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Journal articles on the topic 'Electrostatic zipper'

Author: Grafiati
Published: 8 March 2025

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1

Kornyshev, A. A., and S. Leikin. "Electrostatic Zipper Motif for DNA Aggregation." Physical Review Letters 82, no. 20 (May 17, 1999): 4138–41. http://dx.doi.org/10.1103/physrevlett.82.4138.

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2

Oliveira, Marcos B., Colin B. Davis, Samuel C. Bradford, Thomas P. Disarro, James A. Smith, and Samuel M. Felton. "Design and characterization of electrostatic zipper hinges." Smart Materials and Structures 28, no. 7 (May 21, 2019): 075002. http://dx.doi.org/10.1088/1361-665x/ab1ab3.

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3

Felder, Jason, Eugene Lee, and Don L. DeVoe. "Large Vertical Displacement Electrostatic Zipper Microstage Actuators." Journal of Microelectromechanical Systems 24, no. 4 (August 2015): 896–903. http://dx.doi.org/10.1109/jmems.2014.2358294.

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4

Sitko, J. C., E. M. Mateescu, and H. G. Hansma. "Sequence-Dependent DNA Condensation and the Electrostatic Zipper." Biophysical Journal 84, no. 1 (January 2003): 419–31. http://dx.doi.org/10.1016/s0006-3495(03)74862-0.

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5

Marti, Daniel N., and Hans Rudolf Bosshard. "Inverse Electrostatic Effect: Electrostatic Repulsion in the Unfolded State Stabilizes a Leucine Zipper†,‡." Biochemistry 43, no. 39 (October 2004): 12436–47. http://dx.doi.org/10.1021/bi048771t.

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6

Lumb, K., and P. Kim. "Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper." Science 268, no. 5209 (April 21, 1995): 436–39. http://dx.doi.org/10.1126/science.7716550.

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7

Lee, Sook, Jon D. Shuman, Tad Guszczynski, Krisada Sakchaisri, Thomas Sebastian, Terry D. Copeland, Maria Miller, et al. "RSK-Mediated Phosphorylation in the C/EBPβ Leucine Zipper Regulates DNA Binding, Dimerization, and Growth Arrest Activity." Molecular and Cellular Biology 30, no. 11 (March 29, 2010): 2621–35. http://dx.doi.org/10.1128/mcb.00782-09.

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ABSTRACT The bZIP transcription factor C/EBPβ is a target of Ras signaling that has been implicated in Ras-induced transformation and oncogene-induced senescence (OIS). To gain insights into Ras-C/EBPβ signaling, we investigated C/EBPβ activation by oncogenic Ras. We show that C/EBPβ DNA binding is autorepressed and becomes activated by the Ras-Raf-MEK-ERK-p90 RSK cascade. Inducible phosphorylation by RSK on Ser273 in the leucine zipper was required for DNA binding. In addition, three other modifications (phosphorylation on Tyr109 [p-Tyr109], p-Ser111, and monomethylation of Arg114 [me-Arg114]) within an N-terminal autoinhibitory domain were important for Ras-induced C/EBPβ activation and cytostatic activity. Apart from its role in DNA binding, Ser273 phosphorylation also creates an interhelical g↔e′ salt bridge with Lys268 that increases attractive electrostatic interactions between paired leucine zippers and promotes homodimerization. Mutating Ser273 to Ala or Lys268 to Glu decreased C/EBPβ homodimer formation, whereas heterodimerization with C/EBPγ was relatively unaffected. The S273A substitution also reduced the antiproliferative activity of C/EBPβ in RasV12-expressing fibroblasts and decreased binding to target cell cycle genes, while a phosphomimetic substitution (S273D) maintained growth arrest function. Our findings identify four novel C/EBPβ-activating modifications, including RSK-mediated phosphorylation of a bifunctional residue in the leucine zipper that regulates DNA binding and homodimerization and thereby promotes cell cycle arrest.
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8

Matousek, William M., Barbara Ciani, Carolyn A. Fitch, Bertrand Garcia-Moreno E., Richard A. Kammerer, and Andrei T. Alexandrescu. "Electrostatic Contributions to the Stability of the GCN4 Leucine Zipper Structure." Journal of Molecular Biology 374, no. 1 (November 2007): 206–19. http://dx.doi.org/10.1016/j.jmb.2007.09.007.

