Статті в журналах з теми "Inhibitor Activity"
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Sumanadasa, Subathdrage D. M., Christopher D. Goodman, Andrew J. Lucke, Tina Skinner-Adams, Ishani Sahama, Ashraful Haque, Tram Anh Do, Geoffrey I. McFadden, David P. Fairlie, and Katherine T. Andrews. "Antimalarial Activity of the Anticancer Histone Deacetylase Inhibitor SB939." Antimicrobial Agents and Chemotherapy 56, no. 7 (April 16, 2012): 3849–56. http://dx.doi.org/10.1128/aac.00030-12.
Повний текст джерелаBöhm, Martina, Manuela Krause, Charis Von Auer, Wolfgang Miesbach, and Inge Scharrer. "The Frequency and the Significance of ADAMTS-13 Neutralising Inhibitors in 62 Patients with Non-Familial Thrombotic Thrombocytopenic Purpura." Blood 104, no. 11 (November 16, 2004): 3945. http://dx.doi.org/10.1182/blood.v104.11.3945.3945.
Повний текст джерелаAghaali, Negar, Mohammad Ghadamyari, Vahid Hosseininaveh, and Nasir Saberi Riseh. "PROTEASE INHIBITOR FROM THE CRUDE EXTRACT OF PLANT SEEDS AFFECTS THE DIGESTIVE PROTEASES IN HYPHANTRIA CUNEA (LEP.: ARCTIIDAE)." Journal of Plant Protection Research 53, no. 4 (October 1, 2013): 338–46. http://dx.doi.org/10.2478/jppr-2013-0051.
Повний текст джерелаJang, Seong, Bill Strickland, Lynda Finis, Jeffrey J. Koojiman, Janneke J. Melis, Guido J. Zaman, and Jan V. Tornout. "Abstract 4014: Comparative biochemical kinase activity analysis identifies rivoceranib as the most selective VEGFR-2 inhibitor compared with other TKIs with known activity against VEGFR-2." Cancer Research 83, no. 7_Supplement (April 4, 2023): 4014. http://dx.doi.org/10.1158/1538-7445.am2023-4014.
Повний текст джерелаLi, Qi, Hongyu Yang, Jun Mo, Yao Chen, Yue Wu, Chen Kang, Yuan Sun, and Haopeng Sun. "Identification by shape-based virtual screening and evaluation of new tyrosinase inhibitors." PeerJ 6 (January 26, 2018): e4206. http://dx.doi.org/10.7717/peerj.4206.
Повний текст джерелаSato, Shun, Kana Yamamoto, Moeno Ito, Katsutoshi Nishino, Takanao Otsuka, Kazuhiro Irie, and Masaya Nagao. "Enhancement of Inhibitory Activity by Combining Allosteric Inhibitors Putatively Binding to Different Allosteric Sites on Cathepsin K." Molecules 28, no. 10 (May 19, 2023): 4197. http://dx.doi.org/10.3390/molecules28104197.
Повний текст джерелаPintus, Francesca, Delia Spanò, Angela Corona, and Rosaria Medda. "Antityrosinase activity ofEuphorbia characiasextracts." PeerJ 3 (October 13, 2015): e1305. http://dx.doi.org/10.7717/peerj.1305.
Повний текст джерелаHs, Ranjini, Padmanabha Udupa Eg, Shobha U. Kamath, Manjunath Setty, Basavaraj Hadapad, and Asha Kamath. "AN IN VITRO STUDY OF CINNAMOMUM ZEYLANICUM AS NATURAL INHIBITOR OF ANGIOTENSIN-CONVERTING ENZYME (ACE) ON SHEEP (OVIS ARIES) TISSUES." Asian Journal of Pharmaceutical and Clinical Research 9, no. 5 (September 1, 2016): 249. http://dx.doi.org/10.22159/ajpcr.2016.v9i5.13424.
Повний текст джерелаCHEN, Ching-Jiunn, Hui-Sheng HUANG, Yu-Tsong LEE, Chia-Yi YANG, and Wen-Chang CHANG. "Characterization and purification of a lipoxygenase inhibitor in human epidermoid carcinoma A431 cells." Biochemical Journal 327, no. 1 (October 1, 1997): 193–98. http://dx.doi.org/10.1042/bj3270193.
