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Molecular Cell|July 12, 2024
Chaperones in concert: Orchestrating co-translational protein folding in the cellBob Schiffrin, Antonio N CalabreseBMC Biology|December 23, 2017
Outer membrane protein folding from an energy landscape perspectiveBob Schiffrin, David J Brockwell, Sheena E RadfordProtein Science : a Publication of the Protein Society|June 20, 2020
PyXlinkViewer: A flexible tool for visualization of protein chemical crosslinking data within the PyMOL molecular graphics systemBob Schiffrin, Sheena E Radford, David J Brockwell, et al.ACS Nano|August 19, 2015
Rapid and Robust Polyprotein Production Facilitates Single-Molecule Mechanical Characterization of β-Barrel Assembly Machinery Polypeptide Transport Associated DomainsToni Hoffmann, Katarzyna M Tych, Thomas Crosskey, et al.Communications Biology|June 8, 2022
Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein foldingBob Schiffrin, Jonathan M Machin, Theodoros K Karamanos, et al.Journal of Molecular Biology|February 5, 2019
The Role of SurA PPIase Domains in Preventing Aggregation of the Outer-Membrane Proteins tOmpA and OmpTJulia R Humes, Bob Schiffrin, Antonio N Calabrese, et al.Nature Structural & Molecular Biology|July 26, 2016
Skp is a multivalent chaperone of outer-membrane proteinsBob Schiffrin, Antonio N Calabrese, Paul W A Devine, et al.Nature Communications|October 1, 2016
Lateral opening in the intact β-barrel assembly machinery captured by cryo-EMMatthew G Iadanza, Anna J Higgins, Bob Schiffrin, et al.Journal of Molecular Biology|September 19, 2017
Effects of Periplasmic Chaperones and Membrane Thickness on BamA-Catalyzed Outer-Membrane Protein FoldingBob Schiffrin, Antonio N Calabrese, Anna J Higgins, et al.Analytical Chemistry|May 25, 2026
Nanopipettes Enable Native Mass Spectrometry Studies of the Intrinsically Disordered Protein α-Synuclein in Biochemical BuffersEmily J Byrd, Emma L Norgate, Joel A Crossley, et al.Pageof 2