Log in

Relevant bibliographies by topics / Zinc fingers / Journal articles

To see the other types of publications on this topic, follow the link: Zinc fingers.

Journal articles on the topic 'Zinc fingers'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Zinc fingers.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

2

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

3

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

4

Drummond, I. A., H. D. Rupprecht, P. Rohwer-Nutter, et al. "DNA recognition by splicing variants of the Wilms' tumor suppressor, WT1." Molecular and Cellular Biology 14, no. 6 (1994): 3800–3809. http://dx.doi.org/10.1128/mcb.14.6.3800-3809.1994.

Full text

Abstract:

The Wilms' tumor suppressor, WT1, is a zinc finger transcriptional regulator which exists as multiple forms owing to alternative mRNA splicing. The most abundant splicing variants contain a nine-nucleotide insertion encoding lysine, threonine, and serine (KTS) in the H-C link region between the third and fourth WT1 zinc fingers which disrupts binding to a previously defined WT1-EGR1 binding site. We have identified WT1[+KTS] binding sites in the insulin-like growth factor II gene and show that WT1[+KTS] represses transcription from the insulin-like growth factor II P3 promoter. The highest aff

APA, Harvard, Vancouver, ISO, and other styles

5

Drummond, I. A., H. D. Rupprecht, P. Rohwer-Nutter, et al. "DNA recognition by splicing variants of the Wilms' tumor suppressor, WT1." Molecular and Cellular Biology 14, no. 6 (1994): 3800–3809. http://dx.doi.org/10.1128/mcb.14.6.3800.

Full text

Abstract:

The Wilms' tumor suppressor, WT1, is a zinc finger transcriptional regulator which exists as multiple forms owing to alternative mRNA splicing. The most abundant splicing variants contain a nine-nucleotide insertion encoding lysine, threonine, and serine (KTS) in the H-C link region between the third and fourth WT1 zinc fingers which disrupts binding to a previously defined WT1-EGR1 binding site. We have identified WT1[+KTS] binding sites in the insulin-like growth factor II gene and show that WT1[+KTS] represses transcription from the insulin-like growth factor II P3 promoter. The highest aff

APA, Harvard, Vancouver, ISO, and other styles

6

Heller, Jennifer, Hilde Schjerven, Ju Qiu, Aileen Lee, Stephen Smale, and Liang Zhou. "Selective requirement of Ikaros zinc fingers in Treg and Th17 fate decision. (P1137)." Journal of Immunology 190, no. 1_Supplement (2013): 50.11. http://dx.doi.org/10.4049/jimmunol.190.supp.50.11.

Full text

Abstract:

Abstract TGF-β is a common factor important for the differentiation of pro-inflammatory Th17 and anti-inflammatory inducible Treg cells. However, the precise molecular mechanisms underlying the fate decision of differentiating CD4+ T cells in the presence of TGF-β is poorly understood. Here, we show that distinctive N-terminal DNA-binding zinc fingers of Ikaros play essential roles in Treg and Th17 fate decision. Ikaros has a highly conserved DNA-binding domain near the N-terminus with four tandem zinc fingers. Zinc fingers 2 and 3 are required for stable binding to DNA, whereas fingers 1 and

APA, Harvard, Vancouver, ISO, and other styles

7

Li, Yong, Tomoki Kimura, John H. Laity, and Glen K. Andrews. "The Zinc-Sensing Mechanism of Mouse MTF-1 Involves Linker Peptides between the Zinc Fingers." Molecular and Cellular Biology 26, no. 15 (2006): 5580–87. http://dx.doi.org/10.1128/mcb.00471-06.

Full text

Abstract:

ABSTRACT Mouse metal response element-binding transcription factor-1 (MTF-1) regulates the transcription of genes in response to a variety of stimuli, including exposure to zinc or cadmium, hypoxia, and oxidative stress. Each of these stresses may increase labile cellular zinc, leading to nuclear translocation, DNA binding, and transcriptional activation of metallothionein genes (MT genes) by MTF-1. Several lines of evidence suggest that the highly conserved six-zinc finger DNA-binding domain of MTF-1 also functions as a zinc-sensing domain. In this study, we investigated the potential role of

APA, Harvard, Vancouver, ISO, and other styles

8

Morris, J. F., R. Hromas, and F. J. Rauscher. "Characterization of the DNA-binding properties of the myeloid zinc finger protein MZF1: two independent DNA-binding domains recognize two DNA consensus sequences with a common G-rich core." Molecular and Cellular Biology 14, no. 3 (1994): 1786–95. http://dx.doi.org/10.1128/mcb.14.3.1786-1795.1994.

