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Relevant bibliographies by topics / Zinc finger

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Academic literature on the topic 'Zinc finger'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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Journal articles on the topic "Zinc finger"

1

Li, Huiyu, Xiaomei Chen, Wei Xiong, Fang Liu, and Shiang Huang. "The Regulation of Zinc Finger Proteins by Mirnas Enriched in ALL-Microvesicles." Blood 120, no. 21 (2012): 1448. http://dx.doi.org/10.1182/blood.v120.21.1448.1448.

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Abstract Abstract 1448 Microvesicles (MVs) are submicrometric membrane fragments and they can “hijack” membrane components and engulf cytoplasmic contents from their cellular origin. MVs are enriched in various bioactive molecules of their parental cells, such as proteins, DNA, mRNA and miRNAs. Microvesicles (MVs) released by leukemia cells constitute an important part of the leukemia microenvironment. As a cell-to-cell communication tool, MVs transfer microRNA (miRNA) between cells. MVs miRNAs may also provide an insight in the role of miRNAs playing in the underlying of pathophysiologic proc

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Keller, A. D., and T. Maniatis. "Only two of the five zinc fingers of the eukaryotic transcriptional repressor PRDI-BF1 are required for sequence-specific DNA binding." Molecular and Cellular Biology 12, no. 5 (1992): 1940–49. http://dx.doi.org/10.1128/mcb.12.5.1940-1949.1992.

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The eukaryotic transcriptional repressor PRDI-BF1 contains five zinc fingers of the C2H2 type, and the protein binds specifically to PRDI, a 14-bp regulatory element of the beta interferon gene promoter. We have investigated the amino acid sequence requirements for specific binding to PRDI and found that the five zinc fingers and a short stretch of amino acids N terminal to the first finger are necessary and sufficient for PRDI-specific binding. The contribution of individual zinc fingers to DNA binding was investigated by inserting them in various combinations into another zinc finger-contain

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Keller, A. D., and T. Maniatis. "Only two of the five zinc fingers of the eukaryotic transcriptional repressor PRDI-BF1 are required for sequence-specific DNA binding." Molecular and Cellular Biology 12, no. 5 (1992): 1940–49. http://dx.doi.org/10.1128/mcb.12.5.1940.

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The eukaryotic transcriptional repressor PRDI-BF1 contains five zinc fingers of the C2H2 type, and the protein binds specifically to PRDI, a 14-bp regulatory element of the beta interferon gene promoter. We have investigated the amino acid sequence requirements for specific binding to PRDI and found that the five zinc fingers and a short stretch of amino acids N terminal to the first finger are necessary and sufficient for PRDI-specific binding. The contribution of individual zinc fingers to DNA binding was investigated by inserting them in various combinations into another zinc finger-contain

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4

Sievers, Quinlan L., Georg Petzold, Richard D. Bunker, et al. "Defining the human C2H2 zinc finger degrome targeted by thalidomide analogs through CRBN." Science 362, no. 6414 (2018): eaat0572. http://dx.doi.org/10.1126/science.aat0572.

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The small molecules thalidomide, lenalidomide, and pomalidomide induce the ubiquitination and proteasomal degradation of the transcription factors Ikaros (IKZF1) and Aiolos (IKZF3) by recruiting a Cys2-His2 (C2H2) zinc finger domain to Cereblon (CRBN), the substrate receptor of the CRL4CRBN E3 ubiquitin ligase. We screened the human C2H2 zinc finger proteome for degradation in the presence of thalidomide analogs, identifying 11 zinc finger degrons. Structural and functional characterization of the C2H2 zinc finger degrons demonstrates how diverse zinc finger domains bind the permissive drug-CR

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Witte, M. M., and R. C. Dickson. "The C6 zinc finger and adjacent amino acids determine DNA-binding specificity and affinity in the yeast activator proteins LAC9 and PPR1." Molecular and Cellular Biology 10, no. 10 (1990): 5128–37. http://dx.doi.org/10.1128/mcb.10.10.5128-5137.1990.

