Disorders caused by imbalances in the protein homeostasis network - synthesis, folding, and transport of proteins; post-translational modifications; and degradation or clearance of misfolded proteins.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
Endoproteases that contain proteolytic core domains and ATPase-containing regulatory domains.
A cellular response to environmental insults that cause disruptions in PROTEIN FOLDING and/or accumulation of defectively folded protein in the ENDOPLASMIC RETICULUM. It consists of a group of regulatory cascades that are triggered as a response to altered levels of calcium and/or the redox state of the endoplasmic reticulum. Persistent activation of the unfolded protein response leads to the induction of APOPTOSIS.
A degradation process whereby incorrectly folded proteins are selectively transported out of the ENDOPLASMIC RETICULUM and into the CYTOSOL. The misfolded proteins are subsequently ubiquitinated and degraded by the PROTEASOME.
Cleavage of proteins into smaller peptides or amino acids either by PROTEASES or non-enzymatically (e.g., Hydrolysis). It does not include Protein Processing, Post-Translational.
An autosomal recessive disorder caused by a deficiency of acid beta-glucosidase (GLUCOSYLCERAMIDASE) leading to intralysosomal accumulation of glycosylceramide mainly in cells of the MONONUCLEAR PHAGOCYTE SYSTEM. The characteristic Gaucher cells, glycosphingolipid-filled HISTIOCYTES, displace normal cells in BONE MARROW and visceral organs causing skeletal deterioration, hepatosplenomegaly, and organ dysfunction. There are several subtypes based on the presence and severity of neurological involvement.
A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.
A constellation of responses that occur when an organism is exposed to excessive heat. Responses include synthesis of new proteins and regulation of others.
The processes whereby the internal environment of an organism tends to remain balanced and stable.
A glycosidase that hydrolyzes a glucosylceramide to yield free ceramide plus glucose. Deficiency of this enzyme leads to abnormally high concentrations of glucosylceramide in the brain in GAUCHER DISEASE. EC 3.2.1.45.
A species of nematode that is widely used in biological, biochemical, and genetic studies.
An autosomal recessive neurodegenerative disorder characterized by the onset in infancy of an exaggerated startle response, followed by paralysis, dementia, and blindness. It is caused by mutation in the alpha subunit of the HEXOSAMINIDASE A resulting in lipid-laden ganglion cells. It is also known as the B variant (with increased HEXOSAMINIDASE B but absence of hexosaminidase A) and is strongly associated with Ashkenazic Jewish ancestry.
Changes in the organism associated with senescence, occurring at an accelerated rate.
A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.
A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)
Proteins from the nematode species CAENORHABDITIS ELEGANS. The proteins from this species are the subject of scientific interest in the area of multicellular organism MORPHOGENESIS.
The unfavorable effect of environmental factors (stressors) on the physiological functions of an organism. Prolonged unresolved physiological stress can affect HOMEOSTASIS of the organism, and may lead to damaging or pathological conditions.
Hereditary and sporadic conditions which are characterized by progressive nervous system dysfunction. These disorders are often associated with atrophy of the affected central or peripheral nervous system structures.
The protein complement of an organism coded for by its genome.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
A gram-positive organism found in dental plaque, in blood, on heart valves in subacute endocarditis, and infrequently in saliva and throat specimens. L-forms are associated with recurrent aphthous stomatitis.
A mercaptoethylamine compound that is endogenously derived from the COENZYME A degradative pathway. The fact that cysteamine is readily transported into LYSOSOMES where it reacts with CYSTINE to form cysteine-cysteamine disulfide and CYSTEINE has led to its use in CYSTINE DEPLETING AGENTS for the treatment of CYSTINOSIS.

Cross currents in protein misfolding disorders: interactions and therapy. (1/141)

Protein Misfolding Disorders (PMDs) are a group of diseases characterized by the accumulation of abnormally folded proteins. Despite the wide range of proteins and tissues involved, PMDs share similar molecular and pathogenic mechanisms. Several epidemiological, clinical and experimental reports have described the co-existence of PMDs, suggesting a possible cross-talk between them. A better knowledge of the molecular basis of PMDs could have important implications for understanding the mechanism by which these diseases appear and progress and ultimately to develop novel strategies for treatment. Due to their similar molecular mechanisms, common therapeutic strategies could be applied for the diseases in this group.  (+info)

A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation. (2/141)

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Misfolded proteins and retinal dystrophies. (3/141)

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Mass spectrometry and the amyloid problem--how far can we go in the gas phase? (4/141)

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The transmembrane segment of a tail-anchored protein determines its degradative fate through dislocation from the endoplasmic reticulum. (5/141)

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Generation of prions in vitro and the protein-only hypothesis. (6/141)

Prions are self-propagating proteinaceous infectious agents capable of transmitting disease in the absence of nucleic acids. The nature of the infectious agent in prion diseases has been at the center of passionate debate for the past 30 years. However, recent reports on the in vitro generation of prions have settled all doubts that the misfolded prion protein (PrP(Sc)) is the key component in propagating infectivity. However, we still do not understand completely the mechanism of prion replication and whether or not other cellular factors besides PrP(Sc) are required for infectivity. In this article, we discuss these recent reports under the context of the protein-only hypothesis and their implications.  (+info)

A single mutation promotes amyloidogenicity through a highly promiscuous dimer interface. (7/141)

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Chaperone networks: tipping the balance in protein folding diseases. (8/141)

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Proteostasis is the process by which cells regulate the proper functioning and folding of proteins within the body to maintain cellular homeostasis. A deficiency in proteostasis refers to an impairment in this regulatory process, leading to the accumulation of misfolded or aggregated proteins. This can result in various diseases, such as neurodegenerative disorders, cancer, and metabolic conditions.

Proteostasis deficiencies can occur due to genetic mutations, environmental factors, or aging, which can affect the function of protein quality control systems, including chaperones, the ubiquitin-proteasome system, and autophagy. These systems are responsible for recognizing and disposing of misfolded proteins, preventing their accumulation and subsequent toxicity.

In summary, proteostasis deficiencies refer to impairments in the regulation of protein homeostasis within cells, leading to the accumulation of misfolded or aggregated proteins and contributing to various diseases.

