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Journal articles on the topic 'Translationally controlled tumour protein'

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Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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1

Bommer, Ulrich-Axel, and Bernd-Joachim Thiele. "The translationally controlled tumour protein (TCTP)." International Journal of Biochemistry & Cell Biology 36, no. 3 (March 2004): 379–85. http://dx.doi.org/10.1016/s1357-2725(03)00213-9.

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2

Newbery, H. J., M. Brueser, I. Phillips, and C. M. Abbott. "The role of translationally controlled tumour protein in tumourigenesis." European Journal of Cancer Supplements 6, no. 9 (July 2008): 72. http://dx.doi.org/10.1016/s1359-6349(08)71451-4.

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3

Bommer, Ulrich-Axel. "Cellular Function and Regulation of the Translationally Controlled Tumour Protein TCTP." Open Allergy Journal 5, no. 1 (May 18, 2012): 19–32. http://dx.doi.org/10.2174/1874838401205010019.

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The ‘translationally controlled tumour protein’ TCTP was originally discovered 30 years ago by researchers interested in proteins regulated at the translational level. Cloning and sequencing confirmed the conservation of this protein among all eukaryotic kingdoms, but did not reveal any functional clue, and TCTP was listed in the databases as a ‘family’ of its own. The functional characterisation of this protein extended over more than a decade, leading to a plethora of individual functions and interactions that have been ascribed to this protein. A major addition to the functional characterisation of TCTP was the identification in 1995 of its histamine releasing factor (HRF) activity in allergic conditions, which for the first time described an extracellular activity for TCTP in human disease. This triggered a host of additional publications aimed at characterising this HRF activity, which are discussed in other articles of this issue. Another milestone in the elucidation of TCTP's function was the demonstration of its anti-apoptotic activity in 2001. Evidence is also accumulating for a role of TCTP in the cell cycle and in early development. This article provides an overview of the main cellular activities of TCTP. The second part will summarise our current knowledge on the mechanisms involved in regulating intracellular TCTP levels.

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4

Kloc, Malgorzata, Jacek Z. Kubiak, and Rafik Mark Ghobrial. "Translationally Controlled Tumor-Associated Protein." Biochemistry Research International 2012 (2012): 1. http://dx.doi.org/10.1155/2012/432590.

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5

Venugopal, Thayanithy. "Evolution and expression of Translationally Controlled Tumour Protein (TCTP) of fish." Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 142, no. 1 (September 2005): 8–17. http://dx.doi.org/10.1016/j.cbpc.2005.04.011.

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6

Chan, Tim Hon Man, Leilei Chen, and Xin-Yuan Guan. "Role of Translationally Controlled Tumor Protein in Cancer Progression." Biochemistry Research International 2012 (2012): 1–5. http://dx.doi.org/10.1155/2012/369384.

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Translationally controlled tumor protein (TCTP) is a highly conserved and ubiquitously expressed protein in all eukaryotes—highlighting its important functions in the cell. Previous studies revealed that TCTP is implicated in many biological processes, including cell growth, tumor reversion, and induction of pluripotent stem cell. A recent study on the solution structure from fission yeast orthologue classifies TCTP under a family of small chaperone proteins. There is growing evidence in the literature that TCTP is a multifunctional protein and exerts its biological activity at the extracellular and intracellular levels. Although TCTP is not a tumor-specific protein, our research group, among several others, focused on the role(s) of TCTP in cancer progression. In this paper, we will summarize the current scientific knowledge of TCTP in different aspects, and the precise oncogenic mechanisms of TCTP will be discussed in detail.

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7

Branco, Rémi, and Josette Masle. "Systemic signalling through translationally controlled tumour protein controls lateral root formation in Arabidopsis." Journal of Experimental Botany 70, no. 15 (April 30, 2019): 3927–40. http://dx.doi.org/10.1093/jxb/erz204.