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LAC9 is a DNA-binding protein that regulates transcription of the lactose-galactose regulon in Kluyveromyces lactis. The DNA-binding domain is composed of a zinc finger and nearby amino acids (M. M. Witte and R. C. Dickson, Mol. Cell. Biol. 8:3726-3733, 1988). The single zinc finger appears to be structurally related to the zinc finger of many other fungal transcription activator proteins that contain positively charged residues and six conserved cysteines with the general form Cys-Xaa2-Cys-Xaa6-Cys-Xaa6-9-Cys-Xaa2-Cys-Xaa 6-Cys, where Xaan indicates a stretch of the indicated number of any am

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Witte, M. M., and R. C. Dickson. "The C6 zinc finger and adjacent amino acids determine DNA-binding specificity and affinity in the yeast activator proteins LAC9 and PPR1." Molecular and Cellular Biology 10, no. 10 (1990): 5128–37. http://dx.doi.org/10.1128/mcb.10.10.5128.

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LAC9 is a DNA-binding protein that regulates transcription of the lactose-galactose regulon in Kluyveromyces lactis. The DNA-binding domain is composed of a zinc finger and nearby amino acids (M. M. Witte and R. C. Dickson, Mol. Cell. Biol. 8:3726-3733, 1988). The single zinc finger appears to be structurally related to the zinc finger of many other fungal transcription activator proteins that contain positively charged residues and six conserved cysteines with the general form Cys-Xaa2-Cys-Xaa6-Cys-Xaa6-9-Cys-Xaa2-Cys-Xaa 6-Cys, where Xaan indicates a stretch of the indicated number of any am

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GREEN, Andrew, and Bibudhendra SARKAR. "Alteration of zif268 zinc-finger motifs gives rise to non-native zinc-co-ordination sites but preserves wild-type DNA recognition." Biochemical Journal 333, no. 1 (1998): 85–90. http://dx.doi.org/10.1042/bj3330085.

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Zinc fingers are among the major structural motifs found in proteins that are involved in eukaryotic gene regulation. Many of these zinc-finger domains are involved in DNA binding. This study investigated whether the zinc-co-ordinating (Cys)2(His)2 motif found in the three zinc fingers of zif268 could be replaced by a (Cys)4 motif while still preserving DNA recognition. (Cys)2(His)2-to-(Cys)4 mutations were generated in each of the three zinc fingers of zif268 individually, as well as in fingers 1 and 3, and fingers 2 and 3 together. Whereas finger 1 and finger 3 tolerate the switch, such an a

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Rollins, M. B., S. Del Rio, A. L. Galey, D. R. Setzer, and M. T. Andrews. "Role of TFIIIA zinc fingers in vivo: analysis of single-finger function in developing Xenopus embryos." Molecular and Cellular Biology 13, no. 8 (1993): 4776–83. http://dx.doi.org/10.1128/mcb.13.8.4776-4783.1993.

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The Xenopus 5S RNA gene-specific transcription factor IIIA (TFIIIA) has nine consecutive Cys2His2 zinc finger motifs. Studies were conducted in vivo to determine the contribution of each of the nine zinc fingers to the activity of TFIIIA in living cells. Nine separate TFIIIA mutants were expressed in Xenopus embryos following microinjection of their respective in vitro-derived mRNAs. Each mutant contained a single histidine-to-asparagine substitution in the third zinc ligand position of an individual zinc finger. These mutations result in structural disruption of the mutated finger with little

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Rollins, M. B., S. Del Rio, A. L. Galey, D. R. Setzer, and M. T. Andrews. "Role of TFIIIA zinc fingers in vivo: analysis of single-finger function in developing Xenopus embryos." Molecular and Cellular Biology 13, no. 8 (1993): 4776–83. http://dx.doi.org/10.1128/mcb.13.8.4776.

