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Journal articles on the topic 'Protein engineering'

Author: Grafiati

Published: 4 June 2021

Last updated: 2 November 2024

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1

Leatherbarrow, Robin J., and Alan R. Fersht. "Protein engineering." "Protein Engineering, Design and Selection" 1, no. 1 (1986): 7–16. http://dx.doi.org/10.1093/protein/1.1.7.

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2

Wetzel, R. "What is protein engineering?" "Protein Engineering, Design and Selection" 1, no. 1 (1986): 3–5. http://dx.doi.org/10.1093/protein/1.1.3.

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3

Schwarte, Andreas, Maika Genz, Lilly Skalden, Alberto Nobili, Clare Vickers, Okke Melse, Remko Kuipers, et al. "NewProt – a protein engineering portal." Protein Engineering, Design and Selection 30, no. 6 (May 5, 2017): 441–47. http://dx.doi.org/10.1093/protein/gzx024.

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4

Harris, T. J. R. "Nordic symposium on protein engineering." "Protein Engineering, Design and Selection" 1, no. 2 (1987): 81–82. http://dx.doi.org/10.1093/protein/1.2.81.

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5

Offord, R. E. "Protein engineering by chemical means?" "Protein Engineering, Design and Selection" 1, no. 3 (1987): 151–57. http://dx.doi.org/10.1093/protein/1.3.151.

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6

Gait, Michael, Janet Thornton, and Ronald Wetzel. "Protein Engineering '87—conference report." "Protein Engineering, Design and Selection" 1, no. 4 (1987): 267–70. http://dx.doi.org/10.1093/protein/1.4.267.

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7

Wood, EJ. "Introduction to proteins and protein engineering." Biochemical Education 16, no. 1 (January 1988): 52. http://dx.doi.org/10.1016/0307-4412(88)90036-2.

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8

Scott, Daniel J., Lutz Kummer, Dirk Tremmel, and Andreas Plückthun. "Stabilizing membrane proteins through protein engineering." Current Opinion in Chemical Biology 17, no. 3 (June 2013): 427–35. http://dx.doi.org/10.1016/j.cbpa.2013.04.002.

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9

Cavazza, M. "Introduction to proteins and protein engineering." Biochimie 69, no. 8 (August 1987): 905–6. http://dx.doi.org/10.1016/0300-9084(87)90221-5.

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10

Lluis, M. W., J. I. Godfroy, and H. Yin. "Protein engineering methods applied to membrane protein targets." Protein Engineering Design and Selection 26, no. 2 (October 31, 2012): 91–100. http://dx.doi.org/10.1093/protein/gzs079.

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11

HIRAYAMA, Noriaki. "Protein engineering." Nihon Kessho Gakkaishi 27, no. 5 (1985): 344–49. http://dx.doi.org/10.5940/jcrsj.27.344.

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12

Kornelyuk, A. I. "Protein engineering." Biopolymers and Cell 17, no. 6 (November 20, 2001): 459–66. http://dx.doi.org/10.7124/bc.0005d5.

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13

de Vos, AbrahamM, and Andreas Plückthun. "Protein engineering." Current Opinion in Biotechnology 7, no. 4 (August 1996): 367–68. http://dx.doi.org/10.1016/s0958-1669(96)80109-1.

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14

Davies, Martin J. "Protein engineering." Trends in Biotechnology 19, no. 11 (November 2001): 437. http://dx.doi.org/10.1016/s0167-7799(01)01856-x.

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15

BORMAN, STU. "PROTEIN ENGINEERING." Chemical & Engineering News 72, no. 45 (November 7, 1994): 4–5. http://dx.doi.org/10.1021/cen-v072n045.p004.

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16

Brinkmann, Ulrich. "Protein engineering." Molecular Medicine Today 3, no. 5 (May 1997): 195. http://dx.doi.org/10.1016/s1357-4310(97)01014-9.

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17

Chamberlin, Richard. "Protein Engineering." Tetrahedron 56, no. 48 (November 2000): ix. http://dx.doi.org/10.1016/s0040-4020(00)00901-7.

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18

Keen, Jeff. "Protein Engineering." Biochemical Education 19, no. 3 (July 1991): 159–60. http://dx.doi.org/10.1016/0307-4412(91)90071-f.

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19

Pain, Roger H. "Protein engineering." Trends in Biochemical Sciences 13, no. 5 (May 1988): 191–92. http://dx.doi.org/10.1016/0968-0004(88)90153-3.

