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References 305
https://t.me/med1917
Trans. 36 (Pt 3): 528–530. https://doi.org/10.1042/bst0360528. PubMed PMID:
18481998; PMCID: PMC2562719.
24 Geuens, T., Bouhy, D., and Timmerman, V. (2016). The hnRNP family: insights
into their role in health and disease. Hum Genet. 135 (8): 851–867. Epub
20160523. https://doi.org/10.1007/s00439-016-1683-5 . PubMed PMID: 27215579;
PMCID: PMC4947485.
25 Bradley, T., Cook, M.E., and Blanchette, M. (2015). SR proteins control a com-
plex network of RNA-processing events. RNA 21 (1): 75–92. Epub 20141120.
https://doi.org/10.1261/rna.043893.113. PubMed PMID: 25414008; PMCID:
PMC4274639.
26 Hinman, M.N. and Lou, H. (2008). Diverse molecular functions of Hu proteins.
Cell Mol Life Sci. 65 (20): 3168–3181. https://doi.org/10.1007/s00018-008-8252-6.
PubMed PMID: 18581050; PMCID: PMC2580827.
27 Heraud-Farlow, J.E. and Kiebler, M.A. (2014). The multifunctional Staufen
proteins: conserved roles from neurogenesis to synaptic plasticity. Trends Neu-
rosci. 37 (9): 470–479. Epub 20140707. https://doi.org/10.1016/j.tins.2014.05.009.
PubMed PMID: 25012293; PMCID: PMC4156307.
28 Song, M.S. and Rossi, J.J. (2017). Molecular mechanisms of Dicer: endonuclease
and enzymatic activity. Biochem J. 474 (10): 1603–1618. Epub 20170504. https://
doi.org/10.1042/bcj20160759. PubMed PMID: 28473628; PMCID: PMC5415849.
29 Rybak-Wolf, A., Jens, M., Murakawa, Y. et al. (2014). A variety of dicer sub-
strates in human and C. elegans. Cell. 159 (5): 1153–1167. https://doi.org/10
.1016/j.cell.2014.10.040. PubMed PMID: 25416952.
30 Daniels, S.M. and Gatignol, A. (2012). The multiple functions of TRBP, at the
hub of cell responses to viruses, stress, and cancer. Microbiol Mol Biol Rev. 76
(3): 652–666. https://doi.org/10.1128/mmbr.00012-12. PubMed PMID: 22933564;
PMCID: PMC3429622.
31 Teplova, M. and Patel, D.J. (2008). Structural insights into RNA recognition by
the alternative-splicing regulator muscleblind-like MBNL1. Nat Struct Mol Biol.
15 (12): 1343–1351. Epub 20081130. https://doi.org/10.1038/nsmb.1519. PubMed
PMID: 19043415; PMCID: PMC4689322.
32 Tiedje, C., Diaz-Muñoz, M.D., Trulley, P. et al. (2016). The RNA-binding protein
TTP is a global post-transcriptional regulator of feedback control in inammation. Nucleic Acids Res. 44 (15): 7418–7440. Epub 20160524. https://doi.org/10
.1093/nar/gkw474. PubMed PMID: 27220464; PMCID: PMC5009735.
33 Behrens, G. and Heissmeyer, V. (2022). Cooperation of RNA-binding pro-
teins - a focus on roquin function in T cells. Front Immunol. 13: 839762.
Epub 20220218. https://doi.org/10.3389/mmu.2022.839762. PubMed PMID:
35251035; PMCID: PMC8894612.
34 Meyer, N.H., Tripsianes, K., Vincendeau, M. et al. (2010). Structural basis for
homodimerization of the Src-associated during mitosis, 68-kDa protein (Sam68)
Qua1 domain. J Biol Chem. 285 (37): 28893–28901. Epub 20100706. https://doi
.org/10.1074/jbc.M110.126185. PubMed PMID: 20610388; PMCID: PMC2937916.
306 11 RNA–Protein Interactions: A New Approach for Drugging RNA Biology
https://t.me/med1917
35 Quinn, L.M. (2017). FUBP/KH domain proteins in transcription: back to the
future. Transcription 8 (3): 185–192. Epub 20170216. https://doi.org/10.1080/
21541264.2017.1293595. PubMed PMID: 28301294; PMCID: PMC5501386.
36 Cheng, M.H. and Jansen, R.P. (2017). A jack of all trades: the RNA-binding
protein vigilin. Wiley Interdiscip Rev RNA 8 (6) Epub 20171004. https://doi.org/
10.1002/wrna.1448: PubMed PMID: 28975734.
37 Burmann, B.M. and Rösch, P. (2011). The role of E. coli Nus-factors in tran-
scription regulation and transcription:translation coupling: from structure to
mechanism. Transcription. 2 (3): 130–134. https://doi.org/10.4161/trns.2.3.15671.
PubMed PMID: 21922055; PMCID: PMC3173649.
