Persius/hicric huggingface dataset:
Amelogenesis

# Overview
Amelogenesis is the formation of enamel on teeth and occurs during the crown stage of tooth development after dentinogenesis, which is the formation of dentine.  Since dentine must be present for enamel to be formed, this prerequisite is an example of the biologic concept, termed reciprocal induction.
Amelogenesis is considered to have two stages.  The first stage is known as the secretory phase, and the second stage is known as the maturation stage.  Proteins and an organic matrix form a partially mineralized enamel in the secretory stage. The maturation stage completes enamel mineralization.

# Stages

## Secretory stage
In the secretory stage, ameloblasts are polarized columnar cells.  In the rough endoplasmic reticulum of these cells, enamel proteins are released into the surrounding area and contribute to what is known as the enamel matrix, which is then partially mineralized by the enzyme alkaline phosphatase.  When this first layer is formed, the ameloblasts move away from the dentin, allowing for the development of Tomes processes at the apical pole of the cell.  Enamel formation continues around the adjoining ameloblasts, resulting in a walled area, or pit, that houses a Tomes process, and also around the end of each Tomes process, resulting in a deposition of enamel matrix inside of each pit.  The matrix within the pit will eventually become an enamel rod, and the walls will eventually become interrod enamel. The only distinguishing factor between the two is the orientation of the calcium crystals.

## Maturation stage
In the maturation stage, the ameloblasts transport substances used in the formation of enamel.  Microscopically, the most notable aspect of this phase is that these cells become striated, or have a ruffled border.  These signs demonstrate that the ameloblasts have changed their function from production, as in the secretory stage, to transportation.  Proteins used for the final mineralization process compose most of the transported material.  The noteworthy proteins involved are amelogenins, ameloblastins, enamelins, and tuftelins.  During this process, amelogenins and ameloblastins are removed after use, leaving enamelins and tuftelin in the enamel.  By the end of this stage, the enamel has completed its mineralization.
Amino esters
Structurally, local anesthetics consist of three molecular components:
- a lipophilic part
- an intermediate aliphatic chain
- a hydrophilic (amine) part
The chemical linkage between the lipophilic part and the intermediate chain can be of the amide-type or the ester-type, and is the general basis for the current classification of local anesthetics.
Amino ester-type include:
- Cocaine
- Procaine (Novocain)
- Tetracaine (Pontocaine)
- Benzocaine
Amino esters, in reference to anesthetic agents, are rapidly metabolized in the plasma by butyrlcholinesterase to para-aminobenzoic acid derivatives, then excreted in the urine. This suggests their very short 12 lives.
Allergy is more likely to occur with ester-type agents, as opposed to amide-type.

# Reference
- UT Med School, Pharmacology Syllabus.
- Katsung. 10th edition. Chapter 26.
Carnosinemia
Carnosinemia, also called carnosinase deficiency or aminoacyl-histidine dipeptidase deficiency, is a rare autosomal recessive metabolic disorder caused by a deficiency of carnosinase, a dipeptidase (a type of enzyme that splits dipeptides into their two amino acid constituents).
Carnosine is a dipeptide composed of beta-alanine and histidine, and is found in skeletal muscle and cells of the nervous system. This disorder results in an excess of carnosine in the urine, cerebrospinal fluid (CSF), blood and nervous tissue. Neurological disorders associated with a deficiency of carnosinase, and the resulting carnosinemia ("carnosine in the blood") are common.

# Enzymology
Carnosinase in humans has two forms:
1. Cellular, or tissue carnosinase. This form of the enzyme is found in every bodily tissue. It is a dimer, and hydrolyzes both carnosine and anserine, preferring dipeptides that have a histidine monomer in the c-terminus position. Tissue carnosinase is often considered a "non-specific dipeptidase", based in part on its ability to hydrolyze a range of dipeptide substrates, including those belonging to prolinase.
2. Serum carnosinase. This is the carnosinase found in the blood plasma. Deficiency of this form of carnosinase, along with carnosinuria ("carnosine in the urine"), is the usual metabolic indicator of systemic carnosinase deficiency. Serum carnosinase is a glycoprotein, and splits free carnosine and anserine in the blood. This form of the dipeptidase is not found in human blood until late infancy, slowly rising to adult levels by age 15. Unlike tissue carnosinase, serum carnosinase also hydrolyzes the GABA metabolite homocarnosine. Homocarnosinosis, a neurological disorder resulting in an excess of homocarnosine in the brain, though unaffected by tissue carnosinase, is caused by a deficiency of serum carnosinase in its ability to hydrolyze homocarnosine.
A deficiency of tissue and serum carnosinase, with serum being an indicator, is the underlying metabolic cause of carnosinemia.

