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Articles de revues sur le sujet « Proteins Synthesis »

Auteur : Grafiati

Publié le 4 juin 2021

Mis à jour le 30 juillet 2024

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1

Nilsson, Bradley L., Matthew B. Soellner, and Ronald T. Raines. "Chemical Synthesis of Proteins." Annual Review of Biophysics and Biomolecular Structure 34, no. 1 (June 2005): 91–118. http://dx.doi.org/10.1146/annurev.biophys.34.040204.144700.

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Gibney, Brian R., Francesc Rabanal, and P. Leslie Dutton. "Synthesis of novel proteins." Current Opinion in Chemical Biology 1, no. 4 (December 1997): 537–42. http://dx.doi.org/10.1016/s1367-5931(97)80050-6.

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3

Mejuch, Tom, and Herbert Waldmann. "Synthesis of Lipidated Proteins." Bioconjugate Chemistry 27, no. 8 (August 2016): 1771–83. http://dx.doi.org/10.1021/acs.bioconjchem.6b00261.

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4

Borgia, Jeffrey A., and Gregg B. Fields. "Chemical synthesis of proteins." Trends in Biotechnology 18, no. 6 (June 2000): 243–51. http://dx.doi.org/10.1016/s0167-7799(00)01445-1.

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5

Hilvert, Donald. "Chemical synthesis of proteins." Chemistry & Biology 1, no. 4 (December 1994): 201–3. http://dx.doi.org/10.1016/1074-5521(94)90011-6.

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6

Plocinski, P., N. Arora, K. Sarva, E. Blaszczyk, H. Qin, N. Das, R. Plocinska, et al. "Mycobacterium tuberculosis CwsA Interacts with CrgA and Wag31, and the CrgA-CwsA Complex Is Involved in Peptidoglycan Synthesis and Cell Shape Determination." Journal of Bacteriology 194, no. 23 (September 21, 2012): 6398–409. http://dx.doi.org/10.1128/jb.01005-12.

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ABSTRACTBacterial cell division and cell wall synthesis are highly coordinated processes involving multiple proteins. Here, we show that Rv0008c, a novel small membrane protein fromMycobacterium tuberculosis, localizes to the poles and on membranes and shows an overall punctate localization throughout the cell. Furthermore, Rv0008c interacts with two proteins, CrgA and Wag31, implicated in peptidoglycan (PG) synthesis in mycobacteria. Deletion of the Rv0008c homolog inM. smegmatis, MSMEG_0023, caused bulged cell poles, formation of rounded cells, and defects in polar localization of Wag31 and

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7

Kohen, Amnon, Priyanka Singh, and Qi Guo. "Chemoenzymatic Synthesis of Ubiquitous Biological Redox Cofactors." Synlett 28, no. 10 (April 10, 2017): 1151–59. http://dx.doi.org/10.1055/s-0036-1588768.

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Redox cofactors are utilized by a myriad of proteins, ranging from metabolic enzymes to those performing post-translational modifications. Labeled redox cofactors have served as a vital tool for a broad range of studies. This account describes chemoenzymatic syntheses of the isotopically labeled, biologically important redox cofactors: nicotinamide adenine dinucleotide, methylene tetrahydrofolate, and flavin nucleotides. An overview of the general strategy is presented. These examples demonstrate the utility of enzymatic synthesis.1 Introduction2 Nicotinamide Cofactors2.1 Synthesis of Remote-L

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8

Metanis, Norman, Reem Mousa, and Post Reddy. "Chemical Protein Synthesis through Selenocysteine Chemistry." Synlett 28, no. 12 (March 21, 2017): 1389–93. http://dx.doi.org/10.1055/s-0036-1588762.

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Methods for the preparation of small-to-medium-sized proteins by chemical protein synthesis have matured in recent years and proven valuable for protein science. Thanks to the many recent discoveries and developments in the field, proteins up to 300 amino acids can now be prepared in the lab in a matter of days. This technology gives the scientists the flexibility to substitute any atom in the protein sequence; hence synthesis is not constrained to the 20 canonical amino acids. In this Synpacts article we briefly highlight the recent studies on selenocysteine chemistry in the field of chemical

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9

Whyte, Lyle G., and William E. Inniss. "Cold shock proteins and cold acclimation proteins in a psychrotrophic bacterium." Canadian Journal of Microbiology 38, no. 12 (December 1, 1992): 1281–85. http://dx.doi.org/10.1139/m92-211.

