ARL15 and its Multiple Disease Association: Emerging Functions and Potential Therapeutic Application
- Authors: Saini M.1, Anand V.1, Sharma A.2, Pandey A.3, Thelma B.3, Kundu S.1
-
Affiliations:
- Department of Biochemistry, University of Delhi South Campus
- Department of Genetics,, University of Delhi South Campus
- Department of Genetics, University of Delhi South Campus
- Issue: Vol 25, No 2 (2024)
- Pages: 137-153
- Section: Life Sciences
- URL: https://transsyst.ru/1389-2037/article/view/645528
- DOI: https://doi.org/10.2174/1389203724666230915123217
- ID: 645528
Cite item
Full Text
Abstract
ARL15 is a member of the RAS superfamily of small GTPases and is associated with several metabolic traits, including increased risk of diabetes, rheumatoid arthritis and lipid metabolism disorders. The ARL15 gene encodes for an uncharacterized small GTP binding protein. Its precise role in human physiology remains unknown, but several genetic association studies have recognized different variants in this gene to be statistically associated with numerous traits and complex diseases. Here, we provided the unique features of ARL15 small G protein, its association with varied metabolic and lifestyle diseases, its function in vesicular and lipid trafficking, and its binding partners. We outlined this protein as a promising and emerging therapeutic target to combat metabolic disorders like cardiovascular diseases, diabetes and rheumatoid arthritis. The review provides a comprehensive description of the current advancements in ARL15 research with a perspective that focused research will position this small GTPase as a viable target for the treatment of rheumatoid arthritis.
About the authors
Manisha Saini
Department of Biochemistry, University of Delhi South Campus
Email: info@benthamscience.net
Varnita Anand
Department of Biochemistry, University of Delhi South Campus
Email: info@benthamscience.net
Aditya Sharma
Department of Genetics,, University of Delhi South Campus
Email: info@benthamscience.net
Anuj Pandey
Department of Genetics, University of Delhi South Campus
Email: info@benthamscience.net
Bittianda Thelma
Department of Genetics, University of Delhi South Campus
Email: info@benthamscience.net
Suman Kundu
Department of Biochemistry, University of Delhi South Campus
Author for correspondence.
Email: info@benthamscience.net
References
- Colicelli, J. Human RAS superfamily proteins and related GTPases. Sci. STKE, 2004, 2004(250), RE13. doi: 10.1126/stke.2502004re13 PMID: 15367757
- Wennerberg, K.; Rossman, K.L.; Der, C.J. The Ras superfamily at a glance. J. Cell Sci., 2005, 118(5), 843-846. doi: 10.1242/jcs.01660 PMID: 15731001
- Bokoch, G.M.; Der, C.J. Emerging concepts in the Ras superfamily of GTP‐binding proteins. FASEB J., 1993, 7(9), 750-759. doi: 10.1096/fasebj.7.9.8330683 PMID: 8330683
- Tetlow, A.L.; Tamanoi, F. The ras superfamily G-proteins. Enzymes, 2013, 33(Pt A), 1-14. doi: 10.1016/B978-0-12-416749-0.00001-4 PMID: 25033798
- Heasman, S.J.; Ridley, A.J. Mammalian Rho GTPases: New insights into their functions from in vivo studies. Nat. Rev. Mol. Cell Biol., 2008, 9(9), 690-701. doi: 10.1038/nrm2476 PMID: 18719708
- Chavrier, P.; Goud, B. The role of ARF and Rab GTPases in membrane transport. Curr. Opin. Cell Biol., 1999, 11(4), 466-475. doi: 10.1016/S0955-0674(99)80067-2 PMID: 10449335
- Casanova, J.E. ARFs. Curr. Biol., 2003, 13(4), R123. doi: 10.1016/S0960-9822(03)00069-1 PMID: 12593809
- Matozaki, T.; Nakanishi, H.; Takai, Y. Small G-protein networks. Cell. Signal., 2000, 12(8), 515-524. doi: 10.1016/S0898-6568(00)00102-9 PMID: 11027944
- Klöpper, T.H.; Kienle, N.; Fasshauer, D.; Munro, S. Untangling the evolution of Rab G proteins: Implications of a comprehensive genomic analysis. BMC Biol., 2012, 10(1), 71. doi: 10.1186/1741-7007-10-71 PMID: 22873208
- Randazzo, P.A.; Nie, Z.; Miura, K.; Hsu, V.W. Molecular aspects of the cellular activities of ADP-ribosylation factors. Sci. STKE, 2000, 2000(59), re1. doi: 10.1126/stke.2000.59.re1 PMID: 11752622
- Donaldson, J.G.; Jackson, C.L. Regulators and effectors of the ARF GTPases. Curr. Opin. Cell Biol., 2000, 12(4), 475-482. doi: 10.1016/S0955-0674(00)00119-8 PMID: 10873831
- Adarska, P.; Wong-Dilworth, L.; Bottanelli, F. ARF GTPases and their ubiquitous role in intracellular trafficking beyond the golgi. Front. Cell Dev. Biol., 2021, 9(7), 679046. doi: 10.3389/fcell.2021.679046 PMID: 34368129
- Kalab, P.; Weis, K.; Heald, R. Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts. Science, 2002, 295(5564), 2452-2456. doi: 10.1126/science.1068798 PMID: 11923538
- Moore, M.S.; Blobel, G. The two steps of nuclear import, targeting to the nuclear envelope and translocation through the nuclear pore, require different cytosolic factors. Cell, 1992, 69(6), 939-950. doi: 10.1016/0092-8674(92)90613-H PMID: 1606616
- Kjeldgaard, M.; Nyborg, J.; Clark, B.F.C. The GTP binding motif: Variations on a theme. FASEB J., 1996, 10(12), 1347-1368. doi: 10.1096/fasebj.10.12.8903506 PMID: 8903506
- Zhang, B.; Zhang, Y.; Wang, Z.; Zheng, Y. The role of Mg2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins. J. Biol. Chem., 2000, 275(33), 25299-25307. doi: 10.1074/jbc.M001027200 PMID: 10843989
- Brunsveld, L.; Kuhlmann, J.; Alexandrov, K.; Wittinghofer, A.; Goody, R.S.; Waldmann, H. Lipidated ras and rab peptides and proteins-synthesis, structure, and function. Angew. Chem. Int. Ed., 2006, 45(40), 6622-6646. doi: 10.1002/anie.200600855 PMID: 17031879
- Peurois, F.; Veyron, S.; Ferrandez, Y.; Ladid, I.; Benabdi, S.; Zeghouf, M.; Peyroche, G.; Cherfils, J. Characterization of the activation of small GTPases by their GEFs on membranes using artificial membrane tethering. Biochem. J., 2017, 474(7), 1259-1272. doi: 10.1042/BCJ20170015 PMID: 28196833
- Klooster, J.P.; Hordijk, P.L. Targeting and localized signalling by small GTPases. Biol. Cell, 2007, 99(1), 1-12. doi: 10.1042/BC20060071 PMID: 17155934
- Kahn, R.A.; Cherfils, J.; Elias, M.; Lovering, R.C.; Munro, S.; Schurmann, A. Nomenclature for the human Arf family of GTP-binding proteins: ARF, ARL, and SAR proteins. J. Cell Biol., 2006, 172(5), 645-650. doi: 10.1083/jcb.200512057 PMID: 16505163
- Donaldson, J.G.; Jackson, C.L. ARF family G proteins and their regulators: Roles in membrane transport, development and disease. Nat. Rev. Mol. Cell Biol., 2011, 12(6), 362-375. doi: 10.1038/nrm3117 PMID: 21587297
