Tracy Haldiman
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View article: Structural exposure of different microtubule binding domains determines the propagation and toxicity of pathogenic tau conformers in Alzheimer’s disease
Structural exposure of different microtubule binding domains determines the propagation and toxicity of pathogenic tau conformers in Alzheimer’s disease Open
Deposits of misfolded tau proteins are leading indicators of cognitive decline in Alzheimer’s disease (AD), and our recent data implicate distinctly misfolded conformers of the tau protein with high seeding potency in rapid progression. We…
View article: Propagation of distinct tau strains in neuronal systems with physiological tau expression
Propagation of distinct tau strains in neuronal systems with physiological tau expression Open
Background Pathological tau forms from Alzheimer’s disease (AD) brains act as seeds, replicating in cells and forming tau aggregates in a template‐like manner. The exploration of this prion‐like pathogenic mechanism has predominantly occur…
View article: Detection of prions in matching post-mortem skin and cerebrospinal fluid samples using second-generation real-time quaking-induced conversion assay
Detection of prions in matching post-mortem skin and cerebrospinal fluid samples using second-generation real-time quaking-induced conversion assay Open
View article: Evolving prion-like tau conformers differentially alter postsynaptic proteins in neurons inoculated with distinct isolates of Alzheimer’s disease tau
Evolving prion-like tau conformers differentially alter postsynaptic proteins in neurons inoculated with distinct isolates of Alzheimer’s disease tau Open
View article: Distinct populations of highly potent TAU seed conformers in rapidly progressing Alzheimer’s disease
Distinct populations of highly potent TAU seed conformers in rapidly progressing Alzheimer’s disease Open
Rapid replication in vitro implicates distinct populations of misfolded hippocampal 4R TAU protein in accelerated progression of Alzheimer’s disease.
View article: Distinct conformers of amyloid beta accumulate in the neocortex of patients with rapidly progressive Alzheimer's disease
Distinct conformers of amyloid beta accumulate in the neocortex of patients with rapidly progressive Alzheimer's disease Open
View article: Structurally distinct external solvent-exposed domains drive replication of major human prions
Structurally distinct external solvent-exposed domains drive replication of major human prions Open
There is a limited understanding of structural attributes that encode the iatrogenic transmissibility and various phenotypes of prions causing the most common human prion disease, sporadic Creutzfeldt-Jakob disease (sCJD). Here we report t…
View article: Correction to: Diverse, evolving conformer populations drive distinct phenotypes in frontotemporal lobar degeneration caused by the same MAPT‑P301L mutation
Correction to: Diverse, evolving conformer populations drive distinct phenotypes in frontotemporal lobar degeneration caused by the same MAPT‑P301L mutation Open
View article: Diverse, evolving conformer populations drive distinct phenotypes in frontotemporal lobar degeneration caused by the same MAPT-P301L mutation
Diverse, evolving conformer populations drive distinct phenotypes in frontotemporal lobar degeneration caused by the same MAPT-P301L mutation Open
Tau protein accumulation is a common denominator of major dementias, but this process is inhomogeneous, even when triggered by the same germline mutation. We considered stochastic misfolding of human tau conformers followed by templated co…
View article: Chronic wasting disease (CWD) prion strains evolve via adaptive diversification of conformers in hosts expressing prion protein polymorphisms
Chronic wasting disease (CWD) prion strains evolve via adaptive diversification of conformers in hosts expressing prion protein polymorphisms Open
View article: Artificial strain of human prions created in vitro
Artificial strain of human prions created in vitro Open
The molecular mechanism that determines under physiological conditions transmissibility of the most common human prion disease, sporadic Creutzfeldt-Jakob disease (sCJD) is unknown. We report the synthesis of new human prion from the recom…
View article: Proteomic differences in amyloid plaques in rapidly progressive and sporadic Alzheimer’s disease
Proteomic differences in amyloid plaques in rapidly progressive and sporadic Alzheimer’s disease Open
View article: O5‐04‐02: Altered Protein Expression in Amyloid Plaques in Rapidly Progressive Alzheimer's Disease
O5‐04‐02: Altered Protein Expression in Amyloid Plaques in Rapidly Progressive Alzheimer's Disease Open
Rapidly progressive Alzheimer's disease (rpAD) is a particularly aggressive form of Alzheimer's disease (AD). Survival is limited to 2-3 years after diagnosis. It is not yet known why AD develops so rapidly in these patients and previous r…
View article: Histidine H/D exchange for monomeric PrP<sup>C</sup> (black), MM1 rPrP<sup>Sc</sup> (red) and MM2 rPrP<sup>Sc</sup> (blue).
