fenil210/Med-Lamma huggingface dataset:
What is (are) biotin-thiamine-responsive basal ganglia disease ?
Biotin-thiamine-responsive basal ganglia disease is a disorder that affects the nervous system, including a group of structures in the brain called the basal ganglia, which help control movement. As its name suggests, the condition may improve if the vitamins biotin and thiamine are given as treatment. Without early and lifelong vitamin treatment, people with biotin-thiamine-responsive basal ganglia disease experience a variety of neurological problems that gradually get worse. The occurrence of specific neurological problems and their severity vary even among affected individuals within the same family.  The signs and symptoms of biotin-thiamine-responsive basal ganglia disease usually begin between the ages of 3 and 10, but the disorder can appear at any age. Many of the neurological problems that can occur in biotin-thiamine-responsive basal ganglia disease affect movement, and can include involuntary tensing of various muscles (dystonia), muscle rigidity, muscle weakness on one or both sides of the body (hemiparesis or quadriparesis), problems coordinating movements (ataxia), and exaggerated reflexes (hyperreflexia). Movement problems can also affect the face, and may include the inability to move facial muscles due to facial nerve paralysis (supranuclear facial palsy), paralysis of the eye muscles (external ophthalmoplegia), difficulty chewing or swallowing (dysphagia), and slurred speech. Affected individuals may also experience confusion, loss of previously learned skills, intellectual disability, and seizures. Severe cases may result in coma and become life-threatening.  Typically, the neurological symptoms occur as increasingly severe episodes, which may be triggered by fever, injury, or other stresses on the body. Less commonly, the signs and symptoms persist at the same level or slowly increase in severity over time rather than occurring as episodes that come and go. In these individuals, the neurological problems are usually limited to dystonia, seizure disorders, and delay in the development of mental and motor skills (psychomotor delay). + GHR + biotin-thiamine-responsive basal ganglia disease
How many people are affected by biotin-thiamine-responsive basal ganglia disease ?
Biotin-thiamine-responsive basal ganglia disease is a rare disorder; its prevalence is unknown. Approximately 48 cases have been reported in the medical literature; most of these are individuals from Arab populations. + GHR + biotin-thiamine-responsive basal ganglia disease
What are the genetic changes related to biotin-thiamine-responsive basal ganglia disease ?
Biotin-thiamine-responsive basal ganglia disease is caused by mutations in the SLC19A3 gene. This gene provides instructions for making a protein called a thiamine transporter, which moves thiamine into cells. Thiamine, also known as vitamin B1, is obtained from the diet and is necessary for proper functioning of the nervous system.  Mutations in the SLC19A3 gene likely result in a protein with impaired ability to transport thiamine into cells, resulting in decreased absorption of the vitamin and leading to neurological dysfunction. In this disorder, abnormalities affect several parts of the brain. Using medical imaging, generalized swelling as well as specific areas of damage (lesions) in the brain can often be seen, including in the basal ganglia. The relationship between these specific brain abnormalities and the abnormal thiamine transporter is unknown.  It is unclear how biotin is related to this disorder. Some researchers suggest that the excess biotin given along with thiamine as treatment for the disorder may increase the amount of thiamine transporter that is produced, partially compensating for the impaired efficiency of the abnormal protein. Others propose that biotin transporter proteins may interact with thiamine transporters in such a way that biotin levels influence the course of the disease. + GHR + biotin-thiamine-responsive basal ganglia disease
Is biotin-thiamine-responsive basal ganglia disease inherited ?
This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. + GHR + biotin-thiamine-responsive basal ganglia disease
What are the treatments for biotin-thiamine-responsive basal ganglia disease ?
These resources address the diagnosis or management of biotin-thiamine-responsive basal ganglia disease:  - Gene Review: Gene Review: Biotin-Thiamine-Responsive Basal Ganglia Disease   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care + GHR + biotin-thiamine-responsive basal ganglia disease
What is (are) congenital myasthenic syndrome ?
Congenital myasthenic syndrome is a group of conditions characterized by muscle weakness (myasthenia) that worsens with physical exertion. The muscle weakness typically begins in early childhood but can also appear in adolescence or adulthood. Facial muscles, including muscles that control the eyelids, muscles that move the eyes, and muscles used for chewing and swallowing, are most commonly affected. However, any of the muscles used for movement (skeletal muscles) can be affected in this condition. Due to muscle weakness, affected infants may have feeding difficulties. Development of motor skills such as crawling or walking may be delayed. The severity of the myasthenia varies greatly, with some people experiencing minor weakness and others having such severe weakness that they are unable to walk.  Some individuals have episodes of breathing problems that may be triggered by fevers or infection. Severely affected individuals may also experience short pauses in breathing (apnea) that can lead to a bluish appearance of the skin or lips (cyanosis). + GHR + congenital myasthenic syndrome
How many people are affected by congenital myasthenic syndrome ?