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The synthesis of proteins in the psychrotrophic bacterium Bacillus psychrophilus in response to both cold shock and continuous growth at low temperatures was examined. Cold shocks of 20 to 0, 5, or 10 °C resulted in the induction of nine, seven, and five cold shock proteins, respectively, as determined by 2-dimensional gel electrophoresis and computing scanning laser densitometry. Two cold shock proteins, with molecular masses of 61 and 34 kDa, which were induced in B. psychrophilus by cold shocks of 20 to 0 or 5 °C, were not induced in a cold-sensitive mutant of B. psychrophilus. Analysis of

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10

Kent, Stephen B. H. "Total chemical synthesis of proteins." Chem. Soc. Rev. 38, no. 2 (2009): 338–51. http://dx.doi.org/10.1039/b700141j.

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11

Tam, James P., and Clarence T. T. Wong. "Chemical Synthesis of Circular Proteins." Journal of Biological Chemistry 287, no. 32 (June 14, 2012): 27020–25. http://dx.doi.org/10.1074/jbc.r111.323568.

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12

Muir, Tom W., and Stephen B. H. Kent. "The chemical synthesis of proteins." Current Opinion in Biotechnology 4, no. 4 (August 1993): 420–27. http://dx.doi.org/10.1016/0958-1669(93)90007-j.

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13

Huang, Yichao, and Lei Liu. "Chemical synthesis of crystalline proteins." Science China Chemistry 58, no. 12 (July 8, 2015): 1779–81. http://dx.doi.org/10.1007/s11426-015-5462-2.

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14

Sakakibara, Shumpei. "Editorial: Chemical synthesis of proteins." Biopolymers 51, no. 4 (1999): 245–46. http://dx.doi.org/10.1002/(sici)1097-0282(1999)51:4<245::aid-bip1>3.0.co;2-4.

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15

Merrifield, Bruce. "The chemical synthesis of proteins." Protein Science 5, no. 9 (September 1996): 1947–51. http://dx.doi.org/10.1002/pro.5560050925.

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16

Huang, Yi-Chao, Ge-Min Fang, and Lei Liu. "Chemical synthesis of proteins using hydrazide intermediates." National Science Review 3, no. 1 (November 9, 2015): 107–16. http://dx.doi.org/10.1093/nsr/nwv072.

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Abstract Protein chemical synthesis offers useful and otherwise-difficulty-to-obtain biomacromolecules for biological and pharmaceutical studies. Recently, the hydrazide chemistry has drawn attentions in this field as peptide or protein hydrazides can be used as key intermediates for different synthesis and modification purposes. Besides being a traditional bioorthogonal chemical handle, a hydrazide group can serve as a readily accessible precursor of a thioester. This strategy significantly improves the efficiency and scope of native chemical ligation for protein chemical synthesis. Here we r

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17

Austen, Brian M., Joseph M. Sheridan, Omar M. A. El-Agnaf, Hazel Goodwin, and Emma R. Frears. "Improved solid-phase syntheses of amyloid proteins associated with neurodegenerative diseases." Protein & Peptide Letters 7, no. 1 (February 2000): 1–8. http://dx.doi.org/10.2174/092986650701221205144944.

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P-Amyloid protein, the a-synuclein fragment NAC, and protease-resistant forms of prion proteins are found deposited in the pathological lesions associated with neurodegenerative disease. Chemical syntheses of these proteins are notoriously difficult due to aggregation of the peptides on the resin during synthesis. We report optimised solid-phase syntheses of several amyloid peptides in high yield and >90% initial purity.

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18

Chakraborty, Asit Kumar. "Multi-Alignment Comparison of Coronavirus Non-Structural Proteins Nsp13- Nsp16 with Ribosomal Proteins and other DNA/RNA Modifying Enzymes Suggested their Roles in the Regulation of Host Protein Synthesis." International Journal of Clinical & Medical Informatics 3, no. 1 (June 1, 2020): 7–19. http://dx.doi.org/10.46619/ijcmi.2020.1024.

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19

Vallée, Yannick, and Sparta Youssef-Saliba. "Sulfur Amino Acids: From Prebiotic Chemistry to Biology and Vice Versa." Synthesis 53, no. 16 (April 1, 2021): 2798–808. http://dx.doi.org/10.1055/a-1472-7914.

