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Journal articles on the topic 'Three-finger proteins'

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Published: 5 June 2025

Last updated: 2 August 2025

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1

Iuchi, S. "Three classes of C2H2 zinc finger proteins." Cellular and Molecular Life Sciences 58, no. 4 (2001): 625–35. http://dx.doi.org/10.1007/pl00000885.

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2

Smith, Alexander E. F., Farzin Farzaneh, and Kevin G. Ford. "Single zinc-finger extension: enhancing transcriptional activity and specificity of three-zinc-finger proteins." Biological Chemistry 386, no. 2 (2005): 95–99. http://dx.doi.org/10.1515/bc.2005.012.

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AbstractIn order to demonstrate that an existing zinc-finger protein can be simply modified to enhance DNA binding and sequence discrimination in both episomal and chromatin contexts using existing zinc-finger DNA recognition code data, and without recourse to phage display and selection strategies, we have examined the consequences of a single zinc-finger extension to a synthetic three-zinc-finger VP16 fusion protein, on transcriptional activation from model target promoters harbouring the zinc-finger binding sequences. We report a nearly 10-fold enhanced transcriptional activation by the fou

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Hajikhezri, Zamaneh, Mahmoud Darweesh, Göran Akusjärvi, and Tanel Punga. "Role of CCCH-Type Zinc Finger Proteins in Human Adenovirus Infections." Viruses 12, no. 11 (2020): 1322. http://dx.doi.org/10.3390/v12111322.

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The zinc finger proteins make up a significant part of the proteome and perform a huge variety of functions in the cell. The CCCH-type zinc finger proteins have gained attention due to their unusual ability to interact with RNA and thereby control different steps of RNA metabolism. Since virus infections interfere with RNA metabolism, dynamic changes in the CCCH-type zinc finger proteins and virus replication are expected to happen. In the present review, we will discuss how three CCCH-type zinc finger proteins, ZC3H11A, MKRN1, and U2AF1, interfere with human adenovirus replication. We will su

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4

Tsetlin, Victor. "Snake venom alpha-neurotoxins and other 'three-finger' proteins." European Journal of Biochemistry 264, no. 2 (1999): 281–86. http://dx.doi.org/10.1046/j.1432-1327.1999.00623.x.

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5

Paramonov, Alexander S., Mikhail A. Shulepko, Alexey M. Makhonin, et al. "New Three-Finger Protein from Starfish Asteria rubens Shares Structure and Pharmacology with Human Brain Neuromodulator Lynx2." Marine Drugs 20, no. 8 (2022): 503. http://dx.doi.org/10.3390/md20080503.

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Three-finger proteins (TFPs) are small proteins with characteristic three-finger β-structural fold stabilized by the system of conserved disulfide bonds. These proteins have been found in organisms from different taxonomic groups and perform various important regulatory functions or act as components of snake venoms. Recently, four TFPs (Lystars 1–4) with unknown function were identified in the coelomic fluid proteome of starfish A. rubens. Here we analyzed the genomes of A. rubens and A. planci starfishes and predicted additional five and six proteins containing three-finger domains, respecti

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Lyukmanova, Ekaterina N., Maxim L. Bychkov, Andrei M. Chernikov, et al. "In Search of the Role of Three-Finger Starfish Proteins." Marine Drugs 22, no. 11 (2024): 488. http://dx.doi.org/10.3390/md22110488.

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Three-finger proteins (TFPs), or Ly6/uPAR proteins, are characterized by the beta-structural LU domain containing three protruding “fingers” and stabilized by four conserved disulfide bonds. TFPs were initially characterized as snake alpha-neurotoxins, but later many studies showed their regulatory roles in different organisms. Despite a known expression of TFPs in vertebrates, they are poorly studied in other taxa. The presence of TFPs in starfish was previously shown, but their targets and functional role still remain unknown. Here, we analyzed expression, target, and possible function of th

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7

Liu, Mingli, Wenju Li, Xiaoling Zheng, et al. "Genome-Wide Identification and Expression Analysis of the PHD Finger Gene Family in Pea (Pisum sativum)." Plants 13, no. 11 (2024): 1489. http://dx.doi.org/10.3390/plants13111489.

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The plant homeodomain finger (PHD finger) protein, a type of zinc finger protein extensively distributed in eukaryotes, plays diverse roles in regulating plant growth and development. While PHD finger proteins have been identified in various species, their functions remain largely unexplored in pea (Pisum sativum). In this study, we identified 84 members of the PHD finger gene family in pea, which displayed an uneven distribution across seven chromosomes. Through a comprehensive analysis using data from Arabidopsis thaliana and Medicago truncatula, we categorized the PHD finger proteins into 2

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8

CHANG, LONG-SEN. "GENETIC DIVERSITY IN SNAKE VENOM THREE-FINGER PROTEINS AND PHOSPHOLIPASE A2ENZYMES." Toxin Reviews 26, no. 2 (2007): 143–67. http://dx.doi.org/10.1080/15569540701209716.

