G. W. Beadle and E. L. Tatum, Genetic Control of Biochemical Reactions in Neurospora, Proc Natl Acad Sci, vol.27, pp.499-506, 1941.

J. Piatigorsky and G. J. Wistow, Enzyme/crystallins: gene sharing as an evolutionary strategy, Cell, vol.57, pp.197-199, 1989.

C. J. Jeffery, Moonlighting proteins, Trends Biochem Sci, vol.24, pp.8-11, 1999.

D. Huberts and I. J. Van-der-klei, Moonlighting proteins: an intriguing mode of multitasking, Biochim Biophys Acta, vol.1803, pp.520-525, 2010.

,

C. E. Chapple, B. Robisson, and L. Spinelli, Extreme multifunctional proteins identified from a human protein interaction network, Nat Commun, vol.6, p.7412, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01407399

C. E. Chapple and C. Brun, Redefining protein moonlighting, Oncotarget, vol.6, pp.16812-16813, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01407805

L. Franco-serrano, S. Hernández, and A. Calvo, MultitaskProtDB-II: an update of a database of multitasking/moonlighting proteins, Nucleic Acids Res, vol.46, pp.645-648, 2018.

S. D. Copley, Moonlighting is mainstream: paradigm adjustment required, BioEssays : news and reviews in molecular, cellular and developmental biology, vol.34, pp.578-88, 2012.

C. J. Jeffery, Protein moonlighting: what is it, and why is it important, Philos Trans R Soc Lond, B, Biol Sci, vol.373, 2018.

C. J. Jeffery, An introduction to protein moonlighting, Biochem Soc Trans, vol.42, pp.1679-1683, 2014.

C. Gancedo, C. Flores, and J. M. Gancedo, The Expanding Landscape of Moonlighting Proteins in Yeasts, Microbiol Mol Biol Rev, vol.80, pp.765-777, 2016.

,

A. Espinosa-cantú, D. Ascencio, and S. Herrera-basurto, Protein Moonlighting Revealed by Noncatalytic Phenotypes of Yeast Enzymes, Genetics, vol.208, pp.419-431, 2018.

I. Khan, M. Chitale, C. Rayon, and D. Kihara, Evaluation of function predictions by PFP, ESG,and PSI-BLAST for moonlighting proteins, BMC Proc, vol.6, 2012.

I. K. Khan, M. Bhuiyan, and D. Kihara, DextMP: deep dive into text for predicting moonlighting proteins, Bioinformatics, vol.33, pp.83-91, 2017.

,

I. K. Khan and D. Kihara, Genome-scale prediction of moonlighting proteins using diverse protein association information, Bioinformatics, vol.32, pp.2281-2288, 2016.

,

C. A. Maxwell, J. Mccarthy, and E. Turley, Cell-surface and mitotic-spindle RHAMM: moonlighting or dual oncogenic functions?, J Cell Sci, vol.121, pp.925-932, 2008.

E. Becker, B. Robisson, and C. E. Chapple, Multifunctional proteins revealed by overlapping clustering in protein interaction network, Bioinformatics, vol.28, pp.84-90, 2012.
URL : https://hal.archives-ouvertes.fr/hal-00877694

T. J. Gibson, Cell regulation: determined to signal discrete cooperation, Trends Biochem Sci, vol.34, pp.471-482, 2009.

V. Neduva and R. B. Russell, Linear motifs: evolutionary interaction switches, FEBS letters, vol.579, pp.3342-3347, 2005.

K. Van-roey, T. J. Gibson, and N. E. Davey, Motif switches: decision-making in cell regulation, Curr Opin Struct Biol, vol.22, pp.378-385, 2012.

C. L. Brooks, M. Li, and M. Hu, The p53--Mdm2--HAUSP complex is involved in p53 stabilization by HAUSP, Oncogene, vol.26, pp.7262-7266, 2007.

,

K. Van-roey, H. Dinkel, and R. J. Weatheritt, The switches.ELM resource: a compendium of conditional regulatory interaction interfaces, Science signaling, vol.6, p.7, 2013.

C. Tristan, N. Shahani, T. W. Sedlak, and A. Sawa, The diverse functions of GAPDH: views from different subcellular compartments, Cell Signal, vol.23, pp.317-323, 2011.

M. R. Hara, N. Agrawal, and S. F. Kim, S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding, Nat Cell Biol, vol.7, pp.665-674, 2005.

