Ligands that bind dimers of light chain variable domains inhibit the formation of amyloid fibrils.

The structure of a human antibody in which the variable loops position a human protein LAIR1 for antigen recognition, reveals a novel and indirect mode of antibody function.

Identifying the patient-specific mutation that shifted the antibody light chain to the deadly fibrillar species provides new insight in the molecular pathogenesis of AL amyloidosis.

Computational modeling and in vitro experiments identify a unique conformational state in amyloidogenic light chains, providing a structural basis for amyloidosis and a precise target for drug design.

An anti-influenza receptor binding site antibody acquires breadth through hierarchical sets of epistatic mutations distributed across the light and heavy chains, demonstrating how mutations can interact to shape the evolution of antibody breadth in various antigen exposure regimens.

Using different sets of input sequences to evolutionary reconstruction algorithms results in the exploration of many possible models, the intergration over which produces significantly more accurate models.

The axonal cytoskeletal contains an actomyosin-II network that controls circumferential axonal contraction and expansion with the potential of regulating fluctuations in diameter during action potential firing, trafficking, and degeneration.

Conformational changes occur within extracellular domain of BCR upon antigen engagement, and these conformational changes are related with the strength of BCR activation and are distinct in IgM- and IgG-BCR.

A commonly used immunoglobulin loci-transgenic mouse, the Kymouse, has B cells that go through complete development and have receptor repertoires that show key differences in encoding gene frequencies but structural similarity in their most variable regions.

The first atomic resolution structure of a mitochondrial respiratory complex from plants provides insight into the assembly and evolution of respiration in autotrophic eukaryotes.