Повний текст джерелаMiao, Yuxi, Guanzhu Chen, Xinping Xi, Chengbang Ma, Lei Wang, James F. Burrows, Jinao Duan, Mei Zhou, and Tianbao Chen. "Discovery and Rational Design of a Novel Bowman-Birk Related Protease Inhibitor." Biomolecules 9, no. 7 (July 14, 2019): 280. http://dx.doi.org/10.3390/biom9070280.
Повний текст джерелаDomoney, C., and T. Welham. "Trypsin inhibitors in Pisum: variation in amount and pattern of accumulation in developing seed." Seed Science Research 2, no. 3 (September 1992): 147–54. http://dx.doi.org/10.1017/s0960258500001276.
Повний текст джерелаKUMAR, Priyadarsini, and Donal A. WALSH. "A dual-specificity isoform of the protein kinase inhibitor PKI produced by alternate gene splicing." Biochemical Journal 362, no. 3 (March 8, 2002): 533–37. http://dx.doi.org/10.1042/bj3620533.
Повний текст джерелаTsujimura, Akane, Yukimasa Shiotsu, Hitoshi Kiyoi, Yuichi Ishikawa, Hiroshi Ishida, Tsutomu Toki, Etsuro Ito, and Tomoki Naoe. "Anti–leukemia Activity of a Novel KIT Selective Inhibitor KI–328." Blood 114, no. 22 (November 20, 2009): 4146. http://dx.doi.org/10.1182/blood.v114.22.4146.4146.
Повний текст джерелаSellitepe, Hasan Erdinç, Jong Min Oh, İnci Selin Doğan, Sercan Yildirim, Ahmet Buğra Aksel, Geum Seok Jeong, Ahmed Khames та ін. "Synthesis of N′-(4-/3-/2-/Non-substituted benzylidene)-4-[(4-methylphenyl)sulfonyloxy] Benzohydrazides and Evaluation of Their Inhibitory Activities against Monoamine Oxidases and β-Secretase". Applied Sciences 11, № 13 (23 червня 2021): 5830. http://dx.doi.org/10.3390/app11135830.
Повний текст джерелаWang, Wei-Ya, Chien-Kei Wei, Che-Ming Teng, and Chin-Chung Wu. "Combined blockade of thrombin anion binding exosite-1 and PAR4 produces synergistic antiplatelet effect in human platelets." Thrombosis and Haemostasis 105, no. 01 (2011): 88–95. http://dx.doi.org/10.1160/th10-05-0305.
Повний текст джерелаVolk, Kenneth A., Russell F. Husted, Peter M. Snyder та John B. Stokes. "Kinase regulation of hENaC mediated through a region in the COOH-terminal portion of the α-subunit". American Journal of Physiology-Cell Physiology 278, № 5 (1 травня 2000): C1047—C1054. http://dx.doi.org/10.1152/ajpcell.2000.278.5.c1047.
Повний текст джерелаCoutinho, M., K. S. Aulak, and A. E. Davis. "Functional analysis of the serpin domain of C1 inhibitor." Journal of Immunology 153, no. 8 (October 15, 1994): 3648–54. http://dx.doi.org/10.4049/jimmunol.153.8.3648.
Повний текст джерелаRymerson, Robert T., and Robert P. Bodnaryk. "GUT PROTEINASE ACTIVITY IN INSECT PESTS OF CANOLA." Canadian Entomologist 127, no. 1 (February 1995): 41–48. http://dx.doi.org/10.4039/ent12741-1.
Повний текст джерелаMilner, Malgorzata, Jadwiga Chroboczek, and Wlodzimierz Zagorski-Ostoja. "Engineered resistance against proteinases." Acta Biochimica Polonica 54, no. 3 (September 6, 2007): 523–36. http://dx.doi.org/10.18388/abp.2007_3226.
Повний текст джерелаALIAS, ZAZALI, and NORA ASYIKIN RAMLI. "PURIFICATION AND PARTIAL CHARACTERISATION OF A PROTEASE INHIBITOR FROM Mimosa diplotricha." Malaysian Applied Biology 51, no. 4 (October 31, 2022): 169–75. http://dx.doi.org/10.55230/mabjournal.v51i4.26.
