• Publications
  • Influence
A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug-Repurposing
A human–SARS-CoV-2 protein interaction map highlights cellular processes that are hijacked by the virus and that can be targeted by existing drugs, including inhibitors of mRNA translation and predicted regulators of the sigma receptors. Expand
Structure of a glycerol-conducting channel and the basis for its selectivity.
The crystal structure of the Escherichia coli glycerol facilitator (GlpF) elucidates the mechanism of selective permeability for linear carbohydrates and suggests how ions and water are excluded. Expand
Mechanism of Ammonia Transport by Amt/MEP/Rh: Structure of AmtB at 1.35 Å
The first structure of an ammonia channel from the Amt/MEP/Rh protein superfamily, determined to 1.35 angstrom resolution, shows it to be a channel that spans the membrane 11 times and uses conserved histidines to conduct uncharged NH3. Expand
The signal recognition particle.
Advances in the structure determination of a number of key components in the eukaryotic and prokaryotic SRP pathway provide new insight into the molecular basis of SRP function, and they set the stage for future work toward an integrated picture that takes into account the dynamic and contextual properties of this remarkable cellular machine. Expand
The unfolded protein response signals through high-order assembly of Ire1
It is shown that oligomerization is central to Ire1 function and is an intrinsic attribute of its cytosolic domains in complex with a kinase inhibitor that acts as a potent activator of the Ire1 RNase. Expand
On the mechanism of sensing unfolded protein in the endoplasmic reticulum.
It is proposed that cLD directly binds unfolded proteins, which changes the quaternary association of the monomers in the membrane plane, whichChanges in the ER lumen in turn position Ire1 kinase domains in the cytoplasm optimally for autophosphorylation to initiate the UPR. Expand
Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: a model for viral DNA binding.
Two proteins that bind DNA in a sequence-independent manner are structurally homologous to the HIV-1 IN C-terminal domain, suggesting a similar protein-DNA interaction in which the In C-Terminal domain may serve to bind, bend, and orient viral DNA during integration. Expand
Control of the Selectivity of the Aquaporin Water Channel Family by Global Orientational Tuning
Aquaporins are transmembrane channels found in cell membranes of all life forms. We examine their apparently paradoxical property, facilitation of efficient permeation of water while excludingExpand
Crystal Structure of the Signal Sequence Binding Subunit of the Signal Recognition Particle
The crystal structure of the signal sequence binding subunit of the SRP from Thermus aquaticus reveals a deep groove bounded by a flexible loop and lined with side chains of conserved hydrophobic residues that is likely to contribute to the structural plasticity necessary for SRP to bind signal sequences of different lengths and amino acid sequence. Expand
Substrate twinning activates the signal recognition particle and its receptor
To define the mechanism of reciprocal activation, the 1.9 Å structure of the complex formed between these two GTPases was determined, and the two partners form a quasi-two-fold symmetrical heterodimer. Expand