Full text

Abstract:

The myeloid zinc finger gene 1, MZF1, encodes a transcription factor which is expressed in hematopoietic progenitor cells that are committed to myeloid lineage differentiation. MZF1 contains 13 C2H2 zinc fingers arranged in two domains which are separated by a short glycine- and proline-rich sequence. The first domain consists of zinc fingers 1 to 4, and the second domain is formed by zinc fingers 5 to 13. We have determined that both sets of zinc finger domains bind DNA. Purified, recombinant MZF1 proteins containing either the first set of zinc fingers or the second set were prepared and use

APA, Harvard, Vancouver, ISO, and other styles

9

Morris, J. F., R. Hromas, and F. J. Rauscher. "Characterization of the DNA-binding properties of the myeloid zinc finger protein MZF1: two independent DNA-binding domains recognize two DNA consensus sequences with a common G-rich core." Molecular and Cellular Biology 14, no. 3 (1994): 1786–95. http://dx.doi.org/10.1128/mcb.14.3.1786.

Full text

Abstract:

The myeloid zinc finger gene 1, MZF1, encodes a transcription factor which is expressed in hematopoietic progenitor cells that are committed to myeloid lineage differentiation. MZF1 contains 13 C2H2 zinc fingers arranged in two domains which are separated by a short glycine- and proline-rich sequence. The first domain consists of zinc fingers 1 to 4, and the second domain is formed by zinc fingers 5 to 13. We have determined that both sets of zinc finger domains bind DNA. Purified, recombinant MZF1 proteins containing either the first set of zinc fingers or the second set were prepared and use

APA, Harvard, Vancouver, ISO, and other styles

10

Klug, Aaron, and John W. R. Schwabe. "Zinc fingers." FASEB Journal 9, no. 8 (1995): 597–604. http://dx.doi.org/10.1096/fasebj.9.8.7768350.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Rhodes, Daniela, and Aaron Klug. "Zinc Fingers." Scientific American 268, no. 2 (1993): 56–65. http://dx.doi.org/10.1038/scientificamerican0293-56.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

Kaptein, Robert. "Zinc fingers." Current Opinion in Structural Biology 1, no. 1 (1991): 63–70. http://dx.doi.org/10.1016/0959-440x(91)90013-j.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

Meinke, Peter. "Zinc Fingers." Issues in Science and Technology 39, no. 4 (2023): 38. http://dx.doi.org/10.58875/clid1184.

Full text

APA, Harvard, Vancouver, ISO, and other styles

14

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

15

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

16

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

17

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

18

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

19

Schjerven, Hilde, Seth Frietze, Jami McLaughlin, et al. "Role of Ikaros in hematopoiesis and tumor suppression: Selective functions of individual zinc fingers within the DNA-binding domain of Ikaros. (42.3)." Journal of Immunology 188, no. 1_Supplement (2012): 42.3. http://dx.doi.org/10.4049/jimmunol.188.supp.42.3.

Full text

Abstract:

Abstract Ikaros, a C2H2 zinc finger transcription factor, is a critical regulator of hematopoiesis and tumor suppression in the lymphoid lineage. The C2H2 zinc finger is the most prevalent DNA-binding motif in mammals, with DNA-binding domains usually containing more tandem fingers than are needed for stable sequence-specific DNA recognition. To examine the reason for the frequent presence of multiple zinc fingers, and to investigate in greater depth the role of Ikaros in hematopoiesis and tumor suppression, we generated mice lacking finger 1 or finger 4 of the 4-finger DNA-binding domain of I

APA, Harvard, Vancouver, ISO, and other styles

20

Guo, Jianhui, Tiyun Wu, Bradley F. Kane, et al. "Subtle Alterations of the Native Zinc Finger Structures Have Dramatic Effects on the Nucleic Acid Chaperone Activity of Human Immunodeficiency Virus Type 1 Nucleocapsid Protein." Journal of Virology 76, no. 9 (2002): 4370–78. http://dx.doi.org/10.1128/jvi.76.9.4370-4378.2002.