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Abstract The plant body plan and primary organs are established during embryogenesis. However, in contrast to animals, plants have the ability to generate new organs throughout their whole life. These give them an extraordinary developmental plasticity to modulate their size and architecture according to environmental constraints and opportunities. How this plasticity is regulated at the whole-organism level is elusive. Here we provide evidence for a role for translationally controlled tumour protein (TCTP) in regulating the iterative formation of lateral roots in Arabidopsis. AtTCTP1 modulates root system architecture through a dual function: as a general constitutive growth promoter enhancing root elongation and as a systemic signalling agent via mobility in the vasculature. AtTCTP1 encodes mRNAs with long-distance mobility between the shoot and roots. Mobile shoot-derived TCTP1 gene products act specifically to enhance the frequency of lateral root initiation and emergence sites along the primary root pericycle, while root elongation is controlled by local constitutive TCTP1 expression and scion size. These findings uncover a novel type for an integrative signal in the control of lateral root initiation and the compromise for roots between branching more profusely or elongating further. They also provide the first evidence in plants of an extracellular function of the vital, highly expressed ubiquitous TCTP1.

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8

Jandl, Katharina, Christopher D. Gregory, and Grazyna Kwapiszewska. "Translationally Controlled Tumor Protein in Extracellular Vehicles: Dangerous Cargo?" American Journal of Respiratory Cell and Molecular Biology 59, no. 4 (October 2018): 407–9. http://dx.doi.org/10.1165/rcmb.2018-0160ed.

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9

Hoepflinger, Marion, Johannes Reitsamer, Anja Geretschlaeger, Norbert Mehlmer, and Raimund Tenhaken. "The effect of Translationally Controlled Tumour Protein (TCTP) on programmed cell death in plants." BMC Plant Biology 13, no. 1 (2013): 135. http://dx.doi.org/10.1186/1471-2229-13-135.

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10

Tuynder, M., G. Fiucci, S. Prieur, A. Lespagnol, A. Geant, S. Beaucourt, D. Duflaut, et al. "Translationally controlled tumor protein is a target of tumor reversion." Proceedings of the National Academy of Sciences 101, no. 43 (October 15, 2004): 15364–69. http://dx.doi.org/10.1073/pnas.0406776101.

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11

Ambrosio, Maria R., Bruno J. Rocca, Aurora Barone, Monica Onorati, Lucia Mundo, Filippo Crivelli, Franca Di Nuovo, et al. "Expression of Translationally Controlled Tumor Protein in Human Kidney and in Renal Cell Carcinoma." BioMed Research International 2015 (2015): 1–8. http://dx.doi.org/10.1155/2015/730390.

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Translationally controlled tumor protein is a multifaceted protein involved in several physiological and biological functions. Its expression in normal kidney and in renal carcinomas, once corroborated by functional data, may add elements to elucidate renal physiology and carcinogenesis. In this study, translationally controlled tumor protein expression was evaluated by quantitative real time polymerase chain reaction and western blotting, and its localization was examined by immunohistochemistry on 84 nephrectomies for cancer. In normal kidney protein expression was found in the cytoplasm of proximal and distal tubular cells, in cells of the thick segment of the loop of Henle, and in urothelial cells of the pelvis. It was also detectable in cells of renal carcinoma with different pattern of localization (membranous and cytoplasmic) depending on tumor histotype. Our data may suggest an involvement of translationally controlled tumor protein in normal physiology and carcinogenesis. However, functionalin vitroandin vivostudies are needed to verify this hypothesis.

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12

Maeng, Jeehye, Hyo Young Kim, Dong Hae Shin, and Kyunglim Lee. "Transduction of translationally controlled tumor protein employing TCTP-derived protein transduction domain." Analytical Biochemistry 435, no. 1 (April 2013): 47–53. http://dx.doi.org/10.1016/j.ab.2012.11.029.

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13

Gnanasekar, Munirathinam, and Kalyanasundaram Ramaswamy. "Translationally controlled tumor protein of Brugia malayi functions as an antioxidant protein." Parasitology Research 101, no. 6 (August 9, 2007): 1533–40. http://dx.doi.org/10.1007/s00436-007-0671-z.

