B. Sankaran

ALS mutations disrupt self-association between the Ubiquilin Sti1 hydrophobic groove and internal placeholder sequences

This study presents the first crystal structure of the Ubiquilin Sti1 domain bound to a transmembrane domain, showing that ALS mutations disrupt their interaction and reveal internal placeholder sequences that regulate phase separation.

Improving protein expression, stability, and function with ProteinMPNN

This paper introduces ProteinMPNN, a deep learning model that improves protein expression, stability, and function by incorporating evolutionary and structural information.

Rapid and automated design of two-component protein nanomaterials using ProteinMPNN

This study benchmarks ProteinMPNN against Rosetta in designing two-component protein nanomaterials, showing comparable success with significantly reduced computation and no manual refinement.

Structure of Orthoreovirus RNA Chaperone σNS, a Component of Viral Replication Factories

This paper determines the structure of the reovirus σNS RNA chaperone and shows how its oligomeric state and N-terminal arm regulate RNA binding and chaperone activity.

Blueprinting expandable nanomaterials with standardized protein building blocks

This paper introduces standardized protein building blocks and geometric design principles to create expandable protein nanomaterials, validated through X-ray crystallography and electron microscopy.

Identification of potent and selective N-myristoyltransferase inhibitors of Plasmodium vivax liver stage hypnozoites and schizonts

Design of stimulus-responsive two-state hinge proteins

This paper designs two-state hinge proteins that switch between structural states in response to ligands, demonstrating atomic-level accuracy and tunable kinetics and thermodynamics.

Precisely patterned nanofibers made from extendable protein multiplexes

The paper designs extendable protein multiplexes with symmetric architectures to create precisely patterned nanofibers through controlled repeat propagation and hydrophilic patch placement.

Improving the secretion of designed protein assemblies through negative design of cryptic transmembrane domains

This study identifies cryptic transmembrane domains in designed protein nanoparticles that hinder secretion and introduces a computational tool, Degreaser, to remove them while maintaining stability, improving secretion efficiency.

Robust deep learning based protein sequence design using ProteinMPNN

A deep learning method for protein sequence design shows high performance in both simulations and experiments, applicable to various design challenges.

A Novel Y-Shaped, S-O-N-O-S-Bridged Crosslink between Three Residues C22, C44, and K61 Is a Redox Switch of the SARS-CoV-2 Main Protease

The paper identifies a novel Y-shaped crosslink in SARS-CoV-2 MPro that acts as a redox switch, regulating its catalytic activity and offering new targets for antiviral drug development.

An auto-inhibited state of protein kinase G and implications for selective activation

This study presents crystal structures of PKG Iβ in auto-inhibited and activated states, revealing the mechanism of cGMP-mediated activation and isoform-specific regulation.

The N-Terminal Carbamate is Key to High Cellular and Antiviral Potency for Boceprevir-Based SARS-CoV-2 Main Protease Inhibitors

This paper identifies that a P4 N-terminal carbamate in boceprevir-based inhibitors is crucial for high antiviral potency against SARS-CoV-2.

The P3 O-Tert-Butyl-Threonine is Key to High Cellular and Antiviral Potency for Aldehyde-Based SARS-CoV-2 Main Protease Inhibitors

This study identifies O-tert-butyl-threonine at the P3 site as critical for enhancing cellular and antiviral potency of MPro inhibitors.

A Speedy Route to Multiple Highly Potent SARS-CoV-2 Main Protease Inhibitors

This study designs and synthesizes potent SARS-CoV-2 main protease inhibitors, with some showing IC50 values below 100 nM and high virus inhibition potency in cell assays.

Minimally disruptive optical control of protein tyrosine phosphatase 1B

This study develops an optical method to control PTP1B activity and shows that small activity changes lead to large shifts in phosphorylation of its targets.