Статті в журналах з теми "Substrate-binding proteins"
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Berntsson, Ronnie P. A., Sander H. J. Smits, Lutz Schmitt, Dirk-Jan Slotboom, and Bert Poolman. "A structural classification of substrate-binding proteins." FEBS Letters 584, no. 12 (April 20, 2010): 2606–17. http://dx.doi.org/10.1016/j.febslet.2010.04.043.
Повний текст джерелаScheepers, Giel H., Jelger A. Lycklama a Nijeholt, and Bert Poolman. "An updated structural classification of substrate-binding proteins." FEBS Letters 590, no. 23 (October 23, 2016): 4393–401. http://dx.doi.org/10.1002/1873-3468.12445.
Повний текст джерелаManjeet, Kaur, Pallinti Purushotham, Chilukoti Neeraja, and Appa Rao Podile. "Bacterial chitin binding proteins show differential substrate binding and synergy with chitinases." Microbiological Research 168, no. 7 (August 2013): 461–68. http://dx.doi.org/10.1016/j.micres.2013.01.006.
Повний текст джерелаM. Counago, Rafael, Christopher A. McDevitt, Miranda P. Ween, and Bostjan Kobe. "Prokaryotic Substrate-Binding Proteins as Targets for Antimicrobial Therapies." Current Drug Targets 13, no. 11 (August 1, 2012): 1400–1410. http://dx.doi.org/10.2174/138945012803530170.
Повний текст джерелаRicharme, Gilbert, and Teresa Dantas Caldas. "Chaperone Properties of the Bacterial Periplasmic Substrate-binding Proteins." Journal of Biological Chemistry 272, no. 25 (June 20, 1997): 15607–12. http://dx.doi.org/10.1074/jbc.272.25.15607.
Повний текст джерелаSpooner, Paul J. R., W. John O’Reilly, Steven W. Homans, Nicholas G. Rutherford, Peter J. F. Henderson, and Anthony Watts. "Weak Substrate Binding to Transport Proteins Studied by NMR." Biophysical Journal 75, no. 6 (December 1998): 2794–800. http://dx.doi.org/10.1016/s0006-3495(98)77722-7.
Повний текст джерелаPratt, R. F. "Substrate specificity of bacterial DD-peptidases (penicillin-binding proteins)." Cellular and Molecular Life Sciences 65, no. 14 (April 14, 2008): 2138–55. http://dx.doi.org/10.1007/s00018-008-7591-7.
Повний текст джерелаAltenberg, Guillermo A. "The Engine of ABC Proteins." Physiology 18, no. 5 (October 2003): 191–95. http://dx.doi.org/10.1152/nips.01445.2003.
Повний текст джерелаSchimpl, Marianne, Alexander W. Schüttelkopf, Vladimir S. Borodkin, and Daan M. F. van Aalten. "Human OGA binds substrates in a conserved peptide recognition groove." Biochemical Journal 432, no. 1 (October 25, 2010): 1–12. http://dx.doi.org/10.1042/bj20101338.
Повний текст джерелаMoutsita, R., J. Botti, MA Doyennette-Moyne, M. Aubery, and P. Codogno. "Cell spreading on laminin substrate involves Con A-binding proteins." Reproduction Nutrition Développement 30, no. 3 (1990): 397–401. http://dx.doi.org/10.1051/rnd:19900312.
Повний текст джерелаVuković, Lela, Hye Ran Koh, Sua Myong, and Klaus Schulten. "Substrate Recognition and Specificity of Double-Stranded RNA Binding Proteins." Biochemistry 53, no. 21 (May 21, 2014): 3457–66. http://dx.doi.org/10.1021/bi500352s.
Повний текст джерелаFarr, George W., Krystyna Furtak, Matthew B. Rowland, Neil A. Ranson, Helen R. Saibil, Tomas Kirchhausen, and Arthur L. Horwich. "Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL." Cell 100, no. 5 (March 2000): 561–73. http://dx.doi.org/10.1016/s0092-8674(00)80692-3.
Повний текст джерелаFischer, Marcus, Qian Yi Zhang, Roderick E. Hubbard, and Gavin H. Thomas. "Caught in a TRAP: substrate-binding proteins in secondary transport." Trends in Microbiology 18, no. 10 (October 2010): 471–78. http://dx.doi.org/10.1016/j.tim.2010.06.009.
