R Andrew Byrd
Affiliations: | Laboratory of Structural Biology | National Cancer Institute - Frederick |
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Collaborators
Sign in to add collaboratorDonald P Bottaro | collaborator | 1994-2016 | National Cancer Institute - Frederick |
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Publications
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Chao FA, Khago D, Byrd RA. (2020) Achieving pure spin effects by artifact suppression in methyl adiabatic relaxation experiments. Journal of Biomolecular Nmr |
Li J, Zhang Y, Soubias O, et al. (2020) Optimization of sortase A ligation for flexible engineering of complex protein systems. The Journal of Biological Chemistry |
Roy NS, Jian X, Soubias O, et al. (2019) Interaction of the N terminus of ADP-ribosylation factor with the PH domain of the GTPase-activating protein ASAP1 requires phosphatidylinositol 4,5-bisphosphate. The Journal of Biological Chemistry |
Li Y, Soubias O, Li J, et al. (2019) Functional expression and characterization of human myristoylated-Arf1 in nanodisc membrane mimetics. Biochemistry |
Chakrabarti KS, Li J, Das R, et al. (2017) Conformational Dynamics and Allostery in E2:E3 Interactions Drive Ubiquitination: gp78 and Ube2g2. Structure (London, England : 1993) |
Chao FA, Byrd RA. (2017) Application of geometric approximation to the CPMG experiment: Two- and three-site exchange. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 277: 8-14 |
Gill ML, Byrd RA, Palmer Iii AG. (2015) Dynamics of GCN4 facilitate DNA interaction: a model-free analysis of an intrinsically disordered region. Physical Chemistry Chemical Physics : Pccp |
Jian X, Tang WK, Zhai P, et al. (2015) Molecular Basis for Cooperative Binding of Anionic Phospholipids to the PH Domain of the Arf GAP ASAP1. Structure (London, England : 1993) |
Das R, Liang YH, Mariano J, et al. (2013) Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine. The Embo Journal. 32: 2504-16 |
Metzger MB, Liang YH, Das R, et al. (2013) A structurally unique E2-binding domain activates ubiquitination by the ERAD E2, Ubc7p, through multiple mechanisms. Molecular Cell. 50: 516-27 |