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14

Batisti, Cinzia, Maria R. Ambrosio, Bruno J. Rocca, Gian M. Tosi, Jean C. Sanchez, Felice Arcuri, Marcella Cintorino, and Sergio A. Tripodi. "Translationally Controlled Tumour Protein (TCTP) is present in human cornea and increases in herpetic keratitis." Diagnostic Pathology 7, no. 1 (2012): 90. http://dx.doi.org/10.1186/1746-1596-7-90.

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15

Gross, Burck, Matthias Gaestel, Hans Böhm, and Heinz Bielka. "cDNA sequence coding for a translationally controlled human tumor protein." Nucleic Acids Research 17, no. 20 (1989): 8367. http://dx.doi.org/10.1093/nar/17.20.8367.

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16

Fischer, Nicolas, Ean-Jeong Seo, Anette Klinger, Edmond Fleischer, and Thomas Efferth. "AMG900 as novel inhibitor of the translationally controlled tumor protein." Chemico-Biological Interactions 334 (January 2021): 109349. http://dx.doi.org/10.1016/j.cbi.2020.109349.

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17

Yan, L., K. Fei, D. Bridge, and M. P. Sarras Jr. "A cnidarian homologue of translationally controlled tumor protein (P23/TCTP)." Development Genes and Evolution 210, no. 10 (September 19, 2000): 507–11. http://dx.doi.org/10.1007/s004270000088.

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18

Kwon, Young V., Bingqing Zhao, Chiwei Xu, Jiae Lee, Chiao-Lin Chen, Arunachalam Vinayagam, Bruce A. Edgar, and Norbert Perrimon. "The role of translationally controlled tumor protein in proliferation ofDrosophilaintestinal stem cells." Proceedings of the National Academy of Sciences 116, no. 52 (December 16, 2019): 26591–98. http://dx.doi.org/10.1073/pnas.1910850116.

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Translationally controlled tumor protein (TCTP) is a highly conserved protein functioning in multiple cellular processes, ranging from growth to immune responses. To explore the role of TCTP in tissue maintenance and regeneration, we employed the adultDrosophilamidgut, where multiple signaling pathways interact to precisely regulate stem cell division for tissue homeostasis. Tctp levels were significantly increased in stem cells and enteroblasts upon tissue damage or activation of the Hippo pathway that promotes regeneration of intestinal epithelium. Stem cells with reduced Tctp levels failed to proliferate during normal tissue homeostasis and regeneration. Mechanistically, Tctp forms a complex with multiple proteins involved in translation and genetically interacts with ribosomal subunits. In addition, Tctp increases both Akt1 protein abundance and phosphorylation in vivo. Altogether, Tctp regulates stem cell proliferation by interacting with key growth regulatory signaling pathways and the translation process in vivo.

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19

XU, Aimin, A. Richard BELLAMY, and John A. TAYLOR. "Expression of translationally controlled tumour protein is regulated by calcium at both the transcriptional and post-transcriptional level." Biochemical Journal 342, no. 3 (September 5, 1999): 683–89. http://dx.doi.org/10.1042/bj3420683.

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We have investigated how the programme of protein synthesis is altered in response to a loss of calcium homoeostasis in Cos-7 cells using a differential proteome mapping approach. Exposure of the cells to the calcium ionophore A23187 or thapsigargin, or alternatively, expression of a viral glycoprotein reported to deplete intracellular calcium stores, resulted in the up-regulated expression of a characteristic set of proteins. One of these is the translationally controlled tumour protein (TCTP), a cytoplasmic protein whose expression has not previously been linked to calcium perturbation. Quantitative Northern blot assay demonstrated that steady-state mRNA abundance of TCTP was also increased under these conditions. Clamping the cytosolic calcium concentration by the introduction of bis-(o-aminophenoxy)-ethane-N,N,N′,N′-tetra-acetic acid (BAPTA) into cells did not affect the increase in steady-state levels of TCTP mRNA observed in response to ionophore. Therefore depletion of endoplasmic reticulum (ER) calcium, but not elevation of the cytosolic calcium concentration, was responsible for increased transcription of the TCTP gene. However, the presence of BAPTA significantly attenuated the ionophore-mediated increase in levels of the protein. Moreover, the level of TCTP in ionophore-treated cells increased in advance of a detectable increase in the corresponding mRNA abundance. These results indicate that expression of TCTP is regulated at two distinct levels in response to the concentration of calcium in different cellular compartments. Whereas depletion of the ER store causes an increase in TCTP mRNA abundance, increased cytosolic calcium concentrations regulate gene expression at the post-transcriptional level.