Повний текст джерелаVukovic, Lela, Hye Ran Koh, Sua Myong, and Klaus Schulten. "Substrate Recognition and Specificity of Double-Stranded RNA Binding Proteins." Biophysical Journal 106, no. 2 (January 2014): 22a. http://dx.doi.org/10.1016/j.bpj.2013.11.175.
Повний текст джерелаKhanra, Nandish, Paolo Rossi, Anastassios Economou, and Charalampos G. Kalodimos. "Recognition and targeting mechanisms by chaperones in flagellum assembly and operation." Proceedings of the National Academy of Sciences 113, no. 35 (August 15, 2016): 9798–803. http://dx.doi.org/10.1073/pnas.1607845113.
Повний текст джерелаRosenzweig, Rina, Patrick Farber, Algirdas Velyvis, Enrico Rennella, Michael P. Latham, and Lewis E. Kay. "ClpB N-terminal domain plays a regulatory role in protein disaggregation." Proceedings of the National Academy of Sciences 112, no. 50 (November 30, 2015): E6872—E6881. http://dx.doi.org/10.1073/pnas.1512783112.
Повний текст джерелаRANSON, Neil A., Helen E. WHITE, and Helen R. SAIBIL. "Chaperonins." Biochemical Journal 333, no. 2 (July 15, 1998): 233–42. http://dx.doi.org/10.1042/bj3330233.
Повний текст джерелаGebauer, Mathias, Matthias Zeiner, and Ulrich Gehring. "Interference between Proteins Hap46 and Hop/p60, Which Bind to Different Domains of the Molecular Chaperone hsp70/hsc70." Molecular and Cellular Biology 18, no. 11 (November 1, 1998): 6238–44. http://dx.doi.org/10.1128/mcb.18.11.6238.
Повний текст джерелаIbarra, Rebeca, Heather R. Borror, Bryce Hart, Richard G. Gardner, and Gary Kleiger. "The San1 Ubiquitin Ligase Avidly Recognizes Misfolded Proteins through Multiple Substrate Binding Sites." Biomolecules 11, no. 11 (November 2, 2021): 1619. http://dx.doi.org/10.3390/biom11111619.
Повний текст джерелаWang, Xing-Guo, J. Michael Kidder, Joanna P. Scagliotti, Mark S. Klempner, Richard Noring, and Linden T. Hu. "Analysis of Differences in the Functional Properties of the Substrate Binding Proteins of the Borrelia burgdorferi Oligopeptide Permease (opp) Operon." Journal of Bacteriology 186, no. 1 (January 1, 2004): 51–60. http://dx.doi.org/10.1128/jb.186.1.51-60.2004.
Повний текст джерелаKhrenova, M. G., I. V. Polyakov, and A. V. Nemukhin. "Molecular Dynamics of Enzyme-Substrate Complexes in Guanosine Trifosphate-Binding Proteins." Russian Journal of Physical Chemistry B 16, no. 3 (June 2022): 455–60. http://dx.doi.org/10.1134/s1990793122030174.
Повний текст джерелаDurrani, Mehvish K., and Jonghoon Kang. "Thermodynamic analysis of the binding of p38 MAPK to substrate proteins." Journal of Biological Chemistry 295, no. 5 (January 2020): 1366. http://dx.doi.org/10.1016/s0021-9258(17)49892-9.
Повний текст джерелаDaleke, David. "Substrate Specificity of the Aminophospholipid Flippase and Other Phosphatidylserine Binding Proteins." Biophysical Journal 98, no. 3 (January 2010): 507a. http://dx.doi.org/10.1016/j.bpj.2009.12.2758.
Повний текст джерелаDurrani, Mehvish K., and Jonghoon Kang. "Thermodynamic analysis of the binding of p38 MAPK to substrate proteins." Journal of Biological Chemistry 295, no. 5 (January 31, 2020): 1366. http://dx.doi.org/10.1074/jbc.l119.011911.
Повний текст джерелаKishimoto, Ayaka, Kenji Takagi, Tsunehiro Mizushima, Keisuke Sakurai, Katsuyoshi Harada, Takashi Hayashi, and Hideo Shimada. "1P095 Substrate access to slow substrate binding P450cam with mutation at the proposed gate for water egress/ingress from/to the active site(02. Heme proteins,Poster)." Seibutsu Butsuri 53, supplement1-2 (2013): S121. http://dx.doi.org/10.2142/biophys.53.s121_5.
Повний текст джерелаHoury, Walid A. "Mechanism of substrate recognition by the chaperonin GroEL." Biochemistry and Cell Biology 79, no. 5 (October 1, 2001): 569–77. http://dx.doi.org/10.1139/o01-131.