# Symptoms
A variety of neurological symptoms have been associated with carnosinemia. They include: hypotonia, developmental delay, mental retardation, degeneration of axons, sensory neuropathy, tremors, demyelinization, gray matter anomalies, myoclonic seizures, and loss of purkinje fibers.

# Genetics
The gene for carnosinase is located on chromosome 18, an autosome. The carnosine dipeptidase-1 gene (CNDP1) controls tissue and serum carnosinase. Mutations in CNDP1 are  responsible for carnosinase deficiency, resulting in carnosinemia.
Carnosinemia is an autosomal recessive disorder, which means the defective gene is located on an autosome, and two copies of the defective gene - one from each parent - are required to inherit the disorder. The parents of an individual with an autosomal recessive disorder both carry one  copy of the defective gene, but usually do not experience any signs or symptoms of the disorder.
Transaminase

# Overview
In biochemistry, a transaminase or an aminotransferase is an enzyme that catalyzes a type of reaction between an amino acid and an -keto acid. Specifically, this reaction (transamination) involves removing the amino group from     the amino acid, leaving behind an -keto acid, and transferring it to the reactant -keto acid and converting it into an amino acid. The enzymes are important in the production of various amino acids, and measuring the concentrations of various transaminases in the blood is important in the diagnosing and tracking many diseases. Transaminases require the coenzyme pyridoxal-phosphate, which is converted into pyridoxamine in the first phase of the reaction, when an amino acid is converted into a keto acid. Enzyme-bound pyridoxamine in turn reacts with pyruvate, oxaloacetate, or alpha-ketoglutarate, giving alanine, aspartic acid, or glutamic acid, respectively.
The presence of elevated transaminases can be an indicator of liver damage.

# Transaminases in amino acid metabolism in animals
Animals must metabolize proteins to amino acids, at the expense of muscle tissue, when blood sugar is low. The preference of liver transaminases for oxaloacetate or alpha-ketoglutarate plays a key role in funneling nitrogen from amino acid metabolism to Asp and Glu for conversion to urea for excretion of nitrogen. Similarly, in muscles the use of pyruvate for transamination gives Ala, which is carried by the bloodstream to the liver. Here other transaminases regenerate pyruvate, which provides a valuable precursor for gluconeogenesis. This alanine cycle is analogous to the Cori cycle which allows anaerobic metabolism by muscles.
Amniotic sac

# Overview
The amniotic sac is the sac in which the fetus develops.
Some sources consider it to be equivalent to the amnion,, while other sources consider it to consist of the amnion and the chorion.
It is also called the amniotic bubble because of its resemblance to a bubble.
When in the light, the amniotic sac is shiny and very smooth, but too tough to pierce through.

# Amniotomy
An artificial rupture of membranes (ARM), also known as an amniotomy, may be performed by a midwife or obstetrician.  This is usually performed using an amnihook and is intended to induce or accelerate labour.

# Diversity
The presence of the amnion identifies humans as amniotes, along with reptiles, dinosaurs, birds, and other mammals, but not amphibians.

# Amniotic fluid
Amniotic fluid is the watery liquid surrounding and cushioning a growing fetus within the amnion.  It allows the fetus to move freely without the walls of the uterus being too tight against its body.  Buoyancy is also provided.
Co-amoxiclav
Synonyms / Brand Names:

# Dosing and Administration
Adults
The usual adult dose is one 500-mg tablet of AUGMENTIN every
12 hours or one 250-mg tablet of AUGMENTIN every 8 hours. For more
severe infections and infections of the respiratory tract, the dose should
be one 875-mg tablet of AUGMENTIN every 12 hours or one 500-mg
tablet of AUGMENTIN every 8 hours.
For more information on Dosing please refer to Instructions for administration
FDA Package Insert Resources
Indications, Contraindications, Side Effects, Drug Interactions, etc.
Calculate Creatine Clearance
On line calculator of your patients Cr Cl by a variety of formulas.
Convert pounds to Kilograms
On line calculator of your patients weight in pounds to Kg for dosing estimates.
 Publication Resources
Recent articles, WikiDoc State of the Art Review, Textbook Information
Trial Resources
Ongoing Trials, Trial Results
Guidelines & Evidence Based Medicine Resources
US National Guidelines, Cochrane Collaboration, etc.
Media Resources
Slides, Video, Images, MP3, Podcasts, etc.
Patient Resources
Discussion Groups, Handouts, Blogs, News, etc.
International Resources
en Espanol

# FDA Package Insert Resources
Indications
Contraindications
Side Effects
Drug Interactions
Precautions
Overdose
Instructions for Administration
How Supplied
FDA label
FDA on Co-amoxiclav
Return to top

# Publication Resources
Most Recent Articles on Co-amoxiclav
Review Articles on Co-amoxiclav
Articles on Co-amoxiclav in N Eng J Med, Lancet, BMJ
WikiDoc State of the Art Review
Textbook Information on Co-amoxiclav
Return to top