Protein folding is the process by which a protein molecule naturally folds into its three-dimensional structure, following the synthesis of its amino acid chain. This complex process is determined by the sequence and properties of the amino acids, as well as various environmental factors such as temperature, pH, and the presence of molecular chaperones. The final folded conformation of a protein is crucial for its proper function, as it enables the formation of specific interactions between different parts of the molecule, which in turn define its biological activity. Protein misfolding can lead to various diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease.

ATP-dependent endopeptidases are a type of enzyme that require ATP (adenosine triphosphate) to catalyze the hydrolysis of peptide bonds within proteins. These enzymes are also known as ATP-dependent proteases or protein-breaking enzymes, and they play important roles in various cellular processes such as protein quality control, regulation of signaling pathways, and programmed cell death (apoptosis).

The ATP-dependent endopeptidases use the energy from ATP to unfold and translocate proteins into their active sites for degradation. They are typically composed of multiple subunits that form a large protein complex, including a catalytic core and regulatory domains. The regulation of these enzymes is critical for maintaining cellular homeostasis, as dysregulation can lead to various diseases such as neurodegenerative disorders, cancer, and infectious diseases.

Examples of ATP-dependent endopeptidases include the proteasome, which plays a central role in protein degradation in eukaryotic cells, and ClpP, which is involved in protein quality control in bacteria.

The Unfolded Protein Response (UPR) is a cellular stress response pathway that is activated when the endoplasmic reticulum (ER), an organelle responsible for protein folding and processing, becomes overwhelmed with misfolded or unfolded proteins. The UPR is initiated by three ER transmembrane sensors: IRE1, PERK, and ATF6. These sensors detect the accumulation of unfolded proteins in the ER lumen and transmit signals to the nucleus to induce a variety of adaptive responses aimed at restoring ER homeostasis.

These responses include:

* Transcriptional upregulation of genes encoding chaperones, folding enzymes, and components of the ER-associated degradation (ERAD) machinery to enhance protein folding capacity and promote the clearance of misfolded proteins.
* Attenuation of global protein synthesis to reduce the influx of new proteins into the ER.
* Activation of autophagy, a process that helps eliminate damaged organelles and aggregated proteins.

If these adaptive responses are insufficient to restore ER homeostasis, the UPR can also trigger apoptosis, or programmed cell death, as a last resort to eliminate damaged cells and prevent the spread of protein misfolding diseases such as neurodegenerative disorders.

Endoplasmic reticulum-associated degradation (ERAD) is a cellular process that targets and degrades misfolded or damaged proteins located in the endoplasmic reticulum (ER). The ER is a network of membrane-bound tubules and sacs within eukaryotic cells where proteins are synthesized, folded, and modified before being transported to their final destinations.

When proteins fail to fold correctly or become damaged in the ER, they can be recognized and tagged for degradation through the ERAD pathway. This process involves several steps:

1. Recognition: Misfolded or damaged proteins are recognized by specific chaperone proteins and ubiquitin ligases in the ER. Chaperones help proteins fold correctly, while ubiquitin ligases tag misfolded proteins with ubiquitin molecules, marking them for degradation.
2. Retrotranslocation: The marked proteins are then retrotranslocated (or "pulled back") across the ER membrane into the cytosol by a protein complex called the ERAD machinery.
3. Ubiquitination: Once in the cytosol, the ubiquitin molecules attached to the misfolded proteins are recognized by another set of ubiquitin ligases, which add more ubiquitin molecules, creating a polyubiquitin chain.
4. Degradation: The polyubiquitinated protein is then targeted to and degraded by the 26S proteasome, a large protein complex responsible for breaking down unwanted or damaged proteins in the cell.

ERAD plays a crucial role in maintaining protein quality control and ensuring proper cellular function. Dysregulation of ERAD has been implicated in various diseases, including neurodegenerative disorders, cancer, and viral infections.

Proteolysis is the biological process of breaking down proteins into smaller polypeptides or individual amino acids by the action of enzymes called proteases. This process is essential for various physiological functions, including digestion, protein catabolism, cell signaling, and regulation of numerous biological activities. Dysregulation of proteolysis can contribute to several pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders.

Gaucher disease is an inherited metabolic disorder caused by the deficiency of the enzyme glucocerebrosidase. This enzyme is responsible for breaking down a complex fatty substance called glucocerebroside, found in the cells of various tissues throughout the body. When the enzyme is not present in sufficient quantities or is entirely absent, glucocerebroside accumulates inside the lysosomes (cellular organelles responsible for waste material breakdown) of certain cell types, particularly within white blood cells called macrophages. This buildup of lipids leads to the formation of characteristic lipid-laden cells known as Gaucher cells.

There are three main types of Gaucher disease, classified based on the absence or presence and severity of neurological symptoms:

1. Type 1 (non-neuronopathic) - This is the most common form of Gaucher disease, accounting for approximately 95% of cases. It primarily affects the spleen, liver, and bone marrow but does not typically involve the central nervous system. Symptoms may include an enlarged spleen and/or liver, low red blood cell counts (anemia), low platelet counts (thrombocytopenia), bone pain and fractures, and fatigue.
2. Type 2 (acute neuronopathic) - This rare and severe form of Gaucher disease affects both visceral organs and the central nervous system. Symptoms usually appear within the first six months of life and progress rapidly, often leading to death before two years of age due to neurological complications.
3. Type 3 (subacute neuronopathic) - This form of Gaucher disease affects both visceral organs and the central nervous system but has a slower progression compared to type 2. Symptoms may include those seen in type 1, as well as neurological issues such as seizures, eye movement abnormalities, and cognitive decline.

Gaucher disease is inherited in an autosomal recessive manner, meaning that an individual must inherit two defective copies of the gene (one from each parent) to develop the condition. Treatment options for Gaucher disease include enzyme replacement therapy (ERT), substrate reduction therapy (SRT), and chaperone therapy, depending on the type and severity of the disease.

Molecular chaperones are a group of proteins that assist in the proper folding and assembly of other protein molecules, helping them achieve their native conformation. They play a crucial role in preventing protein misfolding and aggregation, which can lead to the formation of toxic species associated with various neurodegenerative diseases. Molecular chaperones are also involved in protein transport across membranes, degradation of misfolded proteins, and protection of cells under stress conditions. Their function is generally non-catalytic and ATP-dependent, and they often interact with their client proteins in a transient manner.