N. Sen, M. R. Hara, and M. D. Kornberg, Nitric oxide-induced nuclear GAPDH activates p300/CBP and mediates apoptosis, Nat Cell Biol, vol.10, pp.866-873, 2008.

K. Volz, The functional duality of iron regulatory protein 1, Curr Opin Struct Biol, vol.18, pp.106-111, 2008.

C. Fillebeen, A. Caltagirone, and A. Martelli, IRP1 Ser-711 is a phosphorylation site, critical for regulation of RNA-binding and aconitase activities, Biochem J, vol.388, pp.143-150, 2005.
URL : https://hal.archives-ouvertes.fr/hal-00382029

S. L. Clarke, A. Vasanthakumar, and S. A. Anderson, Iron-responsive degradation of iron-regulatory protein 1 does not require the Fe-S cluster, EMBO J, vol.25, pp.544-553, 2006.

K. M. Deck, A. Vasanthakumar, and S. A. Anderson, Evidence that phosphorylation of iron regulatory protein 1 at Serine 138 destabilizes the [4Fe-4S] cluster in cytosolic aconitase by enhancing 4Fe-3Fe cycling, J Biol Chem, vol.284, pp.12701-12709, 2009.

A. J. Lay, X. M. Jiang, and O. Kisker, Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide reductase, Nature, vol.408, pp.869-873, 2000.

,

P. Shetty, T. Velusamy, and Y. P. Bhandary, Urokinase receptor expression involves tyrosine phosphorylation of phosphoglycerate kinase, Mol Cell Biochem, vol.335, pp.235-247, 2010.

S. J. Royle, Mitotic moonlighting functions for membrane trafficking proteins, Traffic, vol.12, pp.791-798, 2011.

C. M. Smith and M. Chircop, Clathrin-mediated endocytic proteins are involved in regulating mitotic progression and completion, Traffic, vol.13, pp.1628-1641, 2012.

,

S. M. Ferguson, D. Camilli, and P. , Dynamin, a membrane-remodelling GTPase, Nat Rev Mol Cell Biol, vol.13, pp.75-88, 2012.

H. M. Thompson, A. R. Skop, and U. Euteneuer, The large GTPase dynamin associates with the spindle midzone and is required for cytokinesis, Curr Biol, vol.12, pp.2111-2117, 2002.

M. Chircop, B. Sarcevic, and M. R. Larsen, Phosphorylation of dynamin II at serine-764 is associated with cytokinesis, Biochim Biophys Acta, vol.1813, pp.1689-1699, 2011.

R. M. Monaghan and A. J. Whitmarsh, Mitochondrial Proteins Moonlighting in the Nucleus, Trends Biochem Sci, vol.40, pp.728-735, 2015.

L. Chen, D. Liu, and Z. Songyang, Telomere maintenance through spatial control of telomeric proteins, Mol Cell Biol, vol.27, pp.5898-5909, 2007.

L. Chen, Y. Zhang, and Q. Zhang, Mitochondrial localization of telomeric protein TIN2 links telomere regulation to metabolic control, Mol Cell, vol.47, pp.839-850, 2012.

C. Chen, S. Zabad, and H. Liu, MoonProt 2.0: an expansion and update of the moonlighting proteins database, Nucleic Acids Res, vol.46, pp.640-644, 2018.

,

J. S. Amberger, C. A. Bocchini, and F. Schiettecatte, OMIM.org: Online Mendelian Inheritance in Man (OMIM®), an online catalog of human genes and genetic disorders, Nucleic Acids Res, vol.43, pp.789-798, 2015.

, Protein Data Bank: the single global archive for 3D macromolecular structure data, Nucleic Acids Res, 2018.

D. M. Ribeiro, G. Briere, and B. Bely, MoonDB 2.0: an updated database of extreme multifunctional and moonlighting proteins, Nucleic Acids Res, 2018.
URL : https://hal.archives-ouvertes.fr/hal-01907669

A. Zanzoni, C. E. Chapple, and C. Brun, Relationships between predicted moonlighting proteins, human diseases, and comorbidities from a network perspective, Front Physiol, vol.6, p.171, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01202109

C. Corbi-verge and P. M. Kim, Motif mediated protein-protein interactions as drug targets, Cell Commun Signal, vol.14, 2016.