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Journal articles on the topic 'Newly synthesized proteins'

Author: Grafiati

Published: 4 June 2021

Last updated: 14 February 2022

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1

Bukau, Bernd, Elke Deuerling, Christine Pfund, and Elizabeth A. Craig. "Getting Newly Synthesized Proteins into Shape." Cell 101, no. 2 (2000): 119–22. http://dx.doi.org/10.1016/s0092-8674(00)80806-5.

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2

Ma, Yuanhui, Daniel B. McClatchy, Salim Barkallah, William W. Wood, and John R. Yates. "Quantitative analysis of newly synthesized proteins." Nature Protocols 13, no. 8 (2018): 1744–62. http://dx.doi.org/10.1038/s41596-018-0012-y.

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3

Xu, Guilian, Amrutha Pattamatta, Ryan Hildago, Michael C. Pace, Hilda Brown, and David R. Borchelt. "Vulnerability of newly synthesized proteins to proteostasis stress." Journal of Cell Science 129, no. 9 (2016): 1892–901. http://dx.doi.org/10.1242/jcs.176479.

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4

Kramer, Günter, Ayala Shiber, and Bernd Bukau. "Mechanisms of Cotranslational Maturation of Newly Synthesized Proteins." Annual Review of Biochemistry 88, no. 1 (2019): 337–64. http://dx.doi.org/10.1146/annurev-biochem-013118-111717.

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The timely production of functional proteins is of critical importance for the biological activity of cells. To reach the functional state, newly synthesized polypeptides have to become enzymatically processed, folded, and assembled into oligomeric complexes and, for noncytosolic proteins, translocated across membranes. Key activities of these processes occur cotranslationally, assisted by a network of machineries that transiently engage nascent polypeptides at distinct phases of translation. The sequence of events is tuned by intrinsic features of the nascent polypeptides and timely associati

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5

Wang, Feng, Larissa A. Canadeo, and Jon M. Huibregtse. "Ubiquitination of newly synthesized proteins at the ribosome." Biochimie 114 (July 2015): 127–33. http://dx.doi.org/10.1016/j.biochi.2015.02.006.

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6

Beatty, Kimberly E., Julie C. Liu, Fang Xie, et al. "Fluorescence Visualization of Newly Synthesized Proteins in Mammalian Cells." Angewandte Chemie International Edition 45, no. 44 (2006): 7364–67. http://dx.doi.org/10.1002/anie.200602114.

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7

Beatty, Kimberly E., Julie C. Liu, Fang Xie, et al. "Fluorescence Visualization of Newly Synthesized Proteins in Mammalian Cells." Angewandte Chemie 118, no. 44 (2006): 7524–27. http://dx.doi.org/10.1002/ange.200602114.

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8

tom Dieck, Susanne, Lisa Kochen, Cyril Hanus, et al. "Direct visualization of newly synthesized target proteins in situ." Nature Methods 12, no. 5 (2015): 411–14. http://dx.doi.org/10.1038/nmeth.3319.

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9

Ma, Yuanhui, Daniel B. McClatchy, Salvador Martínez-Bartolomé, Casimir Bamberger та John R. Yates. "Temporal Quantitative Profiling of Newly Synthesized Proteins during Aβ Accumulation". Journal of Proteome Research 20, № 1 (2020): 763–75. http://dx.doi.org/10.1021/acs.jproteome.0c00645.

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10

Beatty, Kimberly E., Fang Xie, Qian Wang, and David A. Tirrell. "Selective Dye-Labeling of Newly Synthesized Proteins in Bacterial Cells." Journal of the American Chemical Society 127, no. 41 (2005): 14150–51. http://dx.doi.org/10.1021/ja054643w.

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11

Deuerling, Elke, and Bernd Bukau. "Chaperone-Assisted Folding of Newly Synthesized Proteins in the Cytosol." Critical Reviews in Biochemistry and Molecular Biology 39, no. 5-6 (2004): 261–77. http://dx.doi.org/10.1080/10409230490892496.

