Artículos de revistas sobre el tema "His95"
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Gao, Miaomiao, Kaili Nie, Meng Qin, Haijun Xu, Fang Wang y Luo Liu. "Molecular Mechanism Study on Stereo-Selectivity of α or β Hydroxysteroid Dehydrogenases". Crystals 11, n.º 3 (25 de febrero de 2021): 224. http://dx.doi.org/10.3390/cryst11030224.
Texto completoViles, John H., Mark Klewpatinond y Rebecca C. Nadal. "Copper and the structural biology of the prion protein". Biochemical Society Transactions 36, n.º 6 (19 de noviembre de 2008): 1288–92. http://dx.doi.org/10.1042/bst0361288.
Texto completoBsat, Nada y John D. Helmann. "Interaction of Bacillus subtilis Fur (Ferric Uptake Repressor) with the dhb Operator In Vitro and In Vivo". Journal of Bacteriology 181, n.º 14 (15 de julio de 1999): 4299–307. http://dx.doi.org/10.1128/jb.181.14.4299-4307.1999.
Texto completoWang, Xixi, Jiankai Shan, Wei Liu, Jing Li, Hongwei Tan, Xichen Li y Guangju Chen. "Theoretical Studies on the Binding Mode and Reaction Mechanism of TLP Hydrolase kpHIUH". Molecules 26, n.º 13 (25 de junio de 2021): 3884. http://dx.doi.org/10.3390/molecules26133884.
Texto completoSanyanga, Taremekedzwa Allan, Bilal Nizami y Özlem Tastan Bishop. "Mechanism of Action of Non-Synonymous Single Nucleotide Variations Associated with α-Carbonic Anhydrase II Deficiency". Molecules 24, n.º 21 (4 de noviembre de 2019): 3987. http://dx.doi.org/10.3390/molecules24213987.
Texto completoHempelmann, Franziska, Soraya Hölper, Mirka-Kristin Verhoefen, Andreas C. Woerner, Thomas Köhler, Sarah-Anna Fiedler, Nicole Pfleger, Josef Wachtveitl y Clemens Glaubitz. "His75−Asp97 Cluster in Green Proteorhodopsin". Journal of the American Chemical Society 133, n.º 12 (30 de marzo de 2011): 4645–54. http://dx.doi.org/10.1021/ja111116a.
Texto completoTanley, Simon W. M., Antoine M. M. Schreurs, Loes M. J. Kroon-Batenburg y John R. Helliwell. "Room-temperature X-ray diffraction studies of cisplatin and carboplatin binding to His15 of HEWL after prolonged chemical exposure". Acta Crystallographica Section F Structural Biology and Crystallization Communications 68, n.º 11 (26 de octubre de 2012): 1300–1306. http://dx.doi.org/10.1107/s1744309112042005.
Texto completoPlowman, Jeffrey E. y Lawrence K. Creamer. "Restrained molecular dynamics study of the interaction between bovine κ-casein peptide 98–111 and bovine chymosin and porcine pepsin". Journal of Dairy Research 62, n.º 3 (agosto de 1995): 451–67. http://dx.doi.org/10.1017/s0022029900031150.
Texto completoNi, Jie, Guochao Xu, Wei Dai, Yi-Lei Zhao y Ye Ni. "Hyperconjugation promoted by hydrogen bonding between His98/His241 and a carboxyl group contributes to tyrosine decarboxylase catalysis". Catalysis Science & Technology 9, n.º 22 (2019): 6222–26. http://dx.doi.org/10.1039/c9cy01290g.
Texto completoIshikawa, Yasuko, Tomasz D. Pieczonka, Aneta M. Bragiel-Pieczonka, Harumichi Seta, Tadahiro Ohkuri, Yumi Sasanuma y Yuji Nonaka. "Long-Term Oral Administration of LLHK, LHK, and HK Alters Gene Expression Profile and Restores Age-Dependent Atrophy and Dysfunction of Rat Salivary Glands". Biomedicines 8, n.º 2 (20 de febrero de 2020): 38. http://dx.doi.org/10.3390/biomedicines8020038.