38 Budkina, K.S., Zlobin, N.E., Kononova, S.V. et al. (2020). Cold shock domain
proteins: structure and interaction with nucleic acids. Biochemistry (Mosc). 85
(Suppl 1): S1–s19. https://doi.org/10.1134/s0006297920140011. PubMed PMID:
32087051.
39 Liao, J., Wei, Y., Liang, J. et al. (2022). Insight into the structure, physiological
function, and role in cancer of m6A readers—YTH domain-containing proteins.
Cell Death Discovery. 8 (1): 137. https://doi.org/10.1038/s41420-022-00947-0.
40 Wang, M., Ogé, L., Perez-Garcia, M.D. et al. (2018). The PUF protein family:
overview on PUF RNA targets, biological functions, and post transcriptional
regulation. Int J Mol Sci. 19 (2) Epub 20180130. https://doi.org/10.3390/
ijms19020410: PubMed PMID: 29385744; PMCID: PMC5855632.
41 Maris, C., Dominguez, C., and Allain, F.H. (2005). The RNA recognition motif,
a plastic RNA-binding platform to regulate post-transcriptional gene expression.
FEBS J. 272 (9): 2118–2131. https://doi.org/10.1111/j.1742-4658.2005.04653.x.
PubMed PMID: 15853797.
42 Venter, J.C., Adams, M.D., Myers, E.W. et al. (2001). The sequence of the
human genome. Science. 291 (5507): 1304–1351. https://doi.org/10.1126/science
.1058040. PubMed PMID: 11181995.
43 Dreyfuss, G., Swanson, M.S., and Pinol-Roma, S. (1988). Heterogeneous nuclear
ribonucleoprotein particles and the pathway of mRNA formation. Trends
Biochem Sci. 13 (3): 86–91. https://doi.org/10.1016/0968-0004(88)90046-1.
PubMed PMID: 3072706.
44 Adam, S.A., Nakagawa, T., Swanson, M.S. et al. (1986). mRNA
polyadenylate-binding protein: gene isolation and sequencing and identication
of a ribonucleoprotein consensus sequence. Mol Cell Biol. 6 (8): 2932–2943.
https://doi.org/10.1128/mcb.6.8.2932-2943.1986. PubMed PMID: 3537727;
PMCID: PMC367862.
45 Swanson, M.S., Nakagawa, T.Y., LeVan, K., and Dreyfuss, G. (1987). Primary
structure of human nuclear ribonucleoprotein particle C proteins: conservation
of sequence and domain structures in heterogeneous nuclear RNA, mRNA, and
pre-rRNA-binding proteins. Mol Cell Biol. 7 (5): 1731–1739. https://doi.org/10
.1128/mcb.7.5.1731-1739.1987. PubMed PMID: 3110598; PMCID: PMC365274.
46 Kenan, D.J., Query, C.C., and Keene, J.D. (1991). RNA recognition: towards
identifying determinants of specicity. Trends Biochem Sci. 16 (6): 214–220.
https://doi.org/10.1016/0968-0004(91)90088-d. PubMed PMID: 1716386.
References 307
https://t.me/med1917
47 Birney, E., Kumar, S., and Krainer, A.R. (1993). Analysis of the
RNA-recognition motif and RS and RGG domains: conservation in metazoan
pre-mRNA splicing factors. Nucleic Acids Res. 21 (25): 5803–5816. https://doi
.org/10.1093/nar/21.25.5803. PubMed PMID: 8290338; PMCID: PMC310458.
48 Skrisovska, L., Bourgeois, C.F., Ste, R. et al. (2007). The testis-specic human
protein RBMY recognizes RNA through a novel mode of interaction. EMBO
Rep. 8 (4): 372–379. Epub 20070223. https://doi.org/10.1038/sj.embor.7400910.
PubMed PMID: 17318228; PMCID: PMC1852761.
49 Volpon, L., D’Orso, I., Young, C.R. et al. (2005). NMR structural study of
TcUBP1, a single RRM domain protein from Trypanosoma cruzi: contribu-
tion of a beta hairpin to RNA binding. Biochemistry. 44 (10): 3708–3717. https://
doi.org/10.1021/bi047450e. PubMed PMID: 15751947.
50 Tintaru, A.M., Hautbergue, G.M., Hounslow, A.M. et al. (2007). Structural and
functional analysis of RNA and TAP binding to SF2/ASF. EMBO Rep. 8 (8):
756–762. Epub 20070713. https://doi.org/10.1038/sj.embor.7401031. PubMed
PMID: 17668007; PMCID: PMC1978082.
51 Dominguez, C. and Allain, F.H. (2006). NMR structure of the three quasi RNA
recognition motifs (qRRMs) of human hnRNP F and interaction studies with
Bcl-x G-tract RNA: a novel mode of RNA recognition. Nucleic Acids Res. 34
(13): 3634–3645. Epub 20060802. https://doi.org/10.1093/nar/gkl488. PubMed
PMID: 16885237; PMCID: PMC1540728.
52 Ste, R., Skrisovska, L., and Allain, F.H. (2005). RNA sequence- and
shape-dependent recognition by proteins in the ribonucleoprotein particle.