- Memon, A.R. The role of ADP-ribosylation factor and SAR1 in vesicular trafficking in plants. Biochim. Biophys. Acta Biomembr., 2004, 1664(1), 9-30. doi: 10.1016/j.bbamem.2004.04.005 PMID: 15238254
- Wu, M.; Lu, L.; Hong, W.; Song, H. Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Arl1. Nat. Struct. Mol. Biol., 2004, 11(1), 86-94. doi: 10.1038/nsmb714 PMID: 14718928
- Bartolini, F.; Bhamidipati, A.; Thomas, S.; Schwahn, U.; Lewis, S.A.; Cowan, N.J. Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C. J. Biol. Chem., 2002, 277(17), 14629-14634. doi: 10.1074/jbc.M200128200 PMID: 11847227
- Bhamidipati, A.; Lewis, S.A.; Cowan, N.J. ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin. J. Cell Biol., 2000, 149(5), 1087-1096. doi: 10.1083/jcb.149.5.1087 PMID: 10831612
- Bowzard, J.B.; Cheng, D.; Peng, J.; Kahn, R.A. ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs. J. Biol. Chem., 2007, 282(24), 17568-17580. doi: 10.1074/jbc.M701347200 PMID: 17452337
- Cai, X.B.; Wu, K.C.; Zhang, X.; Lv, J.N.; Jin, G.H.; Xiang, L.; Chen, J.; Huang, X.F.; Pan, D.; Lu, B.; Lu, F.; Qu, J.; Jin, Z.B. Whole‐exome sequencing identified ARL2 as a novel candidate gene for MRCS (microcornea, rod‐cone dystrophy, cataract, and posterior staphyloma) syndrome. Clin. Genet., 2019, 96(1), 61-71. doi: 10.1111/cge.13541 PMID: 30945270
- Muromoto, R.; Sekine, Y.; Imoto, S.; Ikeda, O.; Okayama, T.; Sato, N.; Matsuda, T. BART is essential for nuclear retention of STAT3. Int. Immunol., 2008, 20(3), 395-403. doi: 10.1093/intimm/dxm154 PMID: 18234692
- Sharer, J.D.; Kahn, R.A. The ARF-like 2 (ARL2)-binding protein, BART. J. Biol. Chem., 1999, 274(39), 27553-27561. doi: 10.1074/jbc.274.39.27553 PMID: 10488091
- Tian, G.; Thomas, S.; Cowan, N.J. Effect of TBCD and its regulatory interactor Arl2 on tubulin and microtubule integrity. Cytoskeleton, 2010, 67(11), 706-714. doi: 10.1002/cm.20480 PMID: 20740604
- Van Valkenburgh, H.; Shern, J.F.; Sharer, J.D.; Zhu, X.; Kahn, R.A. ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: Characterizing ARL1-binding proteins. J. Biol. Chem., 2001, 276(25), 22826-22837. doi: 10.1074/jbc.M102359200 PMID: 11303027
- Veltel, S.; Kravchenko, A.; Ismail, S.; Wittinghofer, A. Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3-effector-GAP complex. FEBS Lett., 2008, 582(17), 2501-2507. doi: 10.1016/j.febslet.2008.05.053 PMID: 18588884
- Zhou, C.; Cunningham, L.; Marcus, A.I.; Li, Y.; Kahn, R.A. Arl2 and Arl3 regulate different microtubule-dependent processes. Mol. Biol. Cell, 2006, 17(5), 2476-2487. doi: 10.1091/mbc.e05-10-0929 PMID: 16525022
- Kühnel, K.; Veltel, S.; Schlichting, I.; Wittinghofer, A. Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3. Structure, 2006, 14(2), 367-378. doi: 10.1016/j.str.2005.11.008 PMID: 16472755
- Wright, K.J.; Baye, L.M.; Olivier-Mason, A.; Mukhopadhyay, S.; Sang, L.; Kwong, M.; Wang, W.; Pretorius, P.R.; Sheffield, V.C.; Sengupta, P.; Slusarski, D.C.; Jackson, P.K. An ARL3-UNC119-RP2 GTPase cycle targets myristoylated NPHP3 to the primary cilium. Genes Dev., 2011, 25(22), 2347-2360. doi: 10.1101/gad.173443.111 PMID: 22085962
- Hofmann, I.; Thompson, A.; Sanderson, C.M.; Munro, S. The Arl4 family of small G proteins can recruit the cytohesin Arf6 exchange factors to the plasma membrane. Curr. Biol., 2007, 17(8), 711-716. doi: 10.1016/j.cub.2007.03.007 PMID: 17398095
- Lin, C.Y.; Huang, P.H.; Liao, W.L.; Cheng, H.J.; Huang, C.F.; Kuo, J.C.; Patton, W.A.; Massenburg, D.; Moss, J.; Lee, F.J.S. ARL4, an ARF-like protein that is developmentally regulated and localized to nuclei and nucleoli. J. Biol. Chem., 2000, 275(48), 37815-37823. doi: 10.1074/jbc.M002470200 PMID: 10980193
- Engel, T.; Lueken, A.; Bode, G.; Hobohm, U.; Lorkowski, S.; Schlueter, B.; Rust, S.; Cullen, P.; Pech, M.; Assmann, G.; Seedorf, U. ADP-ribosylation factor (ARF)-like 7 (ARL7) is induced by cholesterol loading and participates in apolipoprotein AI-dependent cholesterol export. FEBS Lett., 2004, 566(1-3), 241-246. doi: 10.1016/j.febslet.2004.04.048 PMID: 15147902
- Wei, S.; Xie, C.; Abe, Y.; Cai, J. ADP-ribosylation factor like 7 (ARL7) interacts with α-tubulin and modulates intracellular vesicular transport. Biochem. Biophys. Res. Commun., 2009, 384(3), 352-356. doi: 10.1016/j.bbrc.2009.04.125 PMID: 19409876
- Ishida, M.; Bonifacino, J.S. ARFRP1 functions upstream of ARL1 and ARL5 to coordinate recruitment of distinct tethering factors to the trans-golgi network. J. Cell Biol., 2019, 218(11), 3880. doi: 10.1083/jcb.20190509710072019c PMID: 31604800
- Lin, C.Y.; Li, C.C.; Huang, P.H.; Lee, F.J.S. A developmentally regulated ARF-like 5 protein (ARL5), localized to nuclei and nucleoli, interacts with heterochromatin protein 1. J. Cell Sci., 2002, 115(23), 4433-4445. doi: 10.1242/jcs.00123 PMID: 12414990
- Shi, M.; Chen, B.; Mahajan, D.; Boh, B.K.; Zhou, Y.; Dutta, B.; Tie, H.C.; Sze, S.K.; Wu, G.; Lu, L. Amino acids stimulate the endosome-to-Golgi trafficking through Ragulator and small GTPase Arl5. Nat. Commun., 2018, 9(1), 4987. doi: 10.1038/s41467-018-07444-y PMID: 30478271
- Houghton, F.J.; Bellingham, S.A.; Hill, A.F.; Bourges, D.; Ang, D.K.Y.; Gemetzis, T.; Gasnereau, I.; Gleeson, P.A. Arl5b is a Golgi-localised small G protein involved in the regulation of retrograde transport. Exp. Cell Res., 2012, 318(5), 464-477. doi: 10.1016/j.yexcr.2011.12.023 PMID: 22245584
- Jaimon, E.; Tripathi, A.; Khurana, A.; Ghosh, D.; Sugatha, J.; Datta, S. Binding with heat shock cognate protein HSC70 fine-tunes the Golgi association of the small GTPase ARL5B. J. Biol. Chem., 2021, 297(6), 101422. doi: 10.1016/j.jbc.2021.101422 PMID: 34798070
- Rosa-Ferreira, C.; Christis, C.; Torres, I.L.; Munro, S. The small G protein Arl5 contributes to endosome-to-Golgi traffic by aiding the recruitment of the GARP complex to the Golgi. Biol. Open, 2015, 4(4), 474-481. doi: 10.1242/bio.201410975 PMID: 25795912
- Toh, W.H.; Tan, J.Z.A.; Zulkefli, K.L.; Houghton, F.J.; Gleeson, P.A. Amyloid precursor protein traffics from the Golgi directly to early endosomes in an Arl5b- and AP4-dependent pathway. Traffic, 2017, 18(3), 159-175. doi: 10.1111/tra.12465 PMID: 28000370
- Jin, H.; White, S.R.; Shida, T.; Schulz, S.; Aguiar, M.; Gygi, S.P.; Bazan, J.F.; Nachury, M.V. The conserved Bardet-Biedl syndrome proteins assemble a coat that traffics membrane proteins to cilia. Cell, 2010, 141(7), 1208-1219. doi: 10.1016/j.cell.2010.05.015 PMID: 20603001