The prevalence of congenital myasthenic syndrome is unknown. At least 600 families with affected individuals have been described in the scientific literature. + GHR + congenital myasthenic syndrome
What are the genetic changes related to congenital myasthenic syndrome ?
Mutations in many genes can cause congenital myasthenic syndrome. Mutations in the CHRNE gene are responsible for more than half of all cases. A large number of cases are also caused by mutations in the RAPSN, CHAT, COLQ, and DOK7 genes. All of these genes provide instructions for producing proteins that are involved in the normal function of the neuromuscular junction. The neuromuscular junction is the area between the ends of nerve cells and muscle cells where signals are relayed to trigger muscle movement.  Gene mutations lead to changes in proteins that play a role in the function of the neuromuscular junction and disrupt signaling between the ends of nerve cells and muscle cells. Disrupted signaling between these cells results in an impaired ability to move skeletal muscles, muscle weakness, and delayed development of motor skills. The respiratory problems in congenital myasthenic syndrome result from impaired movement of the muscles of the chest wall and the muscle that separates the abdomen from the chest cavity (the diaphragm).  Mutations in other genes that provide instructions for proteins involved in neuromuscular signaling have been found to cause some cases of congenital myasthenic syndrome, although these mutations account for only a small number of cases. Some people with congenital myasthenic syndrome do not have an identified mutation in any of the genes known to be associated with this condition. + GHR + congenital myasthenic syndrome
Is congenital myasthenic syndrome inherited ?
This condition is most commonly inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition.  Rarely, this condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. In some cases, an affected person inherits the mutation from one affected parent. Other cases result from new mutations in the gene and occur in people with no history of the disorder in their family. + GHR + congenital myasthenic syndrome
What are the treatments for congenital myasthenic syndrome ?
These resources address the diagnosis or management of congenital myasthenic syndrome:  - Gene Review: Gene Review: Congenital Myasthenic Syndromes  - Genetic Testing Registry: CHRNA1-Related Congenital Myasthenic Syndrome  - Genetic Testing Registry: Congenital myasthenic syndrome  - Genetic Testing Registry: Congenital myasthenic syndrome 1B, fast-channel  - Genetic Testing Registry: Congenital myasthenic syndrome with tubular aggregates 1  - Genetic Testing Registry: Congenital myasthenic syndrome, acetazolamide-responsive  - Genetic Testing Registry: Endplate acetylcholinesterase deficiency  - Genetic Testing Registry: Familial infantile myasthenia  - Genetic Testing Registry: Myasthenia, limb-girdle, familial  - Genetic Testing Registry: Myasthenic syndrome, congenital, associated with acetylcholine receptor deficiency  - Genetic Testing Registry: Myasthenic syndrome, slow-channel congenital   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care + GHR + congenital myasthenic syndrome
What is (are) tetrahydrobiopterin deficiency ?
Tetrahydrobiopterin deficiency is a rare disorder characterized by a shortage (deficiency) of a molecule called tetrahydrobiopterin or BH4. This condition alters the levels of several substances in the body, including phenylalanine. Phenylalanine is a building block of proteins (an amino acid) that is obtained through the diet. It is found in foods that contain protein and in some artificial sweeteners. High levels of phenylalanine are present from early infancy in people with untreated tetrahydrobiopterin deficiency. This condition also alters the levels of chemicals called neurotransmitters, which transmit signals between nerve cells in the brain.  Infants with tetrahydrobiopterin deficiency appear normal at birth, but medical problems ranging from mild to severe become apparent over time. Signs and symptoms of this condition can include intellectual disability, progressive problems with development, movement disorders, difficulty swallowing, seizures, behavioral problems, and an inability to control body temperature. + GHR + tetrahydrobiopterin deficiency
How many people are affected by tetrahydrobiopterin deficiency ?
This condition is rare, affecting an estimated 1 in 500,000 to 1 in 1 million newborns. In most parts of the world, tetrahydrobiopterin deficiency accounts for 1 to 3 percent of all cases of elevated phenylalanine levels. The remaining cases are caused by a similar condition called phenylketonuria (PKU). In certain countries, including Saudi Arabia, Taiwan, China, and Turkey, it is more common for elevated levels of phenylalanine to be caused by tetrahydrobiopterin deficiency than by PKU. + GHR + tetrahydrobiopterin deficiency
What are the genetic changes related to tetrahydrobiopterin deficiency ?