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12

Eichelbaum, Katrin, Markus Winter, Mauricio Berriel Diaz, Stephan Herzig, and Jeroen Krijgsveld. "Selective enrichment of newly synthesized proteins for quantitative secretome analysis." Nature Biotechnology 30, no. 10 (2012): 984–90. http://dx.doi.org/10.1038/nbt.2356.

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13

Keim, V., G. Rohr, and H. G. Stöcket. "Asynchronous Secretion of Newly Synthesized Pancreatic Proteins in the Rat." Digestion 33, no. 4 (1986): 211–18. http://dx.doi.org/10.1159/000199297.

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14

LIPPINCOTTSCHWARTZ, J. "Degradation from the endoplasmic reticulum: Disposing of newly synthesized proteins." Cell 54, no. 2 (1988): 209–20. http://dx.doi.org/10.1016/0092-8674(88)90553-3.

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15

Shen, Yuqian, Wenhua Liu, Jian Zuo, Junhai Han, and Zi Chao Zhang. "Protocol for visualizing newly synthesized proteins in primary mouse hepatocytes." STAR Protocols 2, no. 3 (2021): 100616. http://dx.doi.org/10.1016/j.xpro.2021.100616.

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16

Gorr, Sven-Ulrik, Xue Fen Huang, Darrin J. Cowley, Regina Kuliawat, and Peter Arvan. "Disruption of disulfide bonds exhibits differential effects on trafficking of regulated secretory proteins." American Journal of Physiology-Cell Physiology 277, no. 1 (1999): C121—C131. http://dx.doi.org/10.1152/ajpcell.1999.277.1.c121.

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For several secretory proteins, it has been hypothesized that disulfide-bonded loop structures are required for sorting to secretory granules. To explore this hypothesis, we employed dithiothreitol (DTT) treatment in live pancreatic islets, as well as in PC-12 and GH4C1cells. In islets, disulfide reduction in the distal secretory pathway did not increase constitutive or constitutive-like secretion of proinsulin (or insulin). In PC-12 cells, DTT treatment caused a dramatic increase in unstimulated secretion of newly synthesized chromogranin B (CgB), presumably as a consequence of reducing the s

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17

Deuerling, Elke, Agnes Schulze-Specking, Toshifumi Tomoyasu, Axel Mogk, and Bernd Bukau. "Trigger factor and DnaK cooperate in folding of newly synthesized proteins." Nature 400, no. 6745 (1999): 693–96. http://dx.doi.org/10.1038/23301.

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18

Marquardt, T., and A. Helenius. "Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum." Journal of Cell Biology 117, no. 3 (1992): 505–13. http://dx.doi.org/10.1083/jcb.117.3.505.

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As a part of our studies on the folding of glycoproteins in the ER, we analyzed the fate of viral glycoproteins that have misfolded either spontaneously or through inhibition of N-linked glycosylation. Newly synthesized Semliki Forest virus spike glycoproteins E1 and p62 and influenza hemagglutinin were studied in infected and transfected tissue culture cells. Misfolded proteins aggregated in less than 1 min after release from polysomes and aberrant interchain disulfide bonds were formed immediately. When more than one protein was misfolded, mixed aggregates were generated. This indicated that

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19

Opanashuk, L. A., and J. N. Finkelstein. "Induction of Newly Synthesized Proteins in Astroglial Cells Exposed to Lead." Toxicology and Applied Pharmacology 131, no. 1 (1995): 21–30. http://dx.doi.org/10.1006/taap.1995.1042.

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20

Lingappa, V. R. "Intracellular traffic of newly synthesized proteins. Current understanding and future prospects." Journal of Clinical Investigation 83, no. 3 (1989): 739–51. http://dx.doi.org/10.1172/jci113952.

