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Journal articles on the topic 'Enzymatically active'

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Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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1

Derkx, Frans H. M., and Maarten A. D. H. Schalekamp. "30. Enzymatically active plasma prorenin." Journal of Hypertension 9, no. 6 (December 1991): S434. http://dx.doi.org/10.1097/00004872-199112000-00221.

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2

Derkx, Frans H. M., and Maarten A. D. H. Schalekamp. "30. Enzymatically active plasma prorenin." Journal of Hypertension 9 (1991): S434. http://dx.doi.org/10.1097/00004872-199112006-00221.

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3

Raaijmakers, Michiel J. T., Thomas Schmidt, Monika Barth, Murat Tutus, Nieck E. Benes, and Matthias Wessling. "Enzymatically Active Ultrathin Pepsin Membranes." Angewandte Chemie 127, no. 20 (March 16, 2015): 6008–12. http://dx.doi.org/10.1002/ange.201411263.

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4

Yu, Aimin, and Zhijian Liang. "Enzymatically active colloidal crystal arrays." Journal of Colloid and Interface Science 330, no. 1 (February 2009): 144–48. http://dx.doi.org/10.1016/j.jcis.2008.10.030.

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5

Raaijmakers, Michiel J. T., Thomas Schmidt, Monika Barth, Murat Tutus, Nieck E. Benes, and Matthias Wessling. "Enzymatically Active Ultrathin Pepsin Membranes." Angewandte Chemie International Edition 54, no. 20 (March 16, 2015): 5910–14. http://dx.doi.org/10.1002/anie.201411263.

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6

Zhang, William H., Graham J. Day, Ioannis Zampetakis, Michele Carrabba, Zhongyang Zhang, Ben M. Carter, Norman Govan, Colin Jackson, Menglin Chen, and Adam W. Perriman. "Three-Dimensional Printable Enzymatically Active Plastics." ACS Applied Polymer Materials 3, no. 12 (November 15, 2021): 6070–77. http://dx.doi.org/10.1021/acsapm.1c00845.

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7

Becker, M., N. Provart, I. Lehmann, M. Ulbricht, and H. G. Hicke. "Polymerization of Glucans by Enzymatically Active Membranes." Biotechnology Progress 18, no. 5 (October 4, 2002): 964–68. http://dx.doi.org/10.1021/bp020013b.

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8

Brumm, Phillip, Spencer Hermanson, Becky Hochstein, Julie Boyum, Nick Hermersmann, Krishne Gowda, and David Mead. "Mining Dictyoglomus turgidum for Enzymatically Active Carbohydrases." Applied Biochemistry and Biotechnology 163, no. 2 (July 16, 2010): 205–14. http://dx.doi.org/10.1007/s12010-010-9029-6.

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9

Müller, Werner E. G., Thorben Link, Heinz C. Schröder, Michael Korzhev, Meik Neufurth, David Brandt, and Xiaohong Wang. "Dissection of the structure-forming activity from the structure-guiding activity of silicatein: a biomimetic molecular approach to print optical fibers." J. Mater. Chem. B 2, no. 33 (2014): 5368–77. http://dx.doi.org/10.1039/c4tb00801d.

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10

Ozdener, Fatih, Satya P. Kunapuli, and James L. Daniel. "Expression of Enzymatically-active Phospholipase Cγ2 in E.coli." BMB Reports 35, no. 5 (September 30, 2002): 508–12. http://dx.doi.org/10.5483/bmbrep.2002.35.5.508.

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11

TATSUMI, Hiroki, Tsutomu MASUDA, and Eiichi NAKANO. "Synthesis of enzymatically active firefly luciferase in yeast." Agricultural and Biological Chemistry 52, no. 5 (1988): 1123–27. http://dx.doi.org/10.1271/bbb1961.52.1123.

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12

Tatsumi, Hiroki, Tsutomu Masuda, and Eiichi Nakano. "Synthesis of Enzymatically Active Firefly Luciferase in Yeast." Agricultural and Biological Chemistry 52, no. 5 (May 1988): 1123–27. http://dx.doi.org/10.1080/00021369.1988.10868837.

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13

Buruaga-Ramiro, Carolina, Susana V. Valenzuela, Cristina Valls, M. Blanca Roncero, F. I. Javier Pastor, Pilar Díaz, and Josefina Martínez. "Bacterial cellulose matrices to develop enzymatically active paper." Cellulose 27, no. 6 (January 31, 2020): 3413–26. http://dx.doi.org/10.1007/s10570-020-03025-9.

