Avijit Chakrabartty

Oxidation-induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis.

The PrP-like protein Doppel binds copper.

Alternate aggregation pathways of the Alzheimer beta-amyloid peptide: Abeta association kinetics at endosomal pH.

Lipopeptide detergents designed for the structural study of membrane proteins.

Co-incorporation of A beta 40 and A beta 42 to form mixed pre-fibrillar aggregates.

Autoinhibition of the kit receptor tyrosine kinase by the cytosolic juxtamembrane region.

Conformational coupling of Mg2+ and Ca2+ on the three-state folding of calexcitin B.

Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis.

Interactions of Alzheimer amyloid peptides with cultured cells and brain tissue, and their biological consequences.

Identification of stable helical bundles from a combinatorial library of amphipathic peptides.

Alzheimer's Abeta40 studied by NMR at low pH reveals that sodium 4,4-dimethyl-4-silapentane-1-sulfonate (DSS) binds and promotes beta-ball oligomerization.

Interaction of human and mouse Abeta peptides.

Reversible assembly of helical filaments by de novo designed minimalist peptides.

Hyperactive antifreeze protein from winter flounder is a very long rod-like dimer of alpha-helices.

Charge substitution shows that repulsive electrostatic interactions impede the oligomerization of Alzheimer amyloid peptides.

NMR-driven secondary and tertiary structure model of Ca2+-loaded calexcitin.

Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis.

Variants of DsRed fluorescent protein: Development of a copper sensor.

Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding.

An immunological epitope selective for pathological monomer-misfolded SOD1 in ALS.

Getting specificity from simplicity in putative proteins from the prebiotic earth.

Metal ion-dependent, reversible, protein filament formation by designed beta-roll polypeptides.

Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants.

Denaturational stress induces formation of zinc-deficient monomers of Cu,Zn superoxide dismutase: implications for pathogenesis in amyotrophic lateral sclerosis.

Two distinct conformations of Abeta aggregates on the surface of living PC12 cells.

Probing Alzheimer amyloid peptide aggregation using a cell-free fluorescent protein refolding method.

Conversion of Abeta42 into a folded soluble native-like protein using a semi-random library of amphipathic helices.

Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form.

Putative one-pot prebiotic polypeptides with ribonucleolytic activity.

Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP.

Cell surface binding and internalization of aβ modulated by degree of aggregation.

Multiphoton ANS fluorescence microscopy as an in vivo sensor for protein misfolding stress.

ALS-causing SOD1 mutations promote production of copper-deficient misfolded species.

CCM3/PDCD10 heterodimerizes with germinal center kinase III (GCKIII) proteins using a mechanism analogous to CCM3 homodimerization.

Aβ behavior on neuronal membranes: aggregation and toxicities.

Relative and regional stabilities of the hamster, mouse, rabbit, and bovine prion proteins toward urea unfolding assessed by nuclear magnetic resonance and circular dichroism spectroscopies.

Conformation specificity and arene binding in a peptide composed only of Lys, Ile, Ala and Gly.

Analyzing complicated protein folding kinetics rapidly by analytical Laplace inversion using a Tikhonov regularization variant.

Early steps in oxidation-induced SOD1 misfolding: implications for non-amyloid protein aggregation in familial ALS.

Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase.

Targeting of monomer/misfolded SOD1 as a therapeutic strategy for amyotrophic lateral sclerosis.

An Arg-rich putative prebiotic protein is as stable as its Lys-rich variant.

Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis.

N-terminal helix-cap in α-helix 2 modulates β-state misfolding in rabbit and hamster prion proteins.

Structure of a simplified β-hairpin and its ATP complex.

Wild-type Cu/Zn superoxide dismutase stabilizes mutant variants by heterodimerization.

"Structural characterization of the minimal segment of TDP-43 competent for aggregation".

Low molecular weight species of TDP-43 generated by abnormal splicing form inclusions in amyotrophic lateral sclerosis and result in motor neuron death.

Determining composition of micron-scale protein deposits in neurodegenerative disease by spatially targeted optical microproteomics.

Electrostatic Repulsion Governs TDP-43 C-terminal Domain Aggregation.

Substoichiometric inhibition of transthyretin misfolding by immune-targeting sparsely populated misfolding intermediates: a potential diagnostic and therapeutic for TTR amyloidoses.

Corrigendum: Substoichiometric inhibition of transthyretin misfolding by immune-targeting sparsely populated misfolding intermediates: a potential diagnostic and therapeutic for TTR amyloidoses.

Phase to Phase with TDP-43.

Transthyretin amyloidosis: an under-recognized neuropathy and cardiomyopathy.

Quercitrin and quercetin 3-β-d-glucoside as chemical chaperones for the A4V SOD1 ALS-causing mutant.