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21

Hanspal, M., and J. Palek. "Synthesis and assembly of membrane skeletal proteins in mammalian red cell precursors." Journal of Cell Biology 105, no. 3 (1987): 1417–24. http://dx.doi.org/10.1083/jcb.105.3.1417.

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The synthesis of membrane skeletal proteins in avian nucleated red cells has been the subject of extensive investigation, whereas little is known about skeletal protein synthesis in bone marrow erythroblasts and peripheral blood reticulocytes in mammals. To address this question, we have isolated nucleated red cell precursors and reticulocytes from spleens and from the peripheral blood, respectively, of rats with phenylhydrazine-induced hemolytic anemia and pulse-labeled them with [35S]methionine. Pulse-labeling of nucleated red cell precursors shows that the newly synthesized alpha- and beta-

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22

Medicherla, Balasubrahmanyam, and Alfred L. Goldberg. "Heat shock and oxygen radicals stimulate ubiquitin-dependent degradation mainly of newly synthesized proteins." Journal of Cell Biology 182, no. 4 (2008): 663–73. http://dx.doi.org/10.1083/jcb.200803022.

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Accumulation of misfolded oxidant-damaged proteins is characteristic of many diseases and aging. To understand how cells handle postsynthetically damaged proteins, we studied in Saccharomyces cerevisiae the effects on overall protein degradation of shifting from 30 to 38°C, exposure to reactive oxygen species generators (paraquat or cadmium), or lack of superoxide dismutases. Degradation rates of long-lived proteins (i.e., most cell proteins) were not affected by these insults, even when there was widespread oxidative damage to proteins. However, exposure to 38°C, paraquat, cadmium, or deletio

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23

Cobbold, C., M. Windsor, and T. Wileman. "A Virally Encoded Chaperone Specialized for Folding of the Major Capsid Protein of African Swine Fever Virus." Journal of Virology 75, no. 16 (2001): 7221–29. http://dx.doi.org/10.1128/jvi.75.16.7221-7229.2001.

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ABSTRACT It is generally believed that cellular chaperones facilitate the folding of virus capsid proteins, or that capsid proteins fold spontaneously. Here we show that p73, the major capsid protein ofAfrican swine fever virus (ASFV) failed to fold and aggregated when expressed alone in cells. This demonstrated that cellular chaperones were unable to aid the folding of p73 and suggested that ASFV may encode a chaperone. An 80-kDa protein encoded by ASFV, termed the capsid-associated protein (CAP) 80, bound to the newly synthesized capsid protein in infected cells. The 80-kDa protein was relea

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24

Beckmann, RP, M. Lovett, and WJ Welch. "Examining the function and regulation of hsp 70 in cells subjected to metabolic stress." Journal of Cell Biology 117, no. 6 (1992): 1137–50. http://dx.doi.org/10.1083/jcb.117.6.1137.

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Members of the heat-shock protein (hsp) 70 family, distributed within various cellular compartments, have been implicated in facilitating protein maturation events. In particular, related hsp 70 family members appear to bind nascent polypeptides which are in the course of synthesis and/or translocation into organelles. We previously reported that in normal, unstressed cells, cytosolic hsp 70 (hsp 72/73) interacted transiently with nascent polypeptides. We suspect that such interactions function to prevent or slow down the folding of the nascent polypeptide chain. Once synthesis is complete, an

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25

Stafford, F. J., and J. S. Bonifacino. "A permeabilized cell system identifies the endoplasmic reticulum as a site of protein degradation." Journal of Cell Biology 115, no. 5 (1991): 1225–36. http://dx.doi.org/10.1083/jcb.115.5.1225.

