Persius/hicric huggingface dataset:
Vascular closure devices

# Vascular Closure Devices
At the very heart of any successful endovascular procedure is successful arterial entry and exit. The first successful cardiac catheterization, according to Andre Cournand, was performed on an equine patient in 1844 utilizing a retrograde approach through both the jugular vein and carotid artery. Human retrograde left heart catheterization was first reported by Zimmerman and Limon-Lason in 1950. Shortly thereafter in 1953, Seldinger developed the percutaneous technique and this technique was quickly adapted to left heart cardiac catheterizations. With the growth of Interventional Cardiology in the years following Gruntzigs introduction of coronary angioplasty in 1977, the percutaneous approach became, and today remains, by far the most common method of performing catheterization, angiography and endovascular intervention.
Within the realm of percutaneous approaches, the majority of the procedures are performed from the femoral approach, with a minority being done from a radial approach. Brachial and axillary are also used in a minority of procedures. Reasons for the continued preference of the femoral route for access includes the vessel size, operator training and equipment, radiation exposure (operator), and the advent of vascular closure devices. Studies have suggested that between 8-10% of all patients selected for a transradial approach will convert to a transfemoral route.  

## Current Limitations of Vascular Closure Devices
- Require long learning curve
- Small vessel size (<4.05.0mm); a contraindication to use
- Non-common femoral artery sticks; a contraindication to use
- Peripheral vascular disease; a contraindication to use (very common problem)
- Significant endoluminal device components (prone to thrombosis)
- High costs
- Require bed rest post closure
- Impaired or delayed common femoral artery re-entry (re-access concerns)
- Non-inert, very reactive, permanent and absorbable device components (therefore may be prone to infection and common femoral artery scarring)
- Catastrophic complications (12%, but may be under-reported)
- Poorly compatible with anticoagulated patients (increased bleeding)

## Complications

### Infection
- After an incubation period of 2 to 29 days (average of 8 days) a vascular closure device infection can occur.
- Symptoms include local pain and fever. The pain may improve and then worsen.
- Blood cultures are positive
- Most common pathogen is staphylococcus aureus infecting a mycotic aneurysm
- Medical and surgical treatment are both required

# 2011 ACCF/AHA/SCAI Guidelines for Percutaneous Coronary Intervention (DO NOT EDIT)

## Vascular Closure Devices (DO NOT EDIT)
Vertebral artery disease

# Overview
Vertebral artery disease can be caused by a number of factors that narrow the vertebral arteries supplying the brain stem. It causes symptoms mainly because the brain stem does not get sufficient blood. The two vertebral arteries join to form a single artery at the base of the brain. Usually, if one vertebral artery is not narrowed it will be sufficient to supply blood to the brainstem.

# Complications
One of the complications is vertebral artery dissection. It is the development of dissection (a flap-like tear) in the vertebral artery. It is commonly associated with physical trauma but may also develop spontaneously. It is a major cause of stroke in young people.

# Diagnosis

# 2011 ASA/ACCF/AHA/AANN/AANS/ACR/ASNR/CNS/SAIP/SCAI/SIR/SNIS/SVM/SVS Guideline on the Management of Patients With Extracranial Carotid and Vertebral Artery Disease (DO NOT EDIT)

## Vascular Imaging in Patients with Vertebral Artery Disease (DO NOT EDIT)

## Management of Atherosclerotic Risk Factors in Patients with Vertebral Artery Disease (DO NOT EDIT)
Vesicointestinal fistula
Synonyms and keywords: Vesicoenteric fistula

# Overview
A vesicointestinal fistula (or intestinovesical fistula) is a form of fistula between the bladder and the bowel.

