Статті в журналах з теми "Enzymatically active"
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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.
Повний текст джерелаDerkx, 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.
Повний текст джерелаRaaijmakers, 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.
Повний текст джерелаYu, 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.
Повний текст джерелаRaaijmakers, 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.
Повний текст джерелаZhang, 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.
Повний текст джерелаBecker, 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.
Повний текст джерелаBrumm, 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.
Повний текст джерелаMüller, 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.
Повний текст джерелаOzdener, Fatih, Satya P. Kunapuli та James L. Daniel. "Expression of Enzymatically-active Phospholipase Cγ2 in E.coli". BMB Reports 35, № 5 (30 вересня 2002): 508–12. http://dx.doi.org/10.5483/bmbrep.2002.35.5.508.
Повний текст джерелаTATSUMI, 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.
Повний текст джерелаTatsumi, 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.
Повний текст джерелаBuruaga-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.
Повний текст джерелаWu, 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.
Повний текст джерелаMiller, Lisa M., Matthew D. Simmons, Callum D. Silver, Thomas F. Krauss, Gavin H. Thomas, Steven D. Johnson та Anne-Kathrin Duhme-Klair. "Antibiotic-functionalized gold nanoparticles for the detection of active β-lactamases". Nanoscale Advances 4, № 2 (2022): 573–81. http://dx.doi.org/10.1039/d1na00635e.
Повний текст джерелаWeirich, 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.
Повний текст джерелаSchakowski, 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.
Повний текст джерелаKrepel, 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.
Повний текст джерелаRickus, 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.
Повний текст джерелаTanese, 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.
Повний текст джерелаNorth, 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.
Повний текст джерелаZagalak, 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.
Повний текст джерелаSingh, 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.
Повний текст джерелаKumar, 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.
Повний текст джерелаDerr, 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.
Повний текст джерелаMcCormick, 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.
Повний текст джерелаRindt, 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.
Повний текст джерелаHenderson, 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.
Повний текст джерелаMa, 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.
Повний текст джерелаMariconti, 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.
Повний текст джерелаKus, 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.
Повний текст джерелаVERONESE, 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.
Повний текст джерелаRofougaran, Reza, Munender Vodnala та Anders Hofer. "Enzymatically Active Mammalian Ribonucleotide Reductase Exists Primarily as an α6β2Octamer". Journal of Biological Chemistry 281, № 38 (22 липня 2006): 27705–11. http://dx.doi.org/10.1074/jbc.m605573200.
Повний текст джерелаTakeda, 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.
Повний текст джерелаFrenette, 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.
Повний текст джерелаChobot, 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.
Повний текст джерелаWalker, 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.
Повний текст джерелаHo, 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.
Повний текст джерелаMasuda, 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.
Повний текст джерелаChambers, 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.
Повний текст джерелаRaaijmakers, 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.
Повний текст джерелаLoew, 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.
Повний текст джерелаGorman, 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.
Повний текст джерелаJancekova, 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.
Повний текст джерелаNonaka, 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.
Повний текст джерелаLorenzen, 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.
Повний текст джерелаBagley, 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.
Повний текст джерелаCriado-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.
Повний текст джерелаThakuri, 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.
Повний текст джерелаVasil'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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