Karna. Gold Nanocluster-DNase 1 Hybrid Materials for DNA Contamination Sensing. Defense Technical Information Center, 2014. http://dx.doi.org/10.21236/ada610452.

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Abley, J., B. Dickson, W. Kumari, and G. Michaelson. AS112 Redirection Using DNAME. RFC Editor, 2015. http://dx.doi.org/10.17487/rfc7535.

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Rose, S., and W. Wijngaards. DNAME Redirection in the DNS. RFC Editor, 2012. http://dx.doi.org/10.17487/rfc6672.

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Isailovic, Slavica. Single-Molecule Imaging of DNAs with Sticky Ends at Water/Fused Silica Interface. Office of Scientific and Technical Information (OSTI), 2005. http://dx.doi.org/10.2172/861626.

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Kistler, Harold Corby, Talma Katan, and Dani Zamir. Molecular Karyotypes of Pathogeic Strains of Fusarium oxysporum. United States Department of Agriculture, 1995. http://dx.doi.org/10.32747/1995.7604927.bard.

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Genetic diversity of pathogenic strains of the fungus Fusarium oxysporum was determied by analysis of electrophoretic karyotype, as well as by DNA variation detected by Restriction Fragment Length Polymorphisms (RFLPs) and Random Amplified Polymorphic DNAs (RAPDs). The electrophoretic karyotypes for 130 isolates of the fungus pathogenic to tomato, melon, and banana were analyzed. Electrophoretic karyotype variation, reflected in differences in apparent chromosome number and genome size, was observed even among isolates from the same host and sub specific category. Sub specific categories studi
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