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20

Fersht, Alan, and Greg Winter. "Protein engineering." Trends in Biochemical Sciences 17, no. 8 (August 1992): 292–94. http://dx.doi.org/10.1016/0968-0004(92)90438-f.

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21

Bryan, Philip N. "Protein engineering." Biotechnology Advances 5, no. 2 (January 1987): 221–24. http://dx.doi.org/10.1016/0734-9750(87)90319-3.

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22

Freedman, Robert B., and Ronald Wetzel. "Protein engineering." Current Opinion in Biotechnology 3, no. 4 (August 1992): 323–25. http://dx.doi.org/10.1016/0958-1669(92)90158-f.

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23

Thornton, JanetM, and JeremyM Berg. "Protein engineering." Current Opinion in Biotechnology 6, no. 4 (January 1995): 367–69. http://dx.doi.org/10.1016/0958-1669(95)80063-8.

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24

Just, Wilhelm. "Protein Engineering." FEBS Letters 588, no. 2 (December 7, 2013): 205. http://dx.doi.org/10.1016/j.febslet.2013.12.001.

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25

Sims, Paul F. G. "Protein engineering." Yeast 4, no. 2 (June 1988): 155. http://dx.doi.org/10.1002/yea.320040210.

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26

Sawyer, Lindsay. "Protein Engineering." International Journal of Biological Macromolecules 10, no. 6 (December 1988): 378. http://dx.doi.org/10.1016/0141-8130(88)90033-5.

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27

Doran, Heather. "Protein engineering." Biochemist 45, no. 1 (March 10, 2023): 1. http://dx.doi.org/10.1042/bio_2023_105.

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28

Shorter, James. "Engineering therapeutic protein disaggregases." Molecular Biology of the Cell 27, no. 10 (May 15, 2016): 1556–60. http://dx.doi.org/10.1091/mbc.e15-10-0693.

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Abstract:

Therapeutic agents are urgently required to cure several common and fatal neurodegenerative disorders caused by protein misfolding and aggregation, including amyotrophic lateral sclerosis (ALS), Parkinson’s disease (PD), and Alzheimer’s disease (AD). Protein disaggregases that reverse protein misfolding and restore proteins to native structure, function, and localization could mitigate neurodegeneration by simultaneously reversing 1) any toxic gain of function of the misfolded form and 2) any loss of function due to misfolding. Potentiated variants of Hsp104, a hexameric AAA+ ATPase and protein disaggregase from yeast, have been engineered to robustly disaggregate misfolded proteins connected with ALS (e.g., TDP-43 and FUS) and PD (e.g., α-synuclein). However, Hsp104 has no metazoan homologue. Metazoa possess protein disaggregase systems distinct from Hsp104, including Hsp110, Hsp70, and Hsp40, as well as HtrA1, which might be harnessed to reverse deleterious protein misfolding. Nevertheless, vicissitudes of aging, environment, or genetics conspire to negate these disaggregase systems in neurodegenerative disease. Thus, engineering potentiated human protein disaggregases or isolating small-molecule enhancers of their activity could yield transformative therapeutics for ALS, PD, and AD.

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29

Evans, TJ. "Protein Structure and Protein Engineering." Biochemical Education 17, no. 4 (October 1989): 219–20. http://dx.doi.org/10.1016/0307-4412(89)90163-5.

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30

Mateu, M. G. "Virus engineering: functionalization and stabilization." Protein Engineering Design and Selection 24, no. 1-2 (October 5, 2010): 53–63. http://dx.doi.org/10.1093/protein/gzq069.

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31

Huston, J. S. "Broadening horizons of antibody engineering." Protein Engineering Design and Selection 24, no. 9 (August 23, 2011): 631–32. http://dx.doi.org/10.1093/protein/gzr040.

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32

Ostermeier, Marc. "Engineering allosteric protein switches by domain insertion." Protein Engineering, Design and Selection 18, no. 8 (July 25, 2005): 359–64. http://dx.doi.org/10.1093/protein/gzi048.

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33

DiTursi, M. K., S. J. Kwon, P. J. Reeder, and J. S. Dordick. "Bioinformatics-driven, rational engineering of protein thermostability." Protein Engineering Design and Selection 19, no. 11 (September 2, 2006): 517–24. http://dx.doi.org/10.1093/protein/gzl039.

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34

Daggett, V. "Shedding light on amyloidosis with protein engineering." Protein Engineering Design and Selection 22, no. 8 (July 31, 2009): 445. http://dx.doi.org/10.1093/protein/gzp049.