# Types
A fistula involving the bladder can have one of many specific names, describing the specific location of its outlet:
- bladder and intestine: "vesicoenteric", "enterovesical", or "vesicointestinal"  GE)
- bladder and colon: "vesicocolic" or "colovesical" (Template:GPnotebook)
- bladder and rectum: "vesicorectal" or "rectovesical" (Template:DiseasesDB)

# Symptoms/signs
If fecal matter passes through the fistula into the bladder, the existence of the fistula may be revealed by pneumaturia or fecaluria.
Voriconazole description

# Description
VFEND (voriconazole), a triazole antifungal agent is available as a lyophilized powder for solution for intravenous infusion, film-coated tablets for oral administration, and as a powder for oral suspension. The structural formula is:
Voriconazole is designated chemically as (2R,3S)-2-(2, 4-difluorophenyl)-3-(5-fluoro-4-pyrimidinyl)-1-(1H-1,2,4-triazol-1-yl)-2-butanol with an empirical formula of C16H14F3N5O and a molecular weight of 349.3.
Voriconazole drug substance is a white to light-colored powder.
VFEND I.V. is a white lyophilized powder containing nominally 200 mg voriconazole and 3200 mg sulfobutyl ether beta-cyclodextrin sodium in a 30 mL Type I clear glass vial.
VFEND I.V. is intended for administration by intravenous infusion. It is a single-dose, unpreserved product. Vials containing 200 mg lyophilized voriconazole are intended for reconstitution with Water for Injection to produce a solution containing 10 mg/mL VFEND and 160 mg/mL of sulfobutyl ether beta-cyclodextrin sodium. The resultant solution is further diluted prior to administration as an intravenous infusion.
VFEND Tablets contain 50 mg or 200 mg of voriconazole. The inactive ingredients include lactose monohydrate, pregelatinized starch, croscarmellose sodium, povidone, magnesium stearate and a coating containing hypromellose, titanium dioxide, lactose monohydrate and triacetin.
VFEND for Oral Suspension is a white to off-white powder providing a white to off-white orange-flavored suspension when reconstituted. Bottles containing 45 g powder for oral suspension are intended for reconstitution with water to produce a suspension containing 40 mg/mL voriconazole. The inactive ingredients include colloidal silicon dioxide, titanium dioxide, xanthan gum, sodium citrate dihydrate, sodium benzoate, anhydrous citric acid, natural orange flavor, and sucrose.
Wee1-like protein kinase
WEE1 homolog (S. pombe), also known as WEE1, is a protein which in humans is encoded by the WEE1 gene.

# Function
This gene encodes a nuclear protein, which is a tyrosine kinase belonging to the Ser/Thr family of protein kinases. This protein catalyzes the inhibitory tyrosine phosphorylation of CDC2/cyclin B kinase, and appears to coordinate the transition between DNA replication and mitosis by protecting the nucleus from cytoplasmically activated CDC2 kinase.

# Interactions
Wee1-like protein kinase has been shown to interact with YWHAB and PIN1.
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Women's College Hospital
Women's College Hospital, or The New Women's College Hospital is a teaching hospital in downtown Toronto.
Women's College Hospital maintains a focus on women's health, research in women's health, and ambulatory care. It was given the distinction of being the only 'collaborating centre' in the Western Hemisphere designated by the World Health Organization.
The hospital was founded on October 1, 1883 as Women's Medical College, and was the first medical school in Toronto to admit women as students.  It currently functions as an independent ambulatory care hospital.  It moved to its current location in Toronto in 1935, and became a teaching hospital affiliated with the University of Toronto in 1961.
Women's College Hospital merged with Sunnybrook Hospital and the Orthopedic and Arthritic Hospital in 1998 under the provisions of Ontario Bill 51, and became Sunnybrook and Women's College Health Sciences Centre.  Women's College Hospital de-amalgamated in 2006 to become The New Women's College Hospital.
In 2003, while still part of the erstwhile "Sunnybrook and Women's College Health Sciences Centre", the Women's College site housed the first ambulatory SARS clinic in Canada, (while the Sunnybrook site housed both the first in-patient SARS unit and Intensive Care Unit for SARS in Canada).
The Physician-in-chief is Dr. Gillian Hawker.
Affiliate site: /
Zinc finger protein 804A
Zinc finger protein 804A is a protein that in humans is encoded by the ZNF804A gene. The human gene maps to chromosome 2 q32.1 and consists of 4 exons that code for a protein of 1210 amino acids (137 kDa).
Little is known about the characteristics and function of the encoded protein. However, the protein sequence codes for a domain characteristic of a classical C2H2-type zinc finger near the N-terminal end.