The Heat-Shock Response is a complex and highly conserved stress response mechanism present in virtually all living organisms. It is activated when the cell encounters elevated temperatures or other forms of proteotoxic stress, such as exposure to toxins, radiation, or infectious agents. This response is primarily mediated by a group of proteins known as heat-shock proteins (HSPs) or chaperones, which play crucial roles in protein folding, assembly, transport, and degradation.

The primary function of the Heat-Shock Response is to protect the cell from damage caused by misfolded or aggregated proteins that can accumulate under stress conditions. The activation of this response leads to the rapid transcription and translation of HSP genes, resulting in a significant increase in the intracellular levels of these chaperone proteins. These chaperones then assist in the refolding of denatured proteins or target damaged proteins for degradation via the proteasome or autophagy pathways.

The Heat-Shock Response is critical for maintaining cellular homeostasis and ensuring proper protein function under stress conditions. Dysregulation of this response has been implicated in various diseases, including neurodegenerative disorders, cancer, and cardiovascular diseases.

Homeostasis is a fundamental concept in the field of medicine and physiology, referring to the body's ability to maintain a stable internal environment, despite changes in external conditions. It is the process by which biological systems regulate their internal environment to remain in a state of dynamic equilibrium. This is achieved through various feedback mechanisms that involve sensors, control centers, and effectors, working together to detect, interpret, and respond to disturbances in the system.

For example, the body maintains homeostasis through mechanisms such as temperature regulation (through sweating or shivering), fluid balance (through kidney function and thirst), and blood glucose levels (through insulin and glucagon secretion). When homeostasis is disrupted, it can lead to disease or dysfunction in the body.

In summary, homeostasis is the maintenance of a stable internal environment within biological systems, through various regulatory mechanisms that respond to changes in external conditions.

Glucosylceramidase is an enzyme that is responsible for breaking down glucosylceramide, a type of fatty substance called a lipid, into glucose and ceramide. This process is important in the maintenance of proper functioning of cells, particularly in the nervous system. A deficiency of this enzyme can lead to a genetic disorder known as Gaucher disease, which is characterized by the accumulation of glucosylceramide in various tissues and organs, leading to symptoms such as enlargement of the liver and spleen, bone pain, anemia, and neurological problems.

'Caenorhabditis elegans' is a species of free-living, transparent nematode (roundworm) that is widely used as a model organism in scientific research, particularly in the fields of biology and genetics. It has a simple anatomy, short lifespan, and fully sequenced genome, making it an ideal subject for studying various biological processes and diseases.

Some notable features of C. elegans include:

* Small size: Adult hermaphrodites are about 1 mm in length.
* Short lifespan: The average lifespan of C. elegans is around 2-3 weeks, although some strains can live up to 4 weeks under laboratory conditions.
* Development: C. elegans has a well-characterized developmental process, with adults developing from eggs in just 3 days at 20°C.
* Transparency: The transparent body of C. elegans allows researchers to observe its internal structures and processes easily.
* Genetics: C. elegans has a fully sequenced genome, which contains approximately 20,000 genes. Many of these genes have human homologs, making it an excellent model for studying human diseases.
* Neurobiology: C. elegans has a simple nervous system, with only 302 neurons in the hermaphrodite and 383 in the male. This simplicity makes it an ideal organism for studying neural development, function, and behavior.

Research using C. elegans has contributed significantly to our understanding of various biological processes, including cell division, apoptosis, aging, learning, and memory. Additionally, studies on C. elegans have led to the discovery of many genes associated with human diseases such as cancer, neurodegenerative disorders, and metabolic conditions.

Tay-Sachs Disease is a rare, inherited autosomal recessive disorder that affects the nervous system's functioning. It results from the deficiency of an enzyme called hexosaminidase A (Hex-A), which is necessary for breaking down gangliosides, a type of fatty substance found in nerve cells. When Hex-A is absent or insufficient, gangliosides accumulate abnormally in the nerve cells, leading to their progressive destruction and severe neurological deterioration.

The classic infantile form of Tay-Sachs Disease manifests within the first six months of life with symptoms such as loss of motor skills, seizures, paralysis, dementia, blindness, and eventually death, usually by age four. Late-onset forms of the disease also exist, which may present in childhood or adulthood with milder symptoms.

Tay-Sachs Disease is more prevalent among individuals of Ashkenazi Jewish, French Canadian, and Cajun descent. Genetic counseling and prenatal testing are recommended for couples at risk of passing on the disease.

Premature aging, also known as "accelerated aging" or "early aging," refers to the physiological process in which the body shows signs of aging at an earlier age than typically expected. This can include various symptoms such as wrinkles, graying hair, decreased energy and mobility, cognitive decline, and increased risk of chronic diseases.

The medical definition of premature aging is not well-established, as aging is a complex process influenced by a variety of genetic and environmental factors. However, certain conditions and syndromes are associated with premature aging, such as Hutchinson-Gilford progeria syndrome, Werner syndrome, and Down syndrome.

In general, the signs of premature aging may be caused by a combination of genetic predisposition, lifestyle factors (such as smoking, alcohol consumption, and poor diet), exposure to environmental toxins, and chronic stress. While some aspects of aging are inevitable, maintaining a healthy lifestyle and reducing exposure to harmful factors can help slow down the aging process and improve overall quality of life.

The proteasome endopeptidase complex is a large protein complex found in the cells of eukaryotic organisms, as well as in archaea and some bacteria. It plays a crucial role in the degradation of damaged or unneeded proteins through a process called proteolysis. The proteasome complex contains multiple subunits, including both regulatory and catalytic particles.

The catalytic core of the proteasome is composed of four stacked rings, each containing seven subunits, forming a structure known as the 20S core particle. Three of these rings are made up of beta-subunits that contain the proteolytic active sites, while the fourth ring consists of alpha-subunits that control access to the interior of the complex.

The regulatory particles, called 19S or 11S regulators, cap the ends of the 20S core particle and are responsible for recognizing, unfolding, and translocating targeted proteins into the catalytic chamber. The proteasome endopeptidase complex can cleave peptide bonds in various ways, including hydrolysis of ubiquitinated proteins, which is an essential mechanism for maintaining protein quality control and regulating numerous cellular processes, such as cell cycle progression, signal transduction, and stress response.