Texto completode Cristóbal, Ricardo E., Jose O. Solbiati, Ana M. Zenoff, Paula A. Vincent, Raul A. Salomón, Julia Yuzenkova, Konstantin Severinov y Ricardo N. Farías. "Microcin J25 Uptake: His5 of the MccJ25 Lariat Ring Is Involved in Interaction with the Inner Membrane MccJ25 Transporter Protein SbmA". Journal of Bacteriology 188, n.º 9 (1 de mayo de 2006): 3324–28. http://dx.doi.org/10.1128/jb.188.9.3324-3328.2006.
Texto completoHO, Heng-Chien y Ta-Hsiu LIAO. "Protein structure and gene cloning of Syncephalastrum racemosum nuclease". Biochemical Journal 339, n.º 2 (8 de abril de 1999): 261–67. http://dx.doi.org/10.1042/bj3390261.
Texto completoGras, Stephanie, Zhenjun Chen, John J. Miles, Yu Chih Liu, Melissa J. Bell, Lucy C. Sullivan, Lars Kjer-Nielsen et al. "Allelic polymorphism in the T cell receptor and its impact on immune responses". Journal of Experimental Medicine 207, n.º 7 (21 de junio de 2010): 1555–67. http://dx.doi.org/10.1084/jem.20100603.
Texto completoRan, Tingting, Gabriel Ozorowski, Yanyan Gao, Oleg A. Sineshchekov, Weiwu Wang, John L. Spudich y Hartmut Luecke. "Cross-protomer interaction with the photoactive site in oligomeric proteorhodopsin complexes". Acta Crystallographica Section D Biological Crystallography 69, n.º 10 (20 de septiembre de 2013): 1965–80. http://dx.doi.org/10.1107/s0907444913017575.
Texto completoFunhoff, Enrico G., Yunling Wang, Goran Andersson y Bruce A. Averill. "Substrate positioning by His92 is important in catalysis by purple acid phosphatase". FEBS Journal 272, n.º 12 (14 de junio de 2005): 2968–77. http://dx.doi.org/10.1111/j.1742-4658.2005.04686.x.
Texto completoYang, X., Y. Li, L. Huang, X. Zhang, C. Cheng, H. Gong, L. Ma y K. Huang. "Diethylpyrocarbonate modification reveals HisB5 as an important modulator of insulin amyloid formation". Journal of Biochemistry 157, n.º 1 (28 de agosto de 2014): 45–51. http://dx.doi.org/10.1093/jb/mvu052.
Texto completoLiu, Wen, Corina E. Rogge, Giordano F. Z. da Silva, Vladimir P. Shinkarev, Ah-Lim Tsai, Yury Kamensky, Graham Palmer y Richard J. Kulmacz. "His92 and His110 selectively affect different heme centers of adrenal cytochrome b561". Biochimica et Biophysica Acta (BBA) - Bioenergetics 1777, n.º 9 (septiembre de 2008): 1218–28. http://dx.doi.org/10.1016/j.bbabio.2008.04.039.
Texto completoTanley, Simon W. M., Antoine M. M. Schreurs, Loes M. J. Kroon-Batenburg y John R. Helliwell. "Re-refinement of 4g4a: room-temperature X-ray diffraction study of cisplatin and its binding to His15 of HEWL after 14 months chemical exposure in the presence of DMSO". Acta Crystallographica Section F Structural Biology Communications 72, n.º 3 (19 de febrero de 2016): 253–54. http://dx.doi.org/10.1107/s2053230x16000856.
Texto completoCastro Torres, Mario Eduardo, Pablo Marcelo Vargas-Piérola, Carlos F. Pinto y Rubén Alvarado. "Serial Mediation Model of Social Capital Effects over Academic Stress in University Students". European Journal of Investigation in Health, Psychology and Education 12, n.º 11 (16 de noviembre de 2022): 1644–56. http://dx.doi.org/10.3390/ejihpe12110115.
Texto completoZhang, Liang, Jacqueline Wax, Renliang Huang, Frank Petersen y Xinhua Yu. "Meta-Analysis and Systematic Review of the Association between a Hypoactive NCF1 Variant and Various Autoimmune Diseases". Antioxidants 11, n.º 8 (16 de agosto de 2022): 1589. http://dx.doi.org/10.3390/antiox11081589.
