He has also apparently collaborated on papers of great interest to this forum, especially in light of his work on Morgellons disease as an internet meme. He's got tremendous testicular fortitude considering the key words that appear throughout his work such as:
FILAMENT, 3D CRYSTALS OF RECOMBINANT BOVINE, BACILLUS SUBTILIS, ASSEMBLY, FOLDING,
DICTYOSTELIUM DISCODEM, BACTERIOPHAGES
among others that ring bells for me. What a sack of excrement... So caustic in his assesment of those under the influence of the internet in his scholarly opinion. His work is proudly displayed here if you can stomach more:
www.ncbi.nlm.nih.gov/pubmed www.ncbi.nlm.nih.gov/pubmed/20869367Abstract from paper entitled
Actin filament bundling and different nucleating effects of mouse Diaphanous-related formin FH2 domains on actin/ADF and actin/cofilin complexes
Mouse Diaphanous-related formins (mDias) are members of the formin protein family that nucleate actin polymerization and subsequently promote filamentous actin (F-actin) elongation by monomer addition to fast-growing barbed ends. It has been suggested that mDias preferentially recruit actin complexed to profilin due to their proline-rich FH1 domains. During filament elongation, dimeric mDias remain attached to the barbed ends by their FH2 domains, which form an anti-parallel ring-like structure enclosing the filament barbed ends
Almost sounds like the ring of the lesion....
www.ncbi.nlm.nih.gov/pubmed/16774641From above:
We have obtained 3D crystals of recombinant bovine AQP0 that diffract to 7.0 A resolution.
From the Abstract of paper entitled
Immortality. by Lustig A.
...seeks to anchor its discussion in shared moral and metaphysical concerns--the nature of human nature, and the social and political implications of unfettered choices in altering the human prospect through biotechnology.
www.ncbi.nlm.nih.gov/pubmed/15165232From Abstract of paper above entitled
Oligomeric structure of the Bacillus subtilis cell division protein DivIVA determined by transmission electron microscopy
...These DivIVA oligomers serve as building blocks in the formation of higher order assemblies giving rise to strings, wires and, finally, two-dimensional lattices in a time-dependent manner.
www.ncbi.nlm.nih.gov/pubmed/11243787From Abstract of above paper entitled
Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments.
...Filament formation proceeds via a specific multi-step association of the dimers into the unit-length filaments, which subsequently anneal longitudinally and finally radially compact into mature filaments.
From the Abstract of the paper entitled
The intermediate filament protein consensus motif of helix 2B: its atomic structure and contribution to assembly.
It is surprising that in buffers of low ionic strength and high pH where the full-length proteins form tetramers, both VimIAT and DesIAT associated into various high molecular weight complexes. After initiation of assembly, both VimIAT and DesIAT aggregated into unit-length-type filaments, which rapidly longitudinally annealed to yield filaments of around 20 nm in diameter. Mass measurements by scanning transmission electron microscopy revealed that both VimIAT and DesIAT filaments contained considerably more subunits per cross-section than standard intermediate filaments.
From the Abstract of the paper entitled
An autonomous folding unit mediates the assembly of two-stranded coiled coils.
...Here we report a 13-residue sequence pattern that occurs with limited sequence variations in many two-stranded coiled coils and that is absolutely required for the assembly of the Dictyostelium discoideum actin-bundling protein cortexillin I and the yeast transcriptional activator GCN4
Another paper of note-
www.ncbi.nlm.nih.gov/pubmed/8867326Mechanism of the long tail-fiber deployment of bacteriophages T-even and its role in adsorption, infection and sedimentation