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Molecularly imprinted polymers (MIPs) are where the complexity of receptor proteins meets the tunability of synthetic research. Receptor proteins, such as enzymes or antibodies, have functional cavities that act as docking platforms by recognizing and binding to complementary ligands. Once bound, a receptor–ligand complex may generate any multitude of cellular responses, including the regulation, uptake, and/or release of certain hormones, neurotransmitters, inorganic minerals, antigens, enzymes, and other molecules within an organism. Just like receptor proteins, MIPs are polymers with carefully selected functional groups that are spacially arranged to recognize target molecules. MIPs are generated by templating a functionalized polymer with a molecule, leaving a cavity that is complementary to the molecule upon removal. That cavity then has an affinity for the molecule that was templeted for later rebinding. The aim of MIP research is to recognize a desired target molecule with the precision of receptor proteins, and to maintain specificity and sensitivity towards the target molecule while tailoring functional properties for advanced applications. Resarchers are far from perfecting the delicate intricacy of mimicking such elegant biological processes, and improvements in all areas of MIP synthesis remain a vibrant and active topic. Various methods explored to synthesize MIPs with impressive recognition capabilities towards target molecules and the recent applications of MIPs are found herein. This review aims to dissect the synthetic steps required to generate MIPs, with emphasis on the more recent routes utilized and overall application advances.