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Witte, M. M., and R. C. Dickson. "Cysteine residues in the zinc finger and amino acids adjacent to the finger are necessary for DNA binding by the LAC9 regulatory protein of Kluyveromyces lactis." Molecular and Cellular Biology 8, no. 9 (1988): 3726–33. http://dx.doi.org/10.1128/mcb.8.9.3726-3733.1988.

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LAC9 is a positive regulatory protein that controls transcription of the lactose-galactose regulon in Kluyveromyces lactis. LAC9 is homologous to the GAL4 protein of Saccharomyces cerevisiae. Both proteins have a single "zinc finger" which plays a role in DNA binding. We previously hypothesized (L. V. Wray, M. M. Witte, R. C. Dickson, and M. I. Riley, Mol. Cell. Biol. 7:1111-1121, 1987) that the DNA-binding domain of the LAC9 protein consisted of the zinc finger as well as a region of amino acids on the carboxyl-terminal side of the zinc finger. In this study we used oligonucleotide-directed m

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Witte, M. M., and R. C. Dickson. "Cysteine residues in the zinc finger and amino acids adjacent to the finger are necessary for DNA binding by the LAC9 regulatory protein of Kluyveromyces lactis." Molecular and Cellular Biology 8, no. 9 (1988): 3726–33. http://dx.doi.org/10.1128/mcb.8.9.3726.

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LAC9 is a positive regulatory protein that controls transcription of the lactose-galactose regulon in Kluyveromyces lactis. LAC9 is homologous to the GAL4 protein of Saccharomyces cerevisiae. Both proteins have a single "zinc finger" which plays a role in DNA binding. We previously hypothesized (L. V. Wray, M. M. Witte, R. C. Dickson, and M. I. Riley, Mol. Cell. Biol. 7:1111-1121, 1987) that the DNA-binding domain of the LAC9 protein consisted of the zinc finger as well as a region of amino acids on the carboxyl-terminal side of the zinc finger. In this study we used oligonucleotide-directed m

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11

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.

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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

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Hajdu, Bálint, Éva Hunyadi-Gulyás, and Béla Gyurcsik. "Interactions of an Artificial Zinc Finger Protein with Cd(II) and Hg(II): Competition and Metal and DNA Binding." Inorganics 11, no. 2 (2023): 64. http://dx.doi.org/10.3390/inorganics11020064.

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Cys2His2 zinc finger proteins are important for living organisms, as they—among other functions—specifically recognise DNA when Zn(II) is coordinated to the proteins, stabilising their ββα secondary structure. Therefore, competition with other metal ions may alter their original function. Toxic metal ions such as Cd(II) or Hg(II) might be especially dangerous because of their similar chemical properties to Zn(II). Most competition studies carried out so far have involved small zinc finger peptides. Therefore, we have investigated the interactions of toxic metal ions with a zinc finger proteins

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Wang, Qiao, Shangfa Song, Xintong Lu, et al. "Hormone Regulation of CCCH Zinc Finger Proteins in Plants." International Journal of Molecular Sciences 23, no. 22 (2022): 14288. http://dx.doi.org/10.3390/ijms232214288.

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CCCH zinc finger proteins contain one to six tandem CCCH motifs composed of three cysteine and one histidine residues and have been widely found in eukaryotes. Plant CCCH proteins control a wide range of developmental and adaptive processes through DNA–protein, RNA–protein and/or protein–protein interactions. The complex networks underlying these processes regulated by plant CCCH proteins are often involved in phytohormones as signal molecules. In this review, we described the evolution of CCCH proteins from green algae to vascular plants and summarized the functions of plant CCCH proteins tha

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14

Chang, Long-Sen, and Pei-Hsiu Kao. "Origin of Functional Diversities in Taiwan Banded Krait (Bungarus multicinctus) Three-finger Proteins." Fooyin Journal of Health Sciences 1, no. 2 (2009): 57–64. http://dx.doi.org/10.1016/s1877-8607(10)60001-x.

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15

Kini, R. Manjunatha, and Robin Doley. "Structure, function and evolution of three-finger toxins: Mini proteins with multiple targets." Toxicon 56, no. 6 (2010): 855–67. http://dx.doi.org/10.1016/j.toxicon.2010.07.010.