Повний текст джерелаGao, Forson, Amy E. Danson, Fuzhou Ye, Milija Jovanovic, Martin Buck, and Xiaodong Zhang. "Bacterial Enhancer Binding Proteins—AAA+ Proteins in Transcription Activation." Biomolecules 10, no. 3 (February 25, 2020): 351. http://dx.doi.org/10.3390/biom10030351.
Повний текст джерелаLiebl, Martina P., and Thorsten Hoppe. "It's all about talking: two-way communication between proteasomal and lysosomal degradation pathways via ubiquitin." American Journal of Physiology-Cell Physiology 311, no. 2 (August 1, 2016): C166—C178. http://dx.doi.org/10.1152/ajpcell.00074.2016.
Повний текст джерелаRoston, Rebecca L., Jinpeng Gao, Monika W. Murcha, James Whelan, and Christoph Benning. "TGD1, -2, and -3 Proteins Involved in Lipid Trafficking Form ATP-binding Cassette (ABC) Transporter with Multiple Substrate-binding Proteins." Journal of Biological Chemistry 287, no. 25 (April 27, 2012): 21406–15. http://dx.doi.org/10.1074/jbc.m112.370213.
Повний текст джерелаFritz, Jutta, Alexander Strehblow, Andreas Taschner, Sandy Schopoff, Pawel Pasierbek, and Michael F. Jantsch. "RNA-Regulated Interaction of Transportin-1 and Exportin-5 with the Double-Stranded RNA-Binding Domain Regulates Nucleocytoplasmic Shuttling of ADAR1." Molecular and Cellular Biology 29, no. 6 (January 5, 2009): 1487–97. http://dx.doi.org/10.1128/mcb.01519-08.
Повний текст джерелаRaj, Nixon, Timothy H. Click, Haw Yang, and Jhih-Wei Chu. "Structure-mechanics statistical learning uncovers mechanical relay in proteins." Chemical Science 13, no. 13 (2022): 3688–96. http://dx.doi.org/10.1039/d1sc06184d.
Повний текст джерелаSen, Liu, and Xiao Hong Ma. "Binding as a Rate-Limiting Step for Substrate Recognition of ADAM17." Advanced Materials Research 717 (July 2013): 244–48. http://dx.doi.org/10.4028/www.scientific.net/amr.717.244.
Повний текст джерелаSekhar, Ashok, Rina Rosenzweig, Guillaume Bouvignies, and Lewis E. Kay. "Hsp70 biases the folding pathways of client proteins." Proceedings of the National Academy of Sciences 113, no. 20 (May 2, 2016): E2794—E2801. http://dx.doi.org/10.1073/pnas.1601846113.
Повний текст джерелаIGARASHI, Kazuei, and Keiko KASHIWAGI. "Polyamine transport in bacteria and yeast." Biochemical Journal 344, no. 3 (December 8, 1999): 633–42. http://dx.doi.org/10.1042/bj3440633.
Повний текст джерелаSAYED, Yasien, Judith A. T. HORNBY, Marimar LOPEZ, and Heini DIRR. "Thermodynamics of the ligandin function of human class Alpha glutathione transferase A1-1: energetics of organic anion ligand binding." Biochemical Journal 363, no. 2 (April 8, 2002): 341–46. http://dx.doi.org/10.1042/bj3630341.
Повний текст джерелаYu, Qian, Hong Chen, Yanxia Zhang, Lin Yuan, Tieliang Zhao, Xin Li, and Hongwei Wang. "pH-Reversible, High-Capacity Binding of Proteins on a Substrate with Nanostructure." Langmuir 26, no. 23 (December 7, 2010): 17812–15. http://dx.doi.org/10.1021/la103647s.
Повний текст джерелаShukla, Shantanu, Khushboo Bafna, Caeley Gullett, Dean A. A. Myles, Pratul K. Agarwal, and Matthew J. Cuneo. "Differential Substrate Recognition by Maltose Binding Proteins Influenced by Structure and Dynamics." Biochemistry 57, no. 40 (September 11, 2018): 5864–76. http://dx.doi.org/10.1021/acs.biochem.8b00783.
Повний текст джерелаLebreton, B., P. V. Prasad, M. Jayaram, and P. Youderian. "Mutations that improve the binding of yeast FLP recombinase to its substrate." Genetics 118, no. 3 (March 1, 1988): 393–400. http://dx.doi.org/10.1093/genetics/118.3.393.
