Статті в журналах з теми "Binding and catalysis"
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Williams, Ian H. "Catalysis: transition-state molecular recognition?" Beilstein Journal of Organic Chemistry 6 (November 3, 2010): 1026–34. http://dx.doi.org/10.3762/bjoc.6.117.
Повний текст джерелаABBADI, Amine, Monika BRUMMEL, Burkhardt S. SCHüTT, Mary B. SLABAUGH, Ricardo SCHUCH, and Friedrich SPENER. "Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein) synthase III from Cuphea wrightii embryo, a fatty acid synthase type II condensing enzyme." Biochemical Journal 345, no. 1 (December 17, 1999): 153–60. http://dx.doi.org/10.1042/bj3450153.
Повний текст джерелаKhan, Mohammad Niyaz, and Ibrahim Isah Fagge. "Kinetics and Mechanism of Cationic Micelle/Flexible Nanoparticle Catalysis: A Review." Progress in Reaction Kinetics and Mechanism 43, no. 1 (March 2018): 1–20. http://dx.doi.org/10.3184/146867818x15066862094905.
Повний текст джерелаPitson, Stuart M., Paul A. B. Moretti, Julia R. Zebol, Reza Zareie, Claudia K. Derian, Andrew L. Darrow, Jenson Qi, et al. "The Nucleotide-binding Site of Human Sphingosine Kinase 1." Journal of Biological Chemistry 277, no. 51 (October 18, 2002): 49545–53. http://dx.doi.org/10.1074/jbc.m206687200.
Повний текст джерелаBreslow, Ronald. "Bifunctional binding and catalysis." Supramolecular Chemistry 1, no. 2 (February 1993): 111–18. http://dx.doi.org/10.1080/10610279308040656.
Повний текст джерелаOliveira, Maria Teresa, and Ji-Woong Lee. "Asymmetric Cation-Binding Catalysis." ChemCatChem 9, no. 3 (January 12, 2017): 377–84. http://dx.doi.org/10.1002/cctc.201601441.
Повний текст джерелаMacMillan, Fraser, and Carola Hunte. "Quinone binding and catalysis." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1797, no. 12 (December 2010): 1841. http://dx.doi.org/10.1016/j.bbabio.2010.10.021.
Повний текст джерелаZapata-Pérez, Rubén, Fernando Gil-Ortiz, Ana Belén Martínez-Moñino, Antonio Ginés García-Saura, Jordi Juanhuix, and Álvaro Sánchez-Ferrer. "Structural and functional analysis of Oceanobacillus iheyensis macrodomain reveals a network of waters involved in substrate binding and catalysis." Open Biology 7, no. 4 (April 2017): 160327. http://dx.doi.org/10.1098/rsob.160327.
Повний текст джерелаBearne, Stephen L. "Asymmetry in catalysis: ‘unidirectional’ amino acid racemases." Biochemist 43, no. 1 (January 22, 2021): 28–34. http://dx.doi.org/10.1042/bio_2020_101.
Повний текст джерелаPusuluk, Onur, Tristan Farrow, Cemsinan Deliduman, Keith Burnett, and Vlatko Vedral. "Proton tunnelling in hydrogen bonds and its implications in an induced-fit model of enzyme catalysis." Proceedings of the Royal Society A: Mathematical, Physical and Engineering Sciences 474, no. 2218 (October 2018): 20180037. http://dx.doi.org/10.1098/rspa.2018.0037.
Повний текст джерелаHasse, Dirk, Janne Hülsemann, Gunilla H. Carlsson, Karin Valegård, and Inger Andersson. "Structure and mechanism of piperideine-6-carboxylate dehydrogenase from Streptomyces clavuligerus." Acta Crystallographica Section D Structural Biology 75, no. 12 (November 22, 2019): 1107–18. http://dx.doi.org/10.1107/s2059798319014852.
Повний текст джерелаBadarau, Adriana, Christian Damblon та Michael I. Page. "The activity of the dinuclear cobalt-β-lactamase from Bacillus cereus in catalysing the hydrolysis of β-lactams". Biochemical Journal 401, № 1 (11 грудня 2006): 197–203. http://dx.doi.org/10.1042/bj20061002.
Повний текст джерелаJadhav, Amol P., Sang Yeon Park, Ji-Woong Lee, Hailong Yan, and Choong Eui Song. "Cooperative Asymmetric Cation-Binding Catalysis." Accounts of Chemical Research 54, no. 23 (November 16, 2021): 4319–33. http://dx.doi.org/10.1021/acs.accounts.1c00400.