EMBO Rep. 6 (1): 33–38. https://doi.org/10.1038/sj.embor.7400325. PubMed
PMID: 15643449; PMCID: PMC1299235.
53 Ryter, J.M. and Schultz, S.C. (1998). Molecular basis of double-stranded
RNA-protein interactions: structure of a dsRNA-binding domain complexed
with dsRNA. EMBO J. 17 (24): 7505–7513. https://doi.org/10.1093/emboj/17.24
.7505. PubMed PMID: 9857205; PMCID: PMC1171094.
54 Ste, R., Oberstrass, F.C., Hood, J.L. et al. (2010). The solution structure of the
ADAR2 dsRBM-RNA complex reveals a sequence-specic readout of the minor
groove. Cell. 143 (2): 225–237. https://doi.org/10.1016/j.cell.2010.09.026. PubMed
PMID: 20946981; PMCID: PMC2956598.
55 Wang, Z., Hartman, E., Roy, K. et al. (2011). Structure of a yeast RNase III
dsRBD complex with a noncanonical RNA substrate provides new insights into
binding specicity of dsRBDs. Structure. 19 (7): 999–1010. https://doi.org/10
.1016/j.str.2011.03.022. PubMed PMID: 21742266; PMCID: PMC3143303.
56 Barraud, P., Banerjee, S., Mohamed, W.I . et al. (2014). A bimodular nuclear
localization signal assembled via an extended double-stranded RNA-binding
domain acts as an RNA-sensing signal for transportin 1. Proc Natl Acad Sci
USA.111 (18): E1852–E1861. Epub 20140421. https://doi.org/10.1073/pnas
.1323698111. PubMed PMID: 24753571; PMCID: PMC4020056.
57 Chang, K.Y. and Ramos, A. (2005). The double-stranded RNA-binding motif, a
versatile macromolecular docking platform. FEBS J. 272 (9): 2109–2117. https://
doi.org/10.1111/j.1742-4658.2005.04652.x. PubMed PMID: 15853796.
308 11 RNA–Protein Interactions: A New Approach for Drugging RNA Biology
https://t.me/med1917
58 Wolfe, S.A., Nekludova, L., and Pabo, C.O. (2000). DNA recognition by
Cys2His2 zinc nger proteins. Annu Rev Biophys Biomol Struct. 29: 183–212.
https://doi.org/10.1146/annurev.biophys.29.1.183. PubMed PMID: 10940247.
59 Pelham, H.R. and Brown, D.D. (1980). A specic transcription factor that can
bind either the 5S RNA gene or 5S RNA. Proc Natl Acad Sci U S A. 77 (7):
4170–4174. https://doi.org/10.1073/pnas.77.7.4170. PubMed PMID: 7001457;
PMCID: PMC349792.
60 Amarasinghe, G.K., De Guzman, R.N., Turner, R.B. et al. (2000). NMR struc-
ture of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the psi-RNA
packaging signal. Implications for genome recognition. J Mol Biol. 301 (2):
491–511. https://doi.org/10.1006/jmbi.2000.3979. PubMed PMID: 10926523.
61 Hudson, B.P., Martinez-Yamout, M.A., Dyson, H.J., and Wright, P. E. (2004).
Recognition of the mRNA AU-rich element by the zinc nger domain of
TIS11d. Nat Struct Mol Biol. 11 (3): 257–264. Epub 20040208. https://doi.org/10
.1038/nsmb738. PubMed PMID: 14981510.
62 Lu, D., Searles, M.A., and Klug, A. (2003). Crystal structure of a
zinc-nger-RNA complex reveals two modes of molecular recognition. Nature.
426 (6962): 96–100. https://doi.org/10.1038/nature02088. PubMed PMID:
14603324.
63 Blackshear, P.J. (2002). Tristetraprolin and other CCCH tandem zinc-nger
proteins in the regulation of mRNA turnover. Biochem Soc Trans. 30 (Pt 6):
945–952. https://doi.org/10.1042/bst0300945. PubMed PMID: 12440952.
64 Loughlin, F.E., Manseld, R.E., Vaz, P.M. et al. (2009). The zinc ngers of
the SR-like protein ZRANB2 are single-stranded RNA-binding domains that
recognize 5’ splice site-like sequences. Proc Natl Acad Sci U S A. 106 (14):
5581–5586. Epub 20090320. https://doi.org/10.1073/pnas.0802466106. PubMed
PMID: 19304800; PMCID: PMC2667063.
65 Grishin, N.V. (2001). KH domain: one motif, two folds. Nucleic Acids Res. 29
(3): 638–643. https://doi.org/10.1093/nar/29.3.638. PubMed PMID: 11160884;
PMCID: PMC30387.
66 Beuth, B., Pennell, S., Arnvig, K.B. et al. (2005). Structure of a Mycobacterium
tuberculosis NusA-RNA complex. EMBO J. 24 (20): 3576–3587. Epub 20050929.
https://doi.org/10.1038/sj.emboj.7600829. PubMed PMID: 16193062; PMCID:
PMC1276712.