Full text

Abstract:

ABSTRACT The nucleocapsid protein (NC) of human immunodeficiency virus type 1 has two zinc fingers, each containing the invariant CCHC zinc-binding motif; however, the surrounding amino acid context is not identical in the two fingers. Recently, we demonstrated that zinc coordination is required when NC unfolds complex secondary structures in RNA and DNA minus- and plus-strand transfer intermediates; this property of NC reflects its nucleic acid chaperone activity. Here we have analyzed the chaperone activities of mutants having substitutions of alternative zinc-coordinating residues, i.e., CC

APA, Harvard, Vancouver, ISO, and other styles

21

Darby, M. K., and K. E. Joho. "Differential binding of zinc fingers from Xenopus TFIIIA and p43 to 5S RNA and the 5S RNA gene." Molecular and Cellular Biology 12, no. 7 (1992): 3155–64. http://dx.doi.org/10.1128/mcb.12.7.3155-3164.1992.

Full text

Abstract:

Zinc fingers are usually associated with proteins that interact with DNA. Yet in two oocyte-specific Xenopus proteins, TFIIA and p43, zinc fingers are used to bind 5S RNA. One of these, TFIIIA, also binds the 5S RNA gene. Both proteins have nine zinc fingers that are nearly identical with respect to size and spacing. We have determined the relative affinities of groups of zinc fingers from TFIIIA for both 5S RNA and the 5S RNA gene. We have also determined the relative affinities of groups of zinc fingers from p43 for 5S RNA. The primary protein regions for RNA and DNA interaction in TFIIIA ar

APA, Harvard, Vancouver, ISO, and other styles

22

Darby, M. K., and K. E. Joho. "Differential binding of zinc fingers from Xenopus TFIIIA and p43 to 5S RNA and the 5S RNA gene." Molecular and Cellular Biology 12, no. 7 (1992): 3155–64. http://dx.doi.org/10.1128/mcb.12.7.3155.

Full text

Abstract:

Zinc fingers are usually associated with proteins that interact with DNA. Yet in two oocyte-specific Xenopus proteins, TFIIA and p43, zinc fingers are used to bind 5S RNA. One of these, TFIIIA, also binds the 5S RNA gene. Both proteins have nine zinc fingers that are nearly identical with respect to size and spacing. We have determined the relative affinities of groups of zinc fingers from TFIIIA for both 5S RNA and the 5S RNA gene. We have also determined the relative affinities of groups of zinc fingers from p43 for 5S RNA. The primary protein regions for RNA and DNA interaction in TFIIIA ar

APA, Harvard, Vancouver, ISO, and other styles

23

Schulz, T. C., B. Hopwood, P. D. Rathjen, and J. R. Wells. "An unusual arrangement of 13 zinc fingers in the vertebrate gene Z13." Biochemical Journal 311, no. 1 (1995): 219–24. http://dx.doi.org/10.1042/bj3110219.

Full text

Abstract:

The zinc finger is a protein domain that imparts specific nucleic acid-binding activity on a wide range of functionally important proteins. In this paper we report the molecular cloning and characterization of a novel murine zinc-finger gene, mZ13. Analysis of mZ13 cDNAs revealed that the gene expresses a 794-amino-acid protein encoded by a 2.7 kb transcript. The protein has an unusual arrangement of 13 zinc fingers into a ‘hand’ of 12 tandem fingers and a single isolated finger near the C-terminus. This structural organization is conserved with the probable chicken homologue, cZ13. mZ13 also

APA, Harvard, Vancouver, ISO, and other styles

24

Shastry, B. S. "Transcription factor IIIA (TFIIIA) in the second decade." Journal of Cell Science 109, no. 3 (1996): 535–39. http://dx.doi.org/10.1242/jcs.109.3.535.

Full text

Abstract:

Transcription factor IIIA is a very extensively studied eukaryotic gene specific factor. It is a special member of the zinc finger family of nucleic acid binding proteins with multiple functions. Its N-terminal polypeptide (280 amino acid residue containing peptide; finger containing region) carries out sequence specific DNA and RNA binding and the C-terminal peptide (65 amino acid residue containing peptide; non-finger region) is involved in the transactivation process possibly by interacting with other general factors. It is a unique factor in the sense that it binds to two structurally diff

APA, Harvard, Vancouver, ISO, and other styles

25

Weitzman, Jonathan B. "Designer zinc-fingers." Genome Biology 3 (2002): spotlight—20021111–02. http://dx.doi.org/10.1186/gb-spotlight-20021111-02.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Kaminski, Joseph, and James Bradley Summers. "Delivering zinc fingers." Nature Biotechnology 21, no. 5 (2003): 492–93. http://dx.doi.org/10.1038/nbt0503-492b.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Blobel, G. A., M. C. Simon, and S. H. Orkin. "Rescue of GATA-1-deficient embryonic stem cells by heterologous GATA-binding proteins." Molecular and Cellular Biology 15, no. 2 (1995): 626–33. http://dx.doi.org/10.1128/mcb.15.2.626.