In summary, the proteasome endopeptidase complex is a crucial intracellular machinery responsible for targeted protein degradation through proteolysis, contributing to various essential regulatory functions in cells.

The endoplasmic reticulum (ER) is a network of interconnected tubules and sacs that are present in the cytoplasm of eukaryotic cells. It is a continuous membranous organelle that plays a crucial role in the synthesis, folding, modification, and transport of proteins and lipids.

The ER has two main types: rough endoplasmic reticulum (RER) and smooth endoplasmic reticulum (SER). RER is covered with ribosomes, which give it a rough appearance, and is responsible for protein synthesis. On the other hand, SER lacks ribosomes and is involved in lipid synthesis, drug detoxification, calcium homeostasis, and steroid hormone production.

In summary, the endoplasmic reticulum is a vital organelle that functions in various cellular processes, including protein and lipid metabolism, calcium regulation, and detoxification.

'Caenorhabditis elegans' (C. elegans) is a type of free-living, transparent nematode (roundworm) that is often used as a model organism in scientific research. C. elegans proteins refer to the various types of protein molecules that are produced by the organism's genes and play crucial roles in maintaining its biological functions.

Proteins are complex molecules made up of long chains of amino acids, and they are involved in virtually every cellular process, including metabolism, DNA replication, signal transduction, and transportation of molecules within the cell. In C. elegans, proteins are encoded by genes, which are transcribed into messenger RNA (mRNA) molecules that are then translated into protein sequences by ribosomes.

Studying C. elegans proteins is important for understanding the basic biology of this organism and can provide insights into more complex biological systems, including humans. Because C. elegans has a relatively simple nervous system and a short lifespan, it is often used to study neurobiology, aging, and development. Additionally, because many of the genes and proteins in C. elegans have counterparts in other organisms, including humans, studying them can provide insights into human disease processes and potential therapeutic targets.

Physiological stress is a response of the body to a demand or threat that disrupts homeostasis and activates the autonomic nervous system and hypothalamic-pituitary-adrenal (HPA) axis. This results in the release of stress hormones such as adrenaline, cortisol, and noradrenaline, which prepare the body for a "fight or flight" response. Increased heart rate, rapid breathing, heightened sensory perception, and increased alertness are some of the physiological changes that occur during this response. Chronic stress can have negative effects on various bodily functions, including the immune, cardiovascular, and nervous systems.

Neurodegenerative diseases are a group of disorders characterized by progressive and persistent loss of neuronal structure and function, often leading to cognitive decline, functional impairment, and ultimately death. These conditions are associated with the accumulation of abnormal protein aggregates, mitochondrial dysfunction, oxidative stress, chronic inflammation, and genetic mutations in the brain. Examples of neurodegenerative diseases include Alzheimer's disease, Parkinson's disease, Huntington's disease, Amyotrophic Lateral Sclerosis (ALS), and Spinal Muscular Atrophy (SMA). The underlying causes and mechanisms of these diseases are not fully understood, and there is currently no cure for most neurodegenerative disorders. Treatment typically focuses on managing symptoms and slowing disease progression.

The proteome is the entire set of proteins produced or present in an organism, system, organ, or cell at a certain time under specific conditions. It is a dynamic collection of protein species that changes over time, responding to various internal and external stimuli such as disease, stress, or environmental factors. The study of the proteome, known as proteomics, involves the identification and quantification of these protein components and their post-translational modifications, providing valuable insights into biological processes, functional pathways, and disease mechanisms.

An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.

Streptococcus sanguis is a gram-positive, facultatively anaerobic, beta-hemolytic bacterium that belongs to the Streptococcaceae family. It's part of the viridans group streptococci (VGS) and is commonly found in the oral cavity of humans, residing on the surface of teeth and mucous membranes.

S. sanguis is generally considered a commensal organism; however, it can contribute to dental plaque formation and cause endocarditis, particularly in people with pre-existing heart conditions. It's important to note that there are several subspecies of S. sanguis, including S. sanguis I, II, III, and IV, which may have different characteristics and clinical implications.

Medical Definition: Streptococcus sanguis is a gram-positive, facultatively anaerobic, beta-hemolytic bacterium that belongs to the viridans group streptococci (VGS). It is commonly found in the oral cavity and can cause endocarditis in susceptible individuals.

Cysteamine is a medication and a naturally occurring aminothiol compound, which is composed of the amino acid cysteine and a sulfhydryl group. It has various uses in medicine, including as a treatment for cystinosis, a rare genetic disorder that causes an accumulation of cystine crystals in various organs and tissues. Cysteamine works by reacting with cystine to form a compound that can be more easily eliminated from the body. It is available in oral and topical forms and may also be used for other indications, such as treating lung diseases and radiation-induced damage.

