Persius/hicric huggingface dataset:
Ventilation/perfusion scan

# Overview
Ventilation/perfusion scan, also called a V/Q scan, is a medical test to measure the circulation of air and blood within a patient's lungs. The ventilation part of the test evaluates the ability of air to reach all parts of the lungs, while the perfusion part measures how well the blood circulates within the lungs. This test is most commonly done in order to check for the presence of a blood clot or abnormal blood flow inside the lungs (pulmonary embolism or PE), although computed tomography with radiocontrast is now more commonly used for this purpose. A V/Q scan may also be performed in the case of serious lung disorders such as COPD or pneumonia as well as a lung performance quantification tool pre and post lung lobectomy surgery.

# Procedure
The ventilation and perfusion segments of a V/Q scan are to be performed together and must include an X-ray of the chest (posterior-anterior projection) in order to properly diagnose. A defect in the perfusion images requires a mismatched ventilation to be indicative of PE.
In the ventilation phase of the test, a gaseous radionuclide Xenon or technetium DTPA in an aerosol form is inhaled by the patient through a mouthpiece or mask that covers the nose and mouth. The perfusion phase of the test involves the intravenous injection of radioactive technetium macro aggregated albumin (Tc99m-MAA). The patient lies beneath a gamma camera which allows radioactive agents to be visualized within the lungs.

# Significance of results
Decreased uptake of the inhaled radioisotope (perfusion-ventilation match) may indicate one of the following:
- The impaired ability to breathe
- Airway obstruction
- Possible pneumonia.
Decreased circulation of the injected MAA  (perfusion-ventilation mismatch) indicates a problem with blood flow into or within the lungs. A localized area of decreased uptake, usually in a pie shaped wedge configuration when mismatched with a normal ventilation image suggests a pulmonary embolus or blood clot in the lungs.

# Risks
Although this test uses radioactive materials, total amount of radiation exposure is low. However, this test should still be administered with caution to women who are pregnant, especailly during the first trimester. If breastfeeding, patient must be councelled to refrain from this activity for approximately 24 hours.
Ventricular septum anatomy

# Normal Ventricular Septum Anatomy
The ventricular septum can be divided into four components-
- Membranous
- Inlet septum
- Trabecular septum
- Outlet or Infundibular septum
Images below shows the anatomy of normal ventricular septum
The image below shows the different parts of the ventricular septum : 1) Membranous 2) Outflow 3) Trabecular septum 4) Inflow 5) Subarterial/supracristal
In the normal heart, the ventricular septum (VS) is mostly muscular. The fibrous component is the so-called membranous septum, and is only a small part of the VS. It is integrated into the aortic root, and is made of fibrous tissue. It is located inferiorly to the inter-leaflet triangle that fills the space between the ascending hinges of the non-coronary and right coronary leaflets of the aortic valve 
When transilluminated from the right atrioventricular aspect, it can be seen, in most cases, to be crossed by the hinge of the tricuspid valve, thus dividing it into atrioventricular and interventricular components. It is then the position of the hinge which determines the proportions which are atrioventricular as opposed to interventricular 
The atrioventricular component of the septum is itself pierced by the atrioventricular conduction axis as it passes from the apex of the triangle of Koch to reach the crest of the muscular septum

