## 1 Introduction  
N6-methyladenosine (m6A) [1], which is methylated adenosine at the nitrogen-6 position of the base, plays a key role in epigenetics [2] and epitranscriptomics [3]. In addition, m6A alteration (or modification) of RNA, identified first in the 1970s [4], is the most typical and prevalent mRNA alteration found in viral RNAs and the most eukaryotic species. In the transcriptome, m6A is present at a frequency of 0.15 to 0.6% of all adenosines [5]. Its modification is a dynamically reversible biological process, and it generally occurs in a conserved motif defined as \"DRACH\" (D = A or G or U, R = A or G, H = A or C or U) [6]. Furthermore, m6A modification is a post-transcriptional regulatory marker in various RNAs, such as mRNAs, rRNAs (ribosomal RNAs), circRNAs (circular RNAs), tRNAs (transfer RNAs), micro RNAs (miRNAs) [7, 8], and lncRNAs (long non-coding RNAs). As such, m6A modification plays vital roles in various biological processes, such as RNA splicing regulation, translation, translocation, and stability [9, 10, 8], and it is responsible for moderating various biological functions, such as brain development [11], heat shock response [12], chromatin accessibility [13], viral replications [14], the immune response to infection [15], and tumorigenesis [16]. N6-methyladenosine alteration is carried out by three main classes of epitranscriptome proteins: writers, erasers, and readers [8]. Reading proteins act as readers, methyltransferases at as writers, and dimethyltransferases at as erasers. Methyltransferase complexes, such as METTL3, METTL14, VIRMA, WTAP, ZC3H13, and RBM15/15B, catalyze m6A methylation [17]. The methylation is reversed by m6A erasers, such as ALKBH3/5 and FTO [18]. Readers recognize the m6A alteration on noncoding RNAs or mRNAs and mediate various events that include mRNA stability, splicing, export, translation efficiency, and biogenesis of miRNA [19; 20; 21; 22; 23; 24]. The YTH (YT521-B homology) domain family members, such as YTHDF1/2/3 and YTHDC1/2, are considered the most important m6A readers [25]. Different readers have different m6A positioning functions and distinctive mechanisms for various biological functions. Readers unique to the m6A cytoplasm are YTHDF1/2/3, whereas readers in the nucleus are YTHDC1/2 [26]. YTHDC1 promotes exon inclusion in targeted transcripts and facilitates embryonic development. It specifically recognizes the sequence G(m6A)C with its YTH domain to identify m6A modification [27]. After recognition, YTHDC1 unites with m6A-altered pre-RNAs to recruit the SRSF3 (serine and arginine-rich splicing factor 3). However, it inhibits SRSF10 (serine and arginine-rich splicing factor 10) binding to nuclear spots. As a result, the export of mRNA to the cytoplasm from the nucleus is promoted and exon inclusion splicing is then favored [22]. YTHDC1 can recognize various types of RNAs, such as m6A-altered CarRNAs (chromosome-related regulatory RNAs) that include ERNA (enhancer RNA), PaRNA (promoter-related RNA), and repetitive RNA (transposable element transcript RNA). YTHDC1 promotes the interpretation and decay of CarRNAs and regulates the transcription and state of the chromatin [28]. Recent studies [16; 19; 26] revealed that YTHDC1 has a vital role in cancer and other disorders. YTHDC1 mediates various biological processes, such as metastasis, angiogenesis, chemoresistance, and cancer cell proliferation [29; 30; 31; 32]. Furthermore, YTHDC1 can alter the immune response in lung cancer [33] and has been recognized as a pharmaceutical target in the treatment of acute myeloid leukemia (AML) [34]. These results indicate that YTHDC1 has the potential to enhance the therapeutic efficacy of immunotherapy treatments. Structure-based virtual screening is typically used in computer-aided drug design for discovering new scaffolds and identifying lead compounds. Molecular docking, a widely adopted method to perform virtual screening [35], has been used for screening large in-house and commercial compound libraries [36].