Full text

Abstract:

Totipotent murine embryonic stem (ES) cells can be differentiated in vitro to form embryoid bodies (EBs) containing hematopoietic cells of multiple lineages, including erythroid cells. In vitro erythroid development parallels that which is observed in vivo. ES cells in which the gene for the erythroid transcription factor GATA-1 has been disrupted fail to produce mature erythroid cells either in vivo or in vitro. With the EB in vitro differentiation assay, constructs expressing heterologous GATA-binding proteins were tested for their abilities to correct the developmental defect of GATA-1-defi

APA, Harvard, Vancouver, ISO, and other styles

28

Guo, Jianhui, Tiyun Wu, Jada Anderson, et al. "Zinc Finger Structures in the Human Immunodeficiency Virus Type 1 Nucleocapsid Protein Facilitate Efficient Minus- and Plus-Strand Transfer." Journal of Virology 74, no. 19 (2000): 8980–88. http://dx.doi.org/10.1128/jvi.74.19.8980-8988.2000.

Full text

Abstract:

ABSTRACT The nucleocapsid protein (NC) of human immunodeficiency virus type 1 (HIV-1) has two zinc fingers, each containing the invariant metal ion binding residues CCHC. Recent reports indicate that mutations in the CCHC motifs are deleterious for reverse transcription in vivo. To identify reverse transcriptase (RT) reactions affected by such changes, we have probed zinc finger functions in NC-dependent RT-catalyzed HIV-1 minus- and plus-strand transfer model systems. Our approach was to examine the activities of wild-type NC and a mutant in which all six cysteine residues were replaced by se

APA, Harvard, Vancouver, ISO, and other styles

29

Turpin, JA, CA Schaeffer, SJ Terpening, L. Graham, M. Bu, and WG Rice. "Reverse Transcription of Human Immunodeficiency Virus Type 1 is Blocked by Retroviral Zinc Finger Inhibitors." Antiviral Chemistry and Chemotherapy 8, no. 1 (1997): 60–69. http://dx.doi.org/10.1177/095632029700800107.

Full text

Abstract:

The Cys-Xaa2-Cys-Xaa4-His-Xaa4-Cys zinc fingers of retroviral nucleocapsid (NC) proteins are prime antiviral targets due to conservation of the Cys and His chelating residues and the absolute requirement of these fingers in both early and late phases of retroviral replication. Certain 2,2′-dithiobisbenzamides (DIBAs) chemically modify the Cys residues of the fingers, thereby inhibiting in vitro replication of human immunodeficiency virus type 1 (HIV-1). We examined the consequences of DIBA interaction with cell-free virions and their subsequent ability to initiate new rounds of infection. The

APA, Harvard, Vancouver, ISO, and other styles

30

Belczyk-Ciesielska, Agnieszka, Brigitta Csipak, Bálint Hajdu, et al. "Nickel(ii)-promoted specific hydrolysis of zinc finger proteins." Metallomics 10, no. 8 (2018): 1089–98. http://dx.doi.org/10.1039/c8mt00098k.

Full text

Abstract:

The (S/T)XH sequence in Cys<sub>2</sub>His<sub>2</sub>zinc fingers can be hydrolytically cleaved by Ni(ii) ions. This reaction can be applied for purification, inhibition or activation of designed zinc finger fusion proteins.

APA, Harvard, Vancouver, ISO, and other styles

31

Gianfrancesco, Olympia, Bethany Geary, Abigail L. Savage, Kimberley J. Billingsley, Vivien J. Bubb, and John P. Quinn. "The Role of SINE-VNTR-Alu (SVA) Retrotransposons in Shaping the Human Genome." International Journal of Molecular Sciences 20, no. 23 (2019): 5977. http://dx.doi.org/10.3390/ijms20235977.