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14

Wu, Ping, Lei Zhu, Ulf-Håkan Stenman, and Jari Leinonen. "Immunopeptidometric Assay for Enzymatically Active Prostate-Specific Antigen." Clinical Chemistry 50, no. 1 (January 1, 2004): 125–29. http://dx.doi.org/10.1373/clinchem.2003.026146.

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Abstract Background: Determinations of certain forms of prostate-specific antigen (PSA) have been shown to increase the specificity for prostate cancer (PCa). One such variant, proteolytically active PSA, is a potentially useful tumor marker, but it is not specifically recognized by antibodies. Using phage display libraries, we previously identified a “family” of peptides that bind specifically to active PSA. We used these to develop an immunopeptidometric assay (IPMA) that specifically detects this form of PSA. Methods: Microtitration plates coated with a PSA antibody were used to capture PSA, and a PSA-binding glutathione S-transferase (GST) fusion peptide was used as a tracer. Bound tracer was detected with an antibody to GST labeled with a europium chelate. PSA isoenzymes with high and low enzymatic activity were used to study binding specificity. Results: The IPMA detected enzymatically active PSA but not internally cleaved PSA and pro-PSA, which are enzymatically inactive. The assay detected 1–10% of free PSA in serum from PCa patients. Conclusions: Peptides identified by phage display can be used to develop assays with unique specificities for enzymatically active PSA. IPMA represents a new assay principle with wide potential utility.

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15

Miller, Lisa M., Matthew D. Simmons, Callum D. Silver, Thomas F. Krauss, Gavin H. Thomas, Steven D. Johnson, and Anne-Kathrin Duhme-Klair. "Antibiotic-functionalized gold nanoparticles for the detection of active β-lactamases." Nanoscale Advances 4, no. 2 (2022): 573–81. http://dx.doi.org/10.1039/d1na00635e.

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16

Weirich, Kimberly L., Kinjal Dasbiswas, Thomas A. Witten, Suriyanarayanan Vaikuntanathan, and Margaret L. Gardel. "Self-organizing motors divide active liquid droplets." Proceedings of the National Academy of Sciences 116, no. 23 (May 21, 2019): 11125–30. http://dx.doi.org/10.1073/pnas.1814854116.

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The cytoskeleton is a collection of protein assemblies that dynamically impose spatial structure in cells and coordinate processes such as cell division and mechanical regulation. Biopolymer filaments, cross-linking proteins, and enzymatically active motor proteins collectively self-organize into various precise cytoskeletal assemblies critical for specific biological functions. An outstanding question is how the precise spatial organization arises from the component macromolecules. We develop a system to investigate simple physical mechanisms of self-organization in biological assemblies. Using a minimal set of purified proteins, we create droplets of cross-linked biopolymer filaments. Through the addition of enzymatically active motor proteins, we construct composite assemblies, evocative of cellular structures such as spindles, where the inherent anisotropy drives motor self-organization, droplet deformation, and division into two droplets. These results suggest that simple physical principles underlie self-organization in complex biological assemblies and inform bioinspired materials design.

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17

Schakowski, Kai Melvin, Christian Elm, Jürgen Linders, and Michael Kirsch. "Synthesis and characterization of enzymatically active micrometer protein-capsules." Artificial Cells, Nanomedicine, and Biotechnology 49, no. 1 (January 1, 2021): 606–13. http://dx.doi.org/10.1080/21691401.2021.1955698.

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18

Krepel, C. J., C. M. Gohr, A. P. Walker, S. G. Farmer, and C. E. Edmiston. "Enzymatically active Peptostreptococcus magnus: association with site of infection." Journal of Clinical Microbiology 30, no. 9 (1992): 2330–34. http://dx.doi.org/10.1128/jcm.30.9.2330-2334.1992.

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19

Rickus, Jenna L., Pauline L. Chang, Allan J. Tobin, Jeffrey I. Zink, and Bruce Dunn. "Photochemical Coenzyme Regeneration in an Enzymatically Active Optical Material." Journal of Physical Chemistry B 108, no. 26 (July 2004): 9325–32. http://dx.doi.org/10.1021/jp038051g.

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20

Tanese, N., M. Roth, and S. P. Goff. "Expression of enzymatically active reverse transcriptase in Escherichia coli." Proceedings of the National Academy of Sciences 82, no. 15 (August 1, 1985): 4944–48. http://dx.doi.org/10.1073/pnas.82.15.4944.