67 Amir, M., Kumar, V. , Dohare, R. et al. (2018). Sequence, structure and evolu-
tionary analysis of cold shock domain proteins, a member of OB fold family. J
Evol Biol. 31 (12): 1903–1917. Epub 20181019. https://doi.org/10.1111/jeb.13382.
PubMed PMID: 30267552.
68 Hazra, D., Chapat, C., and Graille, M. (2019). m(6)A mRNA destiny: chained
to the rhYTHm by the YTH-containing proteins. Genes (Basel). 10 (1) Epub
20190115. https://doi.org/10.3390/genes10010049: PubMed PMID: 30650668;
PMCID: PMC6356822.
69 Li, J., Xie, H., Ying, Y. et al. (2020). YTHDF2 mediates the mRNA degra-
dation of the tumor suppressors to induce AKT phosphorylation in
N6-methyladenosine-dependent way in prostate cancer. Mol Cancer. 19 (1):
References 309
https://t.me/med1917
152. Epub 20201029. https://doi.org/10.1186/s12943-020-01267-6 . PubMed
PMID: 33121495; PMCID: PMC7599101.
70 Chen, Z., Zhong, X., Xia, M., and Zhong, J. (2021). The roles and mechanisms
of the m6A reader protein YTHDF1 in tumor biology and human diseases.
Mol Ther Nucleic Acids 26: 1270–1279. Epub 20211104. https://doi.org/10.1016/j
.omtn.2021.10.023. PubMed PMID: 34853726; PMCID: PMC8609105.
71 Thandapani, P., O’Connor, T.R., Bailey, T.L., and Richard, S. (2013). Dening
the RGG/RG motif. Mol Cell. 50 (5): 613–623. https://doi.org/10.1016/j.molcel
.2013.05.021. PubMed PMID: 23746349.
72 Dennis, G. Jr.,, Sherman, B.T., Hosack, D.A. et al. (2003). DAVID: database for
annotation, visualization, and integrated discovery. Genome Biol. 4 (5): P3. Epub
20030403. PubMed PMID: 12734009.
73 Blackwell, E. and Ceman, S. (2011). A new regulatory function of the region
proximal to the RGG box in the fragile X mental retardation protein. JCell
Sci. 124 (Pt 18): 3060–3065. Epub 20110824. https://doi.org/10.1242/jcs.086751.
PubMed PMID: 21868366; PMCID: PMC3172185.
74 Ina, S., Tsunekawa, N., Nakamura, A., and Noce, T. (2003). Expression of the
mouse Aven gene during spermatogenesis, analyzed by subtraction screening
using Mvh-knockout mice. Gene Expr Patterns. 3 (5): 635–638. https://doi.org/10
.1016/s1567-133x(03)00111-x. PubMed PMID: 12971998.
75 Matsuoka, S., Ballif, B.A., Smogorzewska, A. et al. (2007). ATM and ATR
substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 316 (5828): 1160–1166. https://doi.org/10.1126/science.1140321.
PubMed PMID: 17525332.
76 Nissan, T., Rajyaguru, P., She, M. et al. (2010). Decapping activators in Sac-
charomyces cerevisiae act by multiple mechanisms. Mol Cell. 39 (5): 773–783.
https://doi.org/10.1016/j.molcel.2010.08.025. PubMed PMID: 20832728; PMCID:
PMC2946179.
77 Rajyaguru, P., She, M., and Parker, R. (2012). Scd6 targets eIF4G to repress
translation: RGG motif proteins as a class of eIF4G-binding proteins. Mol Cell.
45 (2): 244–254. https://doi.org/10.1016/j.molcel.2011.11.026. PubMed PMID:
22284680; PMCID: PMC3277450.
78 Andrisani, O., Liu, Q., Kehn, P. et al. (2022). Biological functions of
DEAD/DEAH-box RNA helicases in health and disease. Nat Immunol. 23 (3):
354–357. https://doi.org/10.1038/s41590-022-01149-7 . PubMed PMID: 35194205.
79 Wickens, M., Bernstein, D.S., Kimble, J., and Parker, R. (2002). A PUF fam-
ily portrait: 3’UTR regulation as a way of life. Trends Genet. 18 (3): 150–157.
https://doi.org/10.1016/s0168-9525(01)02616-6. PubMed PMID: 11858839.
80 Chen, Y. and Varani, G. (2011). Finding the missing code of RNA recognition
by PUF proteins. Chem Biol. 18 (7): 821–823. https://doi.org/10.1016/j.chembiol
.2011.07.001. PubMed PMID: 21802002; PMCID: PMC3161827.
81 Tam, P.P., Barrette-Ng, I.H., Simon, D.M. et al. (2010). The Puf family of
RNA-binding proteins in plants: phylogeny, structural modeling, activity and
subcellular localization. BMC Plant Biol. 10: 44. Epub 20100309. https://doi.org/
10.1186/1471-2229-10-44 . PubMed PMID: 20214804; PMCID: PMC2848763.