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16

Bach, Christian, William Sherman, Jani Pallis, Prabir Patra, and Hassan Bajwa. "Evaluation of Novel Design Strategies for Developing Zinc Finger Nucleases Tools for Treating Human Diseases." Biotechnology Research International 2014 (April 6, 2014): 1–27. http://dx.doi.org/10.1155/2014/970595.

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Zinc finger nucleases (ZFNs) are associated with cell death and apoptosis by binding at countless undesired locations. This cytotoxicity is associated with the binding ability of engineered zinc finger domains to bind dissimilar DNA sequences with high affinity. In general, binding preferences of transcription factors are associated with significant degenerated diversity and complexity which convolutes the design and engineering of precise DNA binding domains. Evolutionary success of natural zinc finger proteins, however, evinces that nature created specific evolutionary traits and strategies,

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17

Kanakoglou, Dimitrios S., Andromachi Pampalou, Lina S. Malakou, et al. "Central Role of C2H2-Type Zinc Finger-Containing Genes in Pediatric Brain Tumors." DNA 2, no. 1 (2022): 1–21. http://dx.doi.org/10.3390/dna2010001.

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Zinc fingers consist of one of the most abundant motifs in transcription factors and DNA-binding proteins. Recent studies provide evidence on the pathological implication of zinc finger proteins in various neurodevelopmental disorders and malignancies but their role in pediatric brain tumors is largely unexplored. To this end, we investigated the differential expression of zinc finger-containing genes along with relevant biological processes and pathways among four main brain tumor categories (pilocytic astrocytomas, ependymomas, medulloblastomas and glioblastomas). By employing an extended bi

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18

Paramonov, Alexander S., Milita V. Kocharovskaya, Andrey V. Tsarev, et al. "Structural Diversity and Dynamics of Human Three-Finger Proteins Acting on Nicotinic Acetylcholine Receptors." International Journal of Molecular Sciences 21, no. 19 (2020): 7280. http://dx.doi.org/10.3390/ijms21197280.

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Ly-6/uPAR or three-finger proteins (TFPs) contain a disulfide-stabilized β-structural core and three protruding loops (fingers). In mammals, TFPs have been found in epithelium and the nervous, endocrine, reproductive, and immune systems. Here, using heteronuclear NMR, we determined the three-dimensional (3D) structure and backbone dynamics of the epithelial secreted protein SLURP-1 and soluble domains of GPI-anchored TFPs from the brain (Lynx2, Lypd6, Lypd6b) acting on nicotinic acetylcholine receptors (nAChRs). Results were compared with the data about human TFPs Lynx1 and SLURP-2 and snake α

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19

Vasilyeva, N. A., E. V. Loktyushov, M. L. Bychkov, Z. O. Shenkarev, and E. N. Lyukmanova. "Three-finger proteins from the Ly6/uPAR family: Functional diversity within one structural motif." Biochemistry (Moscow) 82, no. 13 (2017): 1702–15. http://dx.doi.org/10.1134/s0006297917130090.

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20

Farias, Leonardo P., Greice Krautz-Peterson, Cibele A. Tararam, et al. "On the Three-Finger Protein Domain Fold and CD59-Like Proteins in Schistosoma mansoni." PLoS Neglected Tropical Diseases 7, no. 10 (2013): e2482. http://dx.doi.org/10.1371/journal.pntd.0002482.

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21

Chaitra, Sarika* and Priyanka Purkayastha. "DIFFERENTIAL STRUCTURAL INTERACTIONS OF THREE-FINGER FAMILY PROTEINS FROM SNAKE VENOMS ON ACETYLCHOLINE RECEPTORS." INTERNATIONAL JOURNAL OF ENGINEERING SCIENCES & RESEARCH TECHNOLOGY 6, no. 11 (2017): 169–76. https://doi.org/10.5281/zenodo.1042106.

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Three-finger toxin (short and long neurotoxins) belongs to a super-family of non-enzymatic proteins found in all families of snakes. They have common three-dimensional structures of three beta-stranded loops extending from a central core containing all four conserved disulphide bonds. Despite the common scaffold, they bind to neuronal and muscle receptors with varying binding affinities and exhibit a wide variety of biological activities. In the present studies, we have mapped the binding site residues on short and long neurotoxins by analyzing the docking models of the proteins with nicotinic

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Meng, Xianwen, Jing Liu, and Mingde Zhao. "Genome-wide identification of RING finger genes in flax (Linum usitatissimum) and analyses of their evolution." PeerJ 9 (November 15, 2021): e12491. http://dx.doi.org/10.7717/peerj.12491.