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21

North, Brian J., Bjoern Schwer, Nidhi Ahuja, Brett Marshall, and Eric Verdin. "Preparation of enzymatically active recombinant class III protein deacetylases." Methods 36, no. 4 (August 2005): 338–45. http://dx.doi.org/10.1016/j.ymeth.2005.03.004.

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22

Zagalak, B., F. Neuheiser, U. Redweik, R. Bosshard, and W. Leimbacher. "Synthesis of enzymatically active D-7,8-dihydroneopterin-3′-triphosphate." Biochemical and Biophysical Research Communications 152, no. 3 (May 1988): 1193–99. http://dx.doi.org/10.1016/s0006-291x(88)80411-x.

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23

Singh, Sharda P., Ludwika Zimniak, and Piotr Zimniak. "The human hGSTA5 gene encodes an enzymatically active protein." Biochimica et Biophysica Acta (BBA) - General Subjects 1800, no. 1 (January 2010): 16–22. http://dx.doi.org/10.1016/j.bbagen.2009.07.025.

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24

Kumar, Ravinash Krishna, Mei Li, Sam N. Olof, Avinash J. Patil, and Stephen Mann. "Artificial Cytoskeletal Structures Within Enzymatically Active Bio-inorganic Protocells." Small 9, no. 3 (October 2, 2012): 357–62. http://dx.doi.org/10.1002/smll.201201539.

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25

Derr, Ludmilla, Ralf Dringen, Laura Treccani, Nils Hildebrand, Lucio Colombi Ciacchi, and Kurosch Rezwan. "Physisorption of enzymatically active chymotrypsin on titania colloidal particles." Journal of Colloid and Interface Science 455 (October 2015): 236–44. http://dx.doi.org/10.1016/j.jcis.2015.05.022.

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26

McCormick, Sally, Angela Nelson, and William M. Nauseef. "Proconvertase proteolytic processing of an enzymatically active myeloperoxidase precursor." Archives of Biochemistry and Biophysics 527, no. 1 (November 2012): 31–36. http://dx.doi.org/10.1016/j.abb.2012.07.013.

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27

Rindt, H., B. J. Bauer, and J. Robbins. "In vitro production of enzymatically active myosin heavy chain." Journal of Muscle Research and Cell Motility 14, no. 1 (February 1993): 26–34. http://dx.doi.org/10.1007/bf00132177.

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28

Henderson, D. R., S. B. Friedman, J. D. Harris, W. B. Manning, and M. A. Zoccoli. "CEDIA, a new homogeneous immunoassay system." Clinical Chemistry 32, no. 9 (September 1, 1986): 1637–41. http://dx.doi.org/10.1093/clinchem/32.9.1637.

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Abstract Genetic engineering of beta-galactosidase (EC 3.2.1.23) has led to the development of a new homogeneous assay system, CEDIA. The Z gene of the lac operon of Escherichia coli encodes a large enzymatically inactive polypeptide that spontaneously aggregates and folds to form active beta-galactosidase. Using recombinant DNA techniques, we have been able to engineer beta-galactosidase protein into a large polypeptide (an enzyme acceptor, EA) and a small polypeptide (an enzyme donor, ED). The EAs and EDs are both enzymatically inactive, but spontaneously associate to form enzymatically active tetramers. In the assay, hapten or analyte is attached to an ED, and an analyte-specific antibody is used to inhibit the spontaneous assembly of active enzyme. Analyte in a patient's serum competes with the analyte in the analyte-ED conjugate for antibody, modulating the amount of beta-galactosidase formed. The signal generated by enzyme substrates is directly proportional to the analyte concentrations in the patient's serum. We describe quick (5-15 min) colorimetric tests for digoxin, requiring no serum pretreatments or predilutions and suitable for use with centrifugal and random-access analyzers.

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29

Ma, Yongsheng, Amy E. Bryant, Dan B. Salmi, Susan M. Hayes-Schroer, Eric McIndoo, Michael J. Aldape, and Dennis L. Stevens. "Identification and Characterization of Bicistronic speB and prsA Gene Expression in the Group A Streptococcus." Journal of Bacteriology 188, no. 21 (September 1, 2006): 7626–34. http://dx.doi.org/10.1128/jb.01059-06.