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20

Sanchez, Jean-Charles, Dominique Schaller, Florence Ravier, Olivier Golaz, Sylviane Jaccoud, Monique Belet, Marc R. Wilkins, Richard James, Jacques Deshusses, and Denis Hochstrasser. "Translationally controlled tumor protein: A protein identified in several nontumoral cells including erythrocytes." Electrophoresis 18, no. 1 (1997): 150–55. http://dx.doi.org/10.1002/elps.1150180127.

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21

Bommer, Ulrich-Axel, and Toshiaki Kawakami. "Role of TCTP in Cell Biological and Disease Processes." Cells 10, no. 9 (September 2, 2021): 2290. http://dx.doi.org/10.3390/cells10092290.

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Translationally controlled tumor protein (TCTP), also referred to as histamine-releasing factor (HRF) or fortilin, is a multifunctional protein, expressed in essentially all eukaryotic organisms [...]

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22

Jung, Jiwon, Ji-Sun Lee, Yun-Sil Lee, and Kyunglim Lee. "Radiosensitivity of Cancer Cells Is Regulated by Translationally Controlled Tumor Protein." Cancers 11, no. 3 (March 19, 2019): 386. http://dx.doi.org/10.3390/cancers11030386.

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Translationally controlled tumor protein (TCTP) is a ubiquitous multifunctional protein that is essential for cell survival. This study reveals that the regulation of radiosensitivity of cancer cells is yet another function of TCTP. The relationship between endogenous TCTP levels and sensitivity to radiation was examined in breast cancer cell lines (T47D, MDA-MB-231, and MCF7) and lung cancer cells lines (A549, H1299, and H460). Cancer cells with high expression levels of TCTP were more resistant to radiation. TCTP overexpression inhibited radiation-induced cell death, while silencing TCTP led to an increase in radiosensitivity. DNA damage in the irradiated TCTP-silenced A549 cells was greater than in irradiated control shRNA-transfected A549 cells. p53, a well-known reciprocal regulator of TCTP, was increased in irradiated TCTP down-regulated A549 cells. Moreover, introduction of p53 siRNA in TCTP knocked-down A549 cells abrogated the increased radiosensitivity induced by TCTP knockdown. An in vivo xenograft study also confirmed enhanced radiosensitivity in TCTP down-regulated A549 cells. These findings suggest that TCTP has the potential to serve as a therapeutic target to overcome radiation resistance in cancer, a major problem for the effective treatment of cancers.

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23

Qiang, Ma, Wu Fenfang, Geng Yan, Shu Wen, Huang Maoliang, Wu Yingsong, Xu Weiwen, and Li Ming. "Preparation and Characterization of Monoclonal Antibody Against Translationally Controlled Tumor Protein." Hybridoma 30, no. 1 (February 2011): 81–85. http://dx.doi.org/10.1089/hyb.2010.0075.

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24

Subramanian, Elaiya Raja, Nino Gopi Daisy, Dinesh Kumar Sudalaimani, Kalidas Ramamoorthy, Subburathinam Balakrishnan, Jackson Durairaj Selvan Christyraj, Vaithilingaraja Arumugaswami, and Sudhakar Sivasubramaniam. "Function of translationally controlled tumor protein (TCTP) in Eudrilus eugeniae regeneration." PLOS ONE 12, no. 4 (April 12, 2017): e0175319. http://dx.doi.org/10.1371/journal.pone.0175319.