310 11 RNA–Protein Interactions: A New Approach for Drugging RNA Biology
https://t.me/med1917
82 Rissland, O.S. (2017). The organization and regulation of mRNA-protein com-
plexes. Wiley Interdiscip Rev RNA 8 (1) Epub 20160621. https://doi.org/10.1002/
wrna.1369: PubMed PMID: 27324829; PMCID: PMC5213448.
83 Ransoho, J.D., Wei, Y., and Khavari, P. A . (2018). The functions and unique
features of long intergenic non-coding RNA. Nat Rev Mol Cell Biol. 19 (3):
143–157. Epub 20171115. https://doi.org/10.1038/nrm.2017.104. PubMed PMID:
29138516; PMCID: PMC5889127.
84 Statello, L., Guo, C.J., Chen, L.L., and Huarte, M. (2021). Gene regulation
by long non-coding RNAs and its biological functions. Nat Rev Mol Cell Biol.
22 (2): 96–118. Epub 20201222. https://doi.org/10.1038/s41580-020-00315-9.
PubMed PMID: 33353982; PMCID: PMC7754182.
85 Treiber, T., Treiber, N., and Meister, G. (2019). Regulation of microRNA bio-
genesis and its crosstalk with other cellular pathways. Nature Reviews Molecular
Cell Biology. 20 (1): 5–20. https://doi.org/10.1038/s41580-018-0059-1.
86 Wilkinson, E., Cui, Y.H., and He, Y.Y. (2022). Roles of RNA modications in
diverse cellular functions. Front Cell Dev Biol. 10: 828683. Epub 20220308.
https://doi.org/10.3389/fcell.2022.828683. PubMed PMID: 35350378; PMCID:
PMC8957929.
87 Shi, H., Chai, P. , Jia, R., and Fan, X. (2020). Novel insight into the regulatory
roles of diverse RNA modications: Re-dening the bridge between transcription and translation. Mol Cancer. 19 (1): 78. Epub 20200417. https://doi.org/10
.1186/s12943-020-01194-6 . PubMed PMID: 32303268; PMCID: PMC7164178.
88 Katz, N., Cohen, R., Solomon, O. et al. (2018). RBP-RNA interactions in the 5’
UTR lead to structural changes that alter translation. bioRxiv. 174888. https://
doi.org/10.1101/174888.
89 Szostak, E. and Gebauer, F. (2013). Translational control by 3’-UTR-binding
proteins. Brief Funct Genomics 12 (1): 58–65. Epub 20121128. https://doi.org/10
.1093/bfgp/els056. PubMed PMID: 23196851; PMCID: PMC3548161.
90 Grzybowska, E.A. and Wakula, M. (2021). Protein binding to cis-motifs in
mRNAs coding sequence is common and regulates transcript stability and
the rate of translation. Cells 10 (11) Epub 20211027. https://doi.org/10.3390/
cells10112910: PubMed PMID: 34831133; PMCID: PMC8616275.
91 Savisaar, R. and Hurst, L.D. (2017). Both maintenance and avoidance of
RNA-binding protein interactions constrain coding sequence evolution. Molec-
ular Biology and Evolution. 34 (5): 1110–1126. https://doi.org/10.1093/molbev/
msx061.
92 Leppek, K., Das, R., and Barna, M. (2018). Functional 5’ UTR mRNA structures
in eukaryotic translation regulation and how to nd them. Nat Rev Mol Cell
Biol. 19 (3): 158–174. Epub 20171122. https://doi.org/10.1038/nrm.2017.103.
PubMed PMID: 29165424; PMCID: PMC5820134.
93 Mignone, F., Gissi, C., Liuni, S., and Pesole, G. (2002). Untranslated regions of
mRNAs. Genome Biol. 3 (3) Reviews0004. Epub 20020228. https://doi.org/10
.1186/gb-2002-3-3-reviews0004: PubMed PMID: 11897027; PMCID: PMC139023.
94 Mayya, V. K . and Duchaine, T.F. (2019). Ciphers and executioners: how
3’-untranslated regions determine the fate of messenger RNAs. Front Genet.
References 311
https://t.me/med1917
10 (6) Epub 20190124. https://doi.org/10.3389/fgene.2019.00006: PubMed PMID:
30740123; PMCID: PMC6357968.
95 Kapeli, K., Martinez, F.J., and Yeo, G.W. (2017). Genetic mutations in
RNA-binding proteins and their roles in ALS. Hum Genet. 136 (9): 1193–1214.
Epub 20170731. https://doi.org/10.1007/s00439-017-1830-7. PubMed PMID:
28762175; PMCID: PMC5602095.
96 Khabar, K.S. (2017). Hallmarks of cancer and AU-rich elements. Wiley Interdis-
cip Rev RNA 8 (1) Epub 20160601. https://doi.org/10.1002/wrna.1368: PubMed
PMID: 27251431; PMCID: PMC5215528.
97 Mir, C., Garcia-Mayea, Y., and ME LL (2022). Targeting the "undruggable":
RNA-binding proteins in the spotlight in cancer therapy. Semin Cancer Biol. 86
(Pt 3): 69–83. Epub 20220627. https://doi.org/10.1016/j.semcancer.2022.06.008.