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AbstractTwo sulfur-containing amino acids are included in the list of the 20 classical protein amino acids. A methionine residue is introduced at the start of the synthesis of all current proteins. Cysteine, thanks to its thiol function, plays an essential role in a very large number of catalytic sites. Here we present what is known about the prebiotic synthesis of these two amino acids and homocysteine, and we discuss their introduction into primitive peptides and more elaborate proteins.1 Introduction2 Sulfur Sources3 Prebiotic Synthesis of Cysteine4 Prebiotic Synthesis of Methionine5 Homocy

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20

Bannon, G. A., R. Perkins-Dameron, and A. Allen-Nash. "Structure and expression of two temperature-specific surface proteins in the ciliated protozoan Tetrahymena thermophila." Molecular and Cellular Biology 6, no. 9 (September 1986): 3240–45. http://dx.doi.org/10.1128/mcb.6.9.3240-3245.1986.

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The presence of specific proteins (known as immobilization antigens) on the surface of the ciliated protozoan Tetrahymena thermophila is under environmental regulation. There are five different classes (serotypes) of surface proteins which appear on the cell surface when T. thermophila is cultured under different conditions of temperature or incubation medium; three of these are temperature dependent. The appearance of these proteins on the cell surface is mutually exclusive. We used polyclonal antibodies raised against 30 degrees C (designated SerH3)- and 40 degrees C (designated SerT)-specif

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21

Bannon, G. A., R. Perkins-Dameron, and A. Allen-Nash. "Structure and expression of two temperature-specific surface proteins in the ciliated protozoan Tetrahymena thermophila." Molecular and Cellular Biology 6, no. 9 (September 1986): 3240–45. http://dx.doi.org/10.1128/mcb.6.9.3240.

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The presence of specific proteins (known as immobilization antigens) on the surface of the ciliated protozoan Tetrahymena thermophila is under environmental regulation. There are five different classes (serotypes) of surface proteins which appear on the cell surface when T. thermophila is cultured under different conditions of temperature or incubation medium; three of these are temperature dependent. The appearance of these proteins on the cell surface is mutually exclusive. We used polyclonal antibodies raised against 30 degrees C (designated SerH3)- and 40 degrees C (designated SerT)-specif

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22

Tang, Shao Jun, and Erin M. Schuman. "Protein synthesis in the dendrite." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 357, no. 1420 (April 29, 2002): 521–29. http://dx.doi.org/10.1098/rstb.2001.0887.

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In neurons, many proteins that are involved in the transduction of synaptic activity and the expression of neural plasticity are specifically localized at synapses. How these proteins are targeted is not clearly understood. One mechanism is synaptic protein synthesis. According to this idea, messenger RNA (mRNA) translation from the polyribosomes that are observed at the synaptic regions provides a local source of synaptic proteins. Although an increasing number of mRNA species has been detected in the dendrite, information about the synaptic synthesis of specific proteins in a physiological c

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23

Jaleel, Abdul, Katherine A. Klaus, Dawn M. Morse, Helen Karakelides, Lawrence E. Ward, Brian A. Irving, and K. Sreekumaran Nair. "Differential effects of insulin deprivation and systemic insulin treatment on plasma protein synthesis in type 1 diabetic people." American Journal of Physiology-Endocrinology and Metabolism 297, no. 4 (October 2009): E889—E897. http://dx.doi.org/10.1152/ajpendo.00351.2009.

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It remains to be determined whether systemic insulin replacement normalizes synthesis rates of different plasma proteins and whether there are differential effects on various plasma proteins. We tested a hypothesis that insulin deprivation differentially affects individual plasma protein synthesis and that systemic insulin treatment may not normalize synthesis of all plasma proteins. We measured synthesis rates of 41 plasma proteins in seven each of type 1 diabetic (T1DM) and nondiabetic participants (ND) using [ ring-13C6]phenylalanine as a tracer. T1DM were studied while on chronic insulin t

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24

KURUMA, Yutetsu, and Takuya UEDA. "Cell-free Synthesis of Membrane Proteins." Seibutsu Butsuri 56, no. 3 (2016): 162–64. http://dx.doi.org/10.2142/biophys.56.162.

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25

van Kasteren, Sander. "Synthesis of post-translationally modified proteins." Biochemical Society Transactions 40, no. 5 (September 19, 2012): 929–44. http://dx.doi.org/10.1042/bst20120144.