## Locations of VSD
The disease occurs either due to defective growth or failure to alignment of one of these components. There are two basic different locations of VSD to be distinguished:
a. VSD located over the Crista Supraventricularis (less frequent, 4 -5 % of all VSD), are also called SUPRACRISTAL VSD or subaortic. Defect located in the outflow tract of the right ventricle.
Both the right and posterior coronary aortic valves are directly over the defect. Many times there is aortic insufficiency and rarely the aortic orifice can override the septal defect.
b. VSD located below the Crista Supraventricularis (more frequent). Also known as infracristal or subpulmonar. The defects located in front of the Conus Papillary muscle and behind the Crista are the most common variety.
There are defects behind the Conus Papilary muscle which are the posterior and basal VSD. Usually in this variety the defect size is larger than in the previous type.
There is a third variety located in the muscular interventricular septum (single or multiple orifices) (Roger disease). When the muscular VSD is multiple, resemble Swiss cheese.
Muscular VSD are bounded by muscles and not immediately related to the valves. They can be located in the apical, central, or outlet region of the ventricular septum.
Vesicular stomatitis virus
Vesicular stomatitis virus (VSV) is a virus in the family Rhabdoviridae, order Mononegavirales. The well-known Rabies virus belongs to the same family. VSV can infect insects and mammals. It has particular importance to farmers in certain regions of the world where it can infect cattle. It is also a common laboratory virus used to study the properties of viruses in the Rhabdoviridae family, as well as to study viral evolution.
VSV is an arbovirus: Natural VSV infections encompass two steps, cytolytic infections of mammalian hosts and transmission by insects. In insects, infections are non-cytolytic persistent.
Vesicular stomatitis virus (VSV) is the prototypic member of the Vesiculovirus genera of the Rhabdovirus family.  The genome of the virus is a single molecule of negative-sense RNA that encodes five major proteins: glycoprotein (G), matrix protein (M), nucleoprotein, large protein (L) and phosphoprotein.
Half the genome encodes the L protein, which combines with the phosphoprotein to catalyze replication of the mRNA.
The G protein enables viral entry to the cell by mediating both virus attachment to the host cell and fusion of the viral envelope with the endosomal membrane following endocytosis.
The mRNA encoding the vesicular stomatitis virus M protein is 831 nucleotides long, and encodes a protein of 229 amino acids.  The predicted M protein sequence does not contain any long hydrophobic or nonpolar domains that might promote membrane association.  The protein is rich in basic amino acids and contains a highly basic amino terminal domain.
The VSVG does not follow the same path as most vesicles because transport of the G protein from the endoplasmic reticulum to the plasma membrane is interrupted by incubation at 15C.  Under this condition, the molecules accumulate in both the endoplasmic reticulum (ER) and a subcellular vesicle fraction of low density called the lipid-rich vesicle fraction.  The material in the lipid-rich vesicle fraction appears to be a post-ER intermediate in the transport process to the plasma membrane (PM).  When synthesized in polarized epithelial cells, the envelope glycoproteins hemagglutinin of VSVG are targeted to the apical and basolateral plasma membranes.  VSVG is also a common coat protein for lentiviral vector expression systems used to introduce genetic material into in vitro systems or animal models.  It has the advantage or allowing the virus to infect non-dividing cells like B cells in vitro.
Vitamin D deficiency x ray

# Overview
There are no x-ray findings associated with .
OR
An x-ray may be helpful in the diagnosis of . Findings on an x-ray suggestive of/diagnostic of  include , , and .
OR
There are no x-ray findings associated with . However, an x-ray may be helpful in the diagnosis of complications of , which include , , and .

# X Ray
- There are no x-ray findings associated with .
OR
- An x-ray may be helpful in the diagnosis of . Findings on an x-ray suggestive of/diagnostic of  include:
OR
- There are no x-ray findings associated with . However, an x-ray may be helpful in the diagnosis of complications of , which include:
Wandering atrial pacemaker

# Overview
This atrial arrhythmia occurs when the natural cardiac pacemaker site shifts between the SA node, the atria, and/or the AV node. This shifting of the pacemaker from the SA node to adjacent tissues is manifested electrocardiographically by transient changes in the size shape and direction of the P waves.
A wandering pacemaker is usually caused by varying vagal tone. With increased vagal tone the SA node slows,allowing a pacemaker in the atria or AV Nodal area,which may become slightly faster briefly. After vagal tone decreases the SA node becomes the pacemaker again.Note that if the heart rate increases to above 100bpm, it is called multifocal atrial tachycardia. Possible causes are hypoxia, COPD and medication such as digoxin.

# EKG Examples
Shown below is an EKG image of a wandering atrial pacemaker. When several pacemakers are competing, p-waves with different origins and thus configurations occur. The rhythm is slightly different from beat to beat.
Copyleft image obtained courtesy of ECGpedia,
Wellbutrin SR how supplied

# How supplied
100 mg of bupropion hydrochloride
150 mg of bupropion hydrochloride
200 mg of bupropion hydrochloride
Storage

## 100 mg of bupropion hydrochloride
WELLBUTRIN SR Sustained-Release Tablets, 100 mg of bupropion hydrochloride, are blue,
round, biconvex, film-coated tablets printed with WELLBUTRIN SR 100 in bottles of 60
- (NDC 0173-0947-55) tablets. Return to top

## 150 mg of bupropion hydrochloride
WELLBUTRIN SR Sustained-Release Tablets, 150 mg of bupropion hydrochloride, are
purple, round, biconvex, film-coated tablets printed with "WELLBUTRIN SR 150" in bottles of
- (NDC 0173-0135-55) tablets. Return to top

## 200 mg of bupropion hydrochloride
WELLBUTRIN SR Sustained-Release Tablets, 200 mg of bupropion hydrochloride, are light
pink, round, biconvex, film-coated tablets printed with WELLBUTRIN SR 200 in bottles of 60
- (NDC 0173-0722-00) tablets. Return to top