Full text

Abstract:

Retrotransposons can alter the regulation of genes both transcriptionally and post-transcriptionally, through mechanisms such as binding transcription factors and alternative splicing of transcripts. SINE-VNTR-Alu (SVA) retrotransposons are the most recently evolved class of retrotransposable elements, found solely in primates, including humans. SVAs are preferentially found at genic, high GC loci, and have been termed “mobile CpG islands”. We hypothesise that the ability of SVAs to mobilise, and their non-random distribution across the genome, may result in differential regulation of certain

APA, Harvard, Vancouver, ISO, and other styles

32

Kaiming, Cao, Yaping Sheng, Shihui Zheng, Siming Yuan, Guangming Huang, and Yangzhong Liu. "Arsenic trioxide preferentially binds to the ring finger protein PML: understanding target selection of the drug." Metallomics 10, no. 11 (2018): 1564–69. http://dx.doi.org/10.1039/c8mt00202a.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Kim, J. G., and L. D. Hudson. "Novel member of the zinc finger superfamily: A C2-HC finger that recognizes a glia-specific gene." Molecular and Cellular Biology 12, no. 12 (1992): 5632–39. http://dx.doi.org/10.1128/mcb.12.12.5632-5639.1992.

Full text

Abstract:

A novel member of the zinc finger superfamily was cloned by virtue of its binding to cis-regulatory elements of a glia-specific gene, the myelin proteolipid protein (PLP) gene. Named MyTI (myelin transcription factor I), this gene is most highly transcribed in the developing nervous system, where expression precedes induction of its presumptive target, PLP. Low levels of MyTI transcripts can be detected in nonneural tissues only by polymerase chain reaction analysis. Zinc is a necessary cofactor for DNA binding of MyTI, as the zinc-chelating agent 1,10-orthophenanthroline eliminates binding ac

APA, Harvard, Vancouver, ISO, and other styles

34

Kim, J. G., and L. D. Hudson. "Novel member of the zinc finger superfamily: A C2-HC finger that recognizes a glia-specific gene." Molecular and Cellular Biology 12, no. 12 (1992): 5632–39. http://dx.doi.org/10.1128/mcb.12.12.5632.

Full text

Abstract:

A novel member of the zinc finger superfamily was cloned by virtue of its binding to cis-regulatory elements of a glia-specific gene, the myelin proteolipid protein (PLP) gene. Named MyTI (myelin transcription factor I), this gene is most highly transcribed in the developing nervous system, where expression precedes induction of its presumptive target, PLP. Low levels of MyTI transcripts can be detected in nonneural tissues only by polymerase chain reaction analysis. Zinc is a necessary cofactor for DNA binding of MyTI, as the zinc-chelating agent 1,10-orthophenanthroline eliminates binding ac

APA, Harvard, Vancouver, ISO, and other styles

35

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

36

Hoffmann, Anke, Elisabetta Ciani, Joel Boeckardt, Florian Holsboer, Laurent Journot, and Dietmar Spengler. "Transcriptional Activities of the Zinc Finger Protein Zac Are Differentially Controlled by DNA Binding." Molecular and Cellular Biology 23, no. 3 (2003): 988–1003. http://dx.doi.org/10.1128/mcb.23.3.988-1003.2003.

Full text

Abstract:

ABSTRACT Zac encodes a zinc finger protein that promotes apoptosis and cell cycle arrest and is maternally imprinted. Here, we show that Zac contains transactivation and repressor activities and that these transcriptional activities are differentially controlled by DNA binding. Zac transactivation mapped to two distinct domains. One of these contained multiple repeats of the peptide PLE, which behaved as an autonomous activation unit. More importantly, we identified two related high-affinity DNA-binding sites which were differentially bound by seven Zac C2H2 zinc fingers. Zac bound as a monome

APA, Harvard, Vancouver, ISO, and other styles

37

Hu, Shao Wei, Meng Zhang, Ling Xue, and Jian Ming Wen. "Regulation Effect of Zinc Fingers and Homeoboxes 2 on Alpha-Fetoprotein in Human Hepatocellular Carcinoma." Gastroenterology Research and Practice 2013 (2013): 1–8. http://dx.doi.org/10.1155/2013/101083.