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Post-translational modifications of proteins can have dramatic effect on the function of proteins. Significant research effort has gone into understanding the effect of particular modifications on protein parameters. In the present paper, I review some of the recently developed tools for the synthesis of proteins modified with single post-translational modifications at specific sites in the protein, such as amber codon suppression technologies, tag and modify, and native chemical ligation.

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26

Kent, Stephen B. H. "Chemical Synthesis of Peptides and Proteins." Annual Review of Biochemistry 57, no. 1 (June 1988): 957–89. http://dx.doi.org/10.1146/annurev.bi.57.070188.004521.

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27

HANSEN, PAUL ROBERT, ARNE HOLM, and GUNNAR HOUEN. "Solid-phase peptide synthesis on proteins." International Journal of Peptide and Protein Research 41, no. 3 (January 12, 2009): 237–45. http://dx.doi.org/10.1111/j.1399-3011.1993.tb00331.x.

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28

Katz, Y. "Synthesis of complement proteins in amnion." Journal of Clinical Endocrinology & Metabolism 80, no. 7 (July 1, 1995): 2027–32. http://dx.doi.org/10.1210/jc.80.7.2027.

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29

van der Heden van Noort, Gerbrand J., Herman S. Overkleeft, Gijsbert A. van der Marel, and Dmitri V. Filippov. "Synthesis of Nucleotidylated Poliovirus VPg Proteins." Journal of Organic Chemistry 75, no. 16 (August 20, 2010): 5733–36. http://dx.doi.org/10.1021/jo100757t.

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30

Wang, Yanxin J., D. Miklos Szantai-Kis, and E. James Petersson. "Semi-synthesis of thioamide containing proteins." Organic & Biomolecular Chemistry 13, no. 18 (2015): 5074–81. http://dx.doi.org/10.1039/c5ob00224a.

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To make thioamide protein folding experiments applicable to full-sized proteins, our laboratory has used a combination of native chemical ligation of thiopeptide fragments, unnatural amino acid mutagenesis to install fluorophore partners in expressed protein fragments, and chemoenzymatic protein modification to render these expressed protein ligations traceless.

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31

Suttie, J. W. "Synthesis of vitamin K‐dependent proteins." FASEB Journal 7, no. 3 (March 1993): 445–52. http://dx.doi.org/10.1096/fasebj.7.5.8462786.

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32

Katz, Y., S. Gur, M. Aladjem, and R. C. Strunk. "Synthesis of complement proteins in amnion." Journal of Clinical Endocrinology & Metabolism 80, no. 7 (July 1995): 2027–32. http://dx.doi.org/10.1210/jcem.80.7.7608250.

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33

Melnyk, Oleg, and Jérôme Vicogne. "Total chemical synthesis of SUMO proteins." Tetrahedron Letters 57, no. 39 (September 2016): 4319–24. http://dx.doi.org/10.1016/j.tetlet.2016.08.035.

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34

Burkoth, Timothy S., Eric Beausoleil, Surinder Kaur, Dahzi Tang, Fred E. Cohen, and Ronald N. Zuckermann. "Toward the Synthesis of Artificial Proteins." Chemistry & Biology 9, no. 5 (May 2002): 647–54. http://dx.doi.org/10.1016/s1074-5521(02)00140-0.

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35

Rose, Keith. "Facile synthesis of homogeneous artificial proteins." Journal of the American Chemical Society 116, no. 1 (January 1994): 30–33. http://dx.doi.org/10.1021/ja00080a004.

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36

CAULCOTT, C. "Temperature-induced synthesis of recombinant proteins." Trends in Biotechnology 4, no. 6 (June 1986): 142–46. http://dx.doi.org/10.1016/0167-7799(86)90164-2.

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37

Koenig, Edward. "Synthesis of proteins in vertebrate axons." Neurochemistry International 21 (January 1992): A4. http://dx.doi.org/10.1016/0197-0186(92)91910-o.

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38

Boatright, W. L., and G. Lu. "Hexanal Synthesis in Isolated Soy Proteins." Journal of the American Oil Chemists' Society 84, no. 3 (February 1, 2007): 249–57. http://dx.doi.org/10.1007/s11746-007-1036-6.

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39

Yang, Jerry, Irina Gitlin, Vijay M. Krishnamurthy, Jenny A. Vazquez, Catherine E. Costello, and George M. Whitesides. "Synthesis of Monodisperse Polymers from Proteins." Journal of the American Chemical Society 125, no. 41 (October 2003): 12392–93. http://dx.doi.org/10.1021/ja035978l.