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ABSTRACT Severe, invasive group A streptococcal infections have reemerged worldwide, and extracellular toxins, including streptococcal pyrogenic exotoxin B (SpeB), have been implicated in pathogenesis. The genetic regulation of SpeB is not fully understood, and the mechanisms involved in the processing of the protoxin to its enzymatically active form have not been definitively established. The present work demonstrated that the genes encoding SpeB (speB) and a peptidyl-prolyl isomerase (prsA) constitute an operon with transcription initiated from two promoters upstream of speB. Further, the speB-prsA operon was transcribed as a bicistronic mRNA. This finding is in contrast to the generally accepted notion that speB is transcribed only as a monocistronic gene. In addition, prsA has its own promoter, and transcription from this promoter starts in early log phase, prior to the transcription of speB. Genomic disruption of prsA decreased the production of enzymatically active SpeB but not the level of the pro-SpeB zymogen. Taken together, these results demonstrate that prsA is required for production of fully mature, enzymatically active SpeB.

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30

Mariconti, Marina, Mathieu Morel, Damien Baigl, and Sergii Rudiuk. "Enzymatically Active DNA-Protein Nanogels with Tunable Cross-Linking Density." Biomacromolecules 22, no. 8 (July 14, 2021): 3431–39. http://dx.doi.org/10.1021/acs.biomac.1c00501.

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31

Kus, Nicole J., Monika B. Dolinska, Kenneth L. Young, Emilios K. Dimitriadis, Paul T. Wingfield, and Yuri V. Sergeev. "Membrane-associated human tyrosinase is an enzymatically active monomeric glycoprotein." PLOS ONE 13, no. 6 (June 5, 2018): e0198247. http://dx.doi.org/10.1371/journal.pone.0198247.

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32

VERONESE, FRANCESCO M., ODDONE SCHIAVON ENVIRO BOCCÙ, CARLO A. BENASSI, and ANGELO FONTANA. "Enzymatically active subunits of Bacillus stearothermophilus enolase bound to Sepharose." International Journal of Peptide and Protein Research 24, no. 6 (January 12, 2009): 557–62. http://dx.doi.org/10.1111/j.1399-3011.1984.tb03160.x.

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33

Rofougaran, Reza, Munender Vodnala, and Anders Hofer. "Enzymatically Active Mammalian Ribonucleotide Reductase Exists Primarily as an α6β2Octamer." Journal of Biological Chemistry 281, no. 38 (July 22, 2006): 27705–11. http://dx.doi.org/10.1074/jbc.m605573200.

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34

Takeda, Yoichi, Akira Seko, Masakazu Hachisu, Shusaku Daikoku, Masayuki Izumi, Akihiko Koizumi, Kohki Fujikawa, Yasuhiro Kajihara, and Yukishige Ito. "Both isoforms of human UDP-glucose:glycoprotein glucosyltransferase are enzymatically active." Glycobiology 24, no. 4 (January 9, 2014): 344–50. http://dx.doi.org/10.1093/glycob/cwt163.

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35

Frenette, Gilles, David Deperthes, Roland R. Tremblay, Claude Lazure, and Jean Y. Dubé. "Purification of enzymatically active kallikrein hK2 from human seminal plasma." Biochimica et Biophysica Acta (BBA) - General Subjects 1334, no. 1 (February 1997): 109–15. http://dx.doi.org/10.1016/s0304-4165(96)00080-3.

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36

Chobot, Sarah E., Gregory Wiedman, Christopher C. Moser, Bohdana M. Discher, and P. Leslie Dutton. "Design and Characterization of an Enzymatically Active Amphiphilic Maquette Protein." Biophysical Journal 98, no. 3 (January 2010): 639a. http://dx.doi.org/10.1016/j.bpj.2009.12.3504.

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37

Walker, Debora, Benjamin T. Käsdorf, Hyeon-Ho Jeong, Oliver Lieleg, and Peer Fischer. "Enzymatically active biomimetic micropropellers for the penetration of mucin gels." Science Advances 1, no. 11 (December 2015): e1500501. http://dx.doi.org/10.1126/sciadv.1500501.