- Liew, G.M.; Ye, F.; Nager, A.R.; Murphy, J.P.; Lee, J.S.; Aguiar, M.; Breslow, D.K.; Gygi, S.P.; Nachury, M.V. The intraflagellar transport protein IFT27 promotes BBSome exit from cilia through the GTPase ARL6/BBS3. Dev. Cell, 2014, 31(3), 265-278. doi: 10.1016/j.devcel.2014.09.004 PMID: 25443296
- Seo, S.; Zhang, Q.; Bugge, K.; Breslow, D.K.; Searby, C.C.; Nachury, M.V.; Sheffield, V.C. A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and Smoothened. PLoS Genet., 2011, 7(11), e1002358. doi: 10.1371/journal.pgen.1002358 PMID: 22072986
- Wiens, C.J.; Tong, Y.; Esmail, M.A.; Oh, E.; Gerdes, J.M.; Wang, J.; Tempel, W.; Rattner, J.B.; Katsanis, N.; Park, H.W.; Leroux, M.R. Bardet-Biedl syndrome-associated small GTPase ARL6 (BBS3) functions at or near the ciliary gate and modulates Wnt signaling. J. Biol. Chem., 2010, 285(21), 16218-16230. doi: 10.1074/jbc.M109.070953 PMID: 20207729
- Bagshaw, R.D.; Callahan, J.W.; Mahuran, D.J. The Arf-family protein, Arl8b, is involved in the spatial distribution of lysosomes. Biochem. Biophys. Res. Commun., 2006, 344(4), 1186-1191. doi: 10.1016/j.bbrc.2006.03.221 PMID: 16650381
- Marwaha, R.; Arya, S.B.; Jagga, D.; Kaur, H.; Tuli, A.; Sharma, M. The Rab7 effector PLEKHM1 binds Arl8b to promote cargo traffic to lysosomes. J. Cell Biol., 2017, 216(4), 1051-1070. doi: 10.1083/jcb.201607085 PMID: 28325809
- Okai, T.; Araki, Y.; Tada, M.; Tateno, T.; Kontani, K.; Katada, T. Novel small GTPase subfamily capable of associating with tubulin is required for chromosome segregation. J. Cell Sci., 2004, 117(20), 4705-4715. doi: 10.1242/jcs.01347 PMID: 15331635
- Rosa-Ferreira, C.; Munro, S. Arl8 and SKIP act together to link lysosomes to kinesin-1. Dev. Cell, 2011, 21(6), 1171-1178. doi: 10.1016/j.devcel.2011.10.007 PMID: 22172677
- Garg, S.; Sharma, M.; Ung, C.; Tuli, A.; Barral, D.C.; Hava, D.L.; Veerapen, N.; Besra, G.S.; Hacohen, N.; Brenner, M.B. Lysosomal trafficking, antigen presentation, and microbial killing are controlled by the Arf-like GTPase Arl8b. Immunity, 2011, 35(2), 182-193. doi: 10.1016/j.immuni.2011.06.009 PMID: 21802320
- Hofmann, I.; Munro, S. An N-terminally acetylated Arf-like GTPase is localised to lysosomes and affects their motility. J. Cell Sci., 2006, 119(8), 1494-1503. doi: 10.1242/jcs.02958 PMID: 16537643
- Khatter, D.; Raina, V.B.; Dwivedi, D.; Sindhwani, A.; Bahl, S.; Sharma, M. The small GTPase Arl8b regulates assembly of the mammalian HOPS complex to lysosomes. J. Cell Sci., 2015, 128(9), jcs.162651. doi: 10.1242/jcs.162651 PMID: 25908847
- Michelet, X.; Tuli, A.; Gan, H.; Geadas, C.; Sharma, M.; Remold, H.G.; Brenner, M.B. Lysosome-mediated plasma membrane repair is dependent on the small GTPase Arl8b and determines cell death type in mycobacterium tuberculosis infection. J. Immunol., 2018, 200(9), 3160-3169. doi: 10.4049/jimmunol.1700829 PMID: 29592961
- Tuli, A.; Thiery, J.; James, A.M.; Michelet, X.; Sharma, M.; Garg, S.; Sanborn, K.B.; Orange, J.S.; Lieberman, J.; Brenner, M.B. Arf-like GTPase Arl8b regulates lytic granule polarization and natural killer cell-mediated cytotoxicity. Mol. Biol. Cell, 2013, 24(23), 3721-3735. doi: 10.1091/mbc.e13-05-0259 PMID: 24088571
- Arya, S.B.; Kumar, G.; Kaur, H.; Kaur, A.; Tuli, A. ARL11 regulates lipopolysaccharide-stimulated macrophage activation by promoting mitogen-activated protein kinase (MAPK) signaling. J. Biol. Chem., 2018, 293(25), 9892-9909. doi: 10.1074/jbc.RA117.000727 PMID: 29618517
- Calin, G.A.; Trapasso, F.; Shimizu, M.; Dumitru, C.D.; Yendamuri, S.; Godwin, A.K.; Ferracin, M.; Bernardi, G.; Chatterjee, D.; Baldassarre, G.; Rattan, S.; Alder, H.; Mabuchi, H.; Shiraishi, T.; Hansen, L.L.; Overgaard, J.; Herlea, V.; Mauro, F.R.; Dighiero, G.; Movsas, B.; Rassenti, L.; Kipps, T.; Baffa, R.; Fusco, A.; Mori, M.; Russo, G.; Liu, C.G.; Neuberg, D.; Bullrich, F.; Negrini, M.; Croce, C.M. Familial cancer associated with a polymorphism in ARLTS1. N. Engl. J. Med., 2005, 352(16), 1667-1676. doi: 10.1056/NEJMoa042280 PMID: 15843669
- Barral, D.C.; Garg, S.; Casalou, C.; Watts, G.F.M.; Sandoval, J.L.; Ramalho, J.S.; Hsu, V.W.; Brenner, M.B. Arl13b regulates endocytic recycling traffic. Proc. Natl. Acad. Sci., 2012, 109(52), 21354-21359. doi: 10.1073/pnas.1218272110 PMID: 23223633
- Casalou, C.; Seixas, C.; Portelinha, A.; Pintado, P.; Barros, M.; Ramalho, J.S.; Lopes, S.S.; Barral, D.C. Arl13b and the nonmuscle myosin heavy chain IIA are required for circular dorsal ruffle formation and cell migration. J. Cell Sci., 2014, 127(Pt 12), jcs.143446. doi: 10.1242/jcs.143446 PMID: 24777479
- Caspary, T.; Larkins, C.E.; Anderson, K.V. The graded response to Sonic Hedgehog depends on cilia architecture. Dev. Cell, 2007, 12(5), 767-778. doi: 10.1016/j.devcel.2007.03.004 PMID: 17488627
- Cevik, S.; Sanders, A.A.W.M.; Van Wijk, E.; Boldt, K.; Clarke, L.; van Reeuwijk, J.; Hori, Y.; Horn, N.; Hetterschijt, L.; Wdowicz, A.; Mullins, A.; Kida, K.; Kaplan, O.I.; van Beersum, S.E.C.; Man Wu, K.; Letteboer, S.J.F.; Mans, D.A.; Katada, T.; Kontani, K.; Ueffing, M.; Roepman, R.; Kremer, H.; Blacque, O.E. Active transport and diffusion barriers restrict Joubert Syndrome-associated ARL13B/ARL-13 to an Inv-like ciliary membrane subdomain. PLoS Genet., 2013, 9(12), e1003977. doi: 10.1371/journal.pgen.1003977 PMID: 24339792
- Duldulao, N.A.; Lee, S.; Sun, Z. Cilia localization is essential for in vivo functions of the Joubert syndrome protein Arl13b/Scorpion. Development, 2009, 136(23), 4033-4042. doi: 10.1242/dev.036350 PMID: 19906870
- Hori, Y.; Kobayashi, T.; Kikko, Y.; Kontani, K.; Katada, T. Domain architecture of the atypical Arf-family GTPase Arl13b involved in cilia formation. Biochem. Biophys. Res. Commun., 2008, 373(1), 119-124. doi: 10.1016/j.bbrc.2008.06.001 PMID: 18554500
- Humbert, M.C.; Weihbrecht, K.; Searby, C.C.; Li, Y.; Pope, R.M.; Sheffield, V.C.; Seo, S. ARL13B, PDE6D, and CEP164 form a functional network for INPP5E ciliary targeting. Proc. Natl. Acad. Sci., 2012, 109(48), 19691-19696. doi: 10.1073/pnas.1210916109 PMID: 23150559
- Kinzel, D.; Boldt, K.; Davis, E.E.; Burtscher, I.; Trümbach, D.; Diplas, B.; Attié-Bitach, T.; Wurst, W.; Katsanis, N.; Ueffing, M.; Lickert, H. Pitchfork regulates primary cilia disassembly and left-right asymmetry. Dev. Cell, 2010, 19(1), 66-77. doi: 10.1016/j.devcel.2010.06.005 PMID: 20643351
- Paridaen, J.T.M.L.; Wilsch-Bräuninger, M.; Huttner, W.B. Asymmetric inheritance of centrosome-associated primary cilium membrane directs ciliogenesis after cell division. Cell, 2013, 155(2), 333-344. doi: 10.1016/j.cell.2013.08.060 PMID: 24120134
