A soluble amino acid-incorporating system from rat liver, Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects, vol.76, pp.474-477, 1963. ,
DOI : 10.1016/0926-6550(63)90070-7
C]TYROSINE BY A RIBONUCLEASE-INSENSITIVE SYSTEM, Journal of Neurochemistry, vol.145, issue.1, pp.97-108, 1973. ,
DOI : 10.1016/0022-2836(69)90086-2
Alternative Splicing Results in Differential Expression, Activity, and Localization of the Two Forms of Arginyl-tRNA-Protein Transferase, a Component of the N-End Rule Pathway, Molecular and Cellular Biology, vol.19, issue.1, pp.182-193, 1999. ,
DOI : 10.1128/MCB.19.1.182
Protein Arginylation in Rat Brain Cytosol: A Proteomic Analysis, Neurochemical Research, vol.282, issue.3, pp.401-409, 2006. ,
DOI : 10.1007/s11064-005-9037-z
URL : https://hal.archives-ouvertes.fr/hal-00377740
Calreticulin: one protein, one gene, many functions, Biochemical Journal, vol.344, issue.2, pp.281-92, 1999. ,
DOI : 10.1042/bj3440281
Calcium, a signaling molecule in the endoplasmic reticulum?, Trends in Biochemical Sciences, vol.25, issue.7, pp.307-311, 2000. ,
DOI : 10.1016/S0968-0004(00)01588-7
Overexpression of calreticulin increases the Ca2+ capacity of rapidly exchanging Ca2+ stores and reveals aspects of their lumenal microenvironment and function, The Journal of Cell Biology, vol.130, issue.4, pp.847-855, 1995. ,
DOI : 10.1083/jcb.130.4.847
Calreticulin Is a Receptor for Nuclear Export, The Journal of Cell Biology, vol.22, issue.1, pp.127-140, 2001. ,
DOI : 10.1093/nar/23.16.3268
Thrombospondin signaling through the calreticulin/LDL receptor-related protein co-complex stimulates random and directed cell migration, Journal of Cell Science, vol.116, issue.14, pp.2917-2927, 2003. ,
DOI : 10.1242/jcs.00600
Calreticulin is essential for integrin-mediated calcium signalling and cell adhesion, Nature, vol.386, issue.6627, pp.843-847, 1997. ,
DOI : 10.1038/386843a0
Calreticulin Couples Calcium Release and Calcium Influx in Integrin-mediated Calcium Signaling, Molecular Biology of the Cell, vol.11, issue.4, pp.1433-1443, 2000. ,
DOI : 10.1091/mbc.11.4.1433
Retrotranslocation of the Chaperone Calreticulin from the Endoplasmic Reticulum Lumen to the Cytosol, Molecular and Cellular Biology, vol.25, issue.20, pp.8844-8853, 2005. ,
DOI : 10.1128/MCB.25.20.8844-8853.2005
The Posttranslational Arginylation of Proteins in Different Regions of the Rat Brain, Journal of Neurochemistry, vol.43, issue.5, pp.1735-1739, 1991. ,
DOI : 10.1016/0006-291X(66)90537-7
A tool coming of age: thapsigargin as an inhibitor of sarco-endoplasmic reticulum Ca2+-ATPases, Trends in Pharmacological Sciences, vol.19, issue.4, pp.131-135, 1998. ,
DOI : 10.1016/S0165-6147(98)01184-5
Ca2+-Dependent Nuclear Export Mediated by Calreticulin, Molecular and Cellular Biology, vol.22, issue.17, pp.6286-6297, 2002. ,
DOI : 10.1128/MCB.22.17.6286-6297.2002
The Sarco/Endoplasmic Reticulum Calcium-ATPase 2b Is an Endoplasmic Reticulum Stress-inducible Protein, Journal of Biological Chemistry, vol.275, issue.29, pp.22363-22372, 2000. ,
DOI : 10.1074/jbc.M001569200
Regulation of Calreticulin Gene Expression by Calcium, The Journal of Cell Biology, vol.11, issue.3, pp.547-557, 1997. ,
DOI : 10.1074/jbc.270.27.15926
Stress granules and processing bodies are dynamically linked sites of mRNP remodeling, The Journal of Cell Biology, vol.20, issue.6, pp.871-884, 2005. ,
DOI : 10.1242/jcs.01477
Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination, Nature, vol.360, issue.6404, pp.597-599, 1992. ,
DOI : 10.1038/360597a0
RGS4 and RGS5 are in vivo substrates of the N-end rule pathway, Proceedings of the National Academy of Sciences, vol.102, issue.42, pp.15030-15035, 2005. ,
DOI : 10.1073/pnas.0507533102
??2 subunit of G protein heterotrimer is an N-end rule ubiquitylation substrate, Proceedings of the National Academy of Sciences, vol.100, issue.9, pp.5081-5086, 2003. ,
DOI : 10.1073/pnas.0831228100
Arginylation of ??-Actin Regulates Actin Cytoskeleton and Cell Motility, Science, vol.313, issue.5784, pp.192-196, 2006. ,
DOI : 10.1126/science.1129344
Translational Control of Gene Expression. Cold Spring Harbor Laboratory; Cold Spring Harbor, pp.547-560, 2000. ,
Sum1, a Component of the Fission Yeast eIF3 Translation Initiation Complex, Is Rapidly Relocalized During Environmental Stress and Interacts with Components of the 26S Proteasome, Molecular Biology of the Cell, vol.13, issue.5, pp.1626-1640, 2002. ,
DOI : 10.1091/mbc.01-06-0301
Dynamic Shuttling of Tia-1 Accompanies the Recruitment of mRNA to Mammalian Stress Granules, The Journal of Cell Biology, vol.18, issue.6, pp.1257-1268, 2000. ,
DOI : 10.1093/emboj/16.6.1401
Cytoplasmic heat shock granules are formed from precursor particles and are associated with a specific set of mRNAs., Molecular and Cellular Biology, vol.9, issue.3, pp.1298-1308, 1983. ,
DOI : 10.1128/MCB.9.3.1298
HuR binding to cytoplasmic mRNA is perturbed by heat shock, Proceedings of the National Academy of Sciences, vol.97, issue.7, pp.3073-3078, 2000. ,
DOI : 10.1073/pnas.97.7.3073
Identification of calreticulin as a rubella virus RNA binding protein., Proceedings of the National Academy of Sciences, vol.91, issue.26, pp.12770-12774, 1994. ,
DOI : 10.1073/pnas.91.26.12770