Повний текст джерелаHansen, David E., and Ronald T. Raines. "Binding energy and enzymatic catalysis." Journal of Chemical Education 67, no. 6 (June 1990): 483. http://dx.doi.org/10.1021/ed067p483.
Повний текст джерелаCui, Yao, Jixian Wang, Lei Yu, Ying Xu, David J. Young, Haiyan Li та Hongxi Li. "Construction of a (NNN)Ru-Incorporated Porous Organic Polymer with High Catalytic Activity for β-Alkylation of Secondary Alcohols with Primary Alcohols". Polymers 14, № 2 (7 січня 2022): 231. http://dx.doi.org/10.3390/polym14020231.
Повний текст джерелаLeslie, A. G. W., and J. E. Walker. "Structural model of F 1 –ATPase and the implications for rotary catalysis." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 355, no. 1396 (April 29, 2000): 465–71. http://dx.doi.org/10.1098/rstb.2000.0588.
Повний текст джерелаTinker, Henry R., Malavika A. Bhide, Emanuele Magliocca, Thomas S. Miller, and Caroline E. Knapp. "Synthetic tethered silver nanoparticles on reduced graphene oxide for alkaline oxygen reduction catalysis." Journal of Materials Science 56, no. 11 (January 18, 2021): 6966–76. http://dx.doi.org/10.1007/s10853-020-05711-2.
Повний текст джерелаSalgado-Polo, Fernando, and Anastassis Perrakis. "The Structural Binding Mode of the Four Autotaxin Inhibitor Types that Differentially Affect Catalytic and Non-Catalytic Functions." Cancers 11, no. 10 (October 16, 2019): 1577. http://dx.doi.org/10.3390/cancers11101577.
Повний текст джерелаLoh, Tamalette, Kenan C. Murphy, and Martin G. Marinus. "Mutational Analysis of the MutH Protein fromEscherichia coli." Journal of Biological Chemistry 276, no. 15 (December 21, 2000): 12113–19. http://dx.doi.org/10.1074/jbc.m007935200.
Повний текст джерелаCao, Liang, Le Niu, and Tim Mueller. "Computationally generated maps of surface structures and catalytic activities for alloy phase diagrams." Proceedings of the National Academy of Sciences 116, no. 44 (October 14, 2019): 22044–51. http://dx.doi.org/10.1073/pnas.1910724116.
Повний текст джерелаRaven, Emma L., Latesh Lad, Katherine H. Sharp, Martin Mewies, and Peter C. E. Moody. "Defining substrate specificity and catalytic mechanism in ascorbate peroxidase." Biochemical Society Symposia 71 (March 1, 2004): 27–38. http://dx.doi.org/10.1042/bss0710027.
Повний текст джерелаChen, Yang, Joakim Näsvall, Shiying Wu, Dan I. Andersson, and Maria Selmer. "Structure of AadA fromSalmonella enterica: a monomeric aminoglycoside (3′′)(9) adenyltransferase." Acta Crystallographica Section D Biological Crystallography 71, no. 11 (October 31, 2015): 2267–77. http://dx.doi.org/10.1107/s1399004715016429.
Повний текст джерелаLagerbäck, Pernilla, and Karin Carlson. "Amino Acid Residues in the GIY-YIG Endonuclease II of Phage T4 Affecting Sequence Recognition and Binding as Well as Catalysis." Journal of Bacteriology 190, no. 16 (June 6, 2008): 5533–44. http://dx.doi.org/10.1128/jb.00094-08.
Повний текст джерелаZhou, Yibo, Eui-Hyun Ryu, Yan Zhao, and L. Keith Woo. "Solvent-Responsive Metalloporphyrins: Binding and Catalysis." Organometallics 26, no. 2 (January 2007): 358–64. http://dx.doi.org/10.1021/om060791z.
Повний текст джерелаZhao, Chenfei, Christopher A. Sojdak, Wazo Myint, and Daniel Seidel. "Reductive Etherification via Anion-Binding Catalysis." Journal of the American Chemical Society 139, no. 30 (July 25, 2017): 10224–27. http://dx.doi.org/10.1021/jacs.7b05832.
Повний текст джерелаAttard, Jonathan, Kohei Osawa, Yong Guan, Jessica Hatt, Shin-ichi Kondo, and Anita Mattson. "Silanediol Anion Binding and Enantioselective Catalysis." Synthesis 51, no. 10 (March 12, 2019): 2107–15. http://dx.doi.org/10.1055/s-0037-1612217.
