[8][9][10] Garcia's research integrates approaches in structural biology, biochemistry and protein engineering to understand how cell surface receptors sense environmental cues through the engagement of extracellular ligands, and transduce signals.

The overarching theme of the laboratory is to elucidate the structural and mechanistic basis of receptor activation in systems relevant to human disease, and to exploit this information to design and engineer new molecules with therapeutic properties.

Garcia's laboratory at Stanford has published numerous scientific articles describing the molecular structure and signaling mechanisms of proteins important for immunity, neurobiology and development.

[12] As a postdoctoral scholar at The Scripps Research Institute, Garcia conducted a groundbreaking study that revealed how T cells of the immune system survey peptides presented by major histocompatibility complex proteins (MHC), thus allowing them to distinguish between "self" and "non-self".

These structures have revealed a wide range of binding topologies and architectures, and demonstrate how convergent evolution has provided many solutions for cytokine receptors to transduce signals across the cell membrane.

[29] The Wnt-Frizzled structure indicated that Wnts utilize a post-translational lipid modification to directly engage the Frizzled extracellular domain, which represents a highly unusual binding mode among soluble ligands.

[29] More recently, Garcia's laboratory reported a breakthrough in being able to recapitulate canonical Wnt signaling using water-soluble bispecific ligands that dimerize Frizzled and Lrp6, which has important implications for the development of therapeutics for regenerative medicine.

Garcia's 2017 publication also established that Notch-ligand interactions form catch bonds, and that Delta-like and Jagged ligands have different mechanical force thresholds for Notch receptor activation.