PubMed PMID: 35772609.
98 Berson, A., Barbash, S., Shaltiel, G. et al. (2012). Cholinergic-associated loss of
hnRNP-A/B in Alzheimer’s disease impairs cortical splicing and cognitive function in mice. EMBO Mol Med. 4 (8): 730–742. Epub 20120525. https://doi.org/10
.1002/emmm.201100995. PubMed PMID: 22628224; PMCID: PMC3494073.
99 Donev, R., Newall, A., Thome, J., and Sheer, D. (2007). A role for SC35 and
hnRNPA1 in the determination of amyloid precursor protein isoforms. Mol Psy-
chiatry 12 (7): 681–690. Epub 20070313. https://doi.org/10.1038/sj.mp.4001971.
PubMed PMID: 17353911; PMCID: PMC2684093.
100 Kharas, M.G. and Lengner, C.J. (2017). Stem cells, cancer, and MUSASHI in
blood and guts. Trends in Cancer. 3 (5): 347–356. https://doi.org/10.1016/j.trecan
.2017.03.007.
101 Sakakibara, S. and Okano, H. (1997). Expression of neural RNA-binding pro-
teins in the postnatal CNS: implications of their roles in neuronal and glial cell
development. J Neurosci. 17 (21): 8300–8312. https://doi.org/10.1523/jneurosci
.17-21-08300.1997. PubMed PMID: 9334405; PMCID: PMC6573750.
102 Imai, T., Tokunaga, A., Yoshida, T. et al. (2001). The neural RNA-binding pro-
tein Musashi1 translationally regulates mammalian numb gene expression by
interacting with its mRNA. Mol Cell Biol. 21 (12): 3888–3900. https://doi.org/10
.1128/mcb.21.12.3888-3900.2001. PubMed PMID: 11359897; PMCID: PMC87052.
103 Gulino, A., Di Marcotullio, L., and Screpanti, I. (2010). The multiple functions
of Numb. Experimental Cell Research. 316 (6): 900–906. https://doi.org/10.1016/j
.yexcr.2009.11.017.
104 Bentley, D.L. (2014). Coupling mRNA processing with transcription in time and
space. Nature Reviews Genetics. 15 (3): 163–175. https://doi.org/10.1038/nrg3662.
105 Fredericks, A.M., Cygan, K.J., Brown, B.A., and Fairbrother, W. G . (2015).
RNA-binding proteins: splicing factors and disease. Biomolecules 5 (2):
893–909. Epub 20150513. https://doi.org/10.3390/biom5020893. PubMed PMID:
25985083; PMCID: PMC4496701.
106 Jeong, S. (2017). SR proteins: binders, regulators, and connectors of RNA. Mol
Cells. 40 (1): 1–9. Epub 20170126. https://doi.org/10.14348/molcells.2017.2319.
PubMed PMID: 28152302; PMCID: PMC5303883.
312 11 RNA–Protein Interactions: A New Approach for Drugging RNA Biology
https://t.me/med1917
107 Chou, M.Y., Rooke, N., Turck, C.W., and Black, D.L. (1999). hnRNP H is a com-
ponent of a splicing enhancer complex that activates a c-src alternative exon in
neuronal cells. Mol Cell Biol. 19 (1): 69–77. https://doi.org/10.1128/mcb.19.1.69.
PubMed PMID: 9858532; PMCID: PMC83866.
108 Zhang, J. and Manley, J.L. (2013). Misregulation of pre-mRNA alternative
splicing in cancer. Cancer Discov. 3 (11): 1228–1237. Epub 20131021. https://
doi.org/10.1158/2159-8290.Cd-13-0253 . PubMed PMID: 24145039; PMCID:
PMC3823817.
109 Anczuków, O., Rosenberg, A.Z., Akerman, M. et al. (2012). The splicing factor
SRSF1 regulates apoptosis and proliferation to promote mammary epithelial cell
transformation. Nat Struct Mol Biol. 19 (2): 220–228. Epub 20120115. https://doi
.org/10.1038/nsmb.2207. PubMed PMID: 22245967; PMCID: PMC3272117.
110 Arnold, E.S., Ling, S.C., Huelga, S.C. et al. (2013). ALS-linked TDP-43 muta-
tions produce aberrant RNA splicing and adult-onset motor neuron disease
without aggregation or loss of nuclear TDP-43. Proc Natl Acad Sci U S A 110
(8): E736–E745. Epub 20130204. https://doi.org/10.1073/pnas.1222809110.
PubMed PMID: 23382207; PMCID: PMC3581922.
111 Fogel, B.L., Wexler, E., Wahnich, A. et al. (2012). RBFOX1 regulates both splic-
ing and transcriptional networks in human neuronal development. Hum Mol
Genet. 21 (19): 4171–4186. Epub 20120623. https://doi.org/10.1093/hmg/dds240.
PubMed PMID: 22730494; PMCID: PMC3441119.