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9

Moll, Jonathan R., Michelle Olive, and Charles Vinson. "Attractive Interhelical Electrostatic Interactions in the Proline- and Acidic-rich Region (PAR) Leucine Zipper Subfamily Preclude Heterodimerization with Other Basic Leucine Zipper Subfamilies." Journal of Biological Chemistry 275, no. 44 (August 14, 2000): 34826–32. http://dx.doi.org/10.1074/jbc.m004545200.

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10

Kohn, Wayne D., Cyril M. Kay, and Robert S. Hodges. "Protein destabilization by electrostatic repulsions in the two-stranded α-helical coiled-coil/leucine zipper." Protein Science 4, no. 2 (December 31, 2008): 237–50. http://dx.doi.org/10.1002/pro.5560040210.

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11

Hendsch, Zachary S., and Bruce Tidor. "Electrostatic interactions in the GCN4 leucine zipper: Substantial contributions arise from intramolecular interactions enhanced on binding." Protein Science 8, no. 7 (1999): 1381–92. http://dx.doi.org/10.1110/ps.8.7.1381.

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12

Kumar, Sandeep, and Ruth Nussinov. "Fluctuations between stabilizing and destabilizing electrostatic contributions of ion pairs in conformers of the c-Myc-Max leucine zipper." Proteins: Structure, Function, and Genetics 41, no. 4 (2000): 485–97. http://dx.doi.org/10.1002/1097-0134(20001201)41:4<485::aid-prot60>3.0.co;2-e.

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13

Dürr, Eberhard, Ilian Jelesarov, and Hans Rudolf Bosshard. "Extremely Fast Folding of a Very Stable Leucine Zipper with a Strengthened Hydrophobic Core and Lacking Electrostatic Interactions between Helices†." Biochemistry 38, no. 3 (January 1999): 870–80. http://dx.doi.org/10.1021/bi981891e.

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14

Lai, Ying, Xiaochu Lou, Yongseok Jho, Tae-Young Yoon, and Yeon-Kyun Shin. "The synaptotagmin 1 linker may function as an electrostatic zipper that opens for docking but closes for fusion pore opening." Biochemical Journal 456, no. 1 (October 24, 2013): 25–33. http://dx.doi.org/10.1042/bj20130949.

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We used the single-vesicle-fusion assay to dissect the function of the Syt1 linker region, and our results suggest that the Syt1 linker region might have some capacity to extend for docking and fold to facilitate pore opening.
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15

Harvey, S. C. "Zippier zaps: faster electrostatics calculations." Biophysical Journal 65, no. 1 (July 1993): 19–20. http://dx.doi.org/10.1016/s0006-3495(93)81029-4.

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16

McGrath, Kevin P., Michelle M. Butler, Carla M. DiGirolamo, David L. Kaplan, Wendy A. Petka, and Thomas M. Laue. "Electrostatic Interactions in Leucine Zippers: Effects on Stability and Specificity of Interaction." Journal of Bioactive and Compatible Polymers 15, no. 4 (July 2000): 334–56. http://dx.doi.org/10.1177/088391150001500405.

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17

MCGRATH, KEVIN P., MICHELLE M. BUTLER, CARLA M. DIGIROLAMO, DAVID L. KAPLAN, WENDY A. PETKA, and THOMAS M. LAUE. "Electrostatic Interactions in Leucine Zippers: Effects on Stability and Specificity of Interaction." Journal of Bioactive and Compatible Polymers 15, no. 4 (July 1, 2000): 334–56. http://dx.doi.org/10.1106/3dma-hcuv-bqd8-un1p.

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18

Marti, Daniel N., and Hans Rudolf Bosshard. "Electrostatic Interactions in Leucine Zippers: Thermodynamic Analysis of the Contributions of Glu and His Residues and the Effect of Mutating Salt Bridges." Journal of Molecular Biology 330, no. 3 (July 2003): 621–37. http://dx.doi.org/10.1016/s0022-2836(03)00623-5.

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19

Lavigne, Pierre, Leslie H. Kondejewski, Michael E. Houston Jr, Frank D. Sönnichsen, Bruce Lix, Brian D. Sykes, Robert S. Hodges, and Cyril M. Kay. "Preferential Heterodimeric Parallel Coiled-coil Formation by Synthetic Max and c-Myc Leucine Zippers: A Description of Putative Electrostatic Interactions Responsible for the Specificity of Heterodimerization." Journal of Molecular Biology 254, no. 3 (December 1995): 505–20. http://dx.doi.org/10.1006/jmbi.1995.0634.