"Biological and chemical approaches to diseases of proteostasis deficiency". Annual Review of Biochemistry. 78: 959-91. doi: ... Proteostasis is the dynamic regulation of a balanced, functional proteome. The proteostasis network includes competing and ... Therapeutic restoration of proteostasis may treat or resolve these pathologies. Cellular proteostasis is key to ensuring ... Dysfunction in proteostasis can arise from errors in or misregulation of protein folding. The classic examples are missense ...
"Biological and Chemical Approaches to Diseases of Proteostasis Deficiency". Annual Review of Biochemistry. 78: 959-91. doi: ... Protein homeostasis (proteostasis), results from the coordinated action of the different arms of the cellular quality control ... It is becoming more evident that the cellular capacity to maintain proteostasis declines with age, thereby causing the late ... Ben-Zvi, A.; Miller, E. A.; Morimoto, R. I. (2009). "Collapse of proteostasis represents an early molecular event in ...
"Biological and Chemical Approaches to Diseases of Proteostasis Deficiency". Annual Review of Biochemistry. 78: 959-991. doi: ... "Professor Richard Morimoto - Proteostasis Symposium 2017". Proteostasis Symposium 2017. Retrieved 2018-08-01. "Professor ... Shaping Proteostasis at the Cellular, Tissue, and Organismal Level. Journal of Cell Biology 216: DOI: 10.1083/jcb.201612111 ( ... Ben-Zvi-A; Miller, E.A.; Morimoto, R.I. (2009). "The Collapse of Proteostasis Represents an Early Molecular Event in C. elegans ...
Deficiency of PreP is found associated with Alzheimer's disease. Reduced levels of PreP via RNAi mediated knockdown have been ... It is also sometimes called metalloprotease 1 (MP1).PreP facilitates proteostasis by utilizing an ~13300-A(3) catalytic chamber ... The substrates of PreP are vital to proteostasis, as they can insert to mitochondrial membranes, disrupting electrical ... Nabhan JF, Gooch RL, Piatnitski Chekler EL, Pierce B, Bulawa CE (December 2015). "Perturbation of cellular proteostasis ...
X Inborn error of metabolism Mitochondrial diseases Phosphorus metabolism disorders Porphyrias Proteostasis deficiencies ... Metabolic syndrome Metabolic Myopathies Lysosomal storage disease Deficiency disease Hypermetabolism "MeSH Descriptor Data: ... and occur when a defective gene causes an enzyme deficiency. These diseases, of which there are many subtypes, are known as ... Acid-base imbalance Metabolic brain diseases Disorders of calcium metabolism DNA repair-deficiency disorders Glucose metabolism ...
Given the facts that MARCH5 regulates the protein proteostasis of Drp1, mitofusin 1, and mitofusin 2 that are pivotal ... and deficiencies in it promote cellular senescence. Considering that both Drp1 and MAP1B are substrates for MITOL, MITOL is ...
However, none of these diseases are related to an enzyme deficiency. Indeed, thus far no disease has been attributed to the ... Based on its PDI activity, tTG plays an important role in the regulation of proteostasis, by catalyzing the trimerization of ...
Telomerase deficiency in humans has been linked to several aging-related diseases related to loss of regenerative capacity of ... Proteostasis is the homeostatic process of maintaining all the proteins necessary for the functioning of the cell in their ... Kirana, A.N.; Prafiantini, E.; Hardiany, N.S. (2021-02-22). "Protein intake and loss of proteostasis in the eldery". The ... Klaips, Courtney L.; Jayaraj, Gopal Gunanathan; Hartl, F. Ulrich (2017-11-10). "Pathways of cellular proteostasis in aging and ...
Homma S, Iwasaki M, Shelton GD, Engvall E, Reed JC, Takayama S (September 2006). "BAG3 deficiency results in fulminant myopathy ... It is essential for protein homeostasis (proteostasis) in neurons and in mechanically strained cells and tissues such as ... Chaperone-assisted selective autophagy is thus essential for proteostasis in neurons. In mechanically strained cells and ...
2015). "SIRT1 deficiency in microglia contributes to cognitive decline in aging and neurodegeneration via epigenetic regulation ... Gan also studies how mechanisms of proteostasis can contribute to pathogenic protein aggregation. Her lab demonstrated that ...
"Multiple myeloma proteostasis can be targeted via translation initiation factor eIF4E". International Journal of Oncology. 46 ( ... Journal of Acquired Immune Deficiency Syndromes. 40 (1): 47-52. doi:10.1097/01.qai.0000174649.51084.46. PMID 16123681. S2CID ...
May 2020). "SARM1 deficiency promotes rod and cone photoreceptor cell survival in a model of retinal degeneration". Life ... Summers DW, Milbrandt J, DiAntonio A (September 2018). "Palmitoylation enables MAPK-dependent proteostasis of axon survival ... November 2019). "Sarm1 Gene Deficiency Attenuates Diabetic Peripheral Neuropathy in Mice". Diabetes. 68 (11): 2120-2130. doi: ... "SARM1 deletion delays cerebellar but not spinal cord degeneration in an enhanced mouse model of SPG7 deficiency". Brain: A ...
2011). "Growth hormone receptor deficiency is associated with a major reduction in pro-aging signaling, cancer, and diabetes in ... 2016). "Insulin and IGF-1 receptors regulate FoxO-mediated signaling in muscle proteostasis". J Clin Invest. 126 (9): 3433-3346 ...
Oh DH, Rigas D, Cho A, Chan JY (Nov 2012). "Deficiency in the nuclear-related factor erythroid 2 transcription factor (Nrf1) ... Nfe2l1 is also involved in maintaining proteostasis. Brains of mice with conditional knockout of Nfe2l1 in neuronal cells ... cholesterol handling and maintaining proteostasis. NFE2L1 binds DNA as heterodimers with one of small Maf proteins (MAFF, MAFG ...
Rossi DJ, Bryder D, Seita J, Nussenzweig A, Hoeijmakers J, Weissman IL (2007). "Deficiencies in DNA damage repair limit the ... loss of proteostasis, deregulated nutrient sensing, mitochondrial dysfunction, cellular senescence, stem cell exhaustion, ... Lig4 deficiency in the mouse causes a progressive loss of HSCs during aging. These findings suggest that NHEJ is a key ...
Correcting magnesium deficiency for instance could prolong life. Many supplements are researched primarily for potential ... proteostasis maintenance, and recycling mechanisms such as autophagy. The average life expectancy in a population is lowered by ... It is difficult to reconcile the largely protective effects of GH/IGF-1 deficiency on longevity in animals with the ... Sometimes, their use is researched or recommended as a way to correct nutritional deficiencies from switching to otherwise ...