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Background Flax (Linum usitatissimum) is an important crop for its seed oil and stem fiber. Really Interesting New Gene (RING) finger genes play essential roles in growth, development, and biotic and abiotic stress responses in plants. However, little is known about these genes in flax. Methods Here, we performed a systematic genome-wide analysis to identify RING finger genes in flax. Results We identified 587 RING domains in 574 proteins and classified them into RING-H2 (292), RING-HCa (181), RING-HCb (23), RING-v (53), RING-C2 (31), RING-D (2), RING-S/T (3), and RING-G (2). These proteins we

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23

Martin, David G. E., Kristin Baetz, Xiaobing Shi, et al. "The Yng1p Plant Homeodomain Finger Is a Methyl-Histone Binding Module That Recognizes Lysine 4-Methylated Histone H3." Molecular and Cellular Biology 26, no. 21 (2006): 7871–79. http://dx.doi.org/10.1128/mcb.00573-06.

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ABSTRACT The ING (inhibitor of growth) protein family includes a group of homologous nuclear proteins that share a highly conserved plant homeodomain (PHD) finger domain at their carboxyl termini. Members of this family are found in multiprotein complexes that posttranslationally modify histones, suggesting that these proteins serve a general role in permitting various enzymatic activities to interact with nucleosomes. There are three members of the ING family in Saccharomyces cerevisiae: Yng1p, Yng2p, and Pho23p. Yng1p is a component of the NuA3 histone acetyltransferase complex and is requir

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Jia, Bowei, Yan Wang, Dajian Zhang, et al. "Genome-Wide Identification, Characterization and Expression Analysis of Soybean CHYR Gene Family." International Journal of Molecular Sciences 22, no. 22 (2021): 12192. http://dx.doi.org/10.3390/ijms222212192.

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The CHYR (CHY ZINC-FINGER AND RING FINGER PROTEIN) proteins have been functionally characterized in iron regulation and stress response in Arabidopsis, rice and Populus. However, their roles in soybean have not yet been systematically investigated. Here, in this study, 16 GmCHYR genes with conserved Zinc_ribbon, CHY zinc finger and Ring finger domains were obtained and divided into three groups. Moreover, additional 2–3 hemerythrin domains could be found in the N terminus of Group III. Phylogenetic and homology analysis of CHYRs in green plants indicated that three groups might originate from

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Crosby, S. D., J. J. Puetz, K. S. Simburger, T. J. Fahrner, and J. Milbrandt. "The early response gene NGFI-C encodes a zinc finger transcriptional activator and is a member of the GCGGGGGCG (GSG) element-binding protein family." Molecular and Cellular Biology 11, no. 8 (1991): 3835–41. http://dx.doi.org/10.1128/mcb.11.8.3835-3841.1991.

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We have cloned NGFI-C, a nerve growth factor-induced early-response gene which encodes a Cys2/His2 zinc finger protein. RNA blot analysis demonstrates that NGFI-C mRNA is induced within minutes of stimulation of PC12 cells by nerve growth factor and is similarly activated in brain after a Metrazol-induced seizure. The cDNA sequence predicts a protein that contains three zinc fingers which show striking homology to the DNA-binding regions of three previously reported zinc finger proteins, NGFI-A, Krox-20, and the Wilms' tumor gene product. NGFI-C binds to the previously described DNA-binding si

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Crosby, S. D., J. J. Puetz, K. S. Simburger, T. J. Fahrner, and J. Milbrandt. "The early response gene NGFI-C encodes a zinc finger transcriptional activator and is a member of the GCGGGGGCG (GSG) element-binding protein family." Molecular and Cellular Biology 11, no. 8 (1991): 3835–41. http://dx.doi.org/10.1128/mcb.11.8.3835.

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We have cloned NGFI-C, a nerve growth factor-induced early-response gene which encodes a Cys2/His2 zinc finger protein. RNA blot analysis demonstrates that NGFI-C mRNA is induced within minutes of stimulation of PC12 cells by nerve growth factor and is similarly activated in brain after a Metrazol-induced seizure. The cDNA sequence predicts a protein that contains three zinc fingers which show striking homology to the DNA-binding regions of three previously reported zinc finger proteins, NGFI-A, Krox-20, and the Wilms' tumor gene product. NGFI-C binds to the previously described DNA-binding si

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Üresin, Deniz, Jonathan Schulte, Nina Morgner, and Jörg Soppa. "C(P)XCG Proteins of Haloferax volcanii with Predicted Zinc Finger Domains: the Majority Bind Zinc, but Several Do Not." International Journal of Molecular Sciences 25, no. 13 (2024): 7166. http://dx.doi.org/10.3390/ijms25137166.