## Storage
Store at controlled room temperature, 20 to 25C (68 to 77F) . Dispense in a
tight, light-resistant container as defined in the USP. Return to top
Adapted from the FDA Package Insert.
Y chromosome microdeletion
Y chromosome microdeletion (YCM) is a family of genetic disorders caused by missing gene(s) in the Y chromosome. Many men with YCM exhibit no symptoms and lead normal lives.  However, YCM is also known to be present in a significant number of men with reduced fertility. Men with reduced sperm production (in up to 20% of men with reduced sperm count, some form of YCM has been detected) varies from oligozoospermia, significant lack of sperm, or azoospermia, complete lack of sperm.
Various genes shown to have some correlation with spermatogenesis in men with reduced fertility include RBM, DAZ, SPGY, and TSPY.

# Cause
The mechanism of mutation is not different for Y-chromosome microdeletion. However, the ability to repair it differs from other chromosomes. The human Y chromosome is passed directly from father to son, and is not protected against accumulating copying errors, whereas other chromosomes are error corrected by recombining genetic information from mother and father. This may leave natural selection as the primary repair mechanism for the Y chromosome.

# Diagnosis
Y chromosome microdeletion is currently diagnosed by extracting DNA from leukocytes in a man's blood sample, mixing it with some of the about 300 known genetic markers for sequence-tagged sites (STS) on the Y chromosome, and then using polymerase chain reaction amplification and gel electrophoresis in order to test whether the DNA sequence corresponding to the selected markers is present in the DNA.
Such procedures can test only the integrity of a tiny part of the overall 23 million base pair long Y chromosome, therefore the sensitivity of such tests depends on the choice and number of markers used. Present diagnostic techniques can only discover certain types of deletions and mutations on a chromosome and give therefore no complete picture of genetic causes of infertility. They can only demonstrate the presence of some defects, but not the absence of any possible genetic defect on the chromosome.
The gold standard test for genetic mutation, namely complete DNA sequencing of a patient's Y chromosome, is still far too expensive for use in epidemiologic research or even clinical diagnostics.

# Infertility
Microdeletions in the Y chromosome have been found at a much higher rate in infertile men than in fertile controls and the correlation found may still go up as improved genetic testing techniques for the Y chromosome are developed.
18-Hydroxylase deficiency
Synonyms and keywords: CMO I deficiency; Aldosterone deficiency I; familial hyperreninemic hypoaldosteronism 1;  FHHA1A; corticosterone methyloxidase type I deficiency.

# Overview
CMO type I deficiency is an autosomal recessive disorder caused by a defect in the penultimate biochemical step of aldosterone biosynthesis, the 18-hydroxylation of corticosterone (B) to 18-hydroxycorticosterone (18-OHB). This enzymatic defect results in decreased aldosterone and salt-wasting. In CMO I deficiency, aldosterone is undetectable, whereas its immediate precursor, 18-OHB, is low or normal. These patients have an increased ratio of corticosterone to 18-OHB.
The CYP11B2 gene product also catalyzes the final step in aldosterone biosynthesis: the 18-oxidation of 18-OHB to aldosterone. A defect in that enzymatic step results in CMO type II deficiency, an allelic disorder with an overlapping phenotype but distinct biochemical features. In CMO II deficiency, aldosterone can be low or normal, but at the expense of increased secretion of 18-OHB. These patients have a low ratio of corticosterone to 18-OHB.
Aldosterone synthase (or 18-hydroxylase) is a steroid hydroxylase cytochrome P450 oxidase enzyme involved in the generation of aldosterone. The cytochrome P450 proteins are monooxygenases that catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids, and other lipids. This protein is primarily expressed in the zona glomerulosa of the adrenal cortex.  Within the cell, it localizes to the inner membrane of the mitochondria. The enzyme has steroid 18-hydroxylase activity to synthesize aldosterone and 18-oxocortisol as well as steroid 11 beta-hydroxylase activity. Mutations in this gene cause corticosterone methyl oxidase deficiency. It converts 11-deoxycorticosterone to corticosterone, to 18-hydroxycorticosterone, and finally to aldosterone
2-Methyl-2-nitrosopropane
2-Methyl-2-nitrosopropane (MNP or t-nitrosobutane, chemical formula (CH3)3CNO) is a spintrap.  This molecule forms adducts with unstable free radicals to form a more stable paramagnetic nitroxide radical that can be detected by electron spin resonance spectroscopy. It is particularly useful for trapping carbon-centered tyrosyl radicals.
MNP is also the aerial oxidation product of t-butylhydroxylamine (NtBHA),  which in turn is a hydrolysis product of phenylbutylnitrone and similar spintraps.   MNP has pharmacological action, both by scavenging free radicals and possibly by releasing the messenger substance nitric oxide in the presence of light and under oxidizing conditions.  Production of NtHBA and its parent spintrap MNP may account for the sometime antistroke action of the drug NXY-059.
MNP is also an efficient regulator of the radical polymerization of methyl methacrylate through the 'pseudoliving' chain mechanism.