Повний текст джерелаPark, Sang Yeon, Yidong Liu, Joong Suk Oh, Yoo Kyung Kweon, Yong Bok Jeong, Mengying Duan, Yu Tan, Ji-Woong Lee, Hailong Yan, and Choong Eui Song. "Asymmetric Aminalization via Cation-Binding Catalysis." Chemistry - A European Journal 24, no. 5 (December 5, 2017): 1020–25. http://dx.doi.org/10.1002/chem.201703800.
Повний текст джерелаSchafer, Andrew G., Joshua M. Wieting, Thomas J. Fisher, and Anita E. Mattson. "Chiral Silanediols in Anion-Binding Catalysis." Angewandte Chemie 125, no. 43 (September 3, 2013): 11531–34. http://dx.doi.org/10.1002/ange.201305496.
Повний текст джерелаSchafer, Andrew G., Joshua M. Wieting, Thomas J. Fisher, and Anita E. Mattson. "Chiral Silanediols in Anion-Binding Catalysis." Angewandte Chemie International Edition 52, no. 43 (September 3, 2013): 11321–24. http://dx.doi.org/10.1002/anie.201305496.
Повний текст джерелаPATEL, Chandra N., David W. KOH, Myron K. JACOBSON, and Marcos A. OLIVEIRA. "Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: determining the PARG catalytic domain." Biochemical Journal 388, no. 2 (May 24, 2005): 493–500. http://dx.doi.org/10.1042/bj20040942.
Повний текст джерелаHIGHTOWER, Kendra E., Smita DE, Carolyn WEINBAUM, Rebecca A. SPENCE та Patrick J. CASEY. "Lysine164α of protein farnesyltransferase is important for both CaaX substrate binding and catalysis". Biochemical Journal 360, № 3 (10 грудня 2001): 625–31. http://dx.doi.org/10.1042/bj3600625.
Повний текст джерелаChen, Yan-Liang, Yun-Hao Chou, Chia-Lin Hsieh, Shean-Jaw Chiou, Tzu-Pin Wang та Chi-Ching Hwang. "Rational Engineering of 3α-Hydroxysteroid Dehydrogenase/Carbonyl Reductase for a Biomimetic Nicotinamide Mononucleotide Cofactor". Catalysts 12, № 10 (21 вересня 2022): 1094. http://dx.doi.org/10.3390/catal12101094.
Повний текст джерелаRESMINI, Marina, Sheraz GUL, Steve CARTER, Sanjiv SONKARIA, Christopher M. TOPHAM, Gerrard GALLACHER, and Keith BROCKLEHURST. "A general kinetic approach to investigation of active-site availability in macromolecular catalysts." Biochemical Journal 346, no. 1 (February 8, 2000): 117–25. http://dx.doi.org/10.1042/bj3460117.
Повний текст джерелаChen, Aochiu, Jeffrey T. Mindrebo, Tony D. Davis, Woojoo E. Kim, Yohei Katsuyama, Ziran Jiang, Yasuo Ohnishi, Joseph P. Noel, and Michael D. Burkart. "Mechanism-based cross-linking probes capture the Escherichia coli ketosynthase FabB in conformationally distinct catalytic states." Acta Crystallographica Section D Structural Biology 78, no. 9 (August 30, 2022): 1171–79. http://dx.doi.org/10.1107/s2059798322007434.
Повний текст джерелаEIS, Christian, and Bernd NIDETZKY. "Substrate-binding recognition and specificity of trehalose phosphorylase from Schizophyllum commune examined in steady-state kinetic studies with deoxy and deoxyfluoro substrate analogues and inhibitors." Biochemical Journal 363, no. 2 (April 8, 2002): 335–40. http://dx.doi.org/10.1042/bj3630335.
Повний текст джерелаALLARDYCE, Claire S., Paul D. MCDONAGH, Lu-Yun LIAN, C. Roland WOLF, and Gordon C. K. ROBERTS. "The role of tyrosine-9 and the C-terminal helix in the catalytic mechanism of Alpha-class glutathione S-transferases." Biochemical Journal 343, no. 3 (October 25, 1999): 525–31. http://dx.doi.org/10.1042/bj3430525.
Повний текст джерелаSebati, Wilhemina, and Suprakas Ray. "Advances in Nanostructured Metal-Encapsulated Porous Organic-Polymer Composites for Catalyzed Organic Chemical Synthesis." Catalysts 8, no. 11 (October 24, 2018): 492. http://dx.doi.org/10.3390/catal8110492.
Повний текст джерелаMarcus, Yehouda, Hagit Altman-Gueta, Aliza Finkler, and Michael Gurevitz. "Mutagenesis at Two Distinct Phosphate-Binding Sites Unravels Their Differential Roles in Regulation of Rubisco Activation and Catalysis." Journal of Bacteriology 187, no. 12 (June 15, 2005): 4222–28. http://dx.doi.org/10.1128/jb.187.12.4222-4228.2005.