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In recent years, interest in very small proteins (µ-proteins) has increased significantly, and they were found to fulfill important functions in all prokaryotic and eukaryotic species. The halophilic archaeon Haloferax volcanii encodes about 400 µ-proteins of less than 70 amino acids, 49 of which contain at least two C(P)XCG motifs and are, thus, predicted zinc finger proteins. The determination of the NMR solution structure of HVO_2753 revealed that only one of two predicted zinc fingers actually bound zinc, while a second one was metal-free. Therefore, the aim of the current study was the ho

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DUBOVSKII, Peter V., Dmitry M. LESOVOY, Maxim A. DUBINNYI, et al. "Interaction of three-finger toxins with phospholipid membranes: comparison of S- and P-type cytotoxins." Biochemical Journal 387, no. 3 (2005): 807–15. http://dx.doi.org/10.1042/bj20041814.

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The CTs (cytotoxins) I and II are positively charged three-finger folded proteins from venom of Naja oxiana (the Central Asian cobra). They belong to S- and P-type respectively based on Ser-28 and Pro-30 residues within a putative phospholipid bilayer binding site. Previously, we investigated the interaction of CTII with multilamellar liposomes of dipalmitoylphosphatidylglycerol by wide-line 31P-NMR spectroscopy. To compare interactions of these proteins with phospholipids, we investigated the interaction of CTI with the multilamellar liposomes of dipalmitoylphosphatidylglycerol analogously. T

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Ouna, Benard Aswani. "Molecular Functions and Potential Utilization of Zinc Finger Proteins in Protozoan Parasites." Extensive Reviews 5, no. 1 (2025): 17–29. https://doi.org/10.21467/exr.5.1.9879.

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Zinc finger proteins (ZFP) are metalloproteins whose zinc atom interacts with side chains of specific histidines and cysteines of the zinc finger motif, generating functional three dimensional structures. A good number of these proteins from different species are similar while others are divergent in structure and function. Existing literature on the structural features, functions of these proteins and their potential to be targeted for drug development or used as molecular tools in parasitic protozoa was explored. Evidence from reviewed articles revealed that, just like in other eukaryotes, t

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Williams, Amy J., Stephen C. Blacklow, and Tucker Collins. "The Zinc Finger-Associated SCAN Box Is a Conserved Oligomerization Domain." Molecular and Cellular Biology 19, no. 12 (1999): 8526–35. http://dx.doi.org/10.1128/mcb.19.12.8526.

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ABSTRACT A number of Cys2His2 zinc finger proteins contain a highly conserved amino-terminal motif termed the SCAN domain. This element is an 80-residue, leucine-rich region that contains three segments strongly predicted to be α-helices. In this report, we show that the SCAN motif functions as an oligomerization domain mediating self-association or association with other proteins bearing SCAN domains. These findings suggest that the SCAN domain plays an important role in the assembly and function of this newly defined subclass of transcriptional regulators.

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Lyukmanova, Ekaterina N., Zakhar O. Shenkarev, Mikhail A. Shulepko, et al. "NMR Structure and Action on Nicotinic Acetylcholine Receptors of Water-soluble Domain of Human LYNX1." Journal of Biological Chemistry 286, no. 12 (2011): 10618–27. http://dx.doi.org/10.1074/jbc.m110.189100.

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Discovery of proteins expressed in the central nervous system sharing the three-finger structure with snake α-neurotoxins provoked much interest to their role in brain functions. Prototoxin LYNX1, having homology both to Ly6 proteins and three-finger neurotoxins, is the first identified member of this family membrane-tethered by a GPI anchor, which considerably complicates in vitro studies. We report for the first time the NMR spatial structure for the water-soluble domain of human LYNX1 lacking a GPI anchor (ws-LYNX1) and its concentration-dependent activity on nicotinic acetylcholine recepto

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Zonneveld, Anton-Jan van, Harry Veerman, Just P. J. Brakenhoff, Lucien A. Aarden, Jean-Francois Cajot, and Hans Pannekoek. "Mapping of Epitopes on Human Tissue-Type Plasminogen Activator with Recombinant Deletion Mutant Proteins." Thrombosis and Haemostasis 57, no. 01 (1987): 082–86. http://dx.doi.org/10.1055/s-0038-1651067.