Повний текст джерелаCurry, V. A., I. M. Clark, H. Bigg, and T. E. Cawston. "Large inhibitor of metalloproteinases (LIMP) contains tissue inhibitor of metalloproteinases (TIMP)-2 bound to 72,000-Mr progelatinase." Biochemical Journal 285, no. 1 (July 1, 1992): 143–47. http://dx.doi.org/10.1042/bj2850143.
Повний текст джерелаPujirahayu, Niken, Debu Kumar Bhattacharjya, Toshisada Suzuki та Takeshi Katayama. "α-Glucosidase Inhibitory Activity of Cycloartane-Type Triterpenes Isolated from Indonesian Stingless Bee Propolis and Their Structure–Activity Relationship". Pharmaceuticals 12, № 3 (1 липня 2019): 102. http://dx.doi.org/10.3390/ph12030102.
Повний текст джерелаWu, Wei, Hai-Ying Sun, Xiu-Ling Deng, and Gui-Rong Li. "EGFR tyrosine kinase regulates human small-conductance Ca2+-activated K+ (hSKCa1) channels expressed in HEK-293 cells." Biochemical Journal 452, no. 1 (April 25, 2013): 121–29. http://dx.doi.org/10.1042/bj20121324.
Повний текст джерелаKorn, J. H., K. M. Brown, E. Downie, Z. H. Liao, and D. L. Rosenstreich. "Augmentation of IL 1-induced fibroblast PGE2 production by a urine-derived IL 1 inhibitor." Journal of Immunology 138, no. 10 (May 15, 1987): 3290–94. http://dx.doi.org/10.4049/jimmunol.138.10.3290.
Повний текст джерелаThøgersen, I. B., G. Salvesen, F. H. Brucato, S. V. Pizzo та J. J. Enghild. "Purification and characterization of an α-macroglobulin proteinase inhibitor from the mollusc Octopus vulgaris". Biochemical Journal 285, № 2 (15 липня 1992): 521–27. http://dx.doi.org/10.1042/bj2850521.
Повний текст джерелаChandrashekharaiah, K. S. "Studies on the Amylase Inhibitors from the Seeds of Adenanthera Pavonina." Biosciences, Biotechnology Research Asia 14, no. 3 (September 25, 2017): 1009–15. http://dx.doi.org/10.13005/bbra/2535.
Повний текст джерелаEllis, Dorette Z., James A. Nathanson, and Kathleen J. Sweadner. "Carbachol inhibits Na+-K+-ATPase activity in choroid plexus via stimulation of the NO/cGMP pathway." American Journal of Physiology-Cell Physiology 279, no. 6 (December 1, 2000): C1685—C1693. http://dx.doi.org/10.1152/ajpcell.2000.279.6.c1685.
Повний текст джерелаBuzzelli, Mark D., Murali Nagarajan, John F. Radtka, Margaret L. Shumate, Maithili Navaratnarajah, Charles H. Lang та Robert N. Cooney. "Nuclear Factor-κB Mediates the Inhibitory Effects of Tumor Necrosis Factor-α on Growth Hormone-Inducible Gene Expression in Liver". Endocrinology 149, № 12 (21 серпня 2008): 6378–88. http://dx.doi.org/10.1210/en.2007-1574.
Повний текст джерелаScaffa, P. M. C., C. M. P. Vidal, N. Barros, T. F. Gesteira, A. K. Carmona, L. Breschi, D. H. Pashley, et al. "Chlorhexidine Inhibits the Activity of Dental Cysteine Cathepsins." Journal of Dental Research 91, no. 4 (January 19, 2012): 420–25. http://dx.doi.org/10.1177/0022034511435329.
Повний текст джерелаHan, Di, Huiqun Wang, Wei Cui, Beibei Zhang, and Bo-Zhen Chen. "Computational insight into the mechanisms of action and selectivity of Afraxis PAK inhibitors." Future Medicinal Chemistry 12, no. 5 (March 2020): 367–85. http://dx.doi.org/10.4155/fmc-2019-0273.