- Thomas, S.; Cantagrel, V.; Mariani, L.; Serre, V.; Lee, J.E.; Elkhartoufi, N.; de Lonlay, P.; Desguerre, I.; Munnich, A.; Boddaert, N.; Lyonnet, S.; Vekemans, M.; Lisgo, S.N.; Caspary, T.; Gleeson, J.; Attié-Bitach, T. Identification of a novel ARL13B variant in a Joubert syndrome-affected patient with retinal impairment and obesity. Eur. J. Hum. Genet., 2015, 23(5), 621-627. doi: 10.1038/ejhg.2014.156 PMID: 25138100
- Paul, P.; van den Hoorn, T.; Jongsma, M.L.M.; Bakker, M.J.; Hengeveld, R.; Janssen, L.; Cresswell, P.; Egan, D.A.; van Ham, M.; ten Brinke, A.; Ovaa, H.; Beijersbergen, R.L.; Kuijl, C.; Neefjes, J. A Genome-wide multidimensional RNAi screen reveals pathways controlling MHC class II antigen presentation. Cell, 2011, 145(2), 268-283. doi: 10.1016/j.cell.2011.03.023 PMID: 21458045
- Yang, F.; Li, T.; Peng, Z.; Liu, Y.; Guo, Y. The amphipathic helices of Arfrp1 and Arl14 are sufficient to determine subcellular localizations. J. Biol. Chem., 2020, 295(49), 16643-16654. doi: 10.1074/jbc.RA120.014999 PMID: 32972971
- Zhao, J.; Wang, M.; Deng, W.; Zhong, D.; Jiang, Y.; Liao, Y.; Chen, B.; Zhang, X. ADP-ribosylation factor-like GTPase 15 enhances insulin-induced AKT phosphorylation in the IR/IRS1/AKT pathway by interacting with ASAP2 and regulating PDPK1 activity. Biochem. Biophys. Res. Commun., 2017, 486(4), 865-871. doi: 10.1016/j.bbrc.2017.03.079 PMID: 28322786
- Zolotarov, Y.; Ma, C.; González-Recio, I.; Hardy, S.; Franken, G.A.C.; Uetani, N.; Latta, F.; Kostantin, E.; Boulais, J.; Thibault, M.P.; Côté, J.F.; Díaz-Moreno, I.; Quintana, A.D.; Hoenderop, J.G.J.; Martínez-Cruz, L.A.; Tremblay, M.L.; de Baaij, J.H.F. ARL15 modulates magnesium homeostasis through N-glycosylation of CNNMs. Cell. Mol. Life Sci., 2021, 78(13), 5427-5445. doi: 10.1007/s00018-021-03832-8 PMID: 34089346
- Yang, Y.K.; Qu, H.; Gao, D.; Di, W.; Chen, H.W.; Guo, X.; Zhai, Z.H.; Chen, D.Y. ARF-like protein 16 (ARL16) inhibits RIG-I by binding with its C-terminal domain in a GTP-dependent manner. J. Biol. Chem., 2011, 286(12), 10568-10580. doi: 10.1074/jbc.M110.206896 PMID: 21233210
- Behnia, R.; Panic, B.; Whyte, J.R.C.; Munro, S. Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p. Nat. Cell Biol., 2004, 6(5), 405-413. doi: 10.1038/ncb1120 PMID: 15077113
- Setty, S.R.G.; Shin, M.E.; Yoshino, A.; Marks, M.S.; Burd, C.G. Golgi recruitment of GRIP domain proteins by Arf-like GTPase 1 is regulated by Arf-like GTPase 3. Curr. Biol., 2003, 13(5), 401-404. doi: 10.1016/S0960-9822(03)00089-7 PMID: 12620188
- Panic, B.; Whyte, J.R.C.; Munro, S. The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts with vesicle-tethering factors at the Golgi apparatus. Curr. Biol., 2003, 13(5), 405-410. doi: 10.1016/S0960-9822(03)00091-5 PMID: 12620189
- Shin, H.W.; Kobayashi, H.; Kitamura, M.; Waguri, S.; Suganuma, T.; Uchiyama, Y.; Nakayama, K. Roles of ARFRP1 (ADP-ribosylation factor-related protein 1) in post-Golgi membrane trafficking. J. Cell Sci., 2005, 118(17), 4039-4048. doi: 10.1242/jcs.02524 PMID: 16129887
- Richards, J.B.; Waterworth, D.; ORahilly, S.; Hivert, M.F.; Loos, R.J.F.; Perry, J.R.B.; Tanaka, T.; Timpson, N.J.; Semple, R.K.; Soranzo, N.; Song, K.; Rocha, N.; Grundberg, E.; Dupuis, J.; Florez, J.C.; Langenberg, C.; Prokopenko, I.; Saxena, R.; Sladek, R.; Aulchenko, Y.; Evans, D.; Waeber, G.; Erdmann, J.; Burnett, M.S.; Sattar, N.; Devaney, J.; Willenborg, C.; Hingorani, A.; Witteman, J.C.M.; Vollenweider, P.; Glaser, B.; Hengstenberg, C.; Ferrucci, L.; Melzer, D.; Stark, K.; Deanfield, J.; Winogradow, J.; Grassl, M.; Hall, A.S.; Egan, J.M.; Thompson, J.R.; Ricketts, S.L.; König, I.R.; Reinhard, W.; Grundy, S.; Wichmann, H.E.; Barter, P.; Mahley, R.; Kesaniemi, Y.A.; Rader, D.J.; Reilly, M.P.; Epstein, S.E.; Stewart, A.F.R.; Van Duijn, C.M.; Schunkert, H.; Burling, K.; Deloukas, P.; Pastinen, T.; Samani, N.J.; McPherson, R.; Davey Smith, G.; Frayling, T.M.; Wareham, N.J.; Meigs, J.B.; Mooser, V.; Spector, T.D. A genome-wide association study reveals variants in ARL15 that influence adiponectin levels. PLoS Genet., 2009, 5(12), e1000768. doi: 10.1371/journal.pgen.1000768 PMID: 20011104
- Gorski, M.; van der Most, P.J.; Teumer, A.; Chu, A.Y.; Li, M.; Mijatovic, V.; Nolte, I.M.; Cocca, M.; Taliun, D.; Gomez, F.; Li, Y.; Tayo, B.; Tin, A.; Feitosa, M.F.; Aspelund, T.; Attia, J.; Biffar, R.; Bochud, M.; Boerwinkle, E.; Borecki, I.; Bottinger, E.P.; Chen, M.H.; Chouraki, V.; Ciullo, M.; Coresh, J.; Cornelis, M.C.; Curhan, G.C.; dAdamo, A.P.; Dehghan, A.; Dengler, L.; Ding, J.; Eiriksdottir, G.; Endlich, K.; Enroth, S.; Esko, T.; Franco, O.H.; Gasparini, P.; Gieger, C.; Girotto, G.; Gottesman, O.; Gudnason, V.; Gyllensten, U.; Hancock, S.J.; Harris, T.B.; Helmer, C.; Höllerer, S.; Hofer, E.; Hofman, A.; Holliday, E.G.; Homuth, G.; Hu, F.B.; Huth, C.; Hutri-Kähönen, N.; Hwang, S.J.; Imboden, M.; Johansson, Å.; Kähönen, M.; König, W.; Kramer, H.; Krämer, B.K.; Kumar, A.; Kutalik, Z.; Lambert, J.C.; Launer, L.J.; Lehtimäki, T.; de Borst, M.H.; Navis, G.; Swertz, M.; Liu, Y.; Lohman, K.; Loos, R.J.F.; Lu, Y.; Lyytikäinen, L.P.; McEvoy, M.A.; Meisinger, C.; Meitinger, T.; Metspalu, A.; Metzger, M.; Mihailov, E.; Mitchell, P.; Nauck, M.; Oldehinkel, A.J.; Olden, M.; WJH Penninx, B.; Pistis, G.; Pramstaller, P.P.; Probst-Hensch, N.; Raitakari, O.T.; Rettig, R.; Ridker, P.M.; Rivadeneira, F.; Robino, A.; Rosas, S.E.; Ruderfer, D.; Ruggiero, D.; Saba, Y.; Sala, C.; Schmidt, H.; Schmidt, R.; Scott, R.J.; Sedaghat, S.; Smith, A.V.; Sorice, R.; Stengel, B.; Stracke, S.; Strauch, K.; Toniolo, D.; Uitterlinden, A.G.; Ulivi, S.; Viikari, J.S.; Völker, U.; Vollenweider, P.; Völzke, H.; Vuckovic, D.; Waldenberger, M.; Jin Wang, J.; Yang, Q.; Chasman, D.I.; Tromp, G.; Snieder, H.; Heid, I.M.; Fox, C.S.; Köttgen, A.; Pattaro, C.; Böger, C.A.; Fuchsberger, C. 1000 Genomes-based meta-analysis identifies 10 novel loci for kidney function. Sci. Rep., 2017, 7(1), 45040. doi: 10.1038/srep45040 PMID: 28452372
- Corre, T.; Arjona, F.J.; Hayward, C.; Youhanna, S.; de Baaij, J.H.F.; Belge, H.; Nägele, N.; Debaix, H.; Blanchard, M.G.; Traglia, M.; Harris, S.E.; Ulivi, S.; Rueedi, R.; Lamparter, D.; Macé, A.; Sala, C.; Lenarduzzi, S.; Ponte, B.; Pruijm, M.; Ackermann, D.; Ehret, G.; Baptista, D.; Polasek, O.; Rudan, I.; Hurd, T.W.; Hastie, N.D.; Vitart, V.; Waeber, G.; Kutalik, Z.; Bergmann, S.; Vargas-Poussou, R.; Konrad, M.; Gasparini, P.; Deary, I.J.; Starr, J.M.; Toniolo, D.; Vollenweider, P.; Hoenderop, J.G.J.; Bindels, R.J.M.; Bochud, M.; Devuyst, O. Genome-wide meta-analysis unravels interactions between magnesium homeostasis and metabolic phenotypes. J. Am. Soc. Nephrol., 2018, 29(1), 335-348. doi: 10.1681/ASN.2017030267 PMID: 29093028
