A5066589887- Amyotrophic Lateral Sclerosis Research
- Neurogenetic and Muscular Disorders Research
- Alzheimer's disease research and treatments
- Parkinson's Disease Mechanisms and Treatments
- Cancer-related gene regulation
- Calpain Protease Function and Regulation
- RNA Research and Splicing
- Connexins and lens biology
- Histone Deacetylase Inhibitors Research
- Autophagy in Disease and Therapy
- Venomous Animal Envenomation and Studies
- Prion Diseases and Protein Misfolding
- Bacterial Genetics and Biotechnology
- Molecular Biology Techniques and Applications
- MicroRNA in disease regulation
- Insect and Arachnid Ecology and Behavior
- Neurological diseases and metabolism
- RNA and protein synthesis mechanisms
- Bacteriophages and microbial interactions
- Peptidase Inhibition and Analysis
- Cerebrovascular and genetic disorders
- Plant and Fungal Interactions Research
- GDF15 and Related Biomarkers
- Ion channel regulation and function
- Fossil Insects in Amber
University of Kentucky
2012-2024
University of Louisville
2017
University of Science and Technology of China
2017
Physical Sciences (United States)
2017
Hefei National Center for Physical Sciences at Nanoscale
2017
Lexington VA Health Care System
2017
Cellular Research (United States)
2009-2010
Constructor University
2006
National Institutes of Health
2002-2004
Hungarian Academy of Sciences
2000-2004
The p62/sequestosome 1 protein has been identified as a component of pathological inclusions in neurodegenerative diseases including amyotrophic lateral sclerosis (ALS). P62 also implicated autophagy, process mass degradation intracellular proteins and organelles. Autophagy is critical pathway for degrading misfolded and/or damaged proteins, the copper-zinc superoxide dismutase (SOD1) mutants linked to familial ALS. We previously reported that p62 interacted with ALS SOD1...
Amyotrophic lateral sclerosis (ALS) is a progressive neurode-generative disease characterized by motor neuron death. A hallmark of the appearance protein aggregates in affected neurons. We have found that p62, implicated aggregate formation, accumulated progressively G93A mouse spinal cord. The accumulation p62 was parallel to increase polyubiquitinated proteins and mutant SOD1 aggregates. Immunostaining studies showed ubiquitin, co-localized cells selectively interacted with familial ALS...
Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease. Fused in sarcoma (FUS) DNA/RNA binding protein and mutations FUS cause subset of familial ALS. Most ALS are clustered the C-terminal nuclear localization sequence consequently lead to accumulation inclusions cytoplasm. It remains debatable whether loss normal function nucleus or gain toxic cytoplasm plays more critical role etiology. Moreover, physiological be fully understood. In this study, we found that...
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease. Mutations in Cu/Zn superoxide dismutase (SOD1) are responsible for approximately 20 % of the familial ALS cases. ALS-causing SOD1 mutants display gain-of-toxicity phenotype, but nature this toxicity still not fully understood. The Ras GTPase-activating protein-binding protein G3BP1 plays critical role stress granule dynamics. Alterations dynamics granules have been reported several other forms unrelated to SOD1. To our...
To identify essential host genes affecting replication of Tomato bushy stunt virus (TBSV), a small model plant virus, we screened 800 yeast present in the Tet promoters Hughes Collection. In total, have identified 30 new whose down-regulation either increased or decreased accumulation TBSV replicon RNA. The are involved RNA transcription/metabolism, protein metabolism/transport, other cellular processes. Detailed analysis effects some revealed that they might affect by altering (i)...
MicroRNAs (miRNAs) are a novel class of small noncoding RNAs that regulate gene expression at the post-transcriptional level and play critical role in many important biological processes. Most miRNAs conserved between humans mice, which makes it possible to analyze their expressions with set selected array probes. Here, we report simple platform can detect 553 nonredundant encompassing entire for mice. The features carefully designed probes optimized hybridization parameters. Potential...
Abstract Backgound Amyotrophic lateral sclerosis (ALS) is progressive neurodegenerative disease characterized by the loss of motor function. Several ALS genes have been identified as their mutations can lead to familial ALS, including recently reported RNA-binding protein fused in sarcoma (Fus). However, it not clear how Fus neuron degeneration ALS. In this study, we present a Drosophila model examine toxicity Fus, its orthologue Cabeza (Caz), and ALS-related mutants. Results Our results...
Stress granules (SGs) are ribonucleoprotein aggregates that form in response to stress conditions. The regulation of SG dynamics is not fully understood. Permanent pathological SG-like structures were reported neurodegenerative diseases such as amyotrophic lateral sclerosis. Ras GTPase-activating protein-binding protein G3BP1 a central regulator dynamics. We found the lysine 376 residue (K376) G3BP1, which RRM RNA binding domain, was acetylated. Consequently, impaired by K376 acetylation. In...
We use a heterodimerizing leucine zipper system to examine the contribution of interhelical a−a' interaction dimer stability for six amino acids (A, V, L, I, K, and N). Circular dichroism (CD) spectroscopy monitored thermal denaturation 36 heterodimers that generate homotypic 30 heterotypic interactions. Isoleucine (I−I) is most stable interaction, being 9.2 kcal/mol per more than A−A 4.0 either L−L or V−V 7.0 N−N interaction. Only lysine was less alanine. An alanine-based double-mutant...
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease characterized by the preferential death of motor neurons. Approximately 10% ALS cases are familial and 90% sporadic. Fused in sarcoma (FUS) ubiquitously expressed RNA-binding protein implicated frontotemporal dementia (FTD). The physiological function pathological mechanism FUS not well understood, particularly whether post-translational modifications play role regulating function. In this study, we discovered that was...
An important consequence of protein misfolding related to neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), is the formation proteinaceous inclusions or aggregates within central nervous system. We have previously shown that several familial ALS-linked copper-zinc superoxide dismutase (SOD1) mutants (A4V, G85R, and G93A) interact co-localize with dynein-dynactin complex in cultured cells affected tissues ALS mice. In this study, we report interaction between mutant...
// Ke Jiang 1, * , Min Liu Guibin Lin 2 Beibei Mao 3 Wei Cheng 1 Han Jozsef Gal 4 Haining Zhu Zengqiang Yuan Wuguo Deng Quentin Peng Gong Xiaolin Bi Songshu Meng Institute of Cancer Stem Cell, Dalian Medical University Center, Dalian, China Department Hepatobiliary Surgery, The First Affiliated Hospital University, State Key Laboratory Brain and Cognitive Sciences, Biophysics, Chinese Academy Beijing, Molecular Cellular Biochemistry, College Medicine, Kentucky, Lexington, USA These authors...
ABSTRACT The metD d -methionine transporter locus of Escherichia coli was identified as the abc - yaeE-yaeC cluster (now renamed metNIQ genes). open reading frame is preceded by tandem MET boxes bracketed −10 and −35 a promoter. expression driven this promoter controlled MetJ repressor level methionine.
Mutations in Fused sarcoma (FUS) gene cause a subset of familial amyotrophic lateral sclerosis (ALS), fatal motor neuron degenerative disease. Wild-type FUS is largely localized the nucleus, but mutant accumulates cytoplasm and forms inclusions. It unclear whether depletion from nucleus or inclusions triggers degeneration. In this study, we revealed that nuclear cytoplasmic proteins form distinct local distribution patterns. The oligomers appears granular under confocal microscope. contrast,...