A high-throughput technique to characterize the substrate specificities of tyrosine kinases identifies the key features of kinases and substrates that enforce accurate signaling from T cell receptors.

A high-throughput comparison of substrate specificities of the Src-family kinases Lck and c-Src against a library of proteome-derived phosphorylation sites reveals that Lck has evolved divergent electrostatic features reflecting its involvement in T-cell signaling.

Direct control of ligand binding half-life with light shows that lifetime strongly affects T cell signaling.

Structural and functional approaches unambiguously revealed physiologically relevant lateral interactions between FtsZ protofilaments.

KHNYN, a putative endoribonuclease, interacts with the zinc-finger antiviral protein (ZAP) and is required for the inhibition of HIV replication and RNA abundance by CpG dinucleotides.

The membrane nonlinearities of the dendritic arbor of striatal cholinergic interneurons conspire with the spatial distribution of its excitatory inputs to preferentially boost thalamic inputs.

A systematic and quantitative investigation showing how highly specific WW domain-mediated protein-protein interaction network is organized in cell growth and polarity.

Evolution-guided structure-function analyses reveal that CD4 transmembrane and intracellular juxtamembrane motifs play a more profound role in initiating pMHCII-specific TCR-CD3 signaling than previously characterized CD4-Lck interactions.

The T cell response, especially to weak agonists, is enhanced by acute Csk inhibition.

A single point mutation in a Ras activator leads to aberrant constitutive mTOR signaling in peripheral T cells that consequently accumulate as abnormal T helper cells and stimulate the production of autoantibodies by B cells.