- Domínguez-Cruz, M.G.; Muñoz, M.L.; Totomoch-Serra, A.; García-Escalante, M.G.; Burgueño, J.; Valadez-González, N.; Pinto-Escalantes, D.; Díaz-Badillo, Á. Pilot genome-wide association study identifying novel risk loci for type 2 diabetes in a Maya population. Gene, 2018, 677, 324-331. doi: 10.1016/j.gene.2018.08.041 PMID: 30130595
- Li, Y.; Yang, Y.; Yao, Y.; Li, X.; Shi, L.; Zhang, Y.; Xiong, Y.; Yan, M.; Yao, Y.; Xiao, C. Association study of ARL15 and CDH13 with T2DM in a han chinese population. Int. J. Med. Sci., 2014, 11(5), 522-527. doi: 10.7150/ijms.8206 PMID: 24688318
- Shen, J.; Liu, M.; Xu, J.; Sun, B.; Xu, H.; Zhang, W. ARL15 overexpression attenuates high glucose-induced impairment of insulin signaling and oxidative stress in human umbilical vein endothelial cells. Life Sci., 2019, 220(1), 127-135. doi: 10.1016/j.lfs.2019.01.030 PMID: 30682341
- Negi, S.; Juyal, G.; Senapati, S.; Prasad, P.; Gupta, A.; Singh, S.; Kashyap, S.; Kumar, A.; Kumar, U.; Gupta, R.; Kaur, S.; Agrawal, S.; Aggarwal, A.; Ott, J.; Jain, S.; Juyal, R.C.; Thelma, B.K. A genome-wide association study reveals ARL15, a novel non-HLA susceptibility gene for rheumatoid arthritis in North Indians. Arthritis Rheum., 2013, 65(12), 3026-3035. doi: 10.1002/art.38110 PMID: 23918589
- Wu, Y.; Bai, Y.; McEwan, D.G.; Bentley, L.; Aravani, D.; Cox, R.D. Palmitoylated small GTPase ARL15 is translocated within Golgi network during adipogenesis. Biol. Open, 2021, 10(12), bio058420. doi: 10.1242/bio.058420 PMID: 34779483
- Thomsen, S.K.; Ceroni, A.; van de Bunt, M.; Burrows, C.; Barrett, A.; Scharfmann, R.; Ebner, D.; McCarthy, M.I.; Gloyn, A.L. Systematic functional characterization of candidate causal genes for type 2 diabetes risk variants. Diabetes, 2016, 65(12), 3805-3811. doi: 10.2337/db16-0361 PMID: 27554474
- Sun, J.Q.; Yin, R.X.; Shi, G.Y.; Shen, S.W.; Chen, X.; Bin, Y.; Huang, F.; Wang, W.; Lin, W.X.; Pan, S.L. Association of the ARL15 rs6450176 SNP and serum lipid levels in the Jing and Han populations. Int. J. Clin. Exp. Pathol., 2015, 8(10), 12977-12994. PMID: 26722494
- Gillingham, A.K.; Munro, S. The small G proteins of the Arf family and their regulators. Annu. Rev. Cell Dev. Biol., 2007, 23(1), 579-611. doi: 10.1146/annurev.cellbio.23.090506.123209 PMID: 17506703
- Oparil, S.; Acelajado, M.C.; Bakris, G.L.; Berlowitz, D.R.; Cífková, R.; Dominiczak, A.F.; Grassi, G.; Jordan, J.; Poulter, N.R.; Rodgers, A.; Whelton, P.K. Hypertension. Nat. Rev. Dis. Primers, 2018, 4(1), 18014. doi: 10.1038/nrdp.2018.14 PMID: 29565029
- Libby, P.; Theroux, P. Pathophysiology of coronary artery disease. Circulation, 2005, 111(25), 3481-3488. doi: 10.1161/CIRCULATIONAHA.105.537878 PMID: 15983262
- Rocha, N.; Payne, F.; Huang-Doran, I.; Sleigh, A.; Fawcett, K.; Adams, C.; Stears, A.; Saudek, V.; ORahilly, S.; Barroso, I.; Semple, R.K. The metabolic syndrome- associated small G protein ARL15 plays a role in adipocyte differentiation and adiponectin secretion. Sci. Rep., 2017, 7(1), 17593. doi: 10.1038/s41598-017-17746-8 PMID: 29242557
- Chen, Z.; Yu, H.; Shi, X.; Warren, C.R.; Lotta, L.A.; Friesen, M.; Meissner, T.B.; Langenberg, C.; Wabitsch, M.; Wareham, N.; Benson, M.D.; Gerszten, R.E.; Cowan, C.A. Functional screening of candidate causal genes for insulin resistance in human preadipocytes and adipocytes. Circ. Res., 2020, 126(3), 330-346. doi: 10.1161/CIRCRESAHA.119.315246 PMID: 31739742
- Oparil, S.; Schmieder, R.E. New approaches in the treatment of hypertension. Circ. Res., 2015, 116(6), 1074-1095. doi: 10.1161/CIRCRESAHA.116.303603 PMID: 25767291
- Li, C.; He, J.; Chen, J.; Zhao, J.; Gu, D.; Hixson, J.E.; Rao, D.C.; Jaquish, C.E.; Rice, T.K.; Sung, Y.J.; Kelly, T.N. Genome-wide gene-potassium interaction analyses on blood pressure. Circ. Cardiovasc. Genet., 2017, 10(6), e001811. doi: 10.1161/CIRCGENETICS.117.001811 PMID: 29212900
- Scott, R.A.; Lagou, V.; Welch, R.P.; Wheeler, E.; Montasser, M.E.; Luan, J. Large-scale association analyses identify new loci influencing glycemic traits and provide insight into the underlying biological pathways. Nat. Genet., 2012, 44(9), 991-1005. doi: 10.1038/ng.2385 PMID: 22885924
- Taneera, J.; Prasad, R.B.; Dhaiban, S.; Mohammed, A.K.; Haataja, L.; Arvan, P.; Hamad, M.; Groop, L.; Wollheim, C.B. Silencing of the FTO gene inhibits insulin secretion: An in vitro study using GRINCH cells. Mol. Cell. Endocrinol., 2018, 472, 10-17. doi: 10.1016/j.mce.2018.06.003 PMID: 29890211
- Frühbeck, G. Overview of adipose tissue and its role in obesity and metabolic disorders. Methods Mol. Biol., 2008, 456, 1-22. doi: 10.1007/978-1-59745-245-8_1 PMID: 18516549
- Klimentidis, Y.C.; Arora, A. Interaction of insulin resistance and related genetic variants with triglyceride-associated genetic variants. Circ. Cardiovasc. Genet., 2016, 9(2), 154-161. doi: 10.1161/CIRCGENETICS.115.001246 PMID: 26850992
- Glessner, J.T.; Bradfield, J.P.; Wang, K.; Takahashi, N.; Zhang, H.; Sleiman, P.M.; Mentch, F.D.; Kim, C.E.; Hou, C.; Thomas, K.A.; Garris, M.L.; Deliard, S.; Frackelton, E.C.; Otieno, F.G.; Zhao, J.; Chiavacci, R.M.; Li, M.; Buxbaum, J.D.; Berkowitz, R.I.; Hakonarson, H.; Grant, S.F.A. A genome-wide study reveals copy number variants exclusive to childhood obesity cases. Am. J. Hum. Genet., 2010, 87(5), 661-666. doi: 10.1016/j.ajhg.2010.09.014 PMID: 20950786
- Benabdelkamel, H.; Masood, A.; Okla, M.; Al-Naami, M.Y.; Alfadda, A.A. A proteomics-based approach reveals differential regulation of urine proteins between metabolically healthy and unhealthy obese patients. Int. J. Mol. Sci., 2019, 20(19), 4905. doi: 10.3390/ijms20194905 PMID: 31623319
