A new phase of networking: the molecular composition and regulatory dynamics of mammalian stress granules

SR Millar, JQ Huang, KJ Schreiber, YC Tsai… - Chemical …, 2023 - ACS Publications
Stress granules (SGs) are cytosolic biomolecular condensates that form in response to
cellular stress. Weak, multivalent interactions between their protein and RNA constituents …

[HTML][HTML] Disrupting pathologic phase transitions in neurodegeneration

BT Hurtle, L Xie, CJ Donnelly - The Journal of clinical …, 2023 - Am Soc Clin Investig
Solid-like protein deposits found in aged and diseased human brains have revealed a
relationship between insoluble protein accumulations and the resulting deficits in neurologic …

Monomerization of TDP-43 is a key determinant for inducing TDP-43 pathology in amyotrophic lateral sclerosis

K Oiwa, S Watanabe, K Onodera, Y Iguchi… - Science …, 2023 - science.org
The cytoplasmic aggregation of TAR DNA binding protein-43 (TDP-43), also known as TDP-
43 pathology, is the pathological hallmark of amyotrophic lateral sclerosis (ALS). However …

[HTML][HTML] Nucleocytoplasmic mRNA redistribution accompanies RNA binding protein mislocalization in ALS motor neurons and is restored by VCP ATPase inhibition

OJ Ziff, J Harley, Y Wang, J Neeves, G Tyzack… - Neuron, 2023 - cell.com
Amyotrophic lateral sclerosis (ALS) is characterized by nucleocytoplasmic mislocalization of
the RNA-binding protein (RBP) TDP-43. However, emerging evidence suggests more …

Loss of TDP‐43 oligomerization or RNA binding elicits distinct aggregation patterns

M Pérez‐Berlanga, VI Wiersma, A Zbinden… - The EMBO …, 2023 - embopress.org
Aggregation of the RNA‐binding protein TAR DNA‐binding protein 43 (TDP‐43) is the key
neuropathological feature of neurodegenerative diseases, including amyotrophic lateral …

Limbic-predominant age-related TDP43 encephalopathy (LATE) neuropathological change in neurodegenerative diseases

S Nag, JA Schneider - Nature Reviews Neurology, 2023 - nature.com
Abstracts TAR DNA-binding protein 43 (TDP43) is a focus of research in late-onset
dementias. TDP43 pathology in the brain was initially identified in amyotrophic lateral …

SYF2 suppression mitigates neurodegeneration in models of diverse forms of ALS

GR Linares, Y Li, WH Chang, J Rubin-Sigler… - Cell Stem Cell, 2023 - cell.com
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease caused by many
diverse genetic etiologies. Although therapeutics that specifically target causal mutations …

[HTML][HTML] Metamorphism in TDP-43 prion-like domain determines chaperone recognition

J Carrasco, R Antón, A Valbuena… - Nature …, 2023 - nature.com
The RNA binding protein TDP-43 forms cytoplasmic inclusions via its C-terminal prion-like
domain in several neurodegenerative diseases. Aberrant TDP-43 aggregation arises upon …

FAM69C functions as a kinase for eIF2α and promotes stress granule assembly

Z Wu, F Mei, Y Gan, A Liu, J Hu, Y Jin, Y Yin - EMBO reports, 2023 - embopress.org
Stress granules are dynamic cytoplasmic ribonucleoprotein granules that assemble in
response to cellular stress. Aberrant formation of stress granules has been linked to …

[HTML][HTML] Immunotherapy targeting the C-terminal domain of TDP-43 decreases neuropathology and confers neuroprotection in mouse models of ALS/FTD

T Afroz, E Chevalier, M Audrain, C Dumayne… - Neurobiology of …, 2023 - Elsevier
Effective therapies are urgently needed to safely target TDP-43 pathology as it is closely
associated with the onset and development of devastating diseases such as frontotemporal …