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The Xenopus 5S RNA gene-specific transcription factor IIIA (TFIIIA) has nine consecutive Cys2His2 zinc finger motifs. Studies were conducted in vivo to determine the contribution of each of the nine zinc fingers to the activity of TFIIIA in living cells. Nine separate TFIIIA mutants were expressed in Xenopus embryos following microinjection of their respective in vitro-derived mRNAs. Each mutant contained a single histidine-to-asparagine substitution in the third zinc ligand position of an individual zinc finger. These mutations result in structural disruption of the mutated finger with little

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Gebelein, Brian, and Raul Urrutia. "Sequence-Specific Transcriptional Repression by KS1, a Multiple-Zinc-Finger–Krüppel-Associated Box Protein." Molecular and Cellular Biology 21, no. 3 (2001): 928–39. http://dx.doi.org/10.1128/mcb.21.3.928-939.2001.

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ABSTRACT The vertebrate genome contains a large number of Krüppel-associated box–zinc finger genes that encode 10 or more C2-H2 zinc finger motifs. Members of this gene family have been proposed to function as transcription factors by binding DNA through their zinc finger region and repressing gene expression via the KRAB domain. To date, however, no Krüppel-associated box–zinc finger protein (KRAB-ZFP) and few proteins with 10 or more zinc finger motifs have been shown to bind DNA in a sequence-specific manner. Our laboratory has recently identified KS1, a member of the KRAB-ZFP family that

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Dissertations / Theses on the topic "Zinc finger"

1

Looman, Camilla. "The ABC of KRAB zinc finger proteins." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Univ.-bibl. [distributör], 2003. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-3515.

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Lanfear, Jeremy. "The molecular evolution of zinc-finger genes." Thesis, University of Oxford, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.291274.

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Crawford, Catherine. "Characterisation of endogenous KRAB zinc finger proteins." Thesis, University of Edinburgh, 2009. http://hdl.handle.net/1842/4225.

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The Krüppel-associated box (KRAB) zinc finger protein (ZFP) genes comprise one of the largest gene families in the mammalian genome, encoding transcription factors with an N-terminal KRAB domain and C-terminal zinc fingers. The KRAB domain interacts with a co-repressor protein, KAP-1, which can recruit various factors causing transcriptional repression of genes to which KRAB ZFPs bind. Little is currently known about the gene targets of the ~400 human and mouse KRAB ZFPs. Many KRAB ZFPs interact with factors other than KAP-1. To identify proteins that may interact with one particular KRAB ZFP

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Rebar, Edward John. "Selection studies of zinc finger-DNA recognition." Thesis, Massachusetts Institute of Technology, 1997. http://hdl.handle.net/1721.1/10383.

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Simpson, Raina Jui Yu. "The multiple roles of zinc finger domains." Thesis, The University of Sydney, 2004. http://hdl.handle.net/2123/655.

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Zinc finger (ZnF) domains are prevalent in eukaryotes and play crucial roles in mediating protein-DNA and protein-protein interactions. This Thesis focuses on the molecular details underlying interactions mediated by two ZnF domains. The GATA-1 protein is vital for the development of erythrocytes and megakaryocytes. Pertinent to the protein function is the N-terminal ZnF. In particular, this domain mediates interaction with DNA containing GATC motifs and the coactivator protein FOG. The importance of these interactions was illustrated by the findings in Chapter 3 that naturally occurring muta

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Simpson, Raina Jui Yu. "The multiple roles of zinc finger domains." University of Sydney. Molecular and Microbial Biosciences, 2004. http://hdl.handle.net/2123/655.

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Zinc finger (ZnF) domains are prevalent in eukaryotes and play crucial roles in mediating protein-DNA and protein-protein interactions. This Thesis focuses on the molecular details underlying interactions mediated by two ZnF domains. The GATA-1 protein is vital for the development of erythrocytes and megakaryocytes. Pertinent to the protein function is the N-terminal ZnF. In particular, this domain mediates interaction with DNA containing GATC motifs and the coactivator protein FOG. The importance of these interactions was illustrated by the findings in Chapter 3 that naturally occurring muta

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Wang, Zhonghua Laity John H. "Characterization of novel structure-regulatory relationships within interacting two-finger Cys₂His₂ zinc finger protein motifs." Diss., UMK access, 2008.