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25

Berkowitz, Oliver, Ricarda Jost, Stephan Pollmann, and Josette Masle. "Characterization of TCTP, the Translationally Controlled Tumor Protein, from Arabidopsis thaliana." Plant Cell 20, no. 12 (December 2008): 3430–47. http://dx.doi.org/10.1105/tpc.108.061010.

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26

Chung, S. "Expression of translationally controlled tumor protein mRNA in human colon cancer." Cancer Letters 156, no. 2 (August 11, 2000): 185–90. http://dx.doi.org/10.1016/s0304-3835(00)00460-2.

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27

Kim, Moonhee, Yoonwha Jung, Kyunglim Lee, and Choonmi Kim. "Identification of the calcium binding sites in translationally controlled tumor protein." Archives of Pharmacal Research 23, no. 6 (December 2000): 633–36. http://dx.doi.org/10.1007/bf02975253.

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28

Ulambayar, Bastsetseg, Hee Won Lee, Eun Mi Yang, Hae-Sim Park, Kyung Lim Lee, and Young-Min Ye. "The Role of Translationally Controlled Tumor Protein in Chronic Spontaneous Urticaria." Journal of Allergy and Clinical Immunology 141, no. 2 (February 2018): AB178. http://dx.doi.org/10.1016/j.jaci.2017.12.565.

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29

Kumar, Rakesh, Ranjana Maurya, and Shweta Saran. "Identification of novel inhibitors of the translationally controlled tumor protein (TCTP): insights from molecular dynamics." Molecular BioSystems 13, no. 3 (2017): 510–24. http://dx.doi.org/10.1039/c6mb00850j.

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The translationally controlled tumor protein (TCTP) is a highly conserved multifunctional protein, preferentially expressed in mitotically active tissues and is a potential biomarker and a therapeutic target for lung cancers.

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30

Munirathinam, Gnanasekar, and Kalyanasundaram Ramaswamy. "Sumoylation of Human Translationally Controlled Tumor Protein Is Important for Its Nuclear Transport." Biochemistry Research International 2012 (2012): 1–8. http://dx.doi.org/10.1155/2012/831940.

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Translationally controlled tumor protein (TCTP) lacks nuclear bipartite localization signal sequence; yet TCTP is present abundantly in the nucleus. At present it is not known how TCTP gets transported to the nucleus. Sequence analyses showed that all TCTPs described to date have putative small ubiquitin-like modifier (SUMO) motifs. Since SUMO modification plays an important role in the nuclear transport of proteins, we evaluated whether SUMO motifs are important for transport of TCTP into the nucleus. We show that TCTP exists in sumoylated form in cytoplasm and nucleus of mammalian cells. Point mutation of lysine residue in the SUMO motif compromised the ability of TCTP to get sumoylatedin vitro. When cells were transfected with FLAG-tagged mutated TCTP, nuclear transport of TCTP was inhibited confirming that sumoylation is critical for the nuclear transport of TCTP. Our previous studies demonstrated that TCTP can function as an antioxidant protein in the nucleus. When we mutated TCTP at the SUMO motif the antioxidant function of TCTP was compromised. Results presented in this study thus show that sumoylation plays an important role in the transport of TCTP into the nucleus where they function as antioxidant protein.

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31

Maeng, Jeehye, and Kyunglim Lee. "Protein transduction domain of translationally controlled tumor protein: characterization and application in drug delivery." Drug Delivery 29, no. 1 (September 14, 2022): 3009–21. http://dx.doi.org/10.1080/10717544.2022.2122636.

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32

Gnanasekar, Munirathinam, Gajalakshmi Dakshinamoorthy, and Kalyanasundaram Ramaswamy. "Translationally controlled tumor protein is a novel heat shock protein with chaperone-like activity." Biochemical and Biophysical Research Communications 386, no. 2 (August 2009): 333–37. http://dx.doi.org/10.1016/j.bbrc.2009.06.028.

