Sandbox Reserved 595: Difference between revisions
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Connecting the N-terminal and C-terminal domains is the flexible hinge region, which extends approximately from residue 165 to residue 215 '<ref>Phu, MG et al. 2005. Fluorescence resonance energy transfer analysis of apolipoprotein E C-terminal domain and amyloid beta peptide (1-42) interaction. J Neuro Sci Res 80(6):877-86.</ref>' '<ref>Dong L-M and K. H. Weisgraber. 1996. Human apolipoprotein E4 domain interaction. Arginine 61 and glutamic acid 255 interact to direct the preference for very low density | Connecting the N-terminal and C-terminal domains is the flexible hinge region, which extends approximately from residue 165 to residue 215 '<ref>Phu, MG et al. 2005. Fluorescence resonance energy transfer analysis of apolipoprotein E C-terminal domain and amyloid beta peptide (1-42) interaction. J Neuro Sci Res 80(6):877-86.</ref>' '<ref>Dong L-M and K. H. Weisgraber. 1996. Human apolipoprotein E4 domain interaction. Arginine 61 and glutamic acid 255 interact to direct the preference for very low density | ||
lipoproteins. J. Biol. Chem.271:19053–19057.</ref>'. This region is protease sensitive '<ref>Freiden, Carl and K. Garai. 2012. Structural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer’s disease. PNAS 109(23):8913-8919.</ref>'. | lipoproteins. J. Biol. Chem.271:19053–19057.</ref>'. This region is protease sensitive '<ref>Freiden, Carl and K. Garai. 2012. Structural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer’s disease. PNAS 109(23):8913-8919.</ref>'. | ||
[[Image:ApoE_Sandbox_Reserved_595.jpg]] | [[Image:ApoE_Sandbox_Reserved_595.jpg]] | ||