Повний текст джерелаJacquemin, Marc, Abdellah Benhida, Kathelijne Peerlinck, Benoı̂t Desqueper, Luc Vander Elst, Renaud Lavend'homme, Roseline d'Oiron, et al. "A human antibody directed to the factor VIII C1 domain inhibits factor VIII cofactor activity and binding to von Willebrand factor." Blood 95, no. 1 (January 1, 2000): 156–63. http://dx.doi.org/10.1182/blood.v95.1.156.
Повний текст джерелаJacquemin, Marc, Abdellah Benhida, Kathelijne Peerlinck, Benoı̂t Desqueper, Luc Vander Elst, Renaud Lavend'homme, Roseline d'Oiron, et al. "A human antibody directed to the factor VIII C1 domain inhibits factor VIII cofactor activity and binding to von Willebrand factor." Blood 95, no. 1 (January 1, 2000): 156–63. http://dx.doi.org/10.1182/blood.v95.1.156.001k50_156_163.
Повний текст джерелаJavaid, Bushra. "Anti-trypsin and antihypertensive activity of protein extracts from Nigella sativa seeds." Pakistan Journal of Agricultural Sciences 58, no. 04 (September 1, 2021): 1237–43. http://dx.doi.org/10.21162/pakjas/21.204.
Повний текст джерелаDemiroglu, Asuman, E. Joanna Steer, Carol Heath, Kerry Taylor, Mark Bentley, Steven L. Allen, Prasad Koduru, et al. "The t(8;22) in chronic myeloid leukemia fuses BCR to FGFR1: transforming activity and specific inhibition of FGFR1 fusion proteins." Blood 98, no. 13 (December 15, 2001): 3778–83. http://dx.doi.org/10.1182/blood.v98.13.3778.
Повний текст джерелаGanea, D., D. Cearlock, J. Minowada, and S. Dray. "A serine proteinase inhibitor produced by an HTLV I virus-transformed human T lymphocyte line." Journal of Immunology 138, no. 4 (February 15, 1987): 1208–14. http://dx.doi.org/10.4049/jimmunol.138.4.1208.
Повний текст джерелаCao, Jiangying, Wei Zhao, Chunlong Zhao, Qian Liu, Shunda Li, Guozhen Zhang, C. James Chou, and Yingjie Zhang. "Development of a Bestatin-SAHA Hybrid with Dual Inhibitory Activity against APN and HDAC." Molecules 25, no. 21 (October 28, 2020): 4991. http://dx.doi.org/10.3390/molecules25214991.
Повний текст джерелаVest, Rebekah S., Kurtis D. Davies, Heather O'Leary, J. David Port, and K. Ulrich Bayer. "Dual Mechanism of a Natural CaMKII Inhibitor." Molecular Biology of the Cell 18, no. 12 (December 2007): 5024–33. http://dx.doi.org/10.1091/mbc.e07-02-0185.
Повний текст джерелаBishop, P. B., J. Young, T. Peng, and J. F. Richards. "An inhibitor of ornithine decarboxylase in the thymus and spleen of dexamethasone-treated rats." Biochemical Journal 226, no. 1 (February 15, 1985): 105–12. http://dx.doi.org/10.1042/bj2260105.
Повний текст джерелаDong, Wenxiu, Fei Luo, Yuguang Du, Xuefang Bai, and Xianzhen Li. "Production and properties of an inhibitor of the Pseudomonas autoinducer by Pseudomonas aeruginosa." Canadian Journal of Microbiology 51, no. 9 (September 1, 2005): 783–89. http://dx.doi.org/10.1139/w05-066.
Повний текст джерелаSuzuki, Suzuki, Morio Arai, Kagehiro Amano, Kazuhiko Kagawa, and Katsuyuki Fukutake. "Factor VIII Inhibitor Antibodies with C2 Domain Specificity Are Less inhibitory to Factor VIII Complexed with von Willebrand Factor." Thrombosis and Haemostasis 76, no. 05 (1996): 749–54. http://dx.doi.org/10.1055/s-0038-1650655.
Повний текст джерелаMurthy, Karnam S., Huiping Zhou, and Gabriel M. Makhlouf. "PKA-dependent activation of PDE3A and PDE4 and inhibition of adenylyl cyclase V/VI in smooth muscle." American Journal of Physiology-Cell Physiology 282, no. 3 (March 1, 2002): C508—C517. http://dx.doi.org/10.1152/ajpcell.00373.2001.