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33

Pay, Aniko, Erwin Heberle-Bors, and Heribert Hirt. "An alfalfa cDNA encodes a protein with homology to translationally controlled human tumor protein." Plant Molecular Biology 19, no. 3 (June 1992): 501–3. http://dx.doi.org/10.1007/bf00023399.

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34

Thiele, Holger, Mario Berger, Angela Skalweit, and Bernd-Joachim Thiele. "Expression of the gene and processed pseudogenes encoding the human and rabbit translationally controlled tumour protein (TCTP)." European Journal of Biochemistry 267, no. 17 (September 2000): 5473–81. http://dx.doi.org/10.1046/j.1432-1327.2000.01609.x.

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35

Kim, D. K., B. Y. Nam, J. J. Li, J. T. Park, S. H. Lee, D. H. Kim, J. Y. Kim, et al. "Translationally controlled tumour protein is associated with podocyte hypertrophy in a mouse model of type 1 diabetes." Diabetologia 55, no. 4 (February 4, 2012): 1205–17. http://dx.doi.org/10.1007/s00125-012-2467-7.

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36

Diraison, F., K. Hayward, K. L. Sanders, F. Brozzi, S. Lajus, J. Hancock, J. E. Francis, et al. "Translationally controlled tumour protein (TCTP) is a novel glucose-regulated protein that is important for survival of pancreatic beta cells." Diabetologia 54, no. 2 (November 10, 2010): 368–79. http://dx.doi.org/10.1007/s00125-010-1958-7.

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37

Johansson, Helena, Dzeneta Vizlin-Hodzic, Tomas Simonsson, and Stina Simonsson. "Translationally controlled tumor protein interacts with nucleophosmin during mitosis in ES cells." Cell Cycle 9, no. 11 (June 2010): 2160–69. http://dx.doi.org/10.4161/cc.9.11.11841.

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38

Cheng, Xiang, Junhua Li, Jie Deng, Zhenzhen Li, Shuyan Meng, and Huayan Wang. "Translationally controlled tumor protein (TCTP) downregulates Oct4 expression in mouse pluripotent cells." BMB Reports 45, no. 1 (January 31, 2012): 20–25. http://dx.doi.org/10.5483/bmbrep.2012.45.1.20.

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39

Zheng, Kaizhi, Jianliang Wu, Liangyong Guo, Yingyu Ying, Peng Li, Yang Cao, Junfang Jiang, Xin Huang, Chunhua Meng, and Yongqing Jiang. "The involvement of translationally controlled tumor protein during lamb rumen epithelium development." Acta Histochemica 123, no. 5 (July 2021): 151737. http://dx.doi.org/10.1016/j.acthis.2021.151737.

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40

Sheverdin, Vadim, Jiwon Jung, and Kyunglim Lee. "Immunohistochemical localization of translationally controlled tumor protein in the mouse digestive system." Journal of Anatomy 223, no. 3 (July 8, 2013): 278–88. http://dx.doi.org/10.1111/joa.12077.

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41

van de Sande, Wendy W. J., Dirk-Jan Janse, Vishal Hira, Heidy Goedhart, Ruurd van der Zee, Abdalla O. A. Ahmed, Alewijn Ott, Henri Verbrugh, and Alex van Belkum. "Translationally Controlled Tumor Protein fromMadurella mycetomatis, a Marker for Tumorous Mycetoma Progression." Journal of Immunology 177, no. 3 (July 18, 2006): 1997–2005. http://dx.doi.org/10.4049/jimmunol.177.3.1997.

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42

M. MacDonald, Susan. "Histamine Releasing Factor/Translationally Controlled Tumor Protein: History, Functions and Clinical Implications." Open Allergy Journal 5, no. 1 (May 18, 2012): 12–18. http://dx.doi.org/10.2174/1874838401205010012.

