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aging TAR-DNA binding protein of 43 kDa Dementia Hippocampus Phosphorylation population study Age Factors Aged 80 and over aging Dementia Female Hippocampus Humans Inclusion Bodies Male Nerve Degeneration Neurofibrillary Tangles Neurons Phosphorylation TDP-43 Proteinopathies

Alpha-synucleinopathies are a group of progressive neurodegenerative disorders, characterized by intracellular deposits of aggregated α-synuclein (αS). The clinical heterogeneity of these diseases is thought to be attributed to...

Amyloid conformation inclusion Microglia Parkinson’s disease Prion-like Synuclein Animals Disease Models Animal Humans Inclusion Bodies Mice Mice Transgenic Microglia Neurons protein aggregation Pathological Protein Conformation Synucleinopathies ALPHA-SYNUCLEIN

An important function of the endoplasmic reticulum (ER) is to serve as a site of secretory protein folding. When the accumulation of misfolded proteins threatens to disturb luminal homoeostasis, the cell is said to experience ER...

ER overload ER stress Microviscosity ROVI α1-Antitrypsin Animals Biophysical Phenomena Endoplasmic Reticulum Humans Inclusion Bodies Polymerization Viscosity alpha 1-Antitrypsin

A subset of viral genes is required for the long-term latent infection of hematopoietic cells by human cytomegalovirus (HCMV). Here, we show that a latency-associated gene product (LUNA) promotes the disruption of cellular PML...

PML Cytomegalovirus deSUMOylase latency reactivation Amino Acid Sequence Antigens CD34 Carbon-Nitrogen Lyases Catalytic Domain Cytomegalovirus Dendritic Cells Humans Inclusion Bodies Mutation THP-1 Cells Viral Proteins Virus Activation Virus Latency

Difficult to express enzymes Escherichia coli Inclusion Bodies Recombinant industrial enzymes Solubility Systems Biology

Proteinaceous cytoplasmic inclusions are an indicator of dysfunction in normal cellular proteostasis and a hallmark of many neurodegenerative diseases. We describe a simple and rapid new flow cytometry-based method to enumerate...

Calibration Cell Line Cell Nucleus Flow Cytometry Humans Inclusion Bodies Neurodegenerative Diseases Protein Transport Proteins

The self-assembly of α-synuclein (αS) into intraneuronal inclusion bodies is a key characteristic of Parkinson's disease. To define the nature of the species giving rise to neuronal damage, we have investigated the mechanism of...

Amyloid Animals Calcium Cell Line Tumor Cells Cultured Humans Inclusion Bodies Kinetics Microscopy Confocal Neurons Parkinson Disease protein aggregation Pathological Protein Multimerization Rats Sprague-Dawley ALPHA-SYNUCLEIN

Protein aggregation is a pathological feature of neurodegenerative disorders. We previously demonstrated that protein inclusions in the brain are composed of supersaturated proteins, which are abundant and aggregation-prone, and...

Humans Inclusion Bodies Muscular Diseases Myositis Inclusion Body Protein Aggregates Protein Stability Proteome

BACKGROUND: Proteopathic brain lesions are a hallmark of many age-related neurodegenerative diseases including synucleinopathies and develop at least a decade before the onset of clinical symptoms. Thus, understanding of the...

ALPHA-SYNUCLEIN Microglia Neurofilament light chain Slice culture Animals Humans Inclusion Bodies Mice Microglia Neurofilament Proteins Neurons Organ Culture Techniques Synucleinopathies ALPHA-SYNUCLEIN

UNLABELLED: Point mutants of alpha1 -antitrypsin (α1AT) form ordered polymers that are retained as inclusions within the endoplasmic reticulum (ER) of hepatocytes in association with neonatal hepatitis, cirrhosis, and...

Animals Cell Line Cricetinae Cricetulus Endoplasmic reticulum stress Female Inclusion Bodies Models Animal Mutation Polymers Proteins Stress Physiological Unfolded Protein Response alpha 1-Antitrypsin alpha 1-Antitrypsin Deficiency

Abnormal insoluble ubiqitinated protein aggregates are found in the brains of Huntington's disease (HD) patients and in mice transgenic for the HTT mutation. Here, we describe the earliest stages of visible NII formation in...

Animals Female Huntington Disease Inclusion Bodies Male Mice Mice Transgenic Mutation Nerve Tissue Proteins Neurons Proteasome Endopeptidase Complex Ubiquitin Ubiquitinated Proteins Ubiquitination

motor neuron disease protein aggregation Protein homeostasis protein misfolding supersaturation Amyotrophic Lateral Sclerosis Brain DNA-Binding Proteins Humans Inclusion Bodies Motor Neurons Mutation Protein Aggregates protein aggregation Pathological Protein Folding RNA-Binding Protein FUS Spinal Cord Spinal Nerves Superoxide Dismutase Superoxide Dismutase-1

Difficult to express enzymes Escherichia coli Inclusion Bodies Recombinant industrial enzymes Solubility Systems Biology Biotechnology Escherichia coli Gene Expression Inclusion Bodies Industrial Microbiology Recombinant Proteins Research Design Solubility

Aβ40 Aβ42 E22G Amyloid arctic mutant dye labeling Fluorescence Inclusion Bodies ion exchange chromatography mCherry maleimide Alzheimer Disease Amyloid beta-Peptides Animals Escherichia coli Peptide Fragments Recombinant Proteins

Review Escherichia coli Recombinant industrial enzymes Difficult to express enzymes Inclusion Bodies Systems Biology Solubility

IL-8 Apoptosis corticosteroids Eosinophils Hypoxia Anti-Inflammatory Agents Apoptosis Cell Hypoxia Cells Cultured Dexamethasone Eosinophils Glucocorticoids Humans Inclusion Bodies Inflammation Interleukin-8