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SummaryAn antigen assay based on a monoclonal antibody directed against the light chain of tissue-type plasminogen activator (t-PA) was developed to quantify seven recombinant (r) t-PA deletion mutant proteins. These recombinant proteins were then employed to map different epitopes on t-PA which interact with a panel of twenty-three monoclonal anti-t-PA antibodies. Twenty were directed against domains on the heavy chain, two against the “finger” domain, three against the “epidermal growth factor-like” domain, five against the kringle 1 domain, and ten against the kringle 2 domain. Only three m

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Dyba, Barbara, Elżbieta Rudolphi-Szydło, Anna Barbasz, et al. "Effects of 3FTx Protein Fraction from Naja ashei Venom on the Model and Native Membranes: Recognition and Implications for the Mechanisms of Toxicity." Molecules 26, no. 8 (2021): 2164. http://dx.doi.org/10.3390/molecules26082164.

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Three-finger toxins are naturally occurring proteins in Elapidae snake venoms. Nowadays, they are gaining popularity because of their therapeutic potential. On the other hand, these proteins may cause undesirable reactions inside the body′s cells. A full assessment of the safety of Naja ashei venom components for human cell application is still unknown. The aim of the study was to determine the effect of the exogenous application of three-finger toxins on the cells of monocytes (U-937) and promyelocytes (HL-60), with particular emphasis on the modification of their membranes under the influenc

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Fursenko, D. V., P. G. Georgiev, and A. N. Bonchuk. "Study of the N-Terminal Domain Homodimerization in Human Proteins with Zinc Finger Clusters." Doklady Biochemistry and Biophysics 499, no. 1 (2021): 257–59. http://dx.doi.org/10.1134/s1607672921040050.

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Abstract CTCF belongs to a large family of transcription factors with clusters of C2H2-type zinc finger domains (C2H2 proteins) and is a main architectural protein in mammals. Human CTCF has a homodimerizing unstructured domain at the N-terminus which is involved in long-distance interactions. To test the presence of similar N-terminal domains in other human C2H2 proteins, a yeast two-hybrid system was used. In total, the ability of unstructured N-terminal domains to homodimerize was investigated for six human C2H2 proteins with an expression profile similar to CTCF. The data indicate the lack

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Babenko, Vladislav V., Rustam H. Ziganshin, Christoph Weise, et al. "Novel Bradykinin-Potentiating Peptides and Three-Finger Toxins from Viper Venom: Combined NGS Venom Gland Transcriptomics and Quantitative Venom Proteomics of the Azemiops feae Viper." Biomedicines 8, no. 8 (2020): 249. http://dx.doi.org/10.3390/biomedicines8080249.

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Feae’s viper Azemipos feae belongs to the Azemiopinae subfamily of the Viperidae family. The effects of Viperidae venoms are mostly coagulopathic with limited neurotoxicity manifested by phospholipases A2. From A. feae venom, we have earlier isolated azemiopsin, a novel neurotoxin inhibiting the nicotinic acetylcholine receptor. To characterize other A. feae toxins, we applied label-free quantitative proteomics, which revealed 120 unique proteins, the most abundant being serine proteinases and phospholipases A2. In total, toxins representing 14 families were identified, among which bradykinin-

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Sadia Erum Khan, Humera Waheed, and Syed Faraz Moin. "Decomplexation of Venom Proteome of Pakistani Cobra (Naja naja naja)." Proceedings of the Pakistan Academy of Sciences: B. Life and Environmental Sciences 60, no. 1 (2023): 125–31. http://dx.doi.org/10.53560/ppasb(60-1)843.

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The venom proteome of Naja naja from Sindh, Pakistan was decomplexed utilizing reverse phase HPLC and SDS PAGE. The results were compared with already reported Naja naja species of the region. The banding pattern represents all the major families of proteins including three-finger toxins, phospholipase A2, snake venom metalloproteases, L-amino acid oxidases, phosphodiesterase, nucleotidases, cysteine-rich secretory proteins, serine proteases, nerve growth factor, cobra venom factor, acetylcholinesterases, Kunitz-type serine protease inhibitors and C-type lectin proteins. The decomplexation of

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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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Seok, Hye-Yeon, Taehyoung Kim, Sun-Young Lee, and Yong-Hwan Moon. "Non-TZF Transcriptional Activator AtC3H12 Negatively Affects Seed Germination and Seedling Development in Arabidopsis." International Journal of Molecular Sciences 23, no. 3 (2022): 1572. http://dx.doi.org/10.3390/ijms23031572.