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Histamine Releasing Factor (HRF) also known as Translationally Controlled Tumor Protein (TCTP) is a ubiquitous, novel protein that has both intracellular and extracellular functions. The purpose of this review is to highlight the background history of the molecule, the clinical implications and focus on the extracellular functions. Specifically the cells and the cytokines that are produced when stimulated by HRF/TCTP will be delineated as well as the signal transduction pathway that HRF/TCTP elicits will be described. Originally it was thought that HRF/TCTP interacted with IgE. Subsequently, cells that do not bind IgE also respond to HRF/TCTP and the interaction with IgE was questioned. Now, very recently, HRF/TCTP or at least its mouse counterpart appears to interact with some, but not all IgE and IgG molecules. HRF/TCTP has been shown to activate multiple human cells including basophils, eosinophils, T cells and B cells. Many of the cells that are activated by HRF/TCTP participate in the allergic response, leading to the conclusion that the extracellular functions of HRF/TCTP could exacerbate the allergic, inflammatory response.

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43

Bhisutthibhan, Jamaree, Martin A. Philbert, Hisashi Fujioka, Masamichi Aikawa, and Steven R. Meshnick. "The Plasmodium falciparum translationally controlled tumor protein: subcellular localization and calcium binding." European Journal of Cell Biology 78, no. 9 (September 1999): 665–70. http://dx.doi.org/10.1016/s0171-9335(99)80052-1.

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44

Kim, Miyoung, Junho Chung, Chulhee Lee, Jaehoon Jung, Youngjoo Kwon, and Kyunglim Lee. "A peptide binding to dimerized translationally controlled tumor protein modulates allergic reactions." Journal of Molecular Medicine 89, no. 6 (March 8, 2011): 603–10. http://dx.doi.org/10.1007/s00109-011-0740-8.

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45

Guillaume, Elisabeth, Charles Pineau, Bertrand Evrard, Alain Dupaix, Ejvind Moertz, Jean-Charles Sanchez, Denis F. Hochstrasser, and Bernard Jégou. "Cellular distribution of translationally controlled tumor protein in rat and human testes." PROTEOMICS 1, no. 7 (July 2001): 880–89. http://dx.doi.org/10.1002/1615-9861(200107)1:7<880::aid-prot880>3.0.co;2-2.

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46

Sheverdin, Vadim, Seong-Yeon Bae, Dong Hae Shin, and Kyunglim Lee. "Expression and localization of translationally controlled tumor protein in rat urinary organs." Microscopy Research and Technique 75, no. 11 (July 18, 2012): 1576–81. http://dx.doi.org/10.1002/jemt.22103.

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47

Bommer, U.-A., C. Heng, A. Perrin, P. Dash, S. Lobov, A. Elia, and M. J. Clemens. "Roles of the translationally controlled tumour protein (TCTP) and the double-stranded RNA-dependent protein kinase, PKR, in cellular stress responses." Oncogene 29, no. 5 (November 9, 2009): 763–73. http://dx.doi.org/10.1038/onc.2009.380.

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48

XU, Aimin, A. Richard BELLAMY, and John A. TAYLOR. "Expression of translationally controlled tumour protein is regulated by calcium at both the transcriptional and post-transcriptional level." Biochemical Journal 342, no. 3 (September 15, 1999): 683. http://dx.doi.org/10.1042/0264-6021:3420683.

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49

Bruckner, Fernanda Prieto, André Da Silva Xavier, Renan De Souza Cascardo, Wagner Campos Otoni, Francisco Murilo Zerbini, and Poliane Alfenas-Zerbini. "Translationally controlled tumour protein (TCTP) from tomato and Nicotiana benthamiana is necessary for successful infection by a potyvirus." Molecular Plant Pathology 18, no. 5 (July 27, 2016): 672–83. http://dx.doi.org/10.1111/mpp.12426.

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Funston, Garth, Walter Goh, Siau Jia Wei, Quah Soo Tng, Christopher Brown, Loh Jiah Tong, Chandra Verma, David Lane, and Farid Ghadessy. "Binding of Translationally Controlled Tumour Protein to the N-Terminal Domain of HDM2 Is Inhibited by Nutlin-3." PLoS ONE 7, no. 8 (August 13, 2012): e42642. http://dx.doi.org/10.1371/journal.pone.0042642.

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