Повний текст джерелаJaya, Nomalie, Victor Garcia, and Elizabeth Vierling. "Substrate binding site flexibility of the small heat shock protein molecular chaperones." Proceedings of the National Academy of Sciences 106, no. 37 (August 26, 2009): 15604–9. http://dx.doi.org/10.1073/pnas.0902177106.
Повний текст джерелаGraef, Martin, Georgeta Seewald, and Thomas Langer. "Substrate Recognition by AAA+ ATPases: Distinct Substrate Binding Modes in ATP-Dependent Protease Yme1 of the Mitochondrial Intermembrane Space." Molecular and Cellular Biology 27, no. 7 (January 29, 2007): 2476–85. http://dx.doi.org/10.1128/mcb.01721-06.
Повний текст джерелаSwain, Joanna F., Renuka Sivendran, and Lila M. Gierasch. "Defining the structure of the substrate-free state of the DnaK molecular chaperone." Biochemical Society Symposia 68 (August 1, 2001): 69–82. http://dx.doi.org/10.1042/bss0680069.
Повний текст джерелаMiyata, Hidefumi, Kazuhiro Yumoto, Kanako Itoh, Miki Sasahara, Hiroki Kawaura, Nobuyuki Oshima, Taiho Shuzuki, Shunsuke Takahashi, Masahiko Oshige, and Shinji Katsura. "Immobilization of His-Tagged Proteins through Interaction with L-Cysteine Electrodeposited on Modified Gold Surfaces." Key Engineering Materials 596 (December 2013): 219–23. http://dx.doi.org/10.4028/www.scientific.net/kem.596.219.
Повний текст джерелаArana, Maite Rocío, and Guillermo Alejandro Altenberg. "ATP-binding Cassette Exporters: Structure and Mechanism with a Focus on P-glycoprotein and MRP1." Current Medicinal Chemistry 26, no. 7 (May 14, 2019): 1062–78. http://dx.doi.org/10.2174/0929867324666171012105143.
Повний текст джерелаPutman, Monique, Hendrik W. van Veen, and Wil N. Konings. "Molecular Properties of Bacterial Multidrug Transporters." Microbiology and Molecular Biology Reviews 64, no. 4 (December 1, 2000): 672–93. http://dx.doi.org/10.1128/mmbr.64.4.672-693.2000.
Повний текст джерелаMaekawa, Masashi, and Shigeki Higashiyama. "The Roles of SPOP in DNA Damage Response and DNA Replication." International Journal of Molecular Sciences 21, no. 19 (October 2, 2020): 7293. http://dx.doi.org/10.3390/ijms21197293.
Повний текст джерелаHarada, Ryuhei, Yu Takano, Takeshi Baba, and Yasuteru Shigeta. "Simple, yet powerful methodologies for conformational sampling of proteins." Physical Chemistry Chemical Physics 17, no. 9 (2015): 6155–73. http://dx.doi.org/10.1039/c4cp05262e.
Повний текст джерелаBolduc, David M., Daniel R. Montagna, Yongli Gu, Dennis J. Selkoe та Michael S. Wolfe. "Nicastrin functions to sterically hinder γ-secretase–substrate interactions driven by substrate transmembrane domain". Proceedings of the National Academy of Sciences 113, № 5 (22 грудня 2015): E509—E518. http://dx.doi.org/10.1073/pnas.1512952113.
Повний текст джерелаBRIX, Lulu A., Ronald G. DUGGLEBY, Andrea GAEDIGK, and Michael E. McMANUS. "Structural characterization of human aryl sulphotransferases." Biochemical Journal 337, no. 2 (January 8, 1999): 337–43. http://dx.doi.org/10.1042/bj3370337.
Повний текст джерелаGorelik, Maryna, Stephen Orlicky, Maria A. Sartori, Xiaojing Tang, Edyta Marcon, Igor Kurinov, Jack F. Greenblatt, et al. "Inhibition of SCF ubiquitin ligases by engineered ubiquitin variants that target the Cul1 binding site on the Skp1–F-box interface." Proceedings of the National Academy of Sciences 113, no. 13 (March 14, 2016): 3527–32. http://dx.doi.org/10.1073/pnas.1519389113.
Повний текст джерелаMORILLAS, Manuel, Colin E. McVEY, James A. BRANNIGAN, Andreas G. LADURNER, Larry J. FORNEY, and Richard VIRDEN. "Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding." Biochemical Journal 371, no. 1 (April 1, 2003): 143–50. http://dx.doi.org/10.1042/bj20021383.
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