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CCCH zinc finger proteins are a large protein family and are classified as either tandem CCCH zinc finger (TZF) or non-TZF proteins. The roles of TZF genes in several plants have been well determined, whereas the functions of many non-TZF genes in plants remain uncharacterized. Herein, we describe biological and molecular functions of AtC3H12, an Arabidopsis non-TZF protein containing three CCCH zinc finger motifs. AtC3H12 has orthologs in several plant species but has no paralog in Arabidopsis. AtC3H12-overexpressing transgenic plants (OXs) germinated slower than wild-type (WT) plants, wherea

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Tsetlin, Victor I. "Three-finger snake neurotoxins and Ly6 proteins targeting nicotinic acetylcholine receptors: pharmacological tools and endogenous modulators." Trends in Pharmacological Sciences 36, no. 2 (2015): 109–23. http://dx.doi.org/10.1016/j.tips.2014.11.003.

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Eroshkin, F. M., N. Y. Martynova, A. V. Bayramov, et al. "Interaction of secreted factor Agr2 with its potential receptors from the family of three-finger proteins." Russian Journal of Bioorganic Chemistry 43, no. 3 (2017): 344–46. http://dx.doi.org/10.1134/s1068162017030049.

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Gulsevin, Alican, and Jens Meiler. "An Investigation of Three-Finger Toxin—nAChR Interactions through Rosetta Protein Docking." Toxins 12, no. 9 (2020): 598. http://dx.doi.org/10.3390/toxins12090598.

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Three-finger toxins (3FTX) are a group of peptides that affect multiple receptor types. One group of proteins affected by 3FTX are nicotinic acetylcholine receptors (nAChR). Structural information on how neurotoxins interact with nAChR is limited and is confined to a small group of neurotoxins. Therefore, in silico methods are valuable in understanding the interactions between 3FTX and different nAChR subtypes, but there are no established protocols to model 3FTX–nAChR interactions. We followed a homology modeling and protein docking protocol to address this issue and tested its success on thr

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Chang, Ching-Jin, Ya-Ling Chen та Sheng-Chung Lee. "Coactivator TIF1β Interacts with Transcription Factor C/EBPβ and Glucocorticoid Receptor To Induce α1-Acid Glycoprotein Gene Expression". Molecular and Cellular Biology 18, № 10 (1998): 5880–87. http://dx.doi.org/10.1128/mcb.18.10.5880.

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ABSTRACT The transcription of the α1-acid glycoprotein gene is induced by inflammatory cytokines and glucocorticoids. C/EBPβ is a major transcription factor involved in the induction of the agpgene by some cytokines. In this report, we have identified a novel transcriptional intermediary factor, TIF1β, which could enhance the transcription of the agp gene by the glucocorticoid receptor (GR) and C/EBPβ. TIF1β belongs to a subgroup of RING (really interesting new gene) finger proteins that contain a RING finger preceding two B box-type fingers and a putative coiled-coil domain (RBCC domain). Imm

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Birot, Adrien, Krzysztof Kus, Emily Priest, et al. "RNA-binding protein Mub1 and the nuclear RNA exosome act to fine-tune environmental stress response." Life Science Alliance 5, no. 2 (2021): e202101111. http://dx.doi.org/10.26508/lsa.202101111.

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The nuclear RNA exosome plays a key role in controlling the levels of multiple protein-coding and non-coding RNAs. Recruitment of the exosome to specific RNA substrates is mediated by RNA-binding co-factors. The transient interaction between co-factors and the exosome as well as the rapid decay of RNA substrates make identification of exosome co-factors challenging. Here, we use comparative poly(A)+ RNA interactome capture in fission yeast expressing three different mutants of the exosome to identify proteins that interact with poly(A)+ RNA in an exosome-dependent manner. Our analyses identify

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Lundin, M., J. O. Nehlin, and H. Ronne. "Importance of a flanking AT-rich region in target site recognition by the GC box-binding zinc finger protein MIG1." Molecular and Cellular Biology 14, no. 3 (1994): 1979–85. http://dx.doi.org/10.1128/mcb.14.3.1979-1985.1994.

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MIG1 is a zinc finger protein that mediates glucose repression in the yeast Saccharomyces cerevisiae. MIG1 is related to the mammalian Krox/Egr, Wilms' tumor, and Sp1 finger proteins. It has two fingers and binds to a GCGGGG motif that resembles the GC boxes recognized by these mammalian proteins. We have performed a complete saturation mutagenesis of a natural MIG1 site in order to elucidate its binding specificity. We found that only three mutations within the GC box retain the ability to bind MIG1: G1 to C, C2 to T, and G5 to A. This result is consistent with current models for zinc finger-

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Lundin, M., J. O. Nehlin, and H. Ronne. "Importance of a flanking AT-rich region in target site recognition by the GC box-binding zinc finger protein MIG1." Molecular and Cellular Biology 14, no. 3 (1994): 1979–85. http://dx.doi.org/10.1128/mcb.14.3.1979.

