Persius/hicric huggingface dataset:
Superior cerebellar artery

# Overview
The superior cerebellar artery arises near the termination of the basilar.
It passes lateralward, immediately below the oculomotor nerve, which separates it from the posterior cerebral artery, winds around the cerebral peduncle, close to the trochlear nerve, and, arriving at the upper surface of the cerebellum, divides into branches which ramify in the pia mater and anastomose with those of the inferior cerebellar arteries.
Several branches are given to the pineal body, the anterior medullary velum, and the tela chorioidea of the third ventricle.

# Areas Supplied
- Superior half of the cerebellum
- Parts of the midbrain
Superior epigastric artery
In human anatomy, superior epigastric artery refers to a blood vessel that carries oxygenated blood and arises from the internal thoracic artery (referred to as the internal mammary artery in the accompanying diagram).  It anastomoses with the inferior epigastric artery at the umbilicus and supplies the anterior part of the abdominal wall and some of the diaphragm.
Along its course, it is accompanied by a similarly named vein, the superior epigastric vein.

# Collateralization in vascular disease and aortic coarctation
The superior epigastric arteries, inferior epigastric arteries, internal thoracic arteries and left subclavian artery/brachiocephalic and right subclavian artery are collateral vessels to the thoracic aorta and abdominal aorta.
If the abdominal aorta develops a significant stenosis and/or blockage (as may be caused by atherosclerosis), this collateral pathway may develop sufficiently, over time, to supply blood to the lower limbs.
A congenitally narrowed aorta, due to coarctation, is often associated with a significant enlargement of the internal thoracic and epigastric arteries.
Superior thoracic aperture
The superior thoracic aperture refers to the superior opening of the thoracic cavity.  It is also referred to anatomically as the thoracic inlet and clinically as the thoracic outlet.  It is important to note that the clinical entity called the Thoracic outlet syndrome does not refer to the inferior thoracic aperture.

# Boundaries
The thoracic inlet is essentially a hole surrounded by a bony ring, through which several vital structures pass.
The superior thoracic aperture is bounded by: the first thoracic vertebra (T1) posteriorly, the first pair of ribs laterally (more specifically, the first ribs form lateral C-shaped curves posterior to anterior), and the superior border of the manubrium anteriorly.

# Relations
The clavicles articulate with the manubrium, so form an anterior relation of thoracic inlet.
Superior to the thoracic inlet is the root of the neck, and the superior mediastinum is related inferiorly.
The brachial plexuses are superolateral relations of the thoracic inlet. The brachial plexus emerges between the anterior and middle scalene muscle, superior to the first rib and pass obliquely and inferiorly, underneath the clavicle, into the shoulder and then the arm.  Impingement of the plexus in the region of the scalenes, ribs and clavicles is responsible for thoracic outlet syndrome.

# Contents
Structures that pass through the superior thoracic aperture include:
- trachea
- oesophagus
- nerves
phrenic nerve
vagus nerve
recurrent laryngeal nerves
sympathetic trunks
- phrenic nerve
- vagus nerve
- recurrent laryngeal nerves
- sympathetic trunks
- vessels
arteries
common carotid arteries
brachiocephalic trunk
subclavian arteries
veins
internal jugular veins
brachiocephalic veins
subclavian veins
- arteries
common carotid arteries
brachiocephalic trunk
subclavian arteries
- common carotid arteries
- brachiocephalic trunk
- subclavian arteries
- veins
internal jugular veins
brachiocephalic veins
subclavian veins
- internal jugular veins
- brachiocephalic veins
- subclavian veins
- lymph nodes and lymphatic vessels
This is not an exhaustive list.  There are several other minor but important vessels and nerves passing through, and an abnormally large thyroid gland may extend inferiorly through the thoracic inlet into the superior mediastinum.
The oesophagus lies against the body of the T1 vertebra, separated from it by the prevertebral fascia, and the trachea lies in front of the oesophagus, in the midline, and may touch the manubrium.  The apices of the lungs lie to either side of the oesophagus and trachea, and separated from them by the other vessels and nerves listed above.
Sydney Children's Hospital
Sydney Children's Hospital is an Australian children's hospital located in the Eastern Suburbs of Sydney, New South Wales.
The Sydney Children's Hospital is located approximately 6 kilometres from the Sydney Central Business District in the suburb of Randwick. Sydney Childrens Hospital is also a major teaching hospital and is a teaching facility for the University of New South Wales.

