Membrane Composition and Raf[CRD]-Membrane Attachment Are

Membrane Composition and Raf[CRD]-Membrane Attachment Are Driving Forces for K-Ras4B Dimer Stability

Structure of the KRAS-RAF1(RBDCRD) complex and SPR analysis a Domain

Interactions at the RAF1-CRD interface with KRAS are required for full

Interfaces of the K-Ras4B−membrane and C-Raf−membrane interactions. (a)

Membrane Composition and Raf[CRD]-Membrane Attachment Are Driving Forces for K-Ras4B Dimer Stability

Three distinct regions of cRaf kinase domain interact with membrane

Membrane Composition and Raf[CRD]-Membrane Attachment Are Driving Forces for K-Ras4B Dimer Stability

CaM interaction and Ser181 phosphorylation as new K-Ras signaling modulators: Small GTPases: Vol 2, No 2

Raf-1 Cysteine-Rich Domain Increases the Affinity of K-Ras/Raf at the Membrane, Promoting MAPK Signaling. - Abstract - Europe PMC