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Thesis (Ph. D.)--School of Biological Sciences. University of Missouri--Kansas City, 2008.<br>"A dissertation in cell biology and biophysics and molecular biology and biochemistry." Advisor: John H. Laity. Typescript. Vita. Title from "catalog record" of the print edition Description based on contents viewed Sept.12, 2008. Includes bibliographical references (leaves 148-166). Online version of the print edition.

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Fairall, Louise. "The interaction of zinc-finger proteins with DNA." Thesis, University of Cambridge, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.314849.

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Knight, Robert D. "C2H2 zinc finger gene evolution in the Metazoa." Thesis, University of Reading, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.312566.

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Younce, Craig. "Zinc-Finger Protein MCPIP in Cell Death and Differentiation." Doctoral diss., University of Central Florida, 2009. http://digital.library.ucf.edu/cdm/ref/collection/ETD/id/2279.

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Monocyte chemotactic protein-1 (MCP-1) plays a critical role in the development of cardiovascular diseases. How MCP-1 contributes to the development of heart disease is not understood. We present evidence that MCP-1 causes death in cardiac myoblasts, H9c2 by inducing oxidative stress, ER stress and autophagy via a novel Zn-finger protein, MCP-1 induced protein (MCPIP). MCPIP expression caused cell death and knockdown of MCPIP, attenuated MCP-1 induced cell death. Expression of MCPIP resulted in induction of iNOS and production of reactive oxygen (ROS). It caused induction of NADPH oxidase subu

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Books on the topic "Zinc finger"

1

Liu, Jia, ed. Zinc Finger Proteins. Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8799-3.

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Iuchi, Shiro, and Natalie Kuldell, eds. Zinc Finger Proteins. Springer US, 2005. http://dx.doi.org/10.1007/b139055.

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Mackay, Joel P., and David J. Segal, eds. Engineered Zinc Finger Proteins. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-753-2.

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Bibudhendra, Sarkar, and International Symposium on "Metals and Genetics" (1st : 1994 : Toronto, Ont.), eds. Genetic response to metals. M. Dekker, 1995.

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1930-, Sluyser M., ed. Zinc-finger proteins in oncogenesis: DNA-binding and gene regulation. New York Academy of Sciences, 1993.

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6

Ferraz de Paiva, Raphael Enoque. Gold(I,III) Complexes Designed for Selective Targeting and Inhibition of Zinc Finger Proteins. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-030-00853-6.

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Pritchard, Jane. Analysis of drongo, a new Drosophila zinc finger gene expressed during oogenesis and neurogenesis. typescript, 1999.

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8

Perakakis, Nikolaos. The role of the zinc-finger transcription factor Krüppel-like factor 11 for gene regulation in pancreatic beta cells. s.n.], 2013.

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Dimitroulakos, Jim. An analysis of growth and differentiation of human neuroblastoma: Identification of HMG-CoA reductase and a novel zinc finger gene as potential mediators. National Library of Canada = Bibliothèque nationale du Canada, 1997.

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Avgousti, Daphne Christina Anastasiades. An Analysis of the Essential Chromatin Factor Zinc Finger Protein 1 (ZFP-1), and a Study of the Involvement of RNAi factors in Histone Processing in Caenorabditis Elegans. [publisher not identified], 2012.

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Book chapters on the topic "Zinc finger"

1

Mudziwapasi, Reagan, Ringisai Chekera, Clophas Zibusiso Ncube, et al. "Zinc Finger Nucleases." In Genome Editing Tools and Gene Drives. CRC Press, 2021. http://dx.doi.org/10.1201/9781003165316-2.

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De Guzman, Roberto N., Maria A. Martinez-Yamout, H. Jane Dyson, and Peter E. Wright. "Structure and Function of the CBP/p300 TAZ Domains." In Zinc Finger Proteins. Springer US, 2005. http://dx.doi.org/10.1007/0-387-27421-9_17.

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Van Roey, Patrick, Marlene Belfort, and Victoria Derbyshire. "Homing Endonuclease I-TevI: An Atypical Zinc Finger with a Novel Function." In Zinc Finger Proteins. Springer US, 2005. http://dx.doi.org/10.1007/0-387-27421-9_7.