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In the body, mucus provides an important defense mechanism by limiting the penetration of pathogens. It is therefore also a major obstacle for the efficient delivery of particle-based drug carriers. The acidic stomach lining in particular is difficult to overcome because mucin glycoproteins form viscoelastic gels under acidic conditions. The bacteriumHelicobacter pylorihas developed a strategy to overcome the mucus barrier by producing the enzyme urease, which locally raises the pH and consequently liquefies the mucus. This allows the bacteria to swim through mucus and to reach the epithelial surface. We present an artificial system of reactive magnetic micropropellers that mimic this strategy to move through gastric mucin gels by making use of surface-immobilized urease. The results demonstrate the validity of this biomimetic approach to penetrate biological gels, and show that externally propelled microstructures can actively and reversibly manipulate the physical state of their surroundings, suggesting that such particles could potentially penetrate native mucus.

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38

Ho, Guojie, Jeffrey Morin, Jeannine Delaney, Garry Cuneo, Wael Yared, Milind Rajopadhye, Jeffrey D. Peterson, and Sylvie Kossodo. "Detection and quantification of enzymatically active prostate-specific antigenin vivo." Journal of Biomedical Optics 18, no. 10 (August 9, 2013): 101319. http://dx.doi.org/10.1117/1.jbo.18.10.101319.

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39

Masuda, Tsutomu, Eiichi Nakano, Shigehisa Hirose, and Kazuo Murakami. "Synthesis of Enzymatically Active Mouse Submandibular Gland Renin inEscherichia coli." Agricultural and Biological Chemistry 50, no. 2 (February 1986): 271–79. http://dx.doi.org/10.1080/00021369.1986.10867390.

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40

Chambers, Louise, Alan Brown, David I. Pritchard, Suneal Sreedharan, Keith Brocklehurst, and Noor A. Kalsheker. "Enzymatically Active Papain Preferentially Induces an Allergic Response in Mice." Biochemical and Biophysical Research Communications 253, no. 3 (December 1998): 837–40. http://dx.doi.org/10.1006/bbrc.1998.9862.

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41

Raaijmakers, Michiel J. T., Thomas Schmidt, Monika Barth, Murat Tutus, Nieck E. Benes, and Matthias Wessling. "Innenrücktitelbild: Enzymatically Active Ultrathin Pepsin Membranes (Angew. Chem. 20/2015)." Angewandte Chemie 127, no. 20 (April 27, 2015): 6165. http://dx.doi.org/10.1002/ange.201503395.

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42

Loew, Gilda H., Leonard M. Hjelmeland, and Robert F. Kirchner. "Models for the enzymatically active state of cytochrome p-450." International Journal of Quantum Chemistry 12, S4 (June 18, 2009): 225–44. http://dx.doi.org/10.1002/qua.560120724.

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43

Gorman, Cornelia M., David Gies, Peter R. Schofield, Helen Kado-Fong, and Bernard Malfroy. "Expression of enzymatically active enkephalinase (neutral endopeptidase) in mammalian cells." Journal of Cellular Biochemistry 39, no. 3 (March 1989): 277–84. http://dx.doi.org/10.1002/jcb.240390307.

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44

Jancekova, Blanka, Eva Ondrouskova, Lucia Knopfova, Jan Smarda, and Petr Benes. "Enzymatically active cathepsin D sensitizes breast carcinoma cells to TRAIL." Tumor Biology 37, no. 8 (February 11, 2016): 10685–96. http://dx.doi.org/10.1007/s13277-016-4958-5.

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45

Nonaka, Tamami, Hiroaki Taguchi, Taizo Uda, and Emi Hifumi. "Obtaining Highly Active Catalytic Antibodies Capable of Enzymatically Cleaving Antigens." International Journal of Molecular Sciences 23, no. 22 (November 18, 2022): 14351. http://dx.doi.org/10.3390/ijms232214351.

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A catalytic antibody has multiple functions compared with a monoclonal antibody because it possesses unique features to digest antigens enzymatically. Therefore, many catalytic antibodies, including their subunits, have been produced since 1989. The catalytic activities often depend on the preparation methods and conditions. In order to elicit the high catalytic activity of the antibodies, the most preferable methods and conditions, which can be generally applicable, must be explored. Based on this view, systematic experiments using two catalytic antibody light chains, #7TR and H34, were performed by varying the purification methods, pH, and chemical reagents. The experimental results obtained by peptidase activity tests and kinetic analysis, revealed that the light chain’s high catalytic activity was observed when it was prepared under a basic condition. These data imply that a small structural modulation of the catalytic antibody occurs during the purification process to increase the catalytic activity while the antigen recognition ability is kept constant. The presence of NaCl enhanced the catalytic activity. When the catalytic light chain was prepared with these preferable conditions, #7TR and H34 hugely enhanced the degradation ability of Amyloid-beta and PD-1 peptide, respectively.