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Analysis of the fate of a variety of newly synthesized proteins in the secretory pathway has provided evidence for the existence of a novel protein degradation system distinct from that of the lysosome. Although current evidence suggests that proteins degraded by this system are localized to a pre-Golgi compartment before degradation, the site of proteolysis has not been determined. A permeabilized cell system was developed to examine whether degradation by this pathway required transport out of the ER, and to define the biochemical characteristics of this process. Studies were performed on fi

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26

Michele, Daniel E., Faris P. Albayya, and Joseph M. Metzger. "Thin Filament Protein Dynamics in Fully Differentiated Adult Cardiac Myocytes: Toward A Model of Sarcomere Maintenance." Journal of Cell Biology 145, no. 7 (1999): 1483–95. http://dx.doi.org/10.1083/jcb.145.7.1483.

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Sarcomere maintenance, the continual process of replacement of contractile proteins of the myofilament lattice with newly synthesized proteins, in fully differentiated contractile cells is not well understood. Adenoviral-mediated gene transfer of epitope-tagged tropomyosin (Tm) and troponin I (TnI) into adult cardiac myocytes in vitro along with confocal microscopy was used to examine the incorporation of these newly synthesized proteins into myofilaments of a fully differentiated contractile cell. The expression of epitope-tagged TnI resulted in greater replacement of the endogenous TnI than

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27

Pattnaik, A. K., and D. Panda. "Biarsenical Labeling of Tetracysteine-Tagged Proteins for Tracking Existing and Newly Synthesized Pools of Proteins." Cold Spring Harbor Protocols 2009, no. 12 (2009): pdb.prot5343. http://dx.doi.org/10.1101/pdb.prot5343.

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28

Mauduit, P., G. Herman, and B. Rossignol. "Newly synthesized protein secretion in rat lacrimal gland: post-second messenger synergism." American Journal of Physiology-Cell Physiology 253, no. 4 (1987): C514—C524. http://dx.doi.org/10.1152/ajpcell.1987.253.4.c514.

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The vasoactive intestinal peptide (VIP) induces a concentration-dependent secretion of newly synthesized (3H labeled) proteins from lacrimal gland fragments. Maximal secretory response is approximately 20% of total labeled proteins secreted for a 40-min stimulation and half-maximal secretory response is obtained at 3.8 +/- 0.2 nM VIP. The cholinergic (muscarinic) and VIPergic stimulations synergistically interact in eliciting newly synthesized protein secretion. Carbachol (0.3 microM) and the phorbol ester PMA (1 microM) potentiate the secretory response to VIP (10 nM), forskolin (3 microM), a

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29

Sobel, Suzanne G., and Sandra L. Wolin. "Two Yeast La Motif-containing Proteins Are RNA-binding Proteins that Associate with Polyribosomes." Molecular Biology of the Cell 10, no. 11 (1999): 3849–62. http://dx.doi.org/10.1091/mbc.10.11.3849.

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We have characterized two Saccharomyces cerevisiaeproteins, Sro9p and Slf1p, which contain a highly conserved motif found in all known La proteins. Originally described as an autoantigen in patients with rheumatic disease, the La protein binds to newly synthesized RNA polymerase III transcripts. In yeast, the La protein homologue Lhp1p is required for the normal pathway of tRNA maturation and also stabilizes newly synthesized U6 RNA. We show that deletions in both SRO9 and SLF1 are not synthetically lethal with a deletion in LHP1, indicating that the three proteins do not function in a single

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30

Nakata, Takao, Sumio Terada, and Nobutaka Hirokawa. "Visualization of the Dynamics of Synaptic Vesicle and Plasma Membrane Proteins in Living Axons." Journal of Cell Biology 140, no. 3 (1998): 659–74. http://dx.doi.org/10.1083/jcb.140.3.659.

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Newly synthesized membrane proteins are transported by fast axonal flow to their targets such as the plasma membrane and synaptic vesicles. However, their transporting vesicles have not yet been identified. We have successfully visualized the transporting vesicles of plasma membrane proteins, synaptic vesicle proteins, and the trans-Golgi network residual proteins in living axons at high resolution using laser scan microscopy of green fluorescent protein-tagged proteins after photobleaching. We found that all of these proteins are transported by tubulovesicular organelles of various sizes and

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31

Sheng, Linfeng, Lesi Cai, Jie Liu, et al. "Imaging specific newly synthesized proteins within cells by fluorescence resonance energy transfer." Chemical Science 8, no. 1 (2017): 748–54. http://dx.doi.org/10.1039/c6sc02610a.