# History
The Sydney Children's Hospital had its origins in 1852 with the formation of the Society for Destitute Children, which established the Asylum for Destitute Children with the first building opened on 21 March 1858 in Paddington. After an appeal for funds in 1870, the Catherine Hayes Hospital opened. The hospital's primary intention was to care for children that suffered from illness, poverty and famine.
As the hospital grew the children's hospital became a wing of the larger general hospital. In 1915, during the First World War the hospital was converted by the NSW Government into a military hospital and then a repatriation hospital, and renamed the Fourth Australian Repatriation Hospital. In 1927 an association between the Coast Hospital and the Fourth Australian Repatriation Hospital at Randwick began. With the opening of the Concord Repatriation General Hospital in 1953, the hospital was renamed the Prince of Wales Hospital, with the attached children's hospital becoming known as the Prince of Wales Children's Hospital.
In 1964 the Prince of Wales Children's Hospital was founded as an independent hospital by Professor John Beveridge, who had the goal of creating a hospital where caring for children was the main agenda. That same year the hospital became the teaching hospital for the University of New South Wales. In 1994 the hospital underwent a $46.5 million (AUD) redevelopment, greatly increasing the capabilities of the hospital.
On Friday the 12th of June 1998, the Prince of Wales Children's Hospital officially became known as the Sydney Children's Hospital, when the then current New South Wales premier, Bob Carr and Dr. Andrew Refshauge officially opened the hospital at 11:00am.
In 2003 the hospital opened a community child health facility on the Randwick campus that provides services for children with development disabilities, mental health disorders and other behavioral issues.
Tetramethylethylenediamine
Tetramethylethylenediamine, commonly known as TMEDA (or TEMED) is the chemical compound with the formula (CH3)2NCH2CH2N(CH3)2.  This species is derived from ethylene diamine by replacement of the four N-H groups with four N-methyl groups.  It has a disagreeable fishy odour.

# As a reagent in organic and inorganic synthesis
TMEDA is widely employed as a ligand for metal ions. It forms stable complexes with many metal halides, e.g. zinc chloride, copper(I) iodide, giving complexes that are soluble in organic solvents.  In such complexes, the TMEDA serves as a bidentate ligand.
Perhaps TMEDA is most renowned for its affinity for lithium ions.  It converts butyl lithium into a cluster of higher reactivity than the hexamer.  BuLi/TMEDA is able to metallate or even doubly metalate many substrates including benzene, furan, thiophene, N-alkylpyrroles, and ferrocene. Many anionic organometallic complexes have been isolated as their + complexes.  In such complexes + behaves like a quaternary ammonium salt, such as +, except that it is more resistant to deprotonation.

# Other uses
Tetramethylethylenediamine is used with ammonium persulfate to catalyze the polymerization of acrylamide in making a polyacrylamide gel, used in gel electrophoresis and Western blotting. Although the amounts used in this technique may vary from method to method, 0.1-0.2% v/v TMEDA is a "traditional" range.
Twist transcription factor
Twist-related protein 1 (TWIST1) also known as class A basic helix-loop-helix protein 38 (bHLHa38) is a basic helix-loop-helix transcription factor that in humans is encoded by the TWIST1 gene.

# Function
Basic helix-loop-helix (bHLH) transcription factors have been implicated in cell lineage determination and differentiation. The protein encoded by this gene is a bHLH transcription factor and shares similarity with another bHLH transcription factor, Dermo1 (a.k.a. TWIST2). The strongest expression of this mRNA is in placental tissue; in adults, mesodermally derived tissues express this mRNA preferentially.
Twist1 is thought to regulate osteogenic lineage.

# Clinical significance
Mutations in the TWIST1 gene are associated with Saethre-Chotzen syndrome, breast cancer, and Sezary Syndrome.