# Notes
-  see J. Biol. Chem. 271 (1996), 15498-15503
-  Dmitry F Grishin,  Lyudmila L Semyonycheva,  Elena V Kolyakina (1999). ""2-Methyl-2-nitrosopropane as a new regulator of the polymer chain growth"". Mendeleev Communications. 9 (6): 250251.CS1 maint: Multiple names: authors list (link) .mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"\"""\"""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{display:none;font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
40S ribosomal protein S10
40S ribosomal protein S10 is a protein that in humans is encoded by the RPS10 gene.

# Function
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S10E family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.

# Clinical significance
Variable expression of this gene in colorectal cancers compared to adjacent normal tissues has been observed, although no correlation between the level of expression and the severity of the disease has been found.
Mutations in the RPS10 gene can cause Diamond-Blackfan anemia, a congenital anemia sometimes associated with bone marrow failure.

# Interactions
RPS10 has been shown to interact with PTTG1.
40S ribosomal protein S19
40S ribosomal protein S19 is a protein that in humans is encoded by the RPS19 gene.

# Function
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S19E family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.

# Clinical significance
Mutations in this gene cause Diamond-Blackfan anemia (DBA), a constitutional erythroblastopenia characterized by absent or decreased erythroid precursors, in a subset of patients. This suggests a possible extra-ribosomal function for this gene in erythropoietic differentiation and proliferation, in addition to its ribosomal function. Higher expression levels of this gene in some primary colon carcinomas compared to matched normal colon tissues has been observed.

# Interactions
Ribosomal protein S19 has been shown to interact with basic fibroblast growth factor. RPS19 is also secreted extracellularly and its extracellular oligomers (crosslinked by the  transglutaminase Coagulation factor XIII) is also known to bind and probably inhibit Macrophage migration inhibitory factor; though S19 oligomers themselves share MCIP's function as another very strong macrophage chemoattractant and bind to anaphylotoxin C5 receptor
40S ribosomal protein S21
40S ribosomal protein S21 is a protein, encoded in humans by the RPS21 gene.

# Function
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S21E family of ribosomal proteins.
It is located in the cytoplasm. Alternative splice variants that encode different protein isoforms have been described, but their existence has not been verified. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.

# Interactions
RPS21 has been shown to interact with Ribosomal protein SA.
40S ribosomal protein S27
40S ribosomal protein S27 also known as metallopan-stimulin 1 or MPS-1 is a protein that in humans is encoded by the RPS27 gene. Metallopanstimulin is a zinc finger protein proposed to be involved DNA repair as well as oncogenesis.

# Function
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S27E family of ribosomal proteins. It contains a C4-type zinc finger domain that can bind to zinc. The encoded protein has been shown to be able to bind to nucleic acid. It is located in the cytoplasm as a ribosomal component, but it has also been detected in the nucleus. Studies in rat indicate that ribosomal protein S27 is located near ribosomal protein S18 in the 40S subunit and is covalently linked to translation initiation factor eIF3. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.

# Clinical significance
Its expression is increased in several types of malignancy and MPS levels have been reported to drop with treatment of some cancers.  It has also been used as a target for some chemotherapies, which aim to chelate out the zinc from the zinc finger motif of the MPS, thus yielding it inactive.  These therapies have shown promise for the treatment of cancer in laboratory experiments and some limited clinical trials.  Head and neck cancer transfected to overexpress this protein have demonstrated suppressed growth.
40S ribosomal protein S29
40S ribosomal protein S29 is a protein that in humans is encoded by the RPS29 gene.

# Function
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit and a member of the S14P family of ribosomal proteins. The protein, which contains a C2-C2 zinc finger-like domain that can bind to zinc, can enhance the tumor suppressor activity of Ras-related protein 1A (KREV1). It is located in the cytoplasm. Variable expression of this gene in colorectal cancers compared to adjacent normal tissues has been observed, although no correlation between the level of expression and the severity of the disease has been found. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.

# Clinical significance
Mutations in RPS29 cause                 Diamond-Blackfan anemia            .