Graphene, the thinnest, strongest, and stiffest material with exceptional thermal conductivity and electron mobility, has increasingly received world‐wide attention in the past few years. These unique properties may lead to novel or improved technologies to address the pressing global challenges in many applications including transparent conducting electrodes, field effect transistors, flexible touch screen, single‐molecule gas detection, desalination, DNA sequencing, osmotic energy production, etc. To realize these applications, it is necessary to transfer graphene films from growth substrate to target substrate with large‐area, clean, and low defect surface, which are crucial to the performances of large‐area graphene devices. This critical review assesses the recent development in transferring large‐area graphene grown on Fe, Ru, Co, Ir, Ni, Pt, Au, Cu, and some nonmetal substrates by using various synthesized methods. Among them, the transfers of the most attention kinds of graphene synthesized on Cu and SiC substrates are discussed emphatically. The advances and the main challenges of each wet and dry transfer method for obtaining the transferred graphene film with large‐area, clean, and low defect surface are also reviewed. Finally, the article concludes the most promising methods and the further prospects of graphene transfer.

The human Y box-binding protein-1 (YB-1) is a deoxyribonucleic acid (DNA)/ribonucleic acid (RNA)-binding protein with pleiotropic functions. Besides its roles in the regulation of transcription and translation, several recent studies indicate that YB-1 is a spliceosome-associated protein and is involved in alternative splicing, but the underlying mechanism has remained elusive. Here, we define both CAUC and CACC as high-affinity binding motifs for YB-1 by systematic evolution of ligands by exponential enrichment (SELEX) and demonstrate that these newly defined motifs function as splicing enhancers. Interestingly, on the endogenous CD44 gene, YB-1 appears to mediate a network interaction to activate exon v5 inclusion via multiple CAUC motifs in both the alternative exon and its upstream polypyrimidine tract. We provide evidence that YB-1 activates splicing by facilitating the recruitment of U2AF65 to weak polypyrimidine tracts through direct protein–protein interactions. Together, these findings suggest a vital role of YB-1 in activating a subset of weak 3′ splice sites in mammalian cells.