## As an oncogene
Twist plays an essential role in cancer metastasis. Over-expression of Twist or methylation of its promoter is common in metastatic carcinomas.  Hence targeting Twist has a great promise as a cancer therapeutic. In cooperation with N-Myc, Twist-1 acts as an oncogene in several cancers including neuroblastoma.
Twist is activated by a variety of signal transduction pathways, including Akt, signal transducer and activator of transcription 3 (STAT3), mitogen-activated protein kinase, Ras, and Wnt signaling. Activated Twist upregulates N-cadherin and downregulates E-cadherin, which are the hallmarks of EMT. Moreover, Twist plays an important role in some physiological processes involved in metastasis, like angiogenesis, invadopodia, extravasation, and chromosomal instability. Twist also protects cancer cells from apoptotic cell death. In addition, Twist is responsible for the maintenance of cancer stem cells and the development of chemotherapy resistance. Twist1 is extensively studied for its role in head- and neck cancers. Here and in epithelial ovarian cancer, Twist1 has been shown to be involved in evading apoptosis, making the tumour cells resistant against platinum-based chemotherapeutic drugs like cisplatin. Moreover, Twist1 has been shown to be expressed under conditions of hypoxia, corresponding to the observation that hypoxic cells respond less to chemotherapeutic drugs.
Another process in which Twist 1 is involved is tumour metastasis. The underlying mechanism is not completely understood, but it has been implicated in the upregulation of matrix metalloproteinases and inhibition of TIMP.
Recently, targeting Twist has gained interest as a target for cancer therapeutics. The inactivation of Twist by small interfering RNA or chemotherapeutic approach has been demonstrated in vitro. Moreover, several inhibitors which are antagonistic to the upstream or downstream molecules of Twist signaling pathways have also been identified.
For example, thymoquinone, a natural product downregulates TWIST1 transcription factor to reduce epithelial to mesenchymal transition, and thus inhibits cancer metastasis in cancer cell lines and xenograft model of breast cancer in mouse 

# Interactions
Twist transcription factor has been shown to interact with EP300, TCF3 and PCAF.
The heart in breast cancer

# Histopathological Findings
Image courtesy of Professor Peter Anderson DVM PhD and published with permission  PEIR, University of Alabama at Birmingham, Department of Pathology
- Heart; Breast intraductal papilloma metastasis. Thrombotic Nonbacterial Endocarditis (Infected): Gross mitral valve natural color vegetations well illustrated these were secondarily infected with staphylococcus case of 8 year survival breast intraductal papillary adenocarcinoma with extensive metastases. Aortic valve also involved
- Thrombotic Nonbacterial Endocarditis Infected: Micro low mag H&E fibrin vegetation with masses of staphylococci and inflammatory cells in valve secondarily infected case 8 year survival breast papillary intraductal adenocarcinoma with extensive metastases gross is aortic valve lesions.
- Thrombotic Nonbacterial Endocarditis Infected: Gross close-up natural color vegetations or aortic cusps well shown secondarily infected with staphylococci micro is mitral valve also involved see and case of 8 year survival breast intraductal papillary adenocarcinoma with extensive metastases
- Thrombotic Nonbacterial Endocarditis Infected: Micro low mag H&E large masses staphylococci in vegetation valvulitis is seen gross is mitral valve also involved and case of 8 year survival breast intraductal papillary adenocarcinoma with extensive metastases
- Heart: Metastatic Carcinoma Breast: Gross, natural color, external view with lesions over right ventricle. Typical and good example
- Heart: Metastatic Carcinoma Breast: Gross, close up view, atrial epicardial lesions, breast cancer is the primary.
The heart in osteosarcomas

# Histopathological Findings
Image courtesy of Professor Peter Anderson DVM PhD and published with permission  PEIR, University of Alabama at Birmingham, Department of Pathology
- HEART; Osteosarcoma. Most cardiac osteosarcomas have spindled areas in addition to differentiated osteosarcoma (note osteoid, lower portion of field). The patient was a 16-year-old boy with a left atrial mass; the tumor recurred in 13 months at the site of the chest wall incision.
- HEART; Osteosarcoma. There are atypical cells within an osteoid matrix.
- HEART: Right atrium. The patient was a 21-year-old woman with a history of osteosarcoma of the humerus resected 9 years previously. Note the relatively sharp demarcation between tumor and cardiac muscle. The specimen was a surgical biopsy of a single cardiac metastasis.
Thiabendazole how supplied