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32

Vukoti, Krishna, Xiaokun Yu, Quanhu Sheng, et al. "Monitoring Newly Synthesized Proteins over the Adult Life Span of Caenorhabditis elegans." Journal of Proteome Research 14, no. 3 (2015): 1483–94. http://dx.doi.org/10.1021/acs.jproteome.5b00021.

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33

Andreose, J. S., G. Fumagalli, F. J. Sigworth, and M. J. Caplan. "Real-time detection of the surface delivery of newly synthesized membrane proteins." Proceedings of the National Academy of Sciences 93, no. 15 (1996): 7661–66. http://dx.doi.org/10.1073/pnas.93.15.7661.

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34

Schubert, Ulrich, Luis C. Antón, James Gibbs, Christopher C. Norbury, Jonathan W. Yewdell, and Jack R. Bennink. "Rapid degradation of a large fraction of newly synthesized proteins by proteasomes." Nature 404, no. 6779 (2000): 770–74. http://dx.doi.org/10.1038/35008096.

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35

Shao, Yuyin, Huimin Bao, Lixiang Ma, et al. "Enhancing Comprehensive Analysis of Newly Synthesized Proteins Based on Cleavable Bioorthogonal Tagging." Analytical Chemistry 93, no. 27 (2021): 9408–17. http://dx.doi.org/10.1021/acs.analchem.1c00965.

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36

PUGLIELLI, Luigi, Attilio RIGOTTI, Ludwig AMIGO, et al. "Modulation of intrahepatic cholesterol trafficking: evidence by in vivo antisense treatment for the involvement of sterol carrier protein-2 in newly synthesized cholesterol transport into rat bile." Biochemical Journal 317, no. 3 (1996): 681–87. http://dx.doi.org/10.1042/bj3170681.

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Biliary cholesterol represents one of the two major excretory pathways for sterol elimination from the body and plays a central role in cholesterol gallstone formation. Biliary cholesterol originates from a precursor pool of preformed and newly synthesized free cholesterol. Although it has been suggested that newly synthesized and preformed biliary cholesterol are secreted by independent pathways, the specific cellular and molecular mechanisms are unknown. We used male Wistar rats to study the time-course of the appearance of newly synthesized cholesterol, phosphatidylcholine and protein into

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37

Howlett, S. K., S. C. Barton, M. L. Norris, and M. A. H. Surani. "Nuclear and cytoplasmic localization of newly synthesized proteins in the early mouse embryo." Development 103, no. 1 (1988): 129–34. http://dx.doi.org/10.1242/dev.103.1.129.

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1-, 2- and 4-cell mouse embryos were labelled with [35S]methionine and the newly synthesized proteins from isolated nuclei were compared with those from cytoplasts and total embryos. There were distinct subsets of translation products present within nuclei compared to those that remained in the cytoplasm. There was no detectable evidence for differences in the presence of newly synthesized proteins in the male and female pronuclei. However, different new proteins associated with nuclei over the time that the embryonic genome becomes active.

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38

Cheng, T. C., and H. P. Benton. "The intracellular Ca2+-pump inhibitors thapsigargin and cyclopiazonic acid induce stress proteins in mammalian chondrocytes." Biochemical Journal 301, no. 2 (1994): 563–68. http://dx.doi.org/10.1042/bj3010563.