Should this depletion continue, a copper health deficiency condition may develop. If too much copper is ingested, an excess ... Chemical process Proteostasis - biological pathways within cells that control the biogenesis, folding, trafficking and ... Both of these conditions, deficiency and excess, can lead to tissue injury and disease. However, due to homeostatic regulation ...
"Proteostasis Deficiencies" by people in this website by year, and whether "Proteostasis Deficiencies" was a major or minor ... "Proteostasis Deficiencies" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... Below are the most recent publications written about "Proteostasis Deficiencies" by people in Profiles. ... Below are MeSH descriptors whose meaning is more general than "Proteostasis Deficiencies". ...
Proteostasis Deficiencies / metabolism * Signal Transduction Substances * Heat-Shock Proteins Grants and funding * 100140/WT_/ ...
"Biological and chemical approaches to diseases of proteostasis deficiency". Annual Review of Biochemistry. 78: 959-91. doi: ... Proteostasis is the dynamic regulation of a balanced, functional proteome. The proteostasis network includes competing and ... Therapeutic restoration of proteostasis may treat or resolve these pathologies. Cellular proteostasis is key to ensuring ... Dysfunction in proteostasis can arise from errors in or misregulation of protein folding. The classic examples are missense ...
Proteostasis Deficiencies Publication Types: Lecture. Webcast Download. NLM Classification: WE 250 NLM ID: 101601863 ...
Proteostasis Deficiencies/chemically induced*; Proteostasis Deficiencies/physiopathology; RNA/biosynthesis; RNA/isolation & ...
span,,b,Introduction,/b,: Homocystinuria due to cystathionine β-synthase (CBS) deficiency, the most frequent inborn error of ... connective tissue deficiency; fatty liver; fibrinogen; homocysteine; mTORC1; protein modification; proteostasis; stroke. ... highlight the involvement of dysregulated proteostasis in pathologies associated with CBS deficiency, including thromboembolism ... Proteomic exploration of cystathionine β-synthase deficiency: implications for the clinic Hieronim Jakubowski 1 2 ...
Small molecule proteostasis regulators that activate the unfolded protein response transcription factor ATF6 reduce the ... 2009) Biological and chemical approaches to diseases of proteostasis deficiency Annual Review of Biochemistry 78:959-991. ... ER proteostasis regulators depend on endogenous ATF6 activation. (A) BIP mRNA measured by qPCR in ATF6+/+ and ATF6-/- MEFs ... profiling for the top 281 ER proteostasis regulator compounds. HEK293T-Rex cells were incubated with 10 μM of each proteostasis ...
RAB18 deficiency causes two conditions with similar signs and symptoms that primarily affect the eyes, brain, and reproductive ... The RAB GTPase RAB18 modulates macroautophagy and proteostasis. Biochem Biophys Res Commun. 2017 May 6;486(3):738-743. doi: ... RAB18 deficiency is caused by mutations in the RAB3GAP1, RAB3GAP2, RAB18, or TBC1D20 gene. RAB3GAP1 gene mutations are the most ... RAB18 deficiency is inherited in an autosomal recessive pattern. , which means both copies of the gene in each cell have ...
History of clinically significant medical conditions (other than ALS) or any other reason, including any physical, psychological, or psychiatric condition that, in the opinion of the Investigator, would compromise the safety or interfere with the subjects participation in the study, or would make the subject an unsuitable candidate to receive study drug, or would put the subject at risk by participating in the study ...
7. Alpha 1-Antitrypsin Deficiency: A Disorder of Proteostasis-Mediated Protein Folding and Trafficking Pathways.. Karatas E; ... Pathways of cellular proteostasis in aging and disease.. Klaips CL; Jayaraj GG; Hartl FU. J Cell Biol; 2018 Jan; 217(1):51-63. ... Proteostasis and Proteotoxicity in the Network Medicine Era.. Lualdi M; Alberio T; Fasano M. Int J Mol Sci; 2020 Sep; 21(17):. ... The biology of proteostasis in aging and disease.. Labbadia J; Morimoto RI. Annu Rev Biochem; 2015; 84():435-64. PubMed ID: ...
Biological and chemical approaches to diseases of proteostasis deficiency. Annual Review of Biochemistry. 78: 959-91. PMID ... Adapting proteostasis for disease intervention. Science (New York, N.Y.). 319: 916-9. PMID 18276881 DOI: 10.1126/Science. ... Small molecule proteostasis regulators that reprogram the ER to reduce extracellular protein aggregation. Elife. 5. PMID ... Endoplasmic Reticulum Proteostasis Influences the Oligomeric State of an Amyloidogenic Protein Secreted from Mammalian Cells. ...
A transgenic mouse line for assaying tissue-specific changes in endoplasmic reticulum proteostasis. Svarcbahs R, Blossom SM, ... KDEL Receptors Are Differentially Regulated to Maintain the ER Proteome under Calcium Deficiency Kathleen A Trychta 1 , Susanne ... KDEL Receptors Are Differentially Regulated to Maintain the ER Proteome under Calcium Deficiency Kathleen A Trychta et al. Cell ...
Nutrient-driven O-GlcNAc in proteostasis and neurodegeneration.. Akan I, Olivier-Van Stichelen S, Bond MR, Hanover JA.. J ... Detection of phosphoglucomutase-3 deficiency by lectin-based flow cytometry.. Carlson RJ, Bond MR, Hutchins S, Brown Y, Wolfe ...
... metabolic deficiencies, and others. It is well established that proteostasis naturally declines during aging. While there has ... The effect of obesity and aging on proteostasis. Jay Chung, NHLBI. Life and death in the inner ear: Heat shock proteins and ... Impact of energy metabolism on neuronal proteostasis. Mark Mattson, NIA. Prion sequestration by the Btn2 and Cur1 proteins; Dr ... The role of proteostasis (protein homeostasis) in health and disease. Thursday, November 07, 2013 - Concurrent Symposia Session ...
8. Stem cell exhaustion, a deficiency of stem cells due to aging. Stem cells are cells that can turn into any cell type and are ... 4. Loss of proteostasis, development of nonnative protein aggregates in tissues. 5. Deregulated nutrient sensing, bodys ...
Proteostasis Deficiencies 3 3 Proteostasis Deficiencies -- complications : Neurodegeneration : metallostasis and proteostasis ... Proteostasis Deficiencies -- See Also Proteostasis Regulation of the concentration, folding, interactions, and cellular ...
Proteostasis Deficiencies Entry term(s). Deficiencies, Proteostasis Deficiency, Proteostasis Dysfunction, Proteostasis ... Dysfunctions, Proteostasis Proteinopathy Proteostasis Deficiency Proteostasis Dysfunction Proteostasis Dysfunctions Protein ... Deficiencies, Proteostasis. Deficiency, Proteostasis. Disease, Protein Folding. Disease, Protein Misfolding. Diseases, Protein ... Proteostasis Deficiencies - Preferred Concept UI. M0534903. Scope note. Disorders caused by imbalances in the PROTEIN ...