112 Wang, E.T., Cody, N.A., Jog, S. et al. (2012). Transcriptome-wide regulation
of pre-mRNA splicing and mRNA localization by muscleblind proteins. Cell.
150 (4): 710–724. https://doi.org/10.1016/j.cell.2012.06.041. PubMed PMID:
22901804; PMCID: PMC3428802.
113 Bradley, R.K. and Anczuków, O. (2023). RNA splicing dysregulation and the
hallmarks of cancer. Nature Reviews Cancer. 23 (3): 135–155. https://doi.org/10
.1038/s41568-022-00541-7 .
114 Borden, K.L.B. (2020). The Nuclear Pore Complex and mRNA Export in Cancer.
Cancers (Basel). 13 (1) Epub 20201225. https://doi.org/10.3390/cancers13010042:
PubMed PMID: 33375634; PMCID: PMC7796397.
115 Hurt, J.A. and Silver, P.A. (2008). mRNA nuclear export and human disease.
Dis Model Mech. 1 (2-3): 103–108. https://doi.org/10.1242/dmm.000745. PubMed
PMID: 19048072; PMCID: PMC2562179.
116 Chau, A. and Kalsotra, A. (2015). Developmental insights into the pathology
of and therapeutic strategies for DM1: Back to the basics. Dev Dyn. 244 (3):
377–390. Epub 20150113. https://doi.org/10.1002/dvdy.24240. PubMed PMID:
25504326.
117 Pettersson, O.J., Aagaard, L., Jensen, T.G., and Damgaard, C.K. (2015). Molecu-
lar mechanisms in DM1 - a focus on foci. Nucleic Acids Res. 43 (4): 2433–2441.
Epub 20150120. https://doi.org/10.1093/nar/gkv029. PubMed PMID: 25605794;
PMCID: PMC4344492.
118 Brook, J.D., McCurrach, M.E., Harley, H.G. et al. (1992). Molecular basis of
myotonic dystrophy: expansion of a trinucleotide (CTG) repeat at the 3’ end
References 313
https://t.me/med1917
of a transcript encoding a protein kinase family member. Cell. 68 (4): 799–808.
https://doi.org/10.1016/0092-8674(92)90154-5. PubMed PMID: 1310900.
119 Buxton, J., Shelbourne, P., Davies, J. et al. (1992). Detection of an unstable
fragment of DNA specic to individuals with myotonic dystrophy. Nature. 355
(6360): 547–548. https://doi.org/10.1038/355547a0. PubMed PMID: 1346924.
120 Fu, Y.H., Pizzuti, A., Fenwick, R.G. Jr., et al. (1992). An unstable triplet
repeat in a gene related to myotonic muscular dystrophy. Science. 255 (5049):
1256–1258. https://doi.org/10.1126/science.1546326. PubMed PMID: 1546326.
121 Harley, H.G., Brook, J.D., Rundle, S.A. et al. (1992). Expansion of an unsta-
ble DNA region and phenotypic variation in myotonic dystrophy. Nature. 355
(6360): 545–546. https://doi.org/10.1038/355545a0. PubMed PMID: 1346923.
122 Mahadevan, M., Tsildis, C., Sabourin, L. et al. (1992). Myotonic dystro-
phy mutation: an unstable CTG repeat in the 3’ untranslated region of the
gene. Science. 255 (5049): 1253–1255. https://doi.org/10.1126/science.1546325.
PubMed PMID: 1546325.
123 Paulson, H. (2018). Repeat expansion diseases. Handb Clin Neurol. 147:
105–123. https://doi.org/10.1016/b978-0-444-63233-3.00009-9 . PubMed PMID:
29325606; PMCID: PMC6485936.
124 Johnson, B.S., Snead, D., Lee, J.J. et al. (2009). TDP-43 is intrinsically
aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate
aggregation and increase toxicity. J Biol Chem. 284 (30): 20329–20339. Epub
20090522. https://doi.org/10.1074/jbc.M109.010264. PubMed PMID: 19465477;
PMCID: PMC2740458.
125 Barmada, S.J., Skibinski, G., Korb, E. et al. (2010). Cytoplasmic mislocaliza-
tion of TDP-43 is toxic to neurons and enhanced by a mutation associated
with familial amyotrophic lateral sclerosis. J Neurosci. 30 (2): 639–649. https://
doi.org/10.1523/jneurosci.4988-09.2010. PubMed PMID: 20071528; PMCID:
PMC2821110.
126 Wang, W. , Wang, L., Lu, J. et al. (2016). The inhibition of TDP-43 mitochon-
drial localization blocks its neuronal toxicity. Nat Med. 22 (8): 869–878. Epub
20160627. https://doi.org/10.1038/nm.4130. PubMed PMID: 27348499; PMCID:
PMC4974139.
127 Paronetto, M.P., Messina, V. , Bianchi, E. et al. (2009). Sam68 regulates transla-
tion of target mRNAs in male germ cells, necessary for mouse spermatogenesis.
Journal of Cell Biology. 185 (2): 235–249. https://doi.org/10.1083/jcb.200811138.