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Primary cultures of mammalian articular chondrocytes respond to treatment with the intracellular Ca(2+)-pump inhibitors thapsigargin (TG) and cyclopiazonic acid by specific changes in protein synthesis consistent with a stress response. Two-dimensional gel electrophoresis of newly synthesized proteins confirmed that the response was consistent with the induction of glucose-regulated proteins. The effects of low-dose TG (10 nM), measured by changes in [35S]methionine labelling of newly synthesized proteins, can first be observed by 10 h and are maximal by 24 h. The pattern of changes induced by

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39

Alpers, D. H., Y. Zhang, and D. J. Ahnen. "Synthesis and parallel secretion of rat intestinal alkaline phosphatase and a surfactant-like particle protein." American Journal of Physiology-Endocrinology and Metabolism 268, no. 6 (1995): E1205—E1214. http://dx.doi.org/10.1152/ajpendo.1995.268.6.e1205.

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Rat intestinal microvillous alkaline phosphatases are secreted bidirectionally from the enterocyte attached to a phospholipid-rich membrane (surfactant-like particle). To determine the intracellular pathways for newly synthesized alkaline phosphatases and for the extracellular enzyme-particle complex in the intestinal mucosa, pulse-chase experiments were performed. Synthesis of both isoforms of alkaline phosphatase in fasted rats peaked in the Golgi at 15–30 min and in the microvillous membrane at 60 min, without intermediate localization in the basolateral membranes. A second peak of incorpor

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40

ROKKA, Anne, Marjaana SUORSA, Ammar SALEEM, Natalia BATTCHIKOVA, and Eva-Mari ARO. "Synthesis and assembly of thylakoid protein complexes: multiple assembly steps of photosystem II." Biochemical Journal 388, no. 1 (2005): 159–68. http://dx.doi.org/10.1042/bj20042098.

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To study the synthesis and assembly of multisubunit thylakoid protein complexes, we performed [35S]Met pulse and chase experiments with isolated chloroplasts and intact leaves of spinach (Spinacia oleracea L.), followed by Blue Native gel separation of the (sub)complexes and subsequent identification of the newly synthesized and assembled protein subunits. PSII (photosystem II) core subunits were the most intensively synthesized proteins, particularly in vitro and at high light intensities in vivo, and could be sequestered in several distinct PSII subassemblies. Newly synthesized D1 was first

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41

Farr, Glen A., Michael Hull, Ira Mellman, and Michael J. Caplan. "Membrane proteins follow multiple pathways to the basolateral cell surface in polarized epithelial cells." Journal of Cell Biology 186, no. 2 (2009): 269–82. http://dx.doi.org/10.1083/jcb.200901021.

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Newly synthesized apical and basolateral membrane proteins are sorted from one another in polarized epithelial cells. The trans-Golgi network participates in this sorting process, but some basolateral proteins travel from the Golgi to recycling endosomes (REs) before their surface delivery. Using a novel system for pulse–chase microscopy, we have visualized the postsynthetic route pursued by a newly synthesized cohort of Na,K-ATPase. We find that the basolateral delivery of newly synthesized Na,K-ATPase occurs via a pathway distinct from that pursued by the vesicular stomatitis virus G protein

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42

Nyfeler, B., and H. P. Hauri. "Visualization of protein interactions inside the secretory pathway." Biochemical Society Transactions 35, no. 5 (2007): 970–73. http://dx.doi.org/10.1042/bst0350970.

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The ER (endoplasmic reticulum) is a major protein folding and modification organelle. In its lumen, the ER processes a third of all newly synthesized proteins. To accomplish this task, numerous resident proteins capture the nascent and newly synthesized proteins. The underlying luminal protein–protein interactions, however, are inherently difficult to analyse, mainly due to their transient nature and the rather specialized environment of the ER. To overcome these limitations, we developed a PCA (protein fragment complementation assay) based on the citrine variant of YFP (yellow fluorescent pro

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43

Jones, Jacob M., James C. Morrell, and Stephen J. Gould. "PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins." Journal of Cell Biology 164, no. 1 (2004): 57–67. http://dx.doi.org/10.1083/jcb.200304111.

