RAS is easily the most frequently mutated oncogene in human cancers, with mutations within 30% of cancers. RAS exists in three different isoforms (K-RAS, H-RAS and N-RAS) rich in sequence homology. K-RAS is easily the most generally mutated RAS isoform. The Ras proteins are a membrane bound protein with natural GTPase activity and it is activated by numerous extracellular stimuli, cycling between a non-active (GDP-bound) and active (GTP-bound) form. When certain to GTP, it’s switched “on” and activates intracellular signaling pathways, crucial for cell proliferation and angiogenesis. Mutated RAS is constitutively activated and persistently switched “on” therefore enhancing downstream signaling and resulting in tumorigenesis. Various tries to hinder Kras previously were unsuccessful. Lately, several small molecules (AMG510, MRTX849, JNJ-74699157, and LY3499446) happen to be designed to particularly target K-RAS G12C. Furthermore, many other approaches including, SHP2, SOS1 and eIF4 inhibition, happen to be employed to abrogate tumor development in K-RAS mutant cells, producing a restored curiosity about this path. Within this review article, we offer a summary around the role of K-RAS in tumorigenesis, past methods to inhibiting Kras, and current and potential customers for targeting Kras.