Texto completoMagrì, Antonio, Giovanni Tabbì, Irina Naletova, Francesco Attanasio, Giuseppe Arena y Enrico Rizzarelli. "A Deeper Insight in Metal Binding to the hCtr1 N-terminus Fragment: Affinity, Speciation and Binding Mode of Binuclear Cu2+ and Mononuclear Ag+ Complex Species". International Journal of Molecular Sciences 23, n.º 6 (8 de marzo de 2022): 2929. http://dx.doi.org/10.3390/ijms23062929.
Texto completoKing, Judy A. y Robert P. Millar. "Identification of His5, Trp7, Tyr8-GnRH (chicken GnRH II) in amphibian brain". Peptides 7, n.º 5 (septiembre de 1986): 827–34. http://dx.doi.org/10.1016/0196-9781(86)90102-6.
Texto completoBergo, Vladislav B., Joel M. Kralj, John L. Spudich y Kenneth J. Rothschild. "His75 in Proteorhodopsin, a Novel Component in Light-Driven Proton Translocation by Primary Pumps". Biophysical Journal 96, n.º 3 (febrero de 2009): 526a. http://dx.doi.org/10.1016/j.bpj.2008.12.2713.
Texto completoBlank, J., T. Kupke, E. Lowe, P. Barth, R. B. Freedman y L. W. Ruddock. "The Influence of His94 and Pro149 in Modulating the Activity of V. cholerae DsbA". Antioxidants & Redox Signaling 5, n.º 4 (agosto de 2003): 359–66. http://dx.doi.org/10.1089/152308603768295087.
Texto completoQiu, Shenshen, Dongqing Xu, Mengxue Xu, Huan Zhou, Ning Sun, Li Zhang, Mengmeng Zhao et al. "Crystal structures of PigF, an O-methyltransferase involved in the prodigiosin synthetic pathway, reveal an induced-fit substrate-recognition mechanism". IUCrJ 9, n.º 2 (1 de marzo de 2022): 316–27. http://dx.doi.org/10.1107/s2052252521011696.
Texto completoTanley, Simon W. M. y John R. Helliwell. "Chemical conversion of cisplatin and carboplatin with histidine in a model protein crystallized under sodium iodide conditions". Acta Crystallographica Section F Structural Biology Communications 70, n.º 9 (29 de agosto de 2014): 1127–31. http://dx.doi.org/10.1107/s2053230x14013995.
Texto completoTsai, H. y L. A. Bobek. "Studies of the mechanism of human salivary histatin-5 candidacidal activity with histatin-5 variants and azole-sensitive and -resistant Candida species." Antimicrobial Agents and Chemotherapy 41, n.º 10 (octubre de 1997): 2224–28. http://dx.doi.org/10.1128/aac.41.10.2224.
Texto completoKIMURA, Shigenobu, Akihiro KIKUCHI, Toshiya SENDA, Yoshitsugu SHIRO y Masao FUKUDA. "Tolerance of the Rieske-type [2Fe-2S] cluster in recombinant ferredoxin BphA3 from Pseudomonas sp. KKS102 to histidine ligand mutations". Biochemical Journal 388, n.º 3 (7 de junio de 2005): 869–78. http://dx.doi.org/10.1042/bj20042077.
Texto completoWang, Chunxue, Leslie L. Lovelace, Shengfang Sun, John H. Dawson y Lukasz Lebioda. "Structures of K42N and K42Y sperm whale myoglobins point to an inhibitory role of distal water in peroxidase activity". Acta Crystallographica Section D Biological Crystallography 70, n.º 11 (16 de octubre de 2014): 2833–39. http://dx.doi.org/10.1107/s1399004714017787.
Texto completoGrinthal, Alison y Guido Guidotti. "Substitution of His59 Converts CD39 Apyrase into an ADPase in a Quaternary Structure Dependent Manner†". Biochemistry 39, n.º 1 (enero de 2000): 9–16. http://dx.doi.org/10.1021/bi991751k.
Texto completoDance, Ian. "New insights into the reaction capabilities of His195 adjacent to the active site of nitrogenase". Journal of Inorganic Biochemistry 169 (abril de 2017): 32–43. http://dx.doi.org/10.1016/j.jinorgbio.2017.01.005.