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20

Akerson, Andrew, and Tianshu Liu. "Mechanics, modeling, and shape optimization of electrostatic zipper actuators." Journal of the Mechanics and Physics of Solids, October 2023, 105446. http://dx.doi.org/10.1016/j.jmps.2023.105446.

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21

Alcock, Felicity, Merel PM Damen, Jesper Levring, and Ben C. Berks. "In vivo experiments do not support the charge zipper model for Tat translocase assembly." eLife 6 (August 31, 2017). http://dx.doi.org/10.7554/elife.30127.

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The twin-arginine translocase (Tat) transports folded proteins across the bacterial cytoplasmic membrane and the plant thylakoid membrane. The Tat translocation site is formed by substrate-triggered oligomerization of the protein TatA. Walther and co-workers have proposed a structural model for the TatA oligomer in which TatA monomers self-assemble using electrostatic ‘charge zippers’ (Cell (2013) 132: 15945). This model was supported by in vitro analysis of the oligomeric state of TatA variants containing charge-inverting substitutions. Here we have used live cell assays of TatA assembly and function in Escherichia coli to re-assess the roles of the charged residues of TatA. Our results do not support the charge zipper model. Instead, we observe that substitutions of charged residues located in the TatA amphipathic helix lock TatA in an assembled state, suggesting that these charged residues play a critical role in the protein translocation step that follows TatA assembly.
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22

Bdira, Fredj Ben, Amanda M. Erkelens, Liang Qin, Alexander N. Volkov, Andrew M. Lippa, Nicholas Bowring, Aimee L. Boyle, Marcellus Ubbink, Simon L. Dove, and Remus T. Dame. "Novel anti-repression mechanism of H-NS proteins by a phage protein." Nucleic Acids Research, September 14, 2021. http://dx.doi.org/10.1093/nar/gkab793.

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Abstract H-NS family proteins, bacterial xenogeneic silencers, play central roles in genome organization and in the regulation of foreign genes. It is thought that gene repression is directly dependent on the DNA binding modes of H-NS family proteins. These proteins form lateral protofilaments along DNA. Under specific environmental conditions they switch to bridging two DNA duplexes. This switching is a direct effect of environmental conditions on electrostatic interactions between the oppositely charged DNA binding and N-terminal domains of H-NS proteins. The Pseudomonas lytic phage LUZ24 encodes the protein gp4, which modulates the DNA binding and function of the H-NS family protein MvaT of Pseudomonas aeruginosa. However, the mechanism by which gp4 affects MvaT activity remains elusive. In this study, we show that gp4 specifically interferes with the formation and stability of the bridged MvaT–DNA complex. Structural investigations suggest that gp4 acts as an ‘electrostatic zipper’ between the oppositely charged domains of MvaT protomers, and stabilizes a structure resembling their ‘half-open’ conformation, resulting in relief of gene silencing and adverse effects on P. aeruginosa growth. The ability to control H-NS conformation and thereby its impact on global gene regulation and growth might open new avenues to fight Pseudomonas multidrug resistance.
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23

Xia, Ji, Qifeng Qiao, Haoyang Sun, Yongjun Huang, Fook Siong Chau, and Guangya Zhou. "Ultrasensitive nanoscale optomechanical electrometer using photonic crystal cavities." Nanophotonics, March 21, 2022. http://dx.doi.org/10.1515/nanoph-2021-0820.

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Abstract High-precision detection of electric charge is critical for physical, chemical, and biological measurements. Nanophotonic optomechanical system confines the optical field at the nanoscale and enables a strong interaction between optical cavity and mechanical resonator. Its high optical quality factor cavity and strong optomechanical coupling are promising for precision sensing applications. Here an integrated optomechanical electrometer is proposed for the electric charge sensing using a zipper cavity with a suspended photonic crystal nanobeam (PCN) acting as a movable mechanical resonator. As the electrostatic force arising from the electric voltage to be measured interacts with the mechanical motion of the movable PCN and modulates its resonance through electrostatic stiffening effect, optomechanical coupling transduces the mechanical motion to the optical field with enhanced sensitivity. The resonance shift of the mechanical resonator can be monitored to detect the electric voltage with a sensitivity of 0.007 Hz / m V 2 $\mathrm{Hz}/\mathrm{m}{\mathrm{V}}^{2}$ . Moreover, the sensing performance can be further enhanced with the operation of the optomechanical electrometer in the self-sustained oscillation above threshold power. Owing to the narrow-linewidth of detector radio frequency (RF) spectrum with a large peak-to-noise floor ratio (up to 73.5 dB), the enhanced electrical sensitivity of 0.014 Hz / m V 2 $\mathrm{Hz}/\mathrm{m}{\mathrm{V}}^{2}$ is achieved with a high resolution of 1.37 m V 2 H z − 1 / 2 $1.37\,\mathrm{m}{\mathrm{V}}^{2}\mathrm{H}{\mathrm{z}}^{-1/2}$ . A theoretical minimal detectable electrostatic charge is calculated as 1.33 × 10 − 2 eH z − 1 / 2 $1.33{\times}{10}^{-2}\,\mathrm{eH}{\mathrm{z}}^{-1/2}$ by converting the measured electric voltage versus RF shift to an approximatively linear relationship. This on-chip optomechanical electrometry scheme provides a powerful solution to the ultrasensitive determination of charged nanoparticles in biological and chemical applications.
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24