# How Supplied
No. 3331  MINTEZOL Suspension, 500 mg per 5 mL, is white to off-white and is supplied as follows:
- NDC 0006-3331-60 in bottles of 120 mL (6505-00-935-5835, 0.5 g/5 mL, 120 mL).
- Storage: Store in a well-closed container at controlled room temperature . Protect from freezing.
No. 3332  MINTEZOL Chewable Tablets, 500 mg, are white to off-white, orange-flavored, round, scored, compressed tablets, coded MSD 907 on one side and MINTEZOL on the other. They are supplied as follows:
- NDC 0006-0907-36 unit dose packages of 36 (6505-01-226-9909, 500 mg chewable, individually sealed 36's).
- Storage: Store in a well-closed container at controlled room temperature .
Thrombotic microangiopathy

# Overview
Thrombotic microangiopathies are a category of pathologies that result in thrombosis in capillaries and arterioles. This process leads to thrombocytopenia and a variety of other symptoms such as: anemia, purpura, renal failure (some), schistocytes (fragmented blood cells severed by fibrin products) and ischemic injury to cells.

# Categories
Bacterial toxins are the primary cause of one category of thrombotic microangiopathy known as HUS or hemolytic uremic syndrome. The other major category is TTP or thrombotic thrombocytopenic purpura caused by autoimmune or hereditary dysfunctions that activate the coagulation cascade or the complement system.
Some sources group TTP and HUS together, while other sources express skepticism about their common pathophysiology.

# Presentation
The clinical presentation typically includes: fever, microangiopathic hemolytic anemia (see schistocytes in a blood smear), renal failure, thrombocytopenia, neurological manifestations.
Thyroxine-binding globulin
Thyroxine-binding globulin (TBG) binds thyroid hormone in circulation. It is one of three proteins (along with transthyretin and albumin) responsible for carrying the thyroid hormones thyroxine (T4) and 3,5,3-triiodothyronine (T3) in the bloodstream. Of these three proteins, TBG has the highest affinity for T4 and T3, but is present in the lowest concentration.  Despite its low concentration, TBG carries the majority of T4 in the blood.  Due to the very low concentration of T4 & T3 in the blood, TBG is rarely more than 25% saturated with its ligand. Unlike transthyretin and albumin, TBG has a single binding site for T4/T3. TBG is synthesized primarily in the liver as a 54 kDa protein. In terms of genomics, TBG is a serpin; however, it has no inhibitory function like many other members of this class of proteins.

# Role in Diagnosis
TBG tests are sometimes used in finding the reason for elevated or diminished levels of thyroid hormone.  This is done by measuring resin binding to labeled thyroid hormone, which happens only when the labeled thyroid hormone is free.
The patient's serum is mixed with the labeled thyroid hormone; then, the resin is added to the whole mixture to measure the amount of free labeled thyroid hormone.  So, for instance, if the patient is truly hypothyroid, and TBG levels are normal, then there are many sites open for binding on the TBG, since the total thyroid hormone level is low.  Therefore, when the labeled hormone is added, it will bind mostly to the TBG, leaving little of it left for binding to the resin.  In contrast, however, if the patient is truly hyperthyroid, and TBG levels are normal, the patient's endogenous hormone will saturate the TBG binding sites more, leaving less room for the labeled hormone, which allows greater binding to the resin.
In the situations described above, TBG testing is not very useful.  However, if total thyroid hormone levels point to hypothyroidism or hyperthyroidism in the absence of accompanying symptoms, the utility of TBG testing becomes more evident, since TBG production can be modified by other factors such as estrogen levels, corticosteroid levels, or liver failure.  If, for example, the TBG level is high, which can occur when estrogen levels are high, the TBG will bind more thyroid hormone, decreasing the free hormone available in the blood, which leads to stimulation of TSH, and the production of more thyroid hormone.  In this case, the total thyroid hormone level will be high.  And so, when labeled hormone is added, since TBG is so high, it will bind to the TBG, leaving little free labeled hormone for uptake into the resin.  On the converse, in the presence of corticosteroids, which lower TBG levels, the total thyroid hormone (bound and free) in the blood will be low.  Thus, when the labeled hormone is added, since so little TBG is available in the blood, only a small portion of it will bind, leaving plenty available for uptake by the resin.
Thyroid hormone resistance

# Overview
Thyroid hormone resistance describes a rare syndrome where the thyroid hormone levels are elevated but the thyroid stimulating hormone (TSH) level is not suppressed, or not completely suppressed as would be expected.