Повний текст джерелаLiang, Mingyu, та Franklyn G. Knox. "Nitric oxide activates PKCα and inhibits Na+-K+-ATPase in opossum kidney cells". American Journal of Physiology-Renal Physiology 277, № 6 (1 грудня 1999): F859—F865. http://dx.doi.org/10.1152/ajprenal.1999.277.6.f859.
Повний текст джерелаSaleh, Neveen M., Yasmine S. Moemen, Sara H. Mohamed, Ghady Fathy, Abdullah A. S. Ahmed, Ahmed A. Al-Ghamdi, Sami Ullah, and Ibrahim El-Tantawy El Sayed. "Experimental and Molecular Docking Studies of Cyclic Diphenyl Phosphonates as DNA Gyrase Inhibitors for Fluoroquinolone-Resistant Pathogens." Antibiotics 11, no. 1 (January 1, 2022): 53. http://dx.doi.org/10.3390/antibiotics11010053.
Повний текст джерелаRajotte, D., S. Tremblay, A. Pelletier, P. Salois, L. Bourgon, R. Coulombe, S. Mason, L. Lamorte, C. F. Sturino, and R. Bethell. "Identification and Characterization of a Novel HIV-1 Nucleotide-Competing Reverse Transcriptase Inhibitor Series." Antimicrobial Agents and Chemotherapy 57, no. 6 (April 1, 2013): 2712–18. http://dx.doi.org/10.1128/aac.00113-13.
Повний текст джерелаZhang, Yilin, Yong Yan, Lufan Liang, Jie Feng, Xuejun Wang, Li Li та Kewu Yang. "Halogen-Substituted Triazolethioacetamides as a Potent Skeleton for the Development of Metallo-β-Lactamase Inhibitors". Molecules 24, № 6 (25 березня 2019): 1174. http://dx.doi.org/10.3390/molecules24061174.
Повний текст джерелаKitano, Mitsutaka, Atsuko Yamamoto, Takeshi Noshi, Makoto Kawai, Ryu Yoshida, Akihiko Sato, Takao Shishido, and Akira Naito. "Synergistic Antiviral Activity of S-033188/S-033447, a Novel Inhibitor of Influenza Virus Cap-Dependent Endonuclease, in Combination with Neuraminidase Inhibitors In Vitro." Open Forum Infectious Diseases 4, suppl_1 (2017): S371. http://dx.doi.org/10.1093/ofid/ofx163.910.
Повний текст джерелаYan, Daojing, Jiakun Xu, Xiang Wang, Jiaxing Zhang, Gang Zhao, Yingwu Lin, and Xiangshi Tan. "Spiro-Oxindole Skeleton Compounds Are Efficient Inhibitors for Indoleamine 2,3-Dioxygenase 1: An Attractive Target for Tumor Immunotherapy." International Journal of Molecular Sciences 23, no. 9 (April 23, 2022): 4668. http://dx.doi.org/10.3390/ijms23094668.
Повний текст джерелаZhu, Yongxia, Xinyi Chen, Qiangsheng Zhang, Lihong Shi, Luoting Yu, and Hongtao Xiao. "Anti-tumor activity of SKLB-0322, a novel EZH2 covalent inhibitor, in ovarian cancer." Journal of Clinical Oncology 39, no. 15_suppl (May 20, 2021): e15052-e15052. http://dx.doi.org/10.1200/jco.2021.39.15_suppl.e15052.
Повний текст джерелаJo, Sooheum, Jin-Hee Kim, Jiyeon Lee, Youngjun Park, and Jaebong Jang. "Azumamides A-E: Isolation, Synthesis, Biological Activity, and Structure–Activity Relationship." Molecules 27, no. 23 (December 2, 2022): 8438. http://dx.doi.org/10.3390/molecules27238438.
Повний текст джерелаArita, Minetaro, Takaji Wakita, and Hiroyuki Shimizu. "Cellular kinase inhibitors that suppress enterovirus replication have a conserved target in viral protein 3A similar to that of enviroxime." Journal of General Virology 90, no. 8 (August 1, 2009): 1869–79. http://dx.doi.org/10.1099/vir.0.012096-0.
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