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40

He, Mingyue, and Ming-Wei Wang. "Arraying proteins by cell-free synthesis." Biomolecular Engineering 24, no. 4 (October 2007): 375–80. http://dx.doi.org/10.1016/j.bioeng.2007.05.002.

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41

HILVERT, D. "ChemInform Abstract: Chemical Synthesis of Proteins." ChemInform 26, no. 34 (August 17, 2010): no. http://dx.doi.org/10.1002/chin.199534307.

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42

Sakakibara, Shumpei. "Chemical synthesis of proteins in solution." Biopolymers 51, no. 4 (1999): 279–96. http://dx.doi.org/10.1002/(sici)1097-0282(1999)51:4<279::aid-bip4>3.0.co;2-h.

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43

Cotton, Graham J., Maria C. Pietanza, and Tom W. Muir. "ChemInform Abstract: Chemical Synthesis of Proteins." ChemInform 32, no. 7 (May 30, 2010): no. http://dx.doi.org/10.1002/chin.200107248.

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44

Borgia, J. A., and G. B. Fields. "ChemInform Abstract: Chemical Synthesis of Proteins." ChemInform 31, no. 47 (November 21, 2000): no. http://dx.doi.org/10.1002/chin.200047263.

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45

Bayer, Ernst. "Towards the Chemical Synthesis of Proteins." Angewandte Chemie International Edition in English 30, no. 2 (February 1991): 113–29. http://dx.doi.org/10.1002/anie.199101133.

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46

Liu, Lei. "ChemInform Abstract: Chemical Synthesis of Proteins." ChemInform 44, no. 17 (April 4, 2013): no. http://dx.doi.org/10.1002/chin.201317232.

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47

Kraemer, Bjoern F., Stephan Lindemann, and Andrew S. Weyrich. "Protein degradation systems in platelets." Thrombosis and Haemostasis 110, no. 11 (2013): 920–24. http://dx.doi.org/10.1160/th13-03-0183.

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SummaryProtein synthesis and degradation are essential processes that allow cells to survive and adapt to their surrounding milieu. In nucleated cells, the degradation and/or cleavage of proteins is required to eliminate aberrant proteins. Cells also degrade proteins as a mechanism for cell signalling and complex cellular functions. Although the last decade has convincingly shown that platelets synthesise proteins, the roles of protein degradation in these anucleate cytoplasts are less clear. Here we review what is known about protein degradation in platelets placing particular emphasis on the

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48

Locke, M., E. G. Noble, and B. G. Atkinson. "Exercising mammals synthesize stress proteins." American Journal of Physiology-Cell Physiology 258, no. 4 (April 1, 1990): C723—C729. http://dx.doi.org/10.1152/ajpcell.1990.258.4.c723.

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Spleen cells, peripheral lymphocytes, and soleus muscles were removed from male Sprague-Dawley rats that had been run on a treadmill (24 m/min) for either 20, 40, or 60 min or to exhaustion (86 +/- 41 min) and were labeled in vitro with [35S]methionine at 37 degrees C. Similar tissues from nonrunning control rats were labeled in vitro at either 37 or 43 degrees C (heat shock). Fluorographic analyses of one- and two-dimensional polyacrylamide gel electrophoretic separations of the proteins from cells and tissues of exercised rats demonstrate the new or enhanced synthesis of proteins of approxim

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Wang, Wen-Hung, Arunee Thitithanyanont, and Sheng-Fan Wang. "Synthesis, Assembly and Processing of Viral Proteins." Viruses 14, no. 8 (July 27, 2022): 1650. http://dx.doi.org/10.3390/v14081650.

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Franklin, James L., and Eugene M. Johnson. "Control of Neuronal Size Homeostasis by Trophic Factor–mediated Coupling of Protein Degradation to Protein Synthesis." Journal of Cell Biology 142, no. 5 (September 7, 1998): 1313–24. http://dx.doi.org/10.1083/jcb.142.5.1313.

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We demonstrate that NGF couples the rate of degradation of long-lived proteins in sympathetic neurons to the rate of protein synthesis. Inhibiting protein synthesis rate by a specific percentage caused an almost equivalent percentage reduction in the degradation rate of long-lived proteins, indicating nearly 1:1 coupling between the two processes. The rate of degradation of short-lived proteins was unaffected by suppressing protein synthesis. Included in the pool of proteins that had increased half-lives when protein synthesis was inhibited were actin and tubulin. Both of these proteins, which

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