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Ferro, M., N. Giommoni, C. T. Baldari, Elisa A. Bellomo, Guy A. Rutter, and Gerd Schmitz. "Zinc Finger Protein 202." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101480.

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Jackson, David A., Jason A. Misurelli, and Sherine F. Elsawa. "GLI Family Zinc Finger 2." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101917.

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Jackson, David A., Jason A. Misurelli, and Sherine F. Elsawa. "GLI Family Zinc Finger 2." In Encyclopedia of Signaling Molecules. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4614-6438-9_101917-1.

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Gewies, Andreas, Jürgen Ruland, Alexey Kotlyarov, et al. "Monocytic Leukemia Zinc-Finger Protein." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100841.

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Matthews, Jacqueline M. "Zinc Finger Folds and Functions." In Encyclopedia of Metalloproteins. Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_203.

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Hudson, Laurie G., Karen L. Cooper, Susan R. Atlas, Brenee S. King, and Ke Jian Liu. "Arsenic Interaction with Zinc Finger Motifs." In Arsenic. John Wiley & Sons, Inc, 2015. http://dx.doi.org/10.1002/9781118876992.ch13.

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Imanishi, Miki, Shigeru Negi, and Yukio Sugiura. "Non-FokI-Based Zinc Finger Nucleases." In Methods in Molecular Biology. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-753-2_21.

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Conference papers on the topic "Zinc finger"

1

Kessler, Stephen M., and Nhung T. Le. "Performance of a New Mill Supply Treatment Program." In CORROSION 1997. NACE International, 1997. https://doi.org/10.5006/c1997-97377.

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Abstract Cooling water treatments containing zinc are being more strictly regulated. Fines are being imposed in some instances where zinc discharge concentrations are as low as 0.5 ppm (mg/L). With regulatory concerns looming, many plants are deciding to eliminate zinc from their cooling loops. Laboratory work was conducted to identify potential zinc replacement technology for use under mill supply conditions typical of those found in pulp and paper applications. This industry segment is one of the largest users of once-through cooling water. An organic replacement able to provide zinc-like pe

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Ashiru, Oluwatoyin. "Improvement in Electroplating of Tin-Zinc Alloy Coating." In CORROSION 2010. NACE International, 2010. https://doi.org/10.5006/c2010-10269.

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Abstract Tin-zinc electrodeposit offers outstanding corrosion protection for steel by combining the barrier protection of tin with the galvanic protection of zinc, without the bulky corrosion product associated with wholly zinc deposit. It has high corrosion resistance, especially against sulfur dioxide and salt water for aircraft parts, automobile components, and equipment used for offshore oilfield applications. Tin-zinc coating was developed as a direct replacement for environmentally unfriendly cadmium coating. In this publication, the technical improvements achieved in the electrodepositi

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Tremberger Jr., G., E. Cheung, R. Subramaniam, et al. "C2H2 Zinc Finger Nucleotide Fluctuation." In 2008 2nd International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2008. http://dx.doi.org/10.1109/icbbe.2008.231.

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Sievers, Quinlan L., Georg Petzold, Richard D. Bunker, et al. "Abstract PL02-03: The zinc-finger degrome." In Abstracts: AACR-NCI-EORTC International Conference on Molecular Targets and Cancer Therapeutics; October 26-30, 2019; Boston, MA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1535-7163.targ-19-pl02-03.

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Tang, Mengxiang, Michael Waterman, and Shibu Yooseph. "Zinc finger gene clusters and tandem gene duplication." In the fifth annual international conference. ACM Press, 2001. http://dx.doi.org/10.1145/369133.369241.

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Novaković, Stefan, and Vladimir Risojević. "Learning Localization of Body and Finger Animation Skeleton Joints on Three-Dimensional Models of Human Bodies." In 2024 Zooming Innovation in Consumer Technologies Conference (ZINC). IEEE, 2024. http://dx.doi.org/10.1109/zinc61849.2024.10579426.