Hsieh, Yi‐Yen, Yu‐Chun Chuang, and Hsing‐Yu Tuan. "Unraveling Dual Mechanisms in Quasi‐Layered Bi2O2Se via Defect Modulation for High‐Performance Aqueous Zn‐Ion Batteries." Advanced Functional Materials, June 12, 2024. http://dx.doi.org/10.1002/adfm.202406975.

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AbstractDeveloping cathode materials for aqueous zinc‐ion batteries (ZIBs) that offer high capacity, rapid charge–discharge rates, and prolonged cycle life remains a significant challenge. This study explores the use of zipper‐type Bi2O2Se nanoplates modified by selenium vacancy (Vse) modulation, which reduces electron scattering, enhances carrier mobility in [Bi2O2] conducting channels, and decreases coulombic interactions within electrostatic layers. The introduction of Se vacancies facilitates electron transfer from the host to [Bi2O2] channels and reduces scattering in the [Bi2O2] framework, thus improving carrier mobility. These Se‐poor Bi2O2Se nanoplates demonstrate a greater affinity for zinc ions, reduced diffusion barriers, and faster transport kinetics, which enable more efficient Zn‐ion insertion, tripling the electrochemical capacity, improving rate capabilities, and extending cycling life. Enhancements such as reinforced structural integrity and expanded interlayer spaces support a dual Zn‐ion‐driven mechanism involving both insertion and conversion reactions, essential for superior electrochemical storage performance. The results include an impressive discharge/charge capacity of 380.3 mA h g−1 at 0.1 A g−1, a cycle life of up to 10 000 cycles at 5 A g−1, and a current tolerance exceeding 10 A g−1. This research highlights how nano‐ and defect engineering of Bi2O2Se can significantly enhance ionic conductivity, expedite electron transfer, and improve Zn‐ion diffusion.
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25

"Novel Trimethine Cyanine Dye as Potential Amyloid Marker." East European Journal of Physics, no. 4 (2018). http://dx.doi.org/10.26565/2312-4334-2018-4-03.

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The applicability of the novel cyanine dye AK 3-1 to the detection and characterization of pathogenic protein aggregates, amyloid fibrils, was tested using the absorption spectroscopy technique. In an organic solvent dimethyl sulfoxide (DMSO), absorption spectra of AK3-1 exhibits vibrational structure with the relative intensity of 0-0 sub-band being higher than that for the 0-1 sub-band. In an aqueous phase the dye absorption band undergoes hypsochromic shift relative to DMSO due to H-aggregation of the dye. The interaction of AK3-1 with the native and fibrillar insulin was followed by the decrease of monomer band and the enhancement of H-dimer band. To evaluate the relative contributions of the monomeric and aggregated forms, the absorption spectra of the protein-bound dye were deconvoluted using the asymmetric log-normal (LN) function. The analysis of the set of fitting parameters provides evidence for the protein-induced AK3-1 self-association into the head-to-head dimers, with the magnitude of this effect being much more pronounced for fibrillar protein form. The molecular docking studies showed that the AK3-1 monomer tends to associate with the specific arrangement of side chains in the β-sheet formed by L17 leucine residues (of the insulin B-chain), located on the dry steric zipper interface of the fibril, while the dye dimers form stable complexes with the amyloid groove formed by the residues Q15 and E17 of the A-chain, and located on the wet interface of the fibril. The latter binding site is more easily accessible and is additionally stabilized by the electrostatic interactions between the positively charged dye and the E17 residue. This binding mode seems to be prevailing over that for the AK3-1 monomers. Based on the results obtained, AK3-1 may be recommended as a prospective amyloid marker complementary to the classical amyloid reporters Thioflavin T and Congo Red.
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