- Ried, J.S.; Jeff, M.J.; Chu, A.Y.; Bragg-Gresham, J.L.; van Dongen, J.; Huffman, J.E.; Ahluwalia, T.S.; Cadby, G.; Eklund, N.; Eriksson, J.; Esko, T.; Feitosa, M.F.; Goel, A.; Gorski, M.; Hayward, C.; Heard-Costa, N.L.; Jackson, A.U.; Jokinen, E.; Kanoni, S.; Kristiansson, K.; Kutalik, Z.; Lahti, J.; Luan, J.; Mägi, R.; Mahajan, A.; Mangino, M.; Medina-Gomez, C.; Monda, K.L.; Nolte, I.M.; Pérusse, L.; Prokopenko, I.; Qi, L.; Rose, L.M.; Salvi, E.; Smith, M.T.; Snieder, H.; Stančáková, A.; Ju Sung, Y.; Tachmazidou, I.; Teumer, A.; Thorleifsson, G.; van der Harst, P.; Walker, R.W.; Wang, S.R.; Wild, S.H.; Willems, S.M.; Wong, A.; Zhang, W.; Albrecht, E.; Couto Alves, A.; Bakker, S.J.L.; Barlassina, C.; Bartz, T.M.; Beilby, J.; Bellis, C.; Bergman, R.N.; Bergmann, S.; Blangero, J.; Blüher, M.; Boerwinkle, E.; Bonnycastle, L.L.; Bornstein, S.R.; Bruinenberg, M.; Campbell, H.; Chen, Y.D.I.; Chiang, C.W.K.; Chines, P.S.; Collins, F.S.; Cucca, F.; Cupples, L.A.; DAvila, F.; de Geus, E.J.C.; Dedoussis, G.; Dimitriou, M.; Döring, A.; Eriksson, J.G.; Farmaki, A.E.; Farrall, M.; Ferreira, T.; Fischer, K.; Forouhi, N.G.; Friedrich, N.; Gjesing, A.P.; Glorioso, N.; Graff, M.; Grallert, H.; Grarup, N.; Gräßler, J.; Grewal, J.; Hamsten, A.; Harder, M.N.; Hartman, C.A.; Hassinen, M.; Hastie, N.; Hattersley, A.T.; Havulinna, A.S.; Heliövaara, M.; Hillege, H.; Hofman, A.; Holmen, O.; Homuth, G.; Hottenga, J.J.; Hui, J.; Husemoen, L.L.; Hysi, P.G.; Isaacs, A.; Ittermann, T.; Jalilzadeh, S.; James, A.L.; Jørgensen, T.; Jousilahti, P.; Jula, A.; Marie Justesen, J.; Justice, A.E.; Kähönen, M.; Karaleftheri, M.; Tee Khaw, K.; Keinanen-Kiukaanniemi, S.M.; Kinnunen, L.; Knekt, P.B.; Koistinen, H.A.; Kolcic, I.; Kooner, I.K.; Koskinen, S.; Kovacs, P.; Kyriakou, T.; Laitinen, T.; Langenberg, C.; Lewin, A.M.; Lichtner, P.; Lindgren, C.M.; Lindström, J.; Linneberg, A.; Lorbeer, R.; Lorentzon, M.; Luben, R.; Lyssenko, V.; Männistö, S.; Manunta, P.; Leach, I.M.; McArdle, W.L.; Mcknight, B.; Mohlke, K.L.; Mihailov, E.; Milani, L.; Mills, R.; Montasser, M.E.; Morris, A.P.; Müller, G.; Musk, A.W.; Narisu, N.; Ong, K.K.; Oostra, B.A.; Osmond, C.; Palotie, A.; Pankow, J.S.; Paternoster, L.; Penninx, B.W.; Pichler, I.; Pilia, M.G.; Polaek, O.; Pramstaller, P.P.; Raitakari, O.T.; Rankinen, T.; Rao, D.C.; Rayner, N.W.; Ribel-Madsen, R.; Rice, T.K.; Richards, M.; Ridker, P.M.; Rivadeneira, F.; Ryan, K.A.; Sanna, S.; Sarzynski, M.A.; Scholtens, S.; Scott, R.A.; Sebert, S.; Southam, L.; Sparsø, T.H.; Steinthorsdottir, V.; Stirrups, K.; Stolk, R.P.; Strauch, K.; Stringham, H.M.; Swertz, M.A.; Swift, A.J.; Tönjes, A.; Tsafantakis, E.; van der Most, P.J.; Van Vliet-Ostaptchouk, J.V.; Vandenput, L.; Vartiainen, E.; Venturini, C.; Verweij, N.; Viikari, J.S.; Vitart, V.; Vohl, M.C.; Vonk, J.M.; Waeber, G.; Widén, E.; Willemsen, G.; Wilsgaard, T.; Winkler, T.W.; Wright, A.F.; Yerges-Armstrong, L.M.; Hua Zhao, J.; Carola Zillikens, M.; Boomsma, D.I.; Bouchard, C.; Chambers, J.C.; Chasman, D.I.; Cusi, D.; Gansevoort, R.T.; Gieger, C.; Hansen, T.; Hicks, A.A.; Hu, F.; Hveem, K.; Jarvelin, M.R.; Kajantie, E.; Kooner, J.S.; Kuh, D.; Kuusisto, J.; Laakso, M.; Lakka, T.A.; Lehtimäki, T.; Metspalu, A.; Njølstad, I.; Ohlsson, C.; Oldehinkel, A.J.; Palmer, L.J.; Pedersen, O.; Perola, M.; Peters, A.; Psaty, B.M.; Puolijoki, H.; Rauramaa, R.; Rudan, I.; Salomaa, V.; Schwarz, P.E.H.; Shudiner, A.R.; Smit, J.H.; Sørensen, T.I.A.; Spector, T.D.; Stefansson, K.; Stumvoll, M.; Tremblay, A.; Tuomilehto, J.; Uitterlinden, A.G.; Uusitupa, M.; Völker, U.; Vollenweider, P.; Wareham, N.J.; Watkins, H.; Wilson, J.F.; Zeggini, E.; Abecasis, G.R.; Boehnke, M.; Borecki, I.B.; Deloukas, P.; van Duijn, C.M.; Fox, C.; Groop, L.C.; Heid, I.M.; Hunter, D.J.; Kaplan, R.C.; McCarthy, M.I.; North, K.E.; OConnell, J.R.; Schlessinger, D.; Thorsteinsdottir, U.; Strachan, D.P.; Frayling, T.; Hirschhorn, J.N.; Müller-Nurasyid, M.; Loos, R.J.F A principal component meta-analysis on multiple anthropometric traits identifies novel loci for body shape. Nat. Commun., 2016, 7(1), 13357. doi: 10.1038/ncomms13357 PMID: 27876822
- Teslovich, T.M.; Musunuru, K.; Smith, A.V.; Edmondson, A.C.; Stylianou, I.M.; Koseki, M.; Pirruccello, J.P.; Ripatti, S.; Chasman, D.I.; Willer, C.J.; Johansen, C.T.; Fouchier, S.W.; Isaacs, A.; Peloso, G.M.; Barbalic, M.; Ricketts, S.L.; Bis, J.C.; Aulchenko, Y.S.; Thorleifsson, G.; Feitosa, M.F.; Chambers, J.; Orho-Melander, M.; Melander, O.; Johnson, T.; Li, X.; Guo, X.; Li, M.; Shin Cho, Y.; Jin Go, M.; Jin Kim, Y.; Lee, J.Y.; Park, T.; Kim, K.; Sim, X.; Twee-Hee Ong, R.; Croteau-Chonka, D.C.; Lange, L.A.; Smith, J.D.; Song, K.; Zhao, H. Biological, clinical and population relevance of 95 loci for blood lipids. Nature, 2010, 466(7307), 707-713. doi: 10.1038/nature09270 PMID: 20686565
- Kapoor, M.; Wang, J.C.; Wetherill, L.; Le, N.; Bertelsen, S.; Hinrichs, A.L.; Budde, J.; Agrawal, A.; Almasy, L.; Bucholz, K.; Dick, D.M.; Harari, O.; Xiaoling, X.; Hesselbrock, V.; Kramer, J.; Nurnberger, J.I., Jr; Rice, J.; Schuckit, M.; Tischfield, J.; Porjesz, B.; Edenberg, H.J.; Bierut, L.; Foroud, T.; Goate, A. Genome-wide survival analysis of age at onset of alcohol dependence in extended high-risk COGA families. Drug Alcohol Depend., 2014, 142, 56-62. doi: 10.1016/j.drugalcdep.2014.05.023 PMID: 24962325
- Mahajan, A.; Go, M.J.; Zhang, W.; Below, J.E.; Gaulton, K.J.; Ferreira, T.; Horikoshi, M.; Johnson, A.D.; Ng, M.C.Y.; Prokopenko, I.; Saleheen, D.; Wang, X.; Zeggini, E.; Abecasis, G.R.; Adair, L.S.; Almgren, P.; Atalay, M.; Aung, T.; Baldassarre, D.; Balkau, B.; Bao, Y.; Barnett, A.H.; Barroso, I.; Basit, A.; Been, L.F.; Beilby, J.; Bell, G.I.; Benediktsson, R.; Bergman, R.N.; Boehm, B.O.; Boerwinkle, E.; Bonnycastle, L.L.; Burtt, N.; Cai, Q.; Campbell, H.; Carey, J.; Cauchi, S.; Caulfield, M.; Chan, J.C.N.; Chang, L.C.; Chang, T.J.; Chang, Y.C.; Charpentier, G.; Chen, C.H.; Chen, H.; Chen, Y.T.; Chia, K.S.; Chidambaram, M.; Chines, P.S.; Cho, N.H.; Cho, Y.M.; Chuang, L.M.; Collins, F.S.; Cornelis, M.C.; Couper, D.J.; Crenshaw, A.T.; van Dam, R.M.; Danesh, J.; Das, D.; de Faire, U.; Dedoussis, G.; Deloukas, P.; Dimas, A.S.; Dina, C.; Doney, A.S.F.; Donnelly, P.J.; Dorkhan, M.; van