Full text

Abstract:

Aim. To investigate the relationship between alpha-fetoprotein and zinc fingers and homeoboxes 2 in hepatocellular carcinoma.Materials and Methods. The expressions of zinc fingers and homeoboxes 2, nuclear factor-YA, and alpha-fetoprotein mRNA in 63 hepatocellular carcinoma were detected by reverse transcriptase-polymerase chain reaction and compared with the clinical parameters of the patients. Selectively, silence of zinc fingers and homeoboxes 2 in HepG2 cells was detected by RNA interference technique.Results. Alpha-fetoprotein mRNA expression was detected in 60.3% of hepatocellular carcin

APA, Harvard, Vancouver, ISO, and other styles

38

Hoffmann, Anke, Thomas Barz, and Dietmar Spengler. "Multitasking C2H2 Zinc Fingers Link Zac DNA Binding to Coordinated Regulation of p300-Histone Acetyltransferase Activity." Molecular and Cellular Biology 26, no. 14 (2006): 5544–57. http://dx.doi.org/10.1128/mcb.02270-05.

Full text

Abstract:

ABSTRACT Zac is a C2H2 zinc finger protein that regulates apoptosis and cell cycle arrest through DNA binding and transactivation. The coactivator proteins p300/CBP enhance transactivation through their histone acetyltransferase (HAT) activity by modulating chromatin structure. Here, we show that p300 increases Zac transactivation in a strictly HAT-dependent manner. Whereas the classic recruitment model proposes that coactivation simply depends on the capacity of the activator to recruit the coactivator, we demonstrate that coordinated binding of Zac zinc fingers and C terminus to p300 regulat

APA, Harvard, Vancouver, ISO, and other styles

39

Watson, James A., Raphaël Pantier, Uma Jayachandran, et al. "Structure of SALL4 zinc finger domain reveals link between AT-rich DNA binding and Okihiro syndrome." Life Science Alliance 6, no. 3 (2023): e202201588. http://dx.doi.org/10.26508/lsa.202201588.

Full text

Abstract:

Spalt-like 4 (SALL4) maintains vertebrate embryonic stem cell identity and is required for the development of multiple organs, including limbs. Mutations in SALL4 are associated with Okihiro syndrome, and SALL4 is also a known target of thalidomide. SALL4 protein has a distinct preference for AT-rich sequences, recognised by a pair of zinc fingers at the C-terminus. However, unlike many characterised zinc finger proteins, SALL4 shows flexible recognition with many different combinations of AT-rich sequences being targeted. SALL4 interacts with the NuRD corepressor complex which potentially med

APA, Harvard, Vancouver, ISO, and other styles

40

Hart, Marilyn C., Lei Wang, and Douglas E. Coulter. "Comparison of the Structure and Expression of odd-skipped and Two Related Genes That Encode a New Family of Zinc Finger Proteins in Drosophila." Genetics 144, no. 1 (1996): 171–82. http://dx.doi.org/10.1093/genetics/144.1.171.

Full text

Abstract:

Abstract The odd-skipped (odd) gene, which was identified on the basis of a pair-rule segmentation phenotype in mutant embryos, is initially expressed in the Drosophila embryo in seven pair-rule stripes, but later exhibits a segment polarity-like pattern for which no phenotypic correlate is apparent. We have molecularly characterized two embryonically expressed odd-cognate genes, sob and bowel (bowl), that encode proteins with highly conserved C2H2 zinc fingers. While the Sob and Bowl proteins each contain five tandem fingers, the Odd protein lacks a fifth (C-terminal) finger and is also less

APA, Harvard, Vancouver, ISO, and other styles

41

Fu, Fengli, and Daniel F. Voytas. "Zinc Finger Database (ZiFDB) v2.0: a comprehensive database of C2H2 zinc fingers and engineered zinc finger arrays." Nucleic Acids Research 41, no. D1 (2012): D452—D455. http://dx.doi.org/10.1093/nar/gks1167.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Fu, F., J. D. Sander, M. Maeder, et al. "Zinc Finger Database (ZiFDB): a repository for information on C2H2 zinc fingers and engineered zinc-finger arrays." Nucleic Acids Research 37, Database (2009): D279—D283. http://dx.doi.org/10.1093/nar/gkn606.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Klug, Aaron. "The discovery of zinc fingers and their development for practical applications in gene regulation and genome manipulation." Quarterly Reviews of Biophysics 43, no. 1 (2010): 1–21. http://dx.doi.org/10.1017/s0033583510000089.