Proteostasis Deficiencies Preferred Term Term UI T749722. Date04/21/2009. LexicalTag NON. ThesaurusID NLM (2010). ... Proteostasis Deficiencies Preferred Concept UI. M0534903. Scope Note. Disorders caused by imbalances in the PROTEIN HOMEOSTASIS ... Proteostasis Dysfunctions See Also. Proteostasis. Public MeSH Note. 2010. History Note. 2010. Date Established. 2010/01/01. ... Proteostasis Deficiencies. Tree Number(s). C18.452.845. Unique ID. D057165. RDF Unique Identifier. http://id.nlm.nih.gov/mesh/ ...
Proteostasis Deficiencies Preferred Term Term UI T749722. Date04/21/2009. LexicalTag NON. ThesaurusID NLM (2010). ... Proteostasis Deficiencies Preferred Concept UI. M0534903. Scope Note. Disorders caused by imbalances in the PROTEIN HOMEOSTASIS ... Proteostasis Dysfunctions See Also. Proteostasis. Public MeSH Note. 2010. History Note. 2010. Date Established. 2010/01/01. ... Proteostasis Deficiencies. Tree Number(s). C18.452.845. Unique ID. D057165. RDF Unique Identifier. http://id.nlm.nih.gov/mesh/ ...
Powers, E. T., et al. (2009). Biological and chemical approaches to diseases of proteostasis deficiency. Annu Rev Biochem 78: ... 2009). Proteostasis imbalances, deficiency and functional collapse are implicated in a broad and increasing spectrum of protein ... Proteostasis Profiler (Pro2) Web-Tool. We designed a web-based Proteostasis Profiler (Pro2) in order to enable visual ... 2008). Cellular proteostasis capacity is limited within the constraints of each cells proteostasis boundary (Powers et al. ...
The effects of mRNA decapping deficiency on stress resistance and longevity are orchestrated by a multimodal stress response ... Maintenance of Proteostasis by P Body-Mediated Regulation of eIF4E Availability during Aging in Caenorhabditis elegans. Cell ... Maintenance of Proteostasis by P Body-Mediated Regulation of eIF4E Availability during Aging in Caenorhabditis elegans ... Our findings elucidate a mechanism of proteostasis control during aging through P body-mediated regulation of protein synthesis ...
"amyloid; cardiovascular diseases; protein aggregates; proteostasis; proteostasis deficiencies; unfolded protein response". *. * ...
Proteostasis deficiencies. *Rickets. *Sex hormone disorders. *Thyroid cancer. *Thyroid hormone resistance. *Water-electrolyte ...
Diaz-Delcastillo, M., MT, G., Andersen, C., Nielsen, A., Møller, H. E. H., Vinholt, P., Asmussen, J. T., Kristensen, I. B., Nyvold, C. G., Abildgaard, N., Andersen, T. & Lund, T., 2022, I: Clinical Lymphoma Myeloma and Leukemia. 22, Suppl. , s. 55 1 s., P-036.. Publikation: Bidrag til tidsskrift › Konferenceabstrakt i tidsskrift › Forskning › peer review ...
Proteostasis Deficiencies}, {ConditionAncestorId=,D000008659, ConditionAncestorTerm=,Metabolic Diseases}, { ...
Proteostasis Deficiencies [C18.452.845]. *Amyloidosis [C18.452.845.500]. Below are MeSH descriptors whose meaning is related to ...
"Proteostasis in Health and Disease," on June 3, 2013. The symposium brought together national experts to address the health ... metabolic deficiencies, aging and other chronic maladies. ... and organized the inaugural symposium for the Proteostasis ...
Proteostasis Deficiencies Medicine & Life Sciences 22% * Peptides Engineering & Materials Science 21% * Pathology Engineering ...
  • In this review, we discuss the functional cross talk of proteostasis and mitostasis in cellular homeodynamics and the impairment of mitochondrial quality control during ageing, cancer, and neurodegeneration. (hindawi.com)
  • Deficiency in ClpP induces an overload of mitochondrial misfolded/unfolded proteins, suppresses mitochondrial respiratory activity, increases mitochondrial oxidative damage and causes cell death. (springer.com)
  • Despite these findings suggesting that mitochondria might be a key link between αSyn toxicity and neuronal degeneration in PD, the field still lacks an understanding of how αSyn abnormality and mitochondrial functional deficiency influence each other. (springer.com)
  • Detoxification is part of a broader "Chemoprotection" system that includes free-radical protection, but extends into many essential aspects of longevity, including mitochondrial function, autophagy, senescence, proteostasis and telomere length. (holisticdental.org)
  • The work from Amy Reeves' team that utilized imaging mass cytometry (IMC) to investigate the role of mitochondrial dysfunction, proteostasis, and quality control in dopaminergic neurons from Parkinson's patients. (athletic.healthcare)
  • Ageing leads to a gradual dysfunction of the proteostasis network and thus to proteome instability due to accumulation of damaged and/or misfolded proteins [ 2 ]. (hindawi.com)
  • The latest studies suggest that, in principle, any deficiency in protein homeostasis (proteostasis) may lead to cell dysfunction thus underscoring the protective key role played by systems regulating the clearance of misfolded or defective proteins in the cell. (unict.it)
  • Because protein molecules are highly dynamic, constant chaperone surveillance is required to ensure protein homeostasis (proteostasis). (nature.com)
  • Finally, we show evidence that abnormal protein homeostasis is a prevalent mechanism responsible for UROS deficiency and that modulators of UROS proteolysis such as proteasome inhibitors or chemical chaperones may represent an attractive therapeutic option to reduce porphyrin accumulation and prevent skin photosensitivity in CEP patients when the genotype includes a missense variant. (qxmd.com)
  • Proteostasis is composed of the two terms proteome (totality of proteins that can be produced in the body) and homeostasis (balance). (moleqlar.de)
  • Therefore, proteins homeostasis (proteostasis) can be central for self-renewal, cell and pluripotency destiny decisions6C9. (irjs.info)
  • Selective autophagy in plants and its role in plant response to environmental stresses (with focus on nutrient deficiency). (cost-proteostasis.eu)
  • In vitro, Pacer deficiency lead to impaired autophagy and accumulation of ALS-associated protein aggregates, which correlated with theinduction of cell death.ConclusionsThis study, therefore, identifies Pacer as a new regulator of proteostasis associated with ALS pathology. (umayor.cl)
  • The proteostasis network includes competing and integrated biological pathways within cells that control the biogenesis, folding, trafficking, and degradation of proteins present within and outside the cell. (wikipedia.org)