Duijn, C.; Dupuis, J.; Edkins, S.; Elliott, P.; Emilsson, V.; Erbel, R.; Eriksson, J.G.; Escobedo, J.; Esko, T.; Eury, E.; Florez, J.C.; Fontanillas, P.; Forouhi, N.G.; Forsen, T.; Fox, C.; Fraser, R.M.; Frayling, T.M.; Froguel, P.; Frossard, P.; Gao, Y.; Gertow, K.; Gieger, C.; Gigante, B.; Grallert, H.; Grant, G.B.; Groop, L.C.; Groves, C.J.; Grundberg, E.; Guiducci, C.; Hamsten, A.; Han, B.G.; Hara, K.; Hassanali, N.; Hattersley, A.T.; Hayward, C.; Hedman, A.K.; Herder, C.; Hofman, A.; Holmen, O.L.; Hovingh, K.; Hreidarsson, A.B.; Hu, C.; Hu, F.B.; Hui, J.; Humphries, S.E.; Hunt, S.E.; Hunter, D.J.; Hveem, K.; Hydrie, Z.I.; Ikegami, H.; Illig, T.; Ingelsson, E.; Islam, M.; Isomaa, B.; Jackson, A.U.; Jafar, T.; James, A.; Jia, W.; Jöckel, K.H.; Jonsson, A.; Jowett, J.B.M.; Kadowaki, T.; Kang, H.M.; Kanoni, S.; Kao, W.H.L.; Kathiresan, S.; Kato, N.; Katulanda, P.; Keinanen-Kiukaanniemi, S.M.; Kelly, A.M.; Khan, H.; Khaw, K.T.; Khor, C.C.; Kim, H.L.; Kim, S.; Kim, Y.J.; Kinnunen, L.; Klopp, N.; Kong, A.; Korpi-Hyövälti, E.; Kowlessur, S.; Kraft, P.; Kravic, J.; Kristensen, M.M.; Krithika, S.; Kumar, A.; Kumate, J.; Kuusisto, J.; Kwak, S.H.; Laakso, M.; Lagou, V.; Lakka, T.A.; Langenberg, C.; Langford, C.; Lawrence, R.; Leander, K.; Lee, J.M.; Lee, N.R.; Li, M.; Li, X.; Li, Y.; Liang, J.; Liju, S.; Lim, W.Y.; Lind, L.; Lindgren, C.M.; Lindholm, E.; Liu, C.T.; Liu, J.J.; Lobbens, S.; Long, J.; Loos, R.J.F.; Lu, W.; Luan, J.; Lyssenko, V.; Ma, R.C.W.; Maeda, S.; Mägi, R.; Männistö, S.; Matthews, D.R.; Meigs, J.B.; Melander, O.; Metspalu, A.; Meyer, J.; Mirza, G.; Mihailov, E.; Moebus, S.; Mohan, V.; Mohlke, K.L.; Morris, A.D.; Mühleisen, T.W.; Müller-Nurasyid, M.; Musk, B.; Nakamura, J.; Nakashima, E.; Navarro, P.; Ng, P.K.; Nica, A.C.; Nilsson, P.M.; Njølstad, I.; Nöthen, M.M.; Ohnaka, K.; Ong, T.H.; Owen, K.R.; Palmer, C.N.A.; Pankow, J.S.; Park, K.S.; Parkin, M.; Pechlivanis, S.; Pedersen, N.L.; Peltonen, L.; Perry, J.R.B.; Peters, A.; Pinidiyapathirage, J.M.; Platou, C.G.P.; Potter, S.; Price, J.F.; Qi, L.; Radha, V.; Rallidis, L.; Rasheed, A.; Rathmann, W.; Rauramaa, R.; Raychaudhuri, S.; Rayner, N.W.; Rees, S.D.; Rehnberg, E.; Ripatti, S.; Robertson, N.; Roden, M.; Rossin, E.J.; Rudan, I.; Rybin, D.; Saaristo, T.E.; Salomaa, V.; Saltevo, J.; Samuel, M.; Sanghera, D.K.; Saramies, J.; Scott, J.; Scott, L.J.; Scott, R.A.; Segrè, A.V.; Sehmi, J.; Sennblad, B.; Shah, N.; Shah, S.; Shera, A.S.; Shu, X.O.; Shuldiner, A.R.; Sigurðsson, G.; Sijbrands, E.; Silveira, A.; Sim, X.; Sivapalaratnam, S.; Small, K.S.; So, W.Y.; Stančáková, A.; Stefansson, K.; Steinbach, G.; Steinthorsdottir, V.; Stirrups, K.; Strawbridge, R.J.; Stringham, H.M.; Sun, Q.; Suo, C.; Syvänen, A.C.; Takayanagi, R.; Takeuchi, F.; Tay, W.T.; Teslovich, T.M.; Thorand, B.; Thorleifsson, G.; Thorsteinsdottir, U.; Tikkanen, E.; Trakalo, J.; Tremoli, E.; Trip, M.D.; Tsai, F.J.; Tuomi, T.; Tuomilehto, J.; Uitterlinden, A.G.; Valladares-Salgado, A.; Vedantam, S.; Veglia, F.; Voight, B.F.; Wang, C.; Wareham, N.J.; Wennauer, R.; Wickremasinghe, A.R.; Wilsgaard, T.; Wilson, J.F.; Wiltshire, S.; Winckler, W.; Wong, T.Y.; Wood, A.R.; Wu, J.Y.; Wu, Y.; Yamamoto, K.; Yamauchi, T.; Yang, M.; Yengo, L.; Yokota, M.; Young, R.; Zabaneh, D.; Zhang, F.; Zhang, R.; Zheng, W.; Zimmet, P.Z.; Altshuler, D.; Bowden, D.W.; Cho, Y.S.; Cox, N.J.; Cruz, M.; Hanis, C.L.; Kooner, J.; Lee, J.Y.; Seielstad, M.; Teo, Y.Y.; Boehnke, M.; Parra, E.J.; Chambers, J.C.; Tai, E.S.; McCarthy, M.I.; Morris, A.P. Genome-wide trans-ancestry meta-analysis provides insight into the genetic architecture of type 2 diabetes susceptibility. Nat. Genet., 2014, 46(3), 234-244. doi: 10.1038/ng.2897 PMID: 24509480
- viatte, S.; Plant, D.; Han, B.; Fu, B.; Yarwood, A.; Thomson, W.; Symmons, D.P.M.; Worthington, J.; Young, A.; Hyrich, K.L.; Morgan, A.W.; Wilson, A.G.; Isaacs, J.D.; Raychaudhuri, S.; Barton, A. Association of HLA-DRB1 haplotypes with rheumatoid arthritis severity, mortality, and treatment response. JAMA, 2015, 313(16), 1645-1656. doi: 10.1001/jama.2015.3435 PMID: 25919528
- Anaya, J-M.; Castiblanco, J.; Lessard, C. Chapter 18Non-HLA genes and autoimmune diseases. In: Autoimmunity: From Bench to Bedside; El Rosario University Press: Bogota, (Colombia), 2013.
- El-Gabalawy, H.S.; Robinson, D.B.; Daha, N.A.; Oen, K.G.; Smolik, I.; Elias, B.; Hart, D.; Bernstein, C.N.; Sun, Y.; Lu, Y.; Houwing-Duistermaat, J.J.; Siminovitch, K.A. Non-HLA genes modulate the risk of rheumatoid arthritis associated with HLA-DRB1 in a susceptible North American Native population. Genes Immun., 2011, 12(7), 568-574. doi: 10.1038/gene.2011.30 PMID: 21614018
- Carrión, M.; Frommer, K.W.; Pérez-García, S.; Müller-Ladner, U.; Gomariz, R.P.; Neumann, E. The adipokine network in rheumatic joint diseases. Int. J. Mol. Sci., 2019, 20(17), 4091. doi: 10.3390/ijms20174091 PMID: 31443349
- Pandey, A.K.; Saxena, A.; Dey, S.K.; Kanjilal, M.; Kumar, U.; Thelma, B.K. Correlation between an intronic SNP genotype and ARL15 level in rheumatoid arthritis. J. Genet., 2021, 100(2), 26. doi: 10.1007/s12041-021-01286-2 PMID: 34187973
- Wang, J.; Qi, X.; Zhang, X.; Yan, W.; You, C. Genetic polymorphisms of ARL15 and HLA-DMA are associated with rheumatoid arthritis in Han population from northwest China. Xibao Yu Fenzi Mianyixue Zazhi, 2017, 33(12), 1681-1685. PMID: 29382430
- Smolen, J.S.; Aletaha, D.; Koeller, M.; Weisman, M.H.; Emery, P. New therapies for treatment of rheumatoid arthritis. Lancet, 2007, 370(9602), 1861-1874. doi: 10.1016/S0140-6736(07)60784-3 PMID: 17570481
- Chaudhari, K.; Rizvi, S.; Syed, B.A. Rheumatoid arthritis: Current and future trends. Nat. Rev. Drug Discov., 2016, 15(5), 305-306. doi: 10.1038/nrd.2016.21 PMID: 27080040
- Scott, D.L.; Wolfe, F.; Huizinga, T.W.J. Rheumatoid arthritis. Lancet, 2010, 376(9746), 1094-1108. doi: 10.1016/S0140-6736(10)60826-4 PMID: 20870100
- Symmons, D.P.M. What is rheumatoid arthritis? Br. Med. Bull., 1995, 51(2), 243-248. doi: 10.1093/oxfordjournals.bmb.a072958 PMID: 7552061
- Schett, G.; Gravallese, E. Bone erosion in rheumatoid arthritis: Mechanisms, diagnosis and treatment. Nat. Rev. Rheumatol., 2012, 8(11), 656-664. doi: 10.1038/nrrheum.2012.153 PMID: 23007741
- Ngian, G.S. Rheumatoid arthritis. Aust. Fam. Physician, 2010, 39(9), 626-628. PMID: 20877764
- Ridgley, L.A.; Anderson, A.E.; Pratt, A.G. What are the dominant cytokines in early rheumatoid arthritis? Curr. Opin. Rheumatol., 2018, 30(2), 207-214. doi: 10.1097/BOR.0000000000000470 PMID: 29206659
- Wasserman, A.M. Diagnosis and management of rheumatoid arthritis. Am. Fam. Physician, 2011, 84(11), 1245-1252.
- Svendsen, A.J.; Kyvik, K.O.; Houen, G.; Junker, P.; Christensen, K.; Christiansen, L.; Nielsen, C.; Skytthe, A.; Hjelmborg, J.V. On the origin of rheumatoid arthritis: The impact of environment and genes--a population based twin study. PLoS One, 2013, 8(2), e57304. doi: 10.1371/journal.pone.0057304 PMID: 23468964
- Liao, K.P.; Alfredsson, L.; Karlson, E.W. Environmental influences on risk for rheumatoid arthritis. Curr. Opin. Rheumatol., 2009, 21(3), 279-283. doi: 10.1097/BOR.0b013e32832a2e16 PMID: 19318947
- Clements, J.N. Treatment of rheumatoid arthritis: A review of recommendations and emerging therapy. Formulary, 2011, 46(12), 532-545.