Full text

Abstract:

AbstractA long-standing goal of molecular biologists has been to construct DNA-binding proteins for the control of gene expression. The classical Cys2His2 (C2H2) zinc finger design is ideally suited for such purposes. Discriminating between closely related DNA sequences both in vitro and in vivo, this naturally occurring design was adopted for engineering zinc finger proteins (ZFPs) to target genes specifically.Zinc fingers were discovered in 1985, arising from the interpretation of our biochemical studies on the interaction of the Xenopus protein transcription factor IIIA (TFIIIA) with 5S RNA

APA, Harvard, Vancouver, ISO, and other styles

44

Rice, W. G., D. C. Baker, C. A. Schaeffer, et al. "Inhibition of multiple phases of human immunodeficiency virus type 1 replication by a dithiane compound that attacks the conserved zinc fingers of retroviral nucleocapsid proteins." Antimicrobial Agents and Chemotherapy 41, no. 2 (1997): 419–26. http://dx.doi.org/10.1128/aac.41.2.419.

Full text

Abstract:

The human immunodeficiency virus type 1 (HIV-1) nucleocapsid p7 protein contains two retrovirus-type zinc finger domains that are required for multiple phases of viral replication. Chelating residues (three Cys residues and one His residue) of the domains are absolutely conserved among all strains of HIV-1 and other retroviruses, and mutations in these residues in noninfectious virions. These properties establish the zinc finger domains as logical targets for antiviral chemotherapy. Selected dithiobis benzamide (R-SS-R) compounds were previously found to inhibit HIV-1 replication by mediating

APA, Harvard, Vancouver, ISO, and other styles

45

Porteus, Matthew H. "Zinc fingers on target." Nature 459, no. 7245 (2009): 337–38. http://dx.doi.org/10.1038/459337a.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Meadows, Lisa. "Zinc fingers and chips." Trends in Genetics 17, no. 10 (2001): 563. http://dx.doi.org/10.1016/s0168-9525(01)02500-8.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

GAMSJAEGER, R., C. LIEW, F. LOUGHLIN, M. CROSSLEY, and J. MACKAY. "Sticky fingers: zinc-fingers as protein-recognition motifs." Trends in Biochemical Sciences 32, no. 2 (2007): 63–70. http://dx.doi.org/10.1016/j.tibs.2006.12.007.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Vrana, K. E., M. E. Churchill, T. D. Tullius, and D. D. Brown. "Mapping functional regions of transcription factor TFIIIA." Molecular and Cellular Biology 8, no. 4 (1988): 1684–96. http://dx.doi.org/10.1128/mcb.8.4.1684-1696.1988.

Full text

Abstract:

Functional deletion mutants of the trans-acting factor TFIIIA, truncated at both ends of the molecule, have been expressed by in vitro transcription of a cDNA clone and subsequent cell-free translation of the synthetic mRNAs. A region of TFIIIA 19 amino acids or less, near the carboxyl terminus, is critical for maximal transcription and lies outside the DNA-binding domain. The elongated protein can be aligned over the internal control region (ICR) of the Xenopus 5S RNA gene with its carboxyl terminus oriented toward the 5' end of the gene and its amino terminus oriented toward the 3' end of th

APA, Harvard, Vancouver, ISO, and other styles

49

Vrana, K. E., M. E. Churchill, T. D. Tullius, and D. D. Brown. "Mapping functional regions of transcription factor TFIIIA." Molecular and Cellular Biology 8, no. 4 (1988): 1684–96. http://dx.doi.org/10.1128/mcb.8.4.1684.

Full text

Abstract:

Functional deletion mutants of the trans-acting factor TFIIIA, truncated at both ends of the molecule, have been expressed by in vitro transcription of a cDNA clone and subsequent cell-free translation of the synthetic mRNAs. A region of TFIIIA 19 amino acids or less, near the carboxyl terminus, is critical for maximal transcription and lies outside the DNA-binding domain. The elongated protein can be aligned over the internal control region (ICR) of the Xenopus 5S RNA gene with its carboxyl terminus oriented toward the 5' end of the gene and its amino terminus oriented toward the 3' end of th

APA, Harvard, Vancouver, ISO, and other styles

50

Bredenberg, Johan, and Lennart Nilsson. "Modeling zinc sulfhydryl bonds in zinc fingers." International Journal of Quantum Chemistry 83, no. 3-4 (2001): 230–44. http://dx.doi.org/10.1002/qua.1214.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!