# Interactions
ZNF804A binds to the N-terminus of ATXN1.

## Binding of DNA
The tertiary structure of the C2H2 finger consists of a beta hairpin folded against an alpha helix. The folding occurs via a zinc(II) ion that coordinates to two cysteine residues (one on each beta sheet) and two histidine residues (both on the -helix). ZNF804A might use its zinc finger to bind DNA in a sequence-specific manner. For example, Carl Pabo and his colleagues in 1991 discovered that mouse transcription factor Zif268 binds DNA using three linked C2H2 zinc fingers. Amino acid residues sticking out from the -helices of the zinc fingers interact with the guanine-rich region of the DNA double helix through hydrogen bonds and electrostatic and hydrophobic interactions. The spacing of the residues matches the spacing of the base pairs. Zinc fingers fit into the major groove and wrap around the DNA helix for almost one turn.

# Association with schizophrenia
In humans, ZNF804A is expressed broadly throughout the brain, especially in the developing hippocampus and the cortex, as well as in the adult cerebellum. ZNF804A is expected to bind DNA and thus regulate gene expression like other zinc finger proteins. The mouse homologue of ZNF804A, zfp804a, has recently been reported as a target for HOXC8, suggesting that ZNF804A may be involved in the regulation of early neurodevelopment.
A Genome-wide association study (GWAS) has identified ZNF804A as a susceptibility gene for schizophrenia. From family, twin, and adoption studies, schizophrenia is found to have heritability of ~80% and it is suspected that risk results from multiple genetic variants of small effect. The single-nucleotide polymorphism (SNP) rs1344706 in intron 2 of ZNF804A has been identified as a variant that is most strongly associated with schizophrenia.
The same SNP has been reported to correlate with slightly disturbed functional coupling of several brain regions in healthy persons, resembling the changes described in schizophrenia. A further study revealed that the SNP rs1344706 was consistent with schizophrenia association in European patients, but not in Han Chinese patients. Moreover, the study showed that SNPs rs1021042 and rs359895 are associated with schizophrenia in Han Chinese patients, and that the rs359895 allele increases the promoter activity of ZNF804A. The results of another study suggest that there is no relationship between variant rs1344706 and impaired cognitive function in schizophrenia patients and the results of yet another study indicate that ZNF804A also plays a role in how schizophrenia symptoms respond to antipsychotics.
Zolmitriptan description

# Description
Zolmitriptan orally disintegrating tablets contain zolmitriptan, which is a selective 5-hydroxytryptamine1B/1D (5-HT1B/1D) receptor agonist. Zolmitriptan is chemically designated as (S)-4--1H-indol-5-yl]methyl]-2-oxazolidinone and has the following chemical structure:
The molecular formula is C16H21N3O2, representing a molecular weight of 287.36. Zolmitriptan is a white to off-white powder that is soluble in methanol and acetone, insoluble in water.
Zolmitriptan orally disintegrating tablets are available as 2.5 mg and 5 mg white uncoated tablets for oral administration. The orally disintegrating tablets contain mannitol, microcrystalline cellulose, crospovidone, aspartame , colloidal silicon dioxide, talc, magnesium stearate and peppermint flavor. The peppermint flavor contains corn starch.
2,3-Bisphosphoglycerate
2,3-Bisphosphoglycerate (2,3-BPG, also known as 2,3-diphosphoglycerate or 2,3-DPG) is a three carbon isomer of the glycolytic intermediate 1,3-bisphosphoglycerate. 2,3-BPG is present in human red blood cells (RBC; erythrocyte) at approximately 5 mmol/L. It binds with greater affinity to deoxygenated hemoglobin (e.g. when the red cell is near respiring tissue) than it does to oxygenated hemoglobin (e.g. in the lungs). In bonding to partially deoxygenated hemoglobin it allosterically upregulates the release of the remaining oxygen molecules bound to the hemoglobin, thus enhancing the ability of RBCs to release oxygen near tissues that need it most.
Recently, scientists have found the similarities between low amounts of 2,3-BPG with the occurrence of HAPE at high altitudes.
Its function was discovered in 1967 by Reinhold Benesch and Ruth Benesch.