- Heidari, B. Rheumatoid Arthritis: Early diagnosis and treatment outcomes. Caspian J. Intern. Med., 2011, 2(1), 161-170. PMID: 24024009
- Demoruelle, M.K.; Deane, K.D. Treatment strategies in early rheumatoid arthritis and prevention of rheumatoid arthritis. Curr. Rheumatol. Rep., 2012, 14(5), 472-480. doi: 10.1007/s11926-012-0275-1 PMID: 22773387
- Burmester, G.R.; Pope, J.E. Novel treatment strategies in rheumatoid arthritis. Lancet, 2017, 389(10086), 2338-2348. doi: 10.1016/S0140-6736(17)31491-5 PMID: 28612748
- Dale, J.; Alcorn, N.; Capell, H.; Madhok, R. Combination therapy for rheumatoid arthritis: Methotrexate and sulfasalazine together or with other DMARDs. Nat. Clin. Pract. Rheumatol., 2007, 3(8), 450-458. doi: 10.1038/ncprheum0562 PMID: 17664952
- Kahlenberg, J.M.; Fox, D.A. Advances in the medical treatment of rheumatoid arthritis. Hand Clin., 2011, 27(1), 11-20. doi: 10.1016/j.hcl.2010.09.002 PMID: 21176795
- Sergeant, J.C.; Hyrich, K.L.; Anderson, J.; Kopec-Harding, K.; Hope, H.F.; Symmons, D.P.M.; Barton, A.; Verstappen, S.M.M. Prediction of primary non-response to methotrexate therapy using demographic, clinical and psychosocial variables: Results from the UK Rheumatoid Arthritis Medication Study (RAMS). Arthritis Res. Ther., 2018, 20(1), 147. doi: 10.1186/s13075-018-1645-5 PMID: 30005689
- Curtis, J.R.; Singh, J.A. Use of biologics in rheumatoid arthritis: Current and emerging paradigms of care. Clin. Ther., 2011, 33(6), 679-707. doi: 10.1016/j.clinthera.2011.05.044 PMID: 21704234
- Baldasseroni, S.; Antenore, A.; Di Serio, C.; Orso, F.; Lonetto, G.; Bartoli, N.; Foschini, A.; Marella, A.; Pratesi, A.; Scarantino, S.; Fumagalli, S.; Monami, M.; Mannucci, E.; Marchionni, N.; Tarantini, F. Adiponectin, diabetes and ischemic heart failure: A challenging relationship. Cardiovasc. Diabetol., 2012, 11(1), 151. doi: 10.1186/1475-2840-11-151 PMID: 23249664
- Chen, X.; Lu, J.; Bao, J.; Guo, J.; Shi, J.; Wang, Y. Adiponectin: A biomarker for rheumatoid arthritis? Cytokine Growth Factor Rev., 2013, 24(1), 83-89. doi: 10.1016/j.cytogfr.2012.07.004 PMID: 22910140
- Tan, W.; Wang, F.; Zhang, M.; Guo, D.; Zhang, Q.; He, S. High adiponectin and adiponectin receptor 1 expression in synovial fluids and synovial tissues of patients with rheumatoid arthritis. Semin. Arthritis Rheum., 2009, 38(6), 420-427. doi: 10.1016/j.semarthrit.2008.01.017 PMID: 18395775
- Frommer, K.W.; Schäffler, A.; Büchler, C.; Steinmeyer, J.; Rickert, M.; Rehart, S.; Brentano, F.; Gay, S.; Müller-Ladner, U.; Neumann, E. Adiponectin isoforms: A potential therapeutic target in rheumatoid arthritis? Ann. Rheum. Dis., 2012, 71(10), 1724-1732. doi: 10.1136/annrheumdis-2011-200924 PMID: 22532632
- Kusunoki, N.; Kitahara, K.; Kojima, F.; Tanaka, N.; Kaneko, K.; Endo, H.; Suguro, T.; Kawai, S. Adiponectin stimulates prostaglandin E2 production in rheumatoid arthritis synovial fibroblasts. Arthritis Rheum., 2010, 62(6), 1641-1649. doi: 10.1002/art.27450 PMID: 20222108
- Kashyap, S.; Kumar, U.; Pandey, A.K.; Kanjilal, M.; Chattopadhyay, P.; Yadav, C.; Thelma, B.K. Functional characterisation of ADP ribosylation factor-like protein 15 in rheumatoid arthritis synovial fibroblasts. Clin. Exp. Rheumatol., 2018, 36(4), 581-588. PMID: 29465355
- Srirangan, S.; Choy, E.H. The role of Interleukin 6 in the pathophysiology of rheumatoid arthritis. Ther. Adv. Musculoskelet. Dis., 2010, 2(5), 247-256. doi: 10.1177/1759720X10378372 PMID: 22870451
- Kim, G.W.; Lee, N.R.; Pi, R.H.; Lim, Y.S.; Lee, Y.M.; Lee, J.M.; Jeong, H.S.; Chung, S.H. IL-6 inhibitors for treatment of rheumatoid arthritis: Past, present, and future. Arch. Pharm. Res., 2015, 38(5), 575-584. doi: 10.1007/s12272-015-0569-8 PMID: 25648633
- Tanaka, T.; Narazaki, M.; Kishimoto, T. IL-6 in inflammation, immunity, and disease. Cold Spring Harb. Perspect. Biol., 2014, 6(10), a016295. doi: 10.1101/cshperspect.a016295 PMID: 25190079
- Hwang, S.Y.; Kim, J.Y.; Kim, K.W.; Park, M.K.; Moon, Y.; Kim, W.U.; Kim, H.Y. IL-17 induces production of IL-6 and IL-8 in rheumatoid arthritis synovial fibroblasts via NF-kappaB- and PI3-kinase/Akt-dependent pathways. Arthritis Res., 2004, 6(2), R120-R128. doi: 10.1186/ar1038 PMID: 15059275
- Burrage, P. S.; Mix, K. S.; Brinckerhoff, C. E. Matrix metalloproteinases: Role in arthritis. Front. Biosci., 2006, 11((1 P.447-888)), 529-543. doi: 10.2741/1817
- Tong, K.M.; Chen, C.P.; Huang, K.C.; Shieh, D.C.; Cheng, H.C.; Tzeng, C.Y.; Chen, K.H.; Chiu, Y.C.; Tang, C.H. Adiponectin increases MMP-3 expression in human chondrocytes through adipor1 signaling pathway. J. Cell. Biochem., 2011, 112(5), 1431-1440. doi: 10.1002/jcb.23059 PMID: 21321996
- Araki, Y.; Mimura, T. Matrix metalloproteinase gene activation resulting from disordred epigenetic mechanisms in rheumatoid arthritis. Int. J. Mol. Sci., 2017, 18(5), 905. doi: 10.3390/ijms18050905 PMID: 28441353
- Robinson, D.R.; Tashjian, A.H., Jr; Levine, L. Prostaglandin-stimulated bone resorption by rheumatoid synovia. A possible mechanism for bone destruction in rheumatoid arthritis. J. Clin. Invest., 1975, 56(5), 1181-1188. doi: 10.1172/JCI108195 PMID: 1184744
- McCoy, J.M.; Wicks, J.R.; Audoly, L.P. The role of prostaglandin E2 receptors in the pathogenesis of rheumatoid arthritis. J. Clin. Invest., 2002, 110(5), 651-658. doi: 10.1172/JCI0215528 PMID: 12208866
- Firestein, G.S. Evolving concepts of rheumatoid arthritis. Nature, 2003, 423(6937), 356-361. doi: 10.1038/nature01661 PMID: 12748655
- Thakur, S.; Riyaz, B.; Patil, A.; Kaur, A.; Kapoor, B.; Mishra, V. Novel drug delivery systems for NSAIDs in management of rheumatoid arthritis: An overview. Biomed. Pharmacother., 2018, 106, 1011-1023. doi: 10.1016/j.biopha.2018.07.027 PMID: 30119166
- Sharma, A.; Saini, M.; Kundu, S.; Thelma, B.K. Computational insight into the three-dimensional structure of ADP ribosylation factor like protein 15, a novel susceptibility gene for rheumatoid arthritis. J. Biomol. Struct. Dyn., 2020, 0(0), 1-16. doi: 10.1080/07391102.2020.1860826 PMID: 33356902
- Yang, J.; Zhang, Y. I-TASSER server: New development for protein structure and function predictions. Nucleic Acids Res., 2015, 43(W1), W174-W181. doi: 10.1093/nar/gkv342 PMID: 25883148
- Zhang, C.; Mortuza, S.M.; He, B.; Wang, Y.; Zhang, Y. Template‐based and free modeling of I‐TASSER and QUARK pipelines using predicted contact maps in CASP12. Proteins, 2018, 86(S1), 136-151. doi: 10.1002/prot.25414 PMID: 29082551
- Jumper, J.; Evans, R.; Pritzel, A.; Green, T.; Figurnov, M.; Ronneberger, O.; Tunyasuvunakool, K.; Bates, R.; ídek, A.; Potapenko, A.; Bridgland, A.; Meyer, C.; Kohl, S.A.A.; Ballard, A.J.; Cowie, A.; Romera-Paredes, B.; Nikolov, S.; Jain, R.; Adler, J.; Back, T.; Petersen, S.; Reiman, D.; Clancy, E.; Zielinski, M.; Steinegger, M.; Pacholska, M.; Berghammer, T.; Bodenstein, S.; Silver, D.; Vinyals, O.; Senior, A.W.; Kavukcuoglu, K.; Kohli, P.; Hassabis, D. Highly accurate protein structure prediction with AlphaFold. Nature, 2021, 596(7873), 583-589. doi: 10.1038/s41586-021-03819-2 PMID: 34265844
- Wiederstein, M.; Sippl, M.J. ProSA-web: Interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Res., 2007, 35(Web Server (S2)), W407-W410. doi: 10.1093/nar/gkm290 PMID: 17517781
- Szklarczyk, D.; Gable, A.L.; Nastou, K.C.; Lyon, D.; Kirsch, R.; Pyysalo, S.; Doncheva, N.T.; Legeay, M.; Fang, T.; Bork, P.; Jensen, L.J.; von Mering, C. The STRING database in 2021: Customizable protein-protein networks, and functional characterization of user-uploaded gene/measurement sets. Nucleic Acids Res., 2021, 49(D1), D605-D612. doi: 10.1093/nar/gkaa1074 PMID: 33237311
Supplementary files