  • We found 32 dementia-associated plasma proteins that were involved in proteostasis, immunity, synaptic function, and extracellular matrix organization. (cdc.gov)
  • Both of these play a role in promoting cell survival in the face of disruption to cellular proteostasis. (cost-proteostasis.eu)
  • MCC was preserved in mice given the chemical chaperone 4-phenylbutyric acid, but was disrupted in mice lacking the transcription factor NRF2, suggesting that oxidative stress and altered proteostasis contribute to the disruption of MCC. (nih.gov)
  • Ageing of the blood-brain barrier (BBB) results from an accumulation of deficiencies with contributions of senescence, increased inflammation, and oxidative stress. (uniklinikum-jena.de)
  • These data indicate RNA metabolism, proteostasis, monoamine metabolism, and cholesterol synthesis are disrupted in the RTT proteome. (biomedcentral.com)
  • Congenital erythropoietic porphyria (CEP) is an inborn error of heme biosynthesis characterized by uroporphyrinogen III synthase (UROS) deficiency resulting in deleterious porphyrin accumulation in blood cells responsible for hemolytic anemia and cutaneous photosensitivity. (qxmd.com)
  • Loss of proteostasis is central to understanding the cause of diseases associated with excessive protein misfolding and degradation leading to loss-of-function phenotypes, as well as aggregation-associated degenerative disorders. (wikipedia.org)
  • Cellular mechanisms for maintaining proteostasis include regulated protein translation, chaperone assisted protein folding, and protein degradation pathways. (wikipedia.org)
  • The third component of the proteostasis network is the protein degradation machinery. (wikipedia.org)
  • Protein degradation occurs in proteostasis when the cellular signals indicate the need to decrease overall cellular protein levels. (wikipedia.org)
  • Recent advances suggest that an age-related decline in proteostasis capacity allows the manifestation of various protein-aggregation diseases, including Alzheimer's disease and Parkinson's disease. (nature.com)
  • Figure 6: Protein fates in the proteostasis network. (nature.com)
  • The proteostasis network (PN) is an assembly of distinct dynamic molecular pathways that control the functionality of the proteome (proteome homeodynamics) during protein synthesis, folding, trafficking, and degradation. (hindawi.com)
  • Through the analysis of enhanced green fluorescent protein-tagged versions of UROS enzyme we experimentally confirmed these data and showed that thermodynamic instability and premature protein degradation is a major mechanism accounting for the enzymatic deficiency associated with twenty UROS mutants in human cells. (qxmd.com)
  • Cellular proteostasis represents a finely tuned equilibrium between protein production, maintenance, and degradation that is crucial for cellular well-being. (umu.se)
  • When proteostasis disruptions exceed the capacity of the PQC system, it leads to toxic protein aggregations with non-native conformations. (umu.se)
  • Proteostasis is the dynamic regulation of a balanced, functional proteome. (wikipedia.org)
  • Proteostasis and Energetics as Proteome Hallmarks of Aging and Influenza Challenge in Pulmonary Disease. (morimotolab.org)
  • Molecular mechanisms responsible for signaling and regulation of plant response to nutrient deficiency stress and other abiotic stresses (with focus on the role of posttranslational processes). (cost-proteostasis.eu)
  • Our research focuses on molecular details underlying the age-related decline of proteostasis and intracellular communication using high-throughput approaches in yeast, with the ultimate goal of validating and translating these findings into higher eukaryotic model systems. (umu.se)
  • As organisms age, maintaining proteostasis becomes increasingly challenging, contributing to the development of diseases such as cancer and neurodegenerative disorders. (umu.se)
  • With our research we aim to understand the interconnections between ageing and proteostasis, focussing on intracellular communication pathways. (umu.se)
  • To identify disease modifier genes that may explain the neuroprotective effects of XBP1 deficiency, we performed gene expression profiling of brain cortex and striatum of these animals and uncovered insulin-like growth factor 2 (Igf2) as the major upregulated gene. (uchile.cl)
  • Loss of hPAF1C binding by NS1 attenuates influenza infection, whereas hPAF1C deficiency reduces antiviral gene expression and renders cells more susceptible to viruses. (mssm.edu)
  • An integral node from the proteostasis network may be the ubiquitin proteasome program (UPS), the main selective proteolytic system in eukaryotic cells10,11. (irjs.info)
  • Using mathematical modeling and genetic and pharmacologic approaches, we revealed that modulation of Sec61-mediated cotranslational translocation selectively impaired glycoprotein proteostasis of influenza as well as HIV and dengue viruses and led to inhibition of viral growth and infectivity. (mssm.edu)
  • RAB18 deficiency is caused by mutations in the RAB3GAP1 , RAB3GAP2 , RAB18 , or TBC1D20 gene. (medlineplus.gov)
  • Impaired neuronal proteostasis is a salient feature of many neurodegenerative diseases, highlighting alterations in the function of the endoplasmic reticulum (ER). (uchile.cl)
  • Furthermore, proteasome inhibition using bortezomib, a clinically available drug, significantly enhanced proteostasis of each unstable UROS mutant. (qxmd.com)
  • One of the first points of regulation for proteostasis is during translation. (wikipedia.org)
  • Regulation of plant response to sulfur deficiency. (cost-proteostasis.eu)
  • Cellular proteostasis is key to ensuring successful development, healthy aging, resistance to environmental stresses, and to minimize homeostatic perturbations from pathogens such as viruses. (wikipedia.org)
  • Another interactor of UBE3A was BCCIP, whose deficiency in mouse leads to impaired neural progenitor self-renewal and differentiation capabilities84. (irjs.info)
  • (R ) Nicotinamide adenine dinucleotide deficiency, or low NAD, plays a significant role in five out of nine hallmarks of aging . (moleqlar.de)
  • Therapeutic restoration of proteostasis may treat or resolve these pathologies. (wikipedia.org)
  • what they do and how to diagnose and treat a deficiency. (holisticdental.org)
  • Prolonged or chronic stress can upset this balance, resulting in proteostasis breakdown, cellular toxicity, and ultimately cell death. (umu.se)