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35

Rawlings, Andrea E. "Membrane protein engineering to the rescue." Biochemical Society Transactions 46, no. 6 (October 31, 2018): 1541–49. http://dx.doi.org/10.1042/bst20180140.

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Abstract:

The inherent hydrophobicity of membrane proteins is a major barrier to membrane protein research and understanding. Their low stability and solubility in aqueous environments coupled with poor expression levels make them a challenging area of research. For many years, the only way of working with membrane proteins was to optimise the environment to suit the protein, through the use of different detergents, solubilising additives, and other adaptations. However, with innovative protein engineering methodologies, the membrane proteins themselves are now being adapted to suit the environment. This mini-review looks at the types of adaptations which are applied to membrane proteins from a variety of different fields, including water solubilising fusion tags, thermostabilising mutation screening, scaffold proteins, stabilising protein chimeras, and isolating water-soluble domains.

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36

MORIYAMA, Hideaki, and Hirosuke OKADA. "Genetic engineering for protein engineering." Nihon Kessho Gakkaishi 29, no. 1 (1987): 14–26. http://dx.doi.org/10.5940/jcrsj.29.14.

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37

Zheng, Ping, and Jibin Sun. "Protein engineering for strain engineering." New Biotechnology 31 (July 2014): S163. http://dx.doi.org/10.1016/j.nbt.2014.05.2024.

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38

Im, H., M. J. Ryu, and M. H. Yu. "Engineering thermostability in serine protease inhibitors." Protein Engineering Design and Selection 17, no. 4 (May 4, 2004): 325–31. http://dx.doi.org/10.1093/protein/gzh036.

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39

Huston, J. S. "Engineering antibodies for the 21st century." Protein Engineering Design and Selection 25, no. 10 (September 17, 2012): 483–84. http://dx.doi.org/10.1093/protein/gzs069.

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40

Liu, W. C., Y. S. Lin, W. Y. Jeng, J. H. Chen, A. H. J. Wang, and L. F. Shyur. "Engineering of dual-functional hybrid glucanases." Protein Engineering Design and Selection 25, no. 11 (October 18, 2012): 771–80. http://dx.doi.org/10.1093/protein/gzs083.

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41

Dandekar, Thomas, and Patrick Argos. "Potential of genetic algorithms in protein folding and protein engineering simulations." "Protein Engineering, Design and Selection" 5, no. 7 (1992): 637–45. http://dx.doi.org/10.1093/protein/5.7.637.

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42

Modarres, H. Pezeshgi, M. R. Mofrad, and A. Sanati-Nezhad. "Protein thermostability engineering." RSC Advances 6, no. 116 (2016): 115252–70. http://dx.doi.org/10.1039/c6ra16992a.

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43

Rusk, Nicole. "Protein circuit engineering." Nature Methods 15, no. 11 (October 30, 2018): 860. http://dx.doi.org/10.1038/s41592-018-0201-1.

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44

Hellinga, H. W. "Computational protein engineering." Nature Structural Biology 5, no. 7 (July 1998): 525–27. http://dx.doi.org/10.1038/776.

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45

MINGARRO, I., G. VONHEIJNE, and P. WHITLEY. "Membrane-protein engineering." Trends in Biotechnology 15, no. 10 (October 1997): 432–37. http://dx.doi.org/10.1016/s0167-7799(97)01101-3.

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46

Hollfelder, Florian, and Stefan Lutz. "Just (protein) engineering?" Current Opinion in Structural Biology 23, no. 4 (August 2013): 569–70. http://dx.doi.org/10.1016/j.sbi.2013.07.003.

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47

Bushuk, Walter. "Plant protein engineering." Trends in Food Science & Technology 4, no. 6 (June 1993): 197–98. http://dx.doi.org/10.1016/0924-2244(93)90129-x.

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48

Feng, Jianwen A., Lee A. Tessler, and Garland R. Marshall. "Chimeric Protein Engineering." International Journal of Peptide Research and Therapeutics 13, no. 1-2 (January 11, 2007): 151–60. http://dx.doi.org/10.1007/s10989-006-9058-8.

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49

Nagayama, Kuniaki. "Protein array engineering." Supramolecular Science 3, no. 1-3 (March 1996): 111–22. http://dx.doi.org/10.1016/0968-5677(96)00033-8.

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50

Svendsen, Allan. "Lipase protein engineering." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1543, no. 2 (December 2000): 223–38. http://dx.doi.org/10.1016/s0167-4838(00)00239-9.

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