Tetrahydrobiopterin deficiency can be caused by mutations in one of several genes, including GCH1, PCBD1, PTS, and QDPR. These genes provide instructions for making enzymes that help produce and recycle tetrahydrobiopterin in the body. Tetrahydrobiopterin normally helps process several amino acids, including phenylalanine. It is also involved in the production of neurotransmitters.  If one of the enzymes fails to function correctly because of a gene mutation, little or no tetrahydrobiopterin is available to help process phenylalanine. As a result, phenylalanine can build up in the blood and other tissues. Because nerve cells in the brain are particularly sensitive to phenylalanine levels, excessive amounts of this substance can cause brain damage. Tetrahydrobiopterin deficiency can also alter the levels of certain neurotransmitters, which disrupts normal brain function. These abnormalities underlie the intellectual disability and other characteristic features of the condition. + GHR + tetrahydrobiopterin deficiency
Is tetrahydrobiopterin deficiency inherited ?
This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. + GHR + tetrahydrobiopterin deficiency
What are the treatments for tetrahydrobiopterin deficiency ?
These resources address the diagnosis or management of tetrahydrobiopterin deficiency:  - Baby's First Test: Biopterin Defect in Cofactor Biosynthesis  - Baby's First Test: Biopterin Defect in Cofactor Regeneration  - Genetic Testing Registry: 6-pyruvoyl-tetrahydropterin synthase deficiency  - Genetic Testing Registry: Dihydropteridine reductase deficiency  - Genetic Testing Registry: GTP cyclohydrolase I deficiency  - Genetic Testing Registry: Hyperphenylalaninemia, BH4-deficient, D  - MedlinePlus Encyclopedia: Serum Phenylalanine Screening   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care + GHR + tetrahydrobiopterin deficiency
What is (are) glycogen storage disease type V ?
Glycogen storage disease type V (also known as GSDV or McArdle disease) is an inherited disorder caused by an inability to break down a complex sugar called glycogen in muscle cells. A lack of glycogen breakdown interferes with the function of muscle cells.  People with GSDV typically experience fatigue, muscle pain, and cramps during the first few minutes of exercise (exercise intolerance). Exercise such as weight lifting or jogging usually triggers these symptoms in affected individuals. The discomfort is generally alleviated with rest. If individuals rest after brief exercise and wait for their pain to go away, they can usually resume exercising with little or no discomfort (a characteristic phenomenon known as "second wind").  Prolonged or intense exercise can cause muscle damage in people with GSDV. About half of people with GSDV experience breakdown of muscle tissue (rhabdomyolysis). In severe episodes, the destruction of muscle tissue releases a protein called myoglobin, which is filtered through the kidneys and released in the urine (myoglobinuria). Myoglobin causes the urine to be red or brown. This protein can also damage the kidneys, and it is estimated that half of those individuals with GSDV who have myoglobinuria will develop life-threatening kidney failure.  The signs and symptoms of GSDV can vary significantly in affected individuals. The features of this condition typically begin in a person's teens or twenties, but they can appear anytime from infancy to adulthood. In most people with GSDV, the muscle weakness worsens over time; however, in about one-third of affected individuals, the muscle weakness is stable. Some people with GSDV experience mild symptoms such as poor stamina; others do not experience any symptoms. + GHR + glycogen storage disease type V
How many people are affected by glycogen storage disease type V ?
GSDV is a rare disorder; however, its prevalence is unknown. In the Dallas-Fort Worth area of Texas, where the prevalence of GSDV has been studied, the condition is estimated to affect 1 in 100,000 individuals. + GHR + glycogen storage disease type V
What are the genetic changes related to glycogen storage disease type V ?
Mutations in the PYGM gene cause GSDV. The PYGM gene provides instructions for making an enzyme called myophosphorylase. This enzyme is found only in muscle cells, where it breaks down glycogen into a simpler sugar called glucose-1-phosphate. Additional steps convert glucose-1-phosphate into glucose, a simple sugar that is the main energy source for most cells.  PYGM gene mutations prevent myophosphorylase from breaking down glycogen effectively. As a result, muscle cells cannot produce enough energy, so muscles become easily fatigued. Reduced energy production in muscle cells leads to the major features of GSDV. + GHR + glycogen storage disease type V
Is glycogen storage disease type V inherited ?
This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. + GHR + glycogen storage disease type V
What are the treatments for glycogen storage disease type V ?
These resources address the diagnosis or management of glycogen storage disease type V:  - Gene Review: Gene Review: Glycogen Storage Disease Type V  - Genetic Testing Registry: Glycogen storage disease, type V  - MedlinePlus Encyclopedia: McArdle syndrome   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care + GHR + glycogen storage disease type V
How many people are affected by dyskeratosis congenita ?
The exact prevalence of dyskeratosis congenita is unknown. It is estimated to occur in approximately 1 in 1 million people. + GHR + dyskeratosis congenita
What are the genetic changes related to dyskeratosis congenita ?