# Trial Resources
Ongoing Trials with Co-amoxiclav at Clinical Trials.gov
Trial Results with Co-amoxiclav
Return to top

# Guidelines & Evidence Based Medicine Resources
US National Guidelines Clearinghouse on Co-amoxiclav
Cochrane Collaboration on Co-amoxiclav
Cost Effectiveness of Co-amoxiclav
Return to top

# Media Resources
Powerpoint Slides on Co-amoxiclav
Images of Co-amoxiclav
Podcasts & MP3s on Co-amoxiclav
Videos on Co-amoxiclav
Return to top

# Patient Resources
Patient Resources on Co-amoxiclav
Discussion Groups on Co-amoxiclav
Patient Handouts on Co-amoxiclav
Blogs on Co-amoxiclav
Co-amoxiclav in the News
Co-amoxiclav in the Marketplace
Return to top

# International Resources
Co-amoxiclav en Espanol
Return to top
Adapted from the FDA Package Insert.
Amphiregulin
Amphiregulin, also known as AREG, is a protein that in humans is encoded by the AREG  gene.

# Function
The protein encoded by this gene is a member of the epidermal growth factor (EGF) family.
It is an autocrine growth factor as well as a mitogen for astrocytes, Schwann cells, fibroblasts. It is related to epidermal growth factor (EGF) and transforming growth factor alpha (TGF-alpha). This protein interacts with the Epidermal growth factor receptor (EGFR) to promote the growth of normal epithelial cells.

# Biological role
Estradiol and progesterone mostly induce amphiregulin expression to mediate ductal development of the mammary glands. Amphiregulin has been found to be essential for mammary ductal development, as evidenced by absence of ductal growth in amphiregulin knockout mice. This is similar to the phenotypes of EGFR and ER knockout mice, which also show absence of ductal growth.

# Clinical significance
Mutations in this encoded protein are associated with a psoriasis-like skin phenotype.
Anal leakage
Anal leakage is a type of fecal incontinence that comes from eating non-digestible, artificial fats such as Olestra and from medicines that prevent the absorption of dietary fats such as Orlistat, where the fat leaks out from the rectum and stains the underpants.    

# Artificial fats
The fat substitute Olestra, used in some reduced-calorie foods, has been proven to cause leakage in some consumers. The United States Food and Drug Administration warning indicated that excessive consumption of Olestra could result in "loose stools." As of 2003, the FDA no longer requires this warning.  

# Medications
Orlistat (Xenical) is a diet pill that works by blocking the enzymes that digest fat. As a result, fat cannot be absorbed from the gut, and instead some fat is excreted in the feces instead of being metabolically digested, and as a result, can cause oily anal leakage.
Annihilation
Annihilation is defined as "total destruction" or "complete obliteration" of an object; having its root in the Latin nihil (nothing). A literal translation is "to make into nothing". Annihilation is the opposite of exnihilation, which means "to create something out of nothing".
In physics, the word is used to denote the process that occurs when a subatomic particle collides with its respective antiparticle. Since energy and momentum must be conserved, the particles are not actually made into nothing, but rather into new particles. Antiparticles have exactly opposite additive quantum numbers from particles, so the sums of all quantum numbers of the original pair are zero. Hence, any set of particles may be produced whose total quantum numbers are also zero as long as conservation of energy and conservation of momentum are obeyed.
During a low-energy annihilation, photon production is favored, since these particles have no mass. However, high-energy particle colliders produce annihilations where a wide variety of exotic heavy particles are created.

# Examples of annihilation
This is an example of renormalization in quantum field theory the field theory being necessary because the number of particles changes from one to two and back again.
When a low-energy electron annihilates a low-energy positron (anti-electron), they can only produce two or more gamma ray photons, since the electron and positron do not carry enough mass-energy to produce heavier particles. However, if one or both particles carry a larger amount of kinetic energy, various other particle pairs can be produced.  See electron-positron annihilation.
The annihilation (or decay) of an electron-positron pair into a single photon, e+ + e-  , cannot occur because energy and momentum would not be conserved in this process. The reverse reaction is also impossible for this reason, except in the presence of another particle that can carry away the excess energy and momentum. However, in quantum field theory this process is allowed as an intermediate quantum state.  Some authors justify this by saying that the photon exists for a time which is short enough that the violation of energy conservation can be accommodated by the uncertainty principle.  Others choose to assign the intermediate photon a non-zero mass.  (The mathematics of the theory are unaffected by which view is taken.) This opens the way for virtual pair production or annihilation in which a one-particle quantum state may fluctuate into a two-particle state and back again (coherent superposition). These processes are important in the vacuum state and renormalization of a quantum field theory. It also allows neutral particle mixing through processes such as the one pictured here.
Anrep effect
The Anrep effect is an autoregulation method in which myocardial contractility increases with afterload. It was experimentally determined that increasing afterload caused a proportional linear increase in ventricular inotropy.
This effect is found in denervated heart preparations, such as the Starling Preparation, and as such, represents an intrinsic autoregulation mechanism.
Functionally, the Anrep effect allows the heart to compensate for an increased end-systolic volume present and the decreased stroke volume that occurs when aortic blood pressure increases. Without the Anrep effect, an increase in aortic blood pressure would create a decrease in stroke volume that would compromise circulation to peripheral and visceral tissues.
CME Category::Cardiology
Ventral root