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Integral peroxisomal membrane proteins (PMPs) are synthesized in the cytoplasm and imported posttranslationally. Here, we demonstrate that PEX19 binds and stabilizes newly synthesized PMPs in the cytosol, binds to multiple PMP targeting signals (mPTSs), interacts with the hydrophobic domains of PMP targeting signals, and is essential for PMP targeting and import. These results show that PEX19 functions as both a chaperone and an import receptor for newly synthesized PMPs. We also demonstrate the existence of two PMP import mechanisms and two classes of mPTSs: class 1 mPTSs, which are bound by

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44

Cohen, Laurie D., Ayub Boulos, and Noam E. Ziv. "A non-fluorescent HaloTag blocker for improved measurement and visualization of protein synthesis in living cells." F1000Research 9 (April 28, 2020): 302. http://dx.doi.org/10.12688/f1000research.23289.1.

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Background: HaloTag is a modified bacterial enzyme that binds rapidly and irreversibly to an array of synthetic ligands, including chemical dyes. When expressed in live cells in conjunction with a protein of interest, HaloTag can be used to study protein trafficking, synthesis, and degradation. For instance, sequential HaloTag labeling with spectrally separable dyes can be used to separate preexisting protein pools from proteins newly synthesized following experimental manipulations or the passage of time. Unfortunately, incomplete labeling by the first dye, or labeling by residual, trapped dy

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45

Cohen, Laurie D., Ayub Boulos, and Noam E. Ziv. "A non-fluorescent HaloTag blocker for improved measurement and visualization of protein synthesis in living cells." F1000Research 9 (June 8, 2020): 302. http://dx.doi.org/10.12688/f1000research.23289.2.

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Background: HaloTag is a modified bacterial enzyme that binds rapidly and irreversibly to an array of synthetic ligands, including chemical dyes. When expressed in live cells in conjunction with a protein of interest, HaloTag can be used to study protein trafficking, synthesis, and degradation. For instance, sequential HaloTag labeling with spectrally separable dyes can be used to separate preexisting protein pools from proteins newly synthesized following experimental manipulations or the passage of time. Unfortunately, incomplete labeling by the first dye, or labeling by residual, trapped dy

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46

Shabanowitz, Robert B., and Abraham L. Kierszenbaum. "Newly Synthesized Proteins in Seminiferous Intertubular and Intratubular Compartments of the Rat Testis1." Biology of Reproduction 35, no. 1 (1986): 179–90. http://dx.doi.org/10.1095/biolreprod35.1.179.

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47

CUI, Xiu-Yun, Ning-Ning SUN, Xiao-Na XIE, Wan-Chun SUN, Qing ZHAO, and Ning LIU. "Detection of Newly Synthesized Proteins via Metabolic Incorporation of Non-natural Amino Acid." Chinese Journal of Analytical Chemistry 46, no. 11 (2018): 1808–13. http://dx.doi.org/10.1016/s1872-2040(18)61125-9.

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48

Debarba, João Antonio, Karina Mariante Monteiro, Hercules Moura, John R. Barr, Henrique Bunselmeyer Ferreira, and Arnaldo Zaha. "Identification of Newly Synthesized Proteins by Echinococcus granulosus Protoscoleces upon Induction of Strobilation." PLOS Neglected Tropical Diseases 9, no. 9 (2015): e0004085. http://dx.doi.org/10.1371/journal.pntd.0004085.

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49

Nyström, B., J. O. Karlsson, and A. Hamberger. "Secretion of newly synthesized proteins into the extracellular fluid of the rabbit hippocampus." Journal of Neuroscience Research 21, no. 1 (1988): 51–55. http://dx.doi.org/10.1002/jnr.490210108.

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50

Dieterich, Daniela C., Jennifer J. L. Hodas, Géraldine Gouzer, et al. "In situ visualization and dynamics of newly synthesized proteins in rat hippocampal neurons." Nature Neuroscience 13, no. 7 (2010): 897–905. http://dx.doi.org/10.1038/nn.2580.

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