Texto completoMirzabekov, Andrei D., Dmitrii V. Pruss y Konstantin K. Ebralidse. "Chromatin superstructure-dependent crosslinking with DNA of the histone H5 residues Thr1, His25 and His62". Journal of Molecular Biology 211, n.º 2 (enero de 1990): 479–91. http://dx.doi.org/10.1016/0022-2836(90)90366-t.
Texto completoZeidler, Waltraud, Christian Egle, Sofia Ribeiro, Annett Wagner, Vladimir Katunin, Roland Kreutzer, Marina Rodnina, Wolfgang Wintermeyer y Mathias Sprinzl. "Site-Directed Mutagenesis of Thermus thermophilus Elongation Factor Tu. Replacement of His85, Asp81 and Arg300". European Journal of Biochemistry 229, n.º 3 (mayo de 1995): 596–604. http://dx.doi.org/10.1111/j.1432-1033.1995.tb20503.x.
Texto completoVerhoef, Daniël, Mark Schreuder, Ka Lei Cheung, Pieter H. Reitsma y Mettine H. A. Bos. "Engineered Factor Xa Variants Retain Procoagulant Activity Independent of Direct Factor Xa-Inhibitors". Blood 126, n.º 23 (3 de diciembre de 2015): 126. http://dx.doi.org/10.1182/blood.v126.23.126.126.
Texto completoTanley, Simon W. M., Laurina-Victoria Starkey, Lucinda Lamplough, Surasek Kaenket y John R. Helliwell. "The binding of platinum hexahalides (Cl, Br and I) to hen egg-white lysozyme and the chemical transformation of the PtI6octahedral complex to a PtI3moiety bound to His15". Acta Crystallographica Section F Structural Biology Communications 70, n.º 9 (29 de agosto de 2014): 1132–34. http://dx.doi.org/10.1107/s2053230x14014009.
Texto completoPy, Béatrice, Bortoli-German Isabelle, Jacques Haiech, Marc Chippaux y Frédéric Barras. "Cellulase EGZ of Erwinia chrysanthemi: structural organization and importance of His98 and Glu133 residues for catalysis". "Protein Engineering, Design and Selection" 4, n.º 3 (1991): 325–33. http://dx.doi.org/10.1093/protein/4.3.325.
Texto completoTyukhtenko, Sergiy, Karrie Chan, Rubin Jiang, Han Zhou, Richard W. Mercier, De-Ping Yang, Alexandros Makriyannis y Jason J. Guo. "Hydrogen-Bonded His93 As a Sensitive Probe for Identifying Inhibitors of the Endocannabinoid Transport Protein FABP7". Chemical Biology & Drug Design 85, n.º 5 (16 de octubre de 2014): 534–40. http://dx.doi.org/10.1111/cbdd.12440.
Texto completoXue, Yafeng, Bengt-Harald Jonsson, Anders Liljas y Sven Lindskog. "Modification of a metal ligand in carbonic anhydrase: Crystal structure of His94 →Glu human isozyme II". FEBS Letters 352, n.º 2 (26 de septiembre de 1994): 137–40. http://dx.doi.org/10.1016/0014-5793(94)00936-8.
Texto completoBudanov, Andrei V., Tzipora Shoshani, Alexander Faerman, Elena Zelin, Iris Kamer, Hagar Kalinski, Svetlana Gorodin et al. "Identification of a novel stress-responsive gene Hi95 involved in regulation of cell viability". Oncogene 21, n.º 39 (septiembre de 2002): 6017–31. http://dx.doi.org/10.1038/sj.onc.1205877.
Texto completoSakurada, Tkukasa, Akinori Sugiyama, Koichi Tanno, Shinobu Sakurada, Masataka Ohba y Kensuke Kisara. "Pharmacological profile of tachykinin NK1 receptor antagonist, [Tyr6, D-Trp7, D-His9] substance P". Japanese Journal of Pharmacology 67 (1995): 81. http://dx.doi.org/10.1016/s0021-5198(19)46292-6.
Texto completoNishiwaki, Kiyoji, Naoyuki Hayashi, Shinji Irie, Dong-Hyo Chung, Satoshi Harashima y Yasuji Oshima. "Structure of the yeast HIS5 gene responsive to general control of amino acid biosynthesis". Molecular and General Genetics MGG 208, n.º 1-2 (junio de 1987): 159–67. http://dx.doi.org/10.1007/bf00330437.
