User profiles for A. E. Posey
Ammon E. PoseyResearch Scientist, Washington University in St. Louis Verified email at wustl.edu Cited by 964 |
[HTML][HTML] A lethal de novo mutation in the middle domain of the dynamin-related GTPase Drp1 impairs higher order assembly and mitochondrial division
…, CM Manlandro, D Arnoult, J Stadler, AE Posey… - Journal of biological …, 2010 - ASBMB
Mitochondria dynamically fuse and divide within cells, and the proper balance of fusion and
fission is necessary for normal mitochondrial function, morphology, and distribution. Drp1 is …
fission is necessary for normal mitochondrial function, morphology, and distribution. Drp1 is …
Phase separation of intrinsically disordered proteins
There is growing interest in the topic of intracellular phase transitions that lead to the
formation of biologically regulated biomolecular condensates. These condensates are …
formation of biologically regulated biomolecular condensates. These condensates are …
[PDF][PDF] Arginine-enriched mixed-charge domains provide cohesion for nuclear speckle condensation
Low-complexity protein domains promote the formation of various biomolecular condensates.
However, in many cases, the precise sequence features governing condensate formation …
However, in many cases, the precise sequence features governing condensate formation …
Dilute phase oligomerization can oppose phase separation and modulate material properties of a ribonucleoprotein condensate
Ribonucleoprotein bodies are exemplars of membraneless biomolecular condensates that
can form via spontaneous or driven phase transitions. The fungal protein Whi3 forms …
can form via spontaneous or driven phase transitions. The fungal protein Whi3 forms …
[HTML][HTML] Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers
Huntingtin N-terminal fragments (Htt-NTFs) with expanded polyglutamine tracts form a range
of neurotoxic aggregates that are associated with Huntington's disease. Here, we show that …
of neurotoxic aggregates that are associated with Huntington's disease. Here, we show that …
Self-assembly of block heterochiral peptides into helical tapes
Patterned substitution of d-amino acids into the primary sequences of self-assembling
peptides influences molecular-level packing and supramolecular morphology. We report that …
peptides influences molecular-level packing and supramolecular morphology. We report that …
[HTML][HTML] Dynamical control enables the formation of demixed biomolecular condensates
Cellular matter can be organized into compositionally distinct biomolecular condensates.
For example, in Ashbya gossypii, the RNA-binding protein Whi3 forms distinct condensates …
For example, in Ashbya gossypii, the RNA-binding protein Whi3 forms distinct condensates …
Glycine-Rich Peptides from FUS Have an Intrinsic Ability to Self-Assemble into Fibers and Networked Fibrils: Published as part of the Biochemistry virtual special …
Glycine-rich regions feature prominently in intrinsically disordered regions (IDRs) of proteins
that drive phase separation and the regulated formation of membraneless biomolecular …
that drive phase separation and the regulated formation of membraneless biomolecular …
Inhibition of amyloid beta fibril formation by monomeric human transthyretin
Transthyretin (TTR) is a homotetrameric protein that is found in the plasma and cerebrospinal
fluid. Dissociation of TTR tetramers sets off a downhill cascade of amyloid formation …
fluid. Dissociation of TTR tetramers sets off a downhill cascade of amyloid formation …
[HTML][HTML] Quantifying coexistence concentrations in multi-component phase-separating systems using analytical HPLC
A Bremer, AE Posey, MB Borgia, WM Borcherds… - Biomolecules, 2022 - mdpi.com
Over the last decade, evidence has accumulated to suggest that numerous instances of cellular
compartmentalization can be explained by the phenomenon of phase separation. This is …
compartmentalization can be explained by the phenomenon of phase separation. This is …