Повний текст джерелаDo, Hackwon, Dieu Linh Nguyen, Chang Woo Lee, Min Ju Lee, Hoejung Oh, Jisub Hwang, Se Jong Han, Sung Gu Lee, and Jun Hyuck Lee. "Comparative structural insight into the unidirectional catalysis of ornithine carbamoyltransferases from Psychrobacter sp. PAMC 21119." PLOS ONE 17, no. 9 (September 23, 2022): e0274019. http://dx.doi.org/10.1371/journal.pone.0274019.
Повний текст джерелаD'AMOURS, Marc R., and Rick H. COTE. "Regulation of photoreceptor phosphodiesterase catalysis by its non-catalytic cGMP-binding sites." Biochemical Journal 340, no. 3 (June 8, 1999): 863–69. http://dx.doi.org/10.1042/bj3400863.
Повний текст джерелаMozaceanu, Cristina, Christopher G. P. Taylor, Jerico R. Piper, Stephen P. Argent, and Michael D. Ward. "Catalysis of an Aldol Condensation Using a Coordination Cage." Chemistry 2, no. 1 (January 25, 2020): 22–32. http://dx.doi.org/10.3390/chemistry2010004.
Повний текст джерелаHu, Kuan, Meng Zhao, Tianlong Zhang, Manwu Zha, Chen Zhong, Yu Jiang, and Jianping Ding. "Structures of trans-2-enoyl-CoA reductases from Clostridium acetobutylicum and Treponema denticola: insights into the substrate specificity and the catalytic mechanism." Biochemical Journal 449, no. 1 (December 7, 2012): 79–89. http://dx.doi.org/10.1042/bj20120871.
Повний текст джерелаSmith, Andrew T., and Nigel C. Veitch. "Substrate binding and catalysis in heme peroxidases." Current Opinion in Chemical Biology 2, no. 2 (April 1998): 269–78. http://dx.doi.org/10.1016/s1367-5931(98)80069-0.
Повний текст джерелаDorel, Ruth, and Ben L. Feringa. "Stereodivergent Anion Binding Catalysis with Molecular Motors." Angewandte Chemie 132, no. 2 (December 12, 2019): 795–99. http://dx.doi.org/10.1002/ange.201913054.
Повний текст джерелаGerola, Adriana P., Paulo F. A. Costa, Frank H. Quina, Haidi D. Fiedler, and Faruk Nome. "Zwitterionic surfactants in ion binding and catalysis." Current Opinion in Colloid & Interface Science 32 (November 2017): 39–47. http://dx.doi.org/10.1016/j.cocis.2017.10.002.
Повний текст джерелаDorel, Ruth, and Ben L. Feringa. "Stereodivergent Anion Binding Catalysis with Molecular Motors." Angewandte Chemie International Edition 59, no. 2 (January 7, 2020): 785–89. http://dx.doi.org/10.1002/anie.201913054.
Повний текст джерелаSOLANO, Francisco, Celia JIMÉNEZ-CERVANTES, José H. MARTÍNEZ-LIARTE, José C. GARCÍA-BORRÓN, José R. JARA, and José A. LOZANO. "Molecular mechanism for catalysis by a new zinc-enzyme, dopachrome tautomerase." Biochemical Journal 313, no. 2 (January 15, 1996): 447–53. http://dx.doi.org/10.1042/bj3130447.
Повний текст джерелаSzedlacsek, S. E., R. G. Duggleby, and M. O. Vlad. "Enzyme catalysis as a chain reaction." Biochemical Journal 279, no. 3 (November 1, 1991): 855–61. http://dx.doi.org/10.1042/bj2790855.
Повний текст джерелаKrishna, Siddarth H., Casey B. Jones, and Rajamani Gounder. "Dynamic Interconversion of Metal Active Site Ensembles in Zeolite Catalysis." Annual Review of Chemical and Biomolecular Engineering 12, no. 1 (June 7, 2021): 115–36. http://dx.doi.org/10.1146/annurev-chembioeng-092120-010920.
Повний текст джерелаBankhead, Troy M., Bernard J. Etzel, Felise Wolven, Sylvain Bordenave, Jeffrey L. Boldt, Teresa A. Larsen та Anca M. Segall. "Mutations at Residues 282, 286, and 293 of Phage λ Integrase Exert Pathway-Specific Effects on Synapsis and Catalysis in Recombination". Journal of Bacteriology 185, № 8 (15 квітня 2003): 2653–66. http://dx.doi.org/10.1128/jb.185.8.2653-2666.2003.
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