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46

Lorenzen, Inken, Lisa Mullen, Sander Bekeschus, and Eva-Maria Hanschmann. "Redox Regulation of Inflammatory Processes Is Enzymatically Controlled." Oxidative Medicine and Cellular Longevity 2017 (2017): 1–23. http://dx.doi.org/10.1155/2017/8459402.

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Redox regulation depends on the enzymatically controlled production and decay of redox active molecules. NADPH oxidases, superoxide dismutases, nitric oxide synthases, and others produce the redox active molecules superoxide, hydrogen peroxide, nitric oxide, and hydrogen sulfide. These react with target proteins inducing spatiotemporal modifications of cysteine residues within different signaling cascades. Thioredoxin family proteins are key regulators of the redox state of proteins. They regulate the formation and removal of oxidative modifications by specific thiol reduction and oxidation. All of these redox enzymes affect inflammatory processes and the innate and adaptive immune response. Interestingly, this regulation involves different mechanisms in different biological compartments and specialized cell types. The localization and activity of distinct proteins including, for instance, the transcription factor NFκB and the immune mediator HMGB1 are redox-regulated. The transmembrane protein ADAM17 releases proinflammatory mediators, such as TNFα, and is itself regulated by a thiol switch. Moreover, extracellular redox enzymes were shown to modulate the activity and migration behavior of various types of immune cells by acting as cytokines and/or chemokines. Within this review article, we will address the concept of redox signaling and the functions of both redox enzymes and redox active molecules in innate and adaptive immune responses.

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47

Bagley, Kenneth C., Sayed F. Abdelwahab, Robert G. Tuskan, and George K. Lewis. "An Enzymatically Active A Domain Is Required for Cholera-Like Enterotoxins To Induce a Long-Lived Blockade on the Induction of Oral Tolerance: New Method for Screening Mucosal Adjuvants." Infection and Immunity 71, no. 12 (December 2003): 6850–56. http://dx.doi.org/10.1128/iai.71.12.6850-6856.2003.

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ABSTRACT The cholera-like enterotoxins (CLETS), cholera toxin (CT) and Escherichia coli heat-labile toxin (LT), are powerful mucosal adjuvants. Here we show that these toxins also induce a long-lived blockade (of at least 6 months) on the induction of oral tolerance when they are coadministered with the antigen ovalbumin. Strikingly, only enzymatically active CLETS induced this blockade on the induction of oral tolerance. In this regard, the enzymatically inactive mutants of CT and LT, CTK63 and LTK63, and their recombinant B pentamers, rCTB and rLTB, failed to block the induction of oral tolerance, demonstrating a stringent requirement for an enzymatically active A domain in this phenomenon. Together with the results of other recent studies, these results indicate that the enzymatic activity of CLETS, most likely cyclic AMP elevation, is responsible for their adjuvant effects. The results of this study also indicate that measuring the ability of putative mucosal adjuvants to block the induction of oral tolerance may be a superior method for measuring mucosal adjuvanticity.

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48

Criado-Gonzalez, Miryam, Jennifer Rodon Fores, Déborah Wagner, André Pierre Schröder, Alain Carvalho, Marc Schmutz, Eva Harth, Pierre Schaaf, Loïc Jierry, and Fouzia Boulmedais. "Enzyme-assisted self-assembly within a hydrogel induced by peptide diffusion." Chemical Communications 55, no. 8 (2019): 1156–59. http://dx.doi.org/10.1039/c8cc09437c.

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49

Thakuri, Biswash, Amanda B. Graves, Alex Chao, Sommer L. Johansen, Celia W. Goulding, and Matthew D. Liptak. "The affinity of MhuD for heme is consistent with a heme degrading functionin vivo." Metallomics 10, no. 11 (2018): 1560–63. http://dx.doi.org/10.1039/c8mt00238j.

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50

Vasil'eva, Irina S., Galina P. Shumakovich, Maria E. Khlupova, Roman B. Vasiliev, Viktor V. Emets, Vera A. Bogdanovskaya, Olga V. Morozova, and Alexander I. Yaropolov. "Enzymatic synthesis and electrochemical characterization of sodium 1,2-naphthoquinone-4-sulfonate-doped PEDOT/MWCNT composite." RSC Advances 10, no. 55 (2020): 33010–17. http://dx.doi.org/10.1039/d0ra05589a.

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