# Causes
The most common cause of the syndrome are mutations of the  (beta) form of the thyroid hormone receptor, of which over 100 different mutations have been documented.

# Incidence
Thyroid hormone resistance syndrome is rare, incidence is variously quotes as 1 in 50,000 or 1 in 40,000 live births.

# Presentation
The syndrome can present with variable symptoms, even between members of the same family harboring the same mutation. Typically most or all tissues are resistant to thyroid hormone, so despite raised measures of serum thyroid hormone the individual may appear euthyroid (have no symptoms of over- or underactivity of the thyroid gland). The most common symptoms are goiter and tachycardia. It has also been linked to some cases of attention deficit hyperactivity disorder (ADHD), although the majority of people with that diagnosis have no thyroid problems.

# Diagnosis
The characteristic blood test results for this disorder can also be found in other disorders (for example TSH-oma (pituitary adenoma), or other pituitary disorders). The diagnosis may involve identifying a mutation of the thyroid receptor. Yet, since discovery of resistance to thyroid hormones in the absence of thyroid hormone receptor beta mutations, lack of a mutation in a patient does not rule out resistance.

# Terminology
Sometimes the phrase thyroid hormone resistance is used to identify cases where patients with autoimmune thyroid disorders respond poorly to normal doses of replacement thyroid hormone, this is thought to occur where patients have developed antibodies to thyroid hormones. Antibodies to thyroid hormones quite commonly occur in such disorders, and may interfere with the normal clinical assays used in monitoring such disorders, and in unusual cases may have further independent clinical significance.
Toledo Children's Hospital
Toledo Children's Hospital is a public, children's hospital located in Toledo, Ohio.
Toledo Children's is located within the The Toledo Hospital and adminstratively is part of the ProMedica Health System.  It is a level I trauma center and has 151 beds, 78 of which being intensive care.

# Statistics
4,856 patients were under the care of Toledo Children's Hospital in 2006. The hospital treated 26,469 emergencies and performed almost 2000 surgeries the same year.
Tramadol drug interactions

# List of drug interactions
Use with Carbamazepine
Use with Quinidine
Use with Inhibitors of CYP2D6
Use with Cimetidine
Use with MAO Inhibitors
Use with Digoxin
Use with Warfarin Like Compounds

## Use with Carbamazepine
Patients taking carbamazepine may have a significantly reduced analgesic effect of tramadol. Because
carbamazepine increases tramadol metabolism and because of the seizure risk associated with tramadol
concomitant administration of Tramadol and carbamazepine is not recommended. Return to top

## Use with Quinidine
Tramadol is metabolized to M1 by CYP2D6. Quinidine is a selective inhibitor of that isoenzyme; so
that concomitant administration of quinidine and tramadol results in increased concentrations of
tramadol and reduced concentrations of M1. The clinical consequences of these findings are unknown.
In vitro drug interaction studies in human liver microsomes indicate that tramadol has no effect on
quinidine metabolism. Return to top

## Use with Inhibitors of CYP2D6
In vitro drug interaction studies in human liver microsomes indicate that concomitant administration
with inhibitors of CYP2D6 such as fluoxetine, paroxetine, and amitriptyline could result in some
inhibition of the metabolism of tramadol. Return to top

## Use with Cimetidine
Concomitant administration of Tramadol and cimetidine has not been studied. Concomitant
administration of tramadol and cimetidine does not result in clinically significant changes in tramadol
pharmacokinetics. Therefore, no alteration of the Tramadol dosage regimen is recommended. Return to top

## Use with MAO Inhibitors
Interactions with MAO Inhibitors, due to interference with detoxification mechanisms, have been
reported for some centrally acting drugs. Return to top

## Use with Digoxin
Post-marketing surveillance of tramadol has revealed rare reports of digoxin toxicity. Return to top

## Use with Warfarin Like Compounds
Post-marketing surveillance of both tramadol and acetaminophen individual products have revealed rare
alterations of warfarin effect, including elevation of prothrombin times.
While such changes have been generally of limited clinical significance for the individual products,
periodic evaluation of prothrombin time should be performed when Tramadol and warfarin-like
compounds are administered concurrently. Return to top
Adapted from the FDA Package Insert.