128 Paronetto, M.P., Zalfa, F., Botti, F. et al. (2006). The nuclear RNA-binding pro-
tein Sam68 translocates to the cytoplasm and associates with the polysomes in
mouse spermatocytes. Mol Biol Cell. 17 (1): 14–24. Epub 20051012. https://doi
.org/10.1091/mbc.e05-06-0548. PubMed PMID: 16221888; PMCID: PMC1345642.
129 Frisone, P., Pradella, D., Di Matteo, A. et al. (2015). SAM68: Signal Transduc-
tion and RNA Metabolism in Human Cancer. Biomed Res Int. 2015: 528954.
Epub 20150726. https://doi.org/10.1155/2015/528954. PubMed PMID: 26273626;
PMCID: PMC4529925.
130 Zhang, Z., Li, J., Zheng, H. et al. (2009). Expression and cytoplasmic localiza-
tion of SAM68 is a signicant and independent prognostic marker for renal
314 11 RNA–Protein Interactions: A New Approach for Drugging RNA Biology
https://t.me/med1917
cell carcinoma. Cancer Epidemiol Biomarkers Prev. 18 (10): 2685–2693. Epub
20090915. https://doi.org/10.1158/1055-9965.Epi-09-0097 . PubMed PMID:
19755649.
131 Song, L., Wang, L., Li, Y. et al. (2010). Sam68 up-regulation correlates with, and
its down-regulation inhibits, proliferation and tumourigenicity of breast cancer
cells. J Pathol. 222 (3): 227–237. https://doi.org/10.1002/path.2751. PubMed
PMID: 20662004.
132 Almasi, S. and Jasmin, B.J. (2021). The multifunctional RNA-binding protein
Staufen1: an emerging regulator of oncogenesis through its various roles in key
cellular events. Cellular and Molecular Life Sciences. 78 (23): 7145–7160. https://
doi.org/10.1007/s00018-021-03965-w .
133 Wickham, L., Duchaîne, T., Luo, M. et al. (1999). Mammalian staufen is a
double-stranded-RNA- and tubulin-binding protein which localizes to the rough
endoplasmic reticulum. Mol Cell Biol. 19 (3): 2220–2230. https://doi.org/10
.1128/mcb.19.3.2220. PubMed PMID: 10022909; PMCID: PMC84015.
134 Liu, H., Luo, M., and Wen, J.K. (2014). mRNA stability in the nucleus.
J Zhejiang Univ Sci B. 15 (5): 444–454. https://doi.org/10.1631/jzus.B1400088.
PubMed PMID: 24793762; PMCID: PMC4076601.
135 Yamaguchi, Y., Naiki, T., and Irie, K. (2012). Stau1 regulates Dvl2 expres-
sion during myoblast dierentiation. Biochem Biophys Res Commun. 417 (1):
427–432. Epub 20111207. https://doi.org/10.1016/j.bbrc.2011.11.133. PubMed
PMID: 22166206.
136 Kim, Y.K., Furic, L., Desgroseillers, L., and Maquat, L.E. (2005). Mammalian
Staufen1 recruits Upf1 to specic mRNA 3’UTRs so as to elicit mRNA decay.
Cell. 120 (2): 195–208. https://doi.org/10.1016/j.cell.2004.11.050. PubMed PMID:
15680326.
137 Yu, Z., Fan, D., Gui, B. et al. (2012). Neurodegeneration-associated TDP-43
interacts with fragile X mental retardation protein (FMRP)/Staufen (STAU1)
and regulates SIRT1 expression in neuronal cells. J Biol Chem. 287 (27):
22560–22572. Epub 20120514. https://doi.org/10.1074/jbc.M112.357582. PubMed
PMID: 22584570; PMCID: PMC3391095.
138 Jing, F., Ruan, X., Liu, X. et al. (2020). The PABPC5/HCG15/ZNF331 feedback
loop regulates vasculogenic mimicry of glioma via STAU1-mediated mRNA
decay. Mol Ther Oncolytics. 17: 216–231. Epub 20200330. https://doi.org/10
.1016/j.omto.2020.03.017. PubMed PMID: 32346611; PMCID: PMC7183103.
139 Su, R., Ma, J., Zheng, J. et al. (2020). PABPC1-induced stabilization of BDNF-AS
inhibits malignant progression of glioblastoma cells through STAU1-mediated
decay. Cell Death Dis. 11 (2): 81. Epub 20200203. https://doi.org/10.1038/
s41419-020-2267-9 . PubMed PMID: 32015336; PMCID: PMC6997171.
140 Cushman, M., Johnson, B.S., King, O.D. et al. (2010). Prion-like disorders:
blurring the divide between transmissibility and infectivity. JCellSci.123 (Pt
8): 1191–1201. https://doi.org/10.1242/jcs.051672. PubMed PMID: 20356930;
PMCID: PMC2848109.
141 Vance, C., Scotter, E.L., Nishimura, A.L. et al. (2013). ALS mutant FUS disrupts
nuclear localization and sequesters wild-type FUS within cytoplasmic stress
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