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Jia, Di, Robyn Loureiro, Patricia D'Amore, Scott Rodig, and Marsha Moses. "Abstract 2392: Transcriptional repression of VEGF by Znf24, a C2H2 zinc finger protein." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2392.

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Hsia, Justin, William J. Holtz, Michel M. Maharbiz, and Murat Arcak. "New architecture for patterning gene expression using zinc finger proteins and small RNAs." In 2012 IEEE 51st Annual Conference on Decision and Control (CDC). IEEE, 2012. http://dx.doi.org/10.1109/cdc.2012.6426642.

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Hightower, Asia. "Functional Specialization of Alternative Zinc Finger Proteins in Vegetative and Reproductive Meristem Regulation." In ASPB PLANT BIOLOGY 2020. ASPB, 2020. http://dx.doi.org/10.46678/pb.20.1332335.

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Al Bataineh, Mohammad Fayez. "Enhanced Detection and Localization of Zinc Finger Proteins Using Advanced Neural Network Techniques." In ICBET 2024: 2024 14th International Conference on Biomedical Engineering and Technology. ACM, 2024. http://dx.doi.org/10.1145/3678935.3678936.

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Reports on the topic "Zinc finger"

1

Hanas, Jay S. DEPSCOR/97-98 Mechanisms and Biomonitoring of Toxicant-Induced Changes in Zinc Finger Proteins. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada399974.

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Gmeiner, William H. Metal Occupancy of Zinc Finger Motifs as Determinants for Zn2+-Mediated Chemosensitization of Prostate Cancer Cells. Defense Technical Information Center, 2013. http://dx.doi.org/10.21236/ada596731.

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Rauscher III, Frank J. A Novel Strategy for Controlling the Metastic Phenotype: Targeting the SNAG Repression Domain in the SNAIL Zinc-Finger Protein. Defense Technical Information Center, 2003. http://dx.doi.org/10.21236/ada417783.

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Rauscher, III, and Frank J. A Novel Strategy for Controlling the Metastatic Phenotype: Targeting the SNAG Repression Domain in the SNAIL Zinc-Finger Protein. Defense Technical Information Center, 2007. http://dx.doi.org/10.21236/ada474599.

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Paran, Ilan, and Allen Van Deynze. Regulation of pepper fruit color, chloroplasts development and their importance in fruit quality. United States Department of Agriculture, 2014. http://dx.doi.org/10.32747/2014.7598173.bard.

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Pepper exhibits large natural variation in chlorophyll content in the immature fruit. To dissect the genetic and molecular basis of this variation, we conducted QTL mapping for chlorophyll content in a cross between light and dark green-fruited parents, PI 152225 and 1154. Two major QTLs, pc1 and pc10, that control chlorophyll content by modulation of chloroplast compartment size in a fruit-specific manner were detected in chromosomes 1 and 10, respectively. The pepper homolog of GOLDEN2- LIKE transcription factor (CaGLK2) was found as underlying pc10, similar to its effect on tomato fruit chl

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Porat, Ron, Gregory T. McCollum, Amnon Lers, and Charles L. Guy. Identification and characterization of genes involved in the acquisition of chilling tolerance in citrus fruit. United States Department of Agriculture, 2007. http://dx.doi.org/10.32747/2007.7587727.bard.

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Citrus, like many other tropical and subtropical fruit are sensitive to chilling temperatures. However, application of a pre-storage temperature conditioning (CD) treatment at 16°C for 7 d or of a hot water brushing (HWB) treatment at 60°C for 20 sec remarkably enhances chilling tolerance and reduces the development of chilling injuries (CI) upon storage at 5°C. In the current research, we proposed to identify and characterize grapefruit genes that are induced by CD, and may contribute to the acquisition of fruit chilling tolerance, by two different molecular approaches: cDNA array analysis an

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Rauscher, Frank J., and III. A Novel Strategy for Controlling the Metastatic Phenotype: Targeting the SNAG Repression Domain in the SNAIL Zing-Finger Protein. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada427153.

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