Histidine H/D exchange for monomeric PrP<sup>C</sup> (black), MM1 rPrP<sup>Sc</sup> (red) and MM2 rPrP<sup>Sc</sup> (blue). Open
The parameter t1/2 represents the half-time of exchange reaction for individual His residues. Error bars indicate standard deviation (3 independent experiments). **, P<0.01; ***, P<0.001.
View article: Sedimentation velocity, conformational stability, and seeding potency of isolated sCJD prions.
Sedimentation velocity, conformational stability, and seeding potency of isolated sCJD prions. Open
(a) Distinct sedimentation velocity profiles of MM1 and MM2 prions. The samples were fractionated by ultracentrifugation in sucrose gradient and fractions were collected from the bottom of the tubes and analyzed for rPrPSc by CD…
View article: Deuterium incorporation for peptic fragments derived from MM1 rPrP<sup>Sc</sup> (red) and MM2 rPrP<sup>Sc</sup>(blue).
Deuterium incorporation for peptic fragments derived from MM1 rPrP<sup>Sc</sup> (red) and MM2 rPrP<sup>Sc</sup>(blue). Open
(a) 5 min incubation in D2O. (b) 240 h incubation in D2O. Error bars indicate standard deviation (3 independent experiments). *, P<0.05; **, P<0.02.
View article: Schematic representation of PK-resistant fragments in rPrP<sup>Sc</sup> corresponding to Type 1 (MM1) and Type 2 (MM2) sCJD prions and molecular characteristics of purified human rPrPSc used in structural studies.
Schematic representation of PK-resistant fragments in rPrP<sup>Sc</sup> corresponding to Type 1 (MM1) and Type 2 (MM2) sCJD prions and molecular characteristics of purified human rPrPSc used in structural studies. Open
(a) Outline of classification of Type 1 and Type 2 human prions based on proteolytic fragmentation of PrPSc [5,52]. Major cleavage sites by PK are indicated by arrows; GLP—glycolipid; CHO- complex N-glycosylation chains. The cod…
View article: Source, biophysical characteristics, and replication rate of Type 1 and Type 2 sCJD prions.
Source, biophysical characteristics, and replication rate of Type 1 and Type 2 sCJD prions. Open
Source, biophysical characteristics, and replication rate of Type 1 and Type 2 sCJD prions.
View article: Prion Infectivity Plateaus and Conversion to Symptomatic Disease Originate from Falling Precursor Levels and Increased Levels of Oligomeric PrP <sup>Sc</sup> Species
Prion Infectivity Plateaus and Conversion to Symptomatic Disease Originate from Falling Precursor Levels and Increased Levels of Oligomeric PrP <sup>Sc</sup> Species Open
In lethal prion neurodegenerative diseases, misfolded prion proteins (PrP Sc ) replicate by redirecting the folding of the cellular prion glycoprotein (PrP C ). Infections of different durations can have a subclinical phase with constant l…
View article: Structural Determinants of Phenotypic Diversity and Replication Rate of Human Prions
Structural Determinants of Phenotypic Diversity and Replication Rate of Human Prions Open
The infectious pathogen responsible for prion diseases is the misfolded, aggregated form of the prion protein, PrPSc. In contrast to recent progress in studies of laboratory rodent-adapted prions, current understanding of the molecular bas…
View article: Rapidly progressive Alzheimer’s disease features distinct structures of amyloid-β
Rapidly progressive Alzheimer’s disease features distinct structures of amyloid-β Open
Genetic and environmental factors that increase the risk of late-onset Alzheimer disease are now well recognized but the cause of variable progression rates and phenotypes of sporadic Alzheimer's disease is largely unknown. We aimed to inv…