Publications
D
Conformational Chaperones for Structural Studies of Membrane Proteins Using Antibody Phage Display with Nanodiscs.,
Dominik, Pawel K., Borowska Marta T., Dalmas Olivier, Kim Sangwoo S., Perozo Eduardo, Keenan Robert J., and Kossiakoff Anthony A.
, Structure, 2016 Feb 02, Volume 24, Issue 2, p.300-9, (2016)
B
Locking the Elbow: Improved Antibody Fab Fragments as Chaperones for Structure Determination.,
Bailey, Lucas J., Sheehy Kimberly M., Dominik Pawel K., Liang Wenguang G., Rui Huan, Clark Michael, Jaskolowski Mateusz, Kim Yejoon, Deneka Dawid, Tang Wei-Jen, et al.
, J Mol Biol, 2018 02 02, Volume 430, Issue 3, p.337-347, (2018)
Publications
- Characterization of synthetic antigen binding fragments targeting Toc75 for the isolation of TOC in A. thaliana and P. sativum.
- Development of a universal nanobody-binding Fab module for fiducial-assisted cryo-EM studies of membrane proteins.
- Development, structure, and mechanism of synthetic antibodies that target claudin and Clostridium perfringens enterotoxin complexes.
- Engineering of a synthetic antibody fragment for structural and functional studies of K+ channels.
- Isoform- and ligand-specific modulation of the adhesion GPCR ADGRL3/Latrophilin3 by a synthetic binder.
- Quaternary structure independent folding of voltage-gated ion channel pore domain subunits.
- Structural basis for assembly and lipid-mediated gating of LRRC8A:C volume-regulated anion channels.
- Structure of an AMPK complex in an inactive, ATP-bound state.
- Structure of human NTCP reveals the basis of recognition and sodium-driven transport of bile salts into the liver.
- Structure, sequon recognition and mechanism of tryptophan C-mannosyltransferase.
- Structures of ABCB4 provide insight into phosphatidylcholine translocation.
- Structures of atypical chemokine receptor 3 reveal the basis for its promiscuity and signaling bias.
- Synthetic Antibodies Detect Distinct Cellular States of Chromosome Passenger Complex Proteins.
- Targeting a proteolytic neoepitope on CUB domain containing protein 1 (CDCP1) for RAS-driven cancers.