# Metabolism
2,3-BPG is formed from 1,3-BPG by an enzyme called bisphosphoglycerate mutase. It is broken down by a phosphatase to form 3-phosphoglycerate. Its synthesis and breakdown are therefore a way around a step of glycolysis.

# Effects of binding
When 2,3-BPG binds deoxyhemoglobin, it acts to stabilize the low oxygen affinity state (T state) of the oxygen carrier. It fits neatly into the cavity of the deoxy- conformation, exploiting the molecular symmetry and positive polarity by forming salt bridges with lysine and histidine residues in the four subunits of hemoglobin. The R state, with oxygen bound to a heme group, has a different conformation and does not allow this interaction.
By selectively binding to deoxyhemoglobin, 2,3-BPG stabilizes the T state conformation, making it harder for oxygen to bind hemoglobin and more likely to be released to adjacent tissues.  2,3-BPG is part of a feedback loop that can help prevent tissue hypoxia in conditions where it is most likely to occur. Conditions of low tissue oxygen concentration such as high altitude (2,3-BPG levels are higher in those acclimated to high altitudes), airway obstruction, or congestive heart failure will tend to cause RBCs to generate more 2,3-BPG in their effort to generate energy by allowing more oxygen to be released in tissues deprived of oxygen. Ultimately, this mechanism increases oxygen release from RBCs under circumstances where it is needed most. This release is potentiated by the Bohr effect in tissues with high energetic demands.

# Fetal hemoglobin
Interestingly, fetal hemoglobin (HbF) exhibits a low affinity for 2,3-BPG, resulting in a higher binding affinity for oxygen.  This increased oxygen binding affinity relative to that of adult hemoglobin (HbA) is due to HbF having two / dimers as opposed to the two / dimers of HbA.  The positive histidine residues of HbA -subunits that are essential for forming the 2,3-BPG binding pocket are replaced by serine residues in HbF -subunits.
Alpha-ketoglutaric acid

# Overview
Alpha-ketoglutaric acid is one of two ketone derivatives of glutaric acid. (The term "ketoglutaric acid," when not further qualified, almost always refers to the alpha variant. Beta-ketoglutaric acid varies only by the position of the ketone functional group, and is much less common.)
Its anion, Alpha-ketoglutarate (also called oxo-glutarate) is an important biological compound.  It is the keto acid produced by de-amination of glutamate, and is an intermediate in the Krebs cycle.

# Functions

## Krebs cycle
It is a key intermediate in the Krebs cycle, coming after isocitrate and before succinyl CoA. Anaplerotic reactions can replenish the cycle at this juncture by synthesizing alpha-ketoglutarate from transamination of glutamate, or through action of glutamate dehydrogenase on glutamate.

## Formation of amino acids
Glutamine is synthesized from glutamate by glutamine synthase, which utilizes an ATP to form glutamyl phosphate; this intermediate is attacked by ammonia as a nucleophile giving glutamine and inorganic phosphate.

## Nitrogen transporter
Another function is to combine with nitrogen released in the cell, therefore preventing nitrogen overload.
Alpha-ketoglutarate is one of the most important nitrogen transporter in metabolic pathways. The amino groups of amino acids are attached to it by transamination and carried to the liver where the urea cycle takes place.
Alpha-ketoglutarate is transaminated, along with glutamine, to form the excitatory neurotransmitter glutamate.  Glutamate can then be decarboxylated (requiring vitamin B6) into the inhibitory neurotransmitter GABA.
It is reported that high ammonia and/or high nitrogen levels may occur with high protein intake, excessive aluminum exposure, autism, Reye's syndrome, cirrhosis, and urea cycle disorder.