Texto completoMashima, Tsuyoshi, Koji Oohora y Takashi Hayashi. "Substitution of an amino acid residue axially coordinating to the heme molecule in hexameric tyrosine-coordinated hemoprotein to enhance peroxidase activity". Journal of Porphyrins and Phthalocyanines 21, n.º 12 (diciembre de 2017): 824–31. http://dx.doi.org/10.1142/s1088424617500936.
Texto completoPlamondon, Pascale, Denis Brochu, Suzanne Thomas, Julie Fradette, Lucie Gauthier, Katy Vaillancourt, Nicole Buckley, Michel Frenette y Christian Vadeboncoeur. "Phenotypic Consequences Resulting from a Methionine-to-Valine Substitution at Position 48 in the HPr Protein of Streptococcus salivarius". Journal of Bacteriology 181, n.º 22 (15 de noviembre de 1999): 6914–21. http://dx.doi.org/10.1128/jb.181.22.6914-6921.1999.
Texto completoLin, Ying-Ju y Suh-Chin Wu. "Histidine at Residue 99 and the Transmembrane Region of the Precursor Membrane prM Protein Are Important for the prM-E Heterodimeric Complex Formation of Japanese Encephalitis Virus". Journal of Virology 79, n.º 13 (1 de julio de 2005): 8535–44. http://dx.doi.org/10.1128/jvi.79.13.8535-8544.2005.
Texto completoPLOWMAN, JEFFREY E., LAWRENCE K. CREAMER, MICHAEL J. LIDDELL y JENNIFER J. CROSS. "Structural features of a peptide corresponding to human κ-casein residues 84–101 by 1H-nuclear magnetic resonance spectroscopy". Journal of Dairy Research 66, n.º 1 (febrero de 1999): 53–63. http://dx.doi.org/10.1017/s0022029998003318.
Texto completoLópez de Maturana, Rakel, Adam J. Pawson, Zhi-Liang Lu, Lindsay Davidson, Stuart Maudsley, Kevin Morgan, Simon P. Langdon y Robert P. Millar. "Gonadotropin-Releasing Hormone Analog Structural Determinants of Selectivity for Inhibition of Cell Growth: Support for the Concept of Ligand-Induced Selective Signaling". Molecular Endocrinology 22, n.º 7 (1 de julio de 2008): 1711–22. http://dx.doi.org/10.1210/me.2006-0537.
Texto completoSchmölzer, Katharina, Manuel Eibinger y Bernd Nidetzky. "Active-Site His85 ofPasteurella dagmatisSialyltransferase Facilitates Productive Sialyl Transfer and So Prevents Futile Hydrolysis of CMP-Neu5Ac". ChemBioChem 18, n.º 15 (21 de junio de 2017): 1544–50. http://dx.doi.org/10.1002/cbic.201700113.
Texto completoLam, Y. W., W. Ammerlaan, W. S. O, F. Kroese y D. Opstelten. "Cell Type- and Differentiation Stage-Dependent Expression of PML Domains in Rat, Detected by Monoclonal Antibody HIS55". Experimental Cell Research 221, n.º 2 (diciembre de 1995): 344–56. http://dx.doi.org/10.1006/excr.1995.1384.
Texto completoKim, Jang Hoon, Sunggun Lee, Saerom Park, Ji Soo Park, Young Ho Kim y Seo Young Yang. "Slow-Binding Inhibition of Tyrosinase by Ecklonia cava Phlorotannins". Marine Drugs 17, n.º 6 (16 de junio de 2019): 359. http://dx.doi.org/10.3390/md17060359.
Texto completoKrishnamoorthi, Ramaswamy, Chan Lan Sun Lin, Yu Xi Gong, David VanderVelde y Karl Hahn. "Proton NMR studies of Cucurbita maxima trypsin inhibitors: evidence for pH-dependent conformational change and His25-Tyr27 interaction". Biochemistry 31, n.º 3 (28 de enero de 1992): 905–10. http://dx.doi.org/10.1021/bi00118a037.
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