In about half of people with dyskeratosis congenita, the disorder is caused by mutations in the TERT, TERC, DKC1, or TINF2 gene. These genes provide instructions for making proteins that help maintain structures known as telomeres, which are found at the ends of chromosomes. In a small number of individuals with dyskeratosis congenita, mutations in other genes involved with telomere maintenance have been identified. Other affected individuals have no mutations in any of the genes currently associated with dyskeratosis congenita. In these cases, the cause of the disorder is unknown, but other unidentified genes related to telomere maintenance are likely involved.  Telomeres help protect chromosomes from abnormally sticking together or breaking down (degrading). In most cells, telomeres become progressively shorter as the cell divides. After a certain number of cell divisions, the telomeres become so short that they trigger the cell to stop dividing or to self-destruct (undergo apoptosis).  Telomeres are maintained by two important protein complexes called telomerase and shelterin. Telomerase helps maintain normal telomere length by adding small repeated segments of DNA to the ends of chromosomes each time the cell divides. The main components of telomerase, called hTR and hTERT, are produced from the TERC and TERT genes, respectively. The hTR component is an RNA molecule, a chemical cousin of DNA. It provides a template for creating the repeated sequence of DNA that telomerase adds to the ends of chromosomes. The function of the hTERT component is to add the new DNA segment to chromosome ends. The DKC1 gene provides instructions for making another protein that is important in telomerase function. This protein, called dyskerin, attaches (binds) to hTR and helps stabilize the telomerase complex.  The shelterin complex helps protect telomeres from the cell's DNA repair process. Without the protection of shelterin, the repair mechanism would sense the chromosome ends as abnormal breaks in the DNA sequence and either attempt to join the ends together or initiate apoptosis. The TINF2 gene provides instructions for making a protein that is part of the shelterin complex.  TERT, TERC, DKC1, or TINF2 gene mutations result in dysfunction of the telomerase or shelterin complexes, leading to impaired maintenance of telomeres and reduced telomere length. Cells that divide rapidly are especially vulnerable to the effects of shortened telomeres. As a result, people with dyskeratosis congenita may experience a variety of problems affecting quickly dividing cells in the body such as cells of the nail beds, hair follicles, skin, lining of the mouth (oral mucosa), and bone marrow.  Breakage and instability of chromosomes resulting from inadequate telomere maintenance may lead to genetic changes that allow cells to divide in an uncontrolled way, resulting in the development of cancer in people with dyskeratosis congenita. + GHR + dyskeratosis congenita
Is dyskeratosis congenita inherited ?
Dyskeratosis congenita can have different inheritance patterns.  When dyskeratosis congenita is caused by DKC1 gene mutations, it is inherited in an X-linked recessive pattern. The DKC1 gene is located on the X chromosome, which is one of the two sex chromosomes. In males (who have only one X chromosome), one altered copy of the gene in each cell is sufficient to cause the condition. In females (who have two X chromosomes), a mutation would have to occur in both copies of the gene to cause the disorder. Because it is unlikely that females will have two altered copies of this gene, males are affected by X-linked recessive disorders much more frequently than females. A characteristic of X-linked inheritance is that fathers cannot pass X-linked traits to their sons.  When dyskeratosis congenita is caused by mutations in other genes, it can be inherited in an autosomal dominant or autosomal recessive pattern. Autosomal dominant means one copy of the altered gene in each cell is sufficient to cause the disorder. Autosomal recessive means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. + GHR + dyskeratosis congenita
What are the treatments for dyskeratosis congenita ?
These resources address the diagnosis or management of dyskeratosis congenita:  - Gene Review: Gene Review: Dyskeratosis Congenita  - Genetic Testing Registry: Dyskeratosis congenita  - Genetic Testing Registry: Dyskeratosis congenita X-linked  - Genetic Testing Registry: Dyskeratosis congenita autosomal dominant  - Genetic Testing Registry: Dyskeratosis congenita autosomal recessive 1  - Seattle Children's Hospital   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care + GHR + dyskeratosis congenita
What is (are) familial encephalopathy with neuroserpin inclusion bodies ?
Familial encephalopathy with neuroserpin inclusion bodies (FENIB) is a disorder that causes progressive dysfunction of the brain (encephalopathy). It is characterized by a loss of intellectual functioning (dementia) and seizures. At first, affected individuals may have difficulty sustaining attention and concentrating. They may experience repetitive thoughts, speech, or movements. As the condition progresses, their personality changes and judgment, insight, and memory become impaired. Affected people lose the ability to perform the activities of daily living, and most eventually require comprehensive care.  The signs and symptoms of FENIB vary in their severity and age of onset. In severe cases, the condition causes seizures and episodes of sudden, involuntary muscle jerking or twitching (myoclonus) in addition to dementia. These signs can appear as early as a person's teens. Less severe cases are characterized by a progressive decline in intellectual functioning beginning in a person's forties or fifties. + GHR + familial encephalopathy with neuroserpin inclusion bodies