## Relationship to molecular oxygen
Acting as a co-substrate, it also plays important function in oxidation reactions involving molecular oxygen.
Molecular oxygen (O2) directly oxidizes many compounds to produce useful products in an organism, such as antibiotics, etc., in reactions catalyzed by oxygenases.  In many oxygenases, alpha-ketoglutarate helps the reaction by being oxidized together with the main substrate.  In fact, one of the alpha-ketoglutarate-dependent oxygenases is an O2 sensor, informing the organism the oxygen level in its environment.

## Dietary supplement
Alpha-ketoglutaric acid is sold as a dietary supplement and to body builders as AKG or a-KG. Some believe it increases stamina.

# Production
Alpha-ketoglutarate can be produced by
- Oxidative decarboxylation of isocitrate by isocitrate dehydrogenase;
- Oxidative deamination of glutamate by glutamate dehydrogenase.
3,4-Dimethylamphetamine
3,4-dimethylamphetamine (Xylopropamine, ,3,4-trimethylphenethylamine) is a stimulant drug derived from amphetamine which was invented in the 1950s.
Xylopropamine was developed as an appetite suppressant in the 1950s and briefly sold as the sulphate salt, but it was not widely marketed. Other related amphetamine derivatives such as 2,4-dimethylamphetamine were also investigated for the same purpose, however these drugs had negative side effects such as high blood pressure and were not very successful, mainly due to the introduction of alternative drugs such as phentermine which had similar efficacy but less side effects.
Xylopropamine was also reported as having analgesic and anti-inflammatory effects but its side effects profile meant that it was never further developed for these applications.
4-Methylthioamphetamine
4-Methylthioamphetamine is a drug known as 4MT, 4-MTA, "Flatliners" or 1-(4-methylthiophenyl)-2-aminopropane. 4-MTA is currently a Class A drug in the United Kingdom although it has been suggested it be rescheduled as a Class B drug.

# Effects
4-MTA is a stimulant and strong serotonin releaser, similar to paramethoxyamphetamine but even more dangerous, as it can cause pronounced hyperthermia which can result in organ failure and death. The subjective effects of 4-MTA are primarily a long-lasting stimulant, with little positive euphoria, in contrast to MDMA. 4MTA is also a MAO-A inhibitor, which may explain its tendency to cause death, as MAOI drugs are not generally considered safe to use with stimulants or serotonin releasers, and 4-MTA fits into all three categories.

# History
It was developed by the research team led by David E. Nichols, but was intended to be used only as an agent for laboratory research into the serotonin transporter protein, and Nichols was reportedly horrified when 4-MTA appeared as a drug of abuse on the street.
4-MTA was briefly sold in smartshops in the Netherlands, though was soon banned by the Dutch government after serious side-effects started to emerge.  It was also briefly sold on the black market as MDMA during the late 1990s, mainly in the USA, but proved unpopular due to its high risk of severe side effects (several deaths were reported) and relative lack of positive euphoria.
5'-3' exoribonuclease 2
5'-3' Exoribonuclease 2 (XRN2) also known as Dhm1-like protein is an exoribonuclease enzyme that in humans is encoded by the XRN2 gene.
The human gene encoding XRN2 shares similarity with the mouse Dhm1 and the yeast's Dhp1 (Schizosaccharomyces pombe) or RAT1 (Saccharomyces) genes. The yeast gene is involved in homologous recombination and RNA metabolism, such as RNA synthesis and RNA trafficking and termination. Complementation studies show that Dhm1 has a similar function in mouse as Dhp1.

# Function
Human XRN2 is involved in the torpedo model of transcription termination.
The C. elegans homologue, XRN-2, is involved in the degradation of certain mature miRNAs and their dislodging from miRISC miRNAs.
In yeast, the Rat1 protein has been shown to also be involved in the torpedo transcription termination model. When a polyadenylation site has been detected on the nascent RNA and cleaved by the RNA polymerase II, the Rtt103 factor recruits Rat1 and attaches it to free end. The exonuclease activity of Rat1 degrades the RNA strand and halts transcriptions upon catching up to the polymerase.