The Study
Abstract A047: KRAS G12C and G12D mutants exhibit distinct conformational flexibility in the helix 3–switch 2 pocket that drives differential protein function
This study is like taking apart two different toy cars to see how their insides work differently. It shows one car’s engine part moves in a weird way compared to the other, but it doesn’t tell you which car will break down faster on the road.
Analysis score
Maximum 0 for a computational/algorithm study.
Where the score came from
Two common cancer mutations in the KRAS protein, G12D and G12C, look different at the molecular level, making G12D better at turning on cancer signals.
Where does this study sit?
Reviews of RCTs (Meta-analyses)
Max 100Randomized Trials
Max 90Reviews of Cohort Studies
Max 85Cohort Studies
Max 72Reviews of Case-Control Studies
Max 63Case-Control Studies
Max 58Cross-Sectional & Case Series
Max 50Expert Opinion
Max 50 / 100
Quality score
Based on clinical experience or non-systematic literature reviews. The lowest level of evidence as they are most susceptible to bias and personal perspective.
Key takeaways
Summary
Based on the study abstract and findings.
- 1Yes — stronger binding means G12D may drive cancer more aggressively and respond differently to drugs than G12C.
- 2KRASG12D binds the cancer signal protein PI3Kα 2x stronger than KRASG12C, and 3x stronger than normal KRAS.
- 3A drug called BBO-11534 works better on G12D than G12C.
Score breakdown, methodology, conflicts of interest, evidence analysis & raw study data
Publication
Journal
Cancer Research
Year
2026
Authors
Alok K. Sharma, Megan Rigby, Marco Tonelli, Nicole Fer, Patrick A Alexander, Jun Pei, Yue Yang, Dana Rabara, Erik K. Larsen, Brian P Smith, R. Ma, V. Kumari, M. Dyba, F. Lightstone, Bin Wang, P. Beltran, Eli Wallace, Andrew G Stephen, D. Nissley, F. McCormick, A. Maciag
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Not medical advice. For informational purposes only. Always consult a qualified healthcare professional before making health decisions.