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MIG1 is a zinc finger protein that mediates glucose repression in the yeast Saccharomyces cerevisiae. MIG1 is related to the mammalian Krox/Egr, Wilms' tumor, and Sp1 finger proteins. It has two fingers and binds to a GCGGGG motif that resembles the GC boxes recognized by these mammalian proteins. We have performed a complete saturation mutagenesis of a natural MIG1 site in order to elucidate its binding specificity. We found that only three mutations within the GC box retain the ability to bind MIG1: G1 to C, C2 to T, and G5 to A. This result is consistent with current models for zinc finger-

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Sala, Claudia, Martina Tarozzi, Giorgia Simonetti, et al. "Impact on the Transcriptome of Proton Beam Irradiation Targeted at Healthy Cardiac Tissue of Mice." Cancers 16, no. 8 (2024): 1471. http://dx.doi.org/10.3390/cancers16081471.

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Proton beam therapy is considered a step forward with respect to electromagnetic radiation, thanks to the reduction in the dose delivered. Among unwanted effects to healthy tissue, cardiovascular complications are a known long-term radiotherapy complication. The transcriptional response of cardiac tissue from xenografted BALB/c nude mice obtained at 3 and 10 days after proton irradiation covering both the tumor region and the underlying healthy tissue was analyzed as a function of dose and time. Three doses were used: 2 Gy, 6 Gy, and 9 Gy. The intermediate dose had caused the greatest impact a

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Bashaw, G. J., and B. S. Baker. "The msl-2 dosage compensation gene of Drosophila encodes a putative DNA-binding protein whose expression is sex specifically regulated by Sex-lethal." Development 121, no. 10 (1995): 3245–58. http://dx.doi.org/10.1242/dev.121.10.3245.

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In Drosophila dosage compensation increases the rate of transcription of the male's X chromosome and depends on four autosomal male-specific lethal genes. We have cloned the msl-2 gene and shown that MSL-2 protein is co-localized with the other three MSL proteins at hundreds of sites along the male polytene X chromosome and that this binding requires the other three MSL proteins. msl-2 encodes a protein with a putative DNA-binding domain: the RING finger. MSL-2 protein is not produced in females and sequences in both the 5′ and 3′ UTRs are important for this sex-specific regulation. Furthermor

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Kinzler, K. W., and B. Vogelstein. "The GLI gene encodes a nuclear protein which binds specific sequences in the human genome." Molecular and Cellular Biology 10, no. 2 (1990): 634–42. http://dx.doi.org/10.1128/mcb.10.2.634-642.1990.

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The GLI gene is amplified in a subset of human tumors and encodes a protein product with five zinc finger DNA-binding motifs. In this study, we show that the GLI gene product has a predominantly nuclear localization and binds DNA in a sequence-specific fashion. Three GLI binding sites were identified by using a novel procedure in which total human DNA was bound to a GLI recombinant fusion protein, and the polymerase chain reaction was used to amplify and recover the bound sequences. The GLI protein protected a 23- to 24-base region within all three binding sites, and the protected region in ea

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Kinzler, K. W., and B. Vogelstein. "The GLI gene encodes a nuclear protein which binds specific sequences in the human genome." Molecular and Cellular Biology 10, no. 2 (1990): 634–42. http://dx.doi.org/10.1128/mcb.10.2.634.

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The GLI gene is amplified in a subset of human tumors and encodes a protein product with five zinc finger DNA-binding motifs. In this study, we show that the GLI gene product has a predominantly nuclear localization and binds DNA in a sequence-specific fashion. Three GLI binding sites were identified by using a novel procedure in which total human DNA was bound to a GLI recombinant fusion protein, and the polymerase chain reaction was used to amplify and recover the bound sequences. The GLI protein protected a 23- to 24-base region within all three binding sites, and the protected region in ea

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Su, Dan, Zhiyong Lou, Fei Sun, et al. "Dodecamer Structure of Severe Acute Respiratory Syndrome Coronavirus Nonstructural Protein nsp10." Journal of Virology 80, no. 16 (2006): 7902–8. http://dx.doi.org/10.1128/jvi.00483-06.

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ABSTRACT The severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural proteins nsp1 to nsp16 have been implicated by genetic analysis in the assembly of a functional replication/transcription complex. We report the crystal structure of nsp10 from SARS-CoV at 2.1-Å resolution. The nsp10 structure has a novel fold, and 12 identical subunits assemble to form a unique spherical dodecameric architecture. Two zinc fingers have been identified from the nsp10 monomer structure with the sequence motifs C-(X)2-C-(X)5-H-(X)6-C and C-(X)2-C-(X)7-C-(X)-C. The nsp10 crystal structure is the f

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