# Overview
In anatomy and neurology, the ventral root (or anterior root) is the efferent motor root of a spinal nerve.
At its distal end, the ventral root joins with the dorsal root to form a mixed spinal nerve.

# Additional images
- Cervical vertebra
- Medulla spinalis
- The mechanism of the reflex arc
- A spinal nerve with its anterior and posterior roots.
- The motor tract.
- Diagrammatic transverse section of the medulla spinalis and its membranes.
- A portion of the spinal cord, showing its right lateral surface. The dura is opened and arranged to show the nerve roots.
- Scheme showing structure of a typical spinal nerve.
Anthelmintic
Anthelmintics are drugs that expel parasitic worms (helminths) from the body, by either killing or stunning them. A traditional remedy of this type is often called a vermifuge or vermicide.

# Classes
Examples of drugs used as anthelmintics include:
- Albendazole - Effective against: threadworms, roundworms, whipworms, tapeworms, hookworms
- Diethylcarbamazine - Effective against: Wuchereria bancrofti, Brugia malayi, Brugia timori, tropical pulmonary eosinophilia, loiasis
- Mebendazole - Effective against: pinworms, roundworms and hookworms
- Niclosamide - Effective against: tapeworms
- Ivermectin - Effective against: most common intestinal worms (except tapeworms)
- Suramin
- Thiabendazole - Effective against: roundworms, hookworms
- Pyrantel pamoate - Effective against: for most nematode infections
- Levamisole
- Praziquantel - Effective against: nematodes, some trematodes
- Triclabendazole - Effective against: liver flukes
- Octadepsipeptides - Eg: Emodepside.  Effective against a variety of gastrointestinal helminths
Many members of the piperazine family are successful anthelmintics.
Natural anthelmintics include black walnut, wormwood (Artemisia absynthium), clove (Syzygium aromaticum), tansy tea (Tanacetum vulgare), Hagenia (Hagenia abyssinica), kalonji (Nigella sativa) seeds, and the male fern (Dryopteris filix-mas). In Brazilian folk medicine, Plumeria P. acutifolia or P. rubra is also an anthelmintic.  Please note that many natural vermifuges or anthelmintics are poisonous and, in improper dosages, dangerous to humans as well as parasites.

# Anthelmintic Resistance
The ability of worms to survive treatments that are generally effective at the recommended dose rate.
It is considered a major threat to the current future control of worm parasites of small ruminants and horses.

# Development of Resistance
Treatment eliminates worms whose genotype renders them susceptible
-Worms that are resistant survive and pass on their "resistance" genes
Resistant worms accumulate and finally treatment failure occurs
-Clinical definition= <95% reduction in Fecal Egg Count

# What causes Resistance?
- Treatment at frequent intervals
3 treatments per year
Many farms >6 Tx per year
- >3 treatments per year
- Many farms >6 Tx per year
- Treating all animals at same time
no refugia
- no refugia
- Treating and moving to clean pasture
no dilution
- no dilution
- Under dosing
worms with low-level resistance survive
- worms with low-level resistance survive
Antipruritic
Antipruritics, also known as anti-itch drugs, are medications that inhibit the itching (Latin: pruritus) that is often associated with sunburns, allergic reactions, eczema, psoriasis, chickenpox, fungal infections, insect bites and stings like those from mosquitoes, fleas, and mites, and contact dermatitis and urticaria caused by plants such as poison ivy (urushiol-induced contact dermatitis) or stinging nettle.

# Common antipruritics
Topical antipruritics in the form of creams and sprays are often available over-the-counter. Oral (by-mouth) anti-itch drugs also exist and are usually prescription drugs. The active ingredients usually belong to the following classes:
- Antihistamines such as diphenhydramine (Benadryl)
- Corticosteroids such as hydrocortisone topical cream
- Local anesthetics such as benzocaine topical cream (Lanacaine)
- Counterirritants, such as mint oil, menthol, or camphor

# Disputed and questionable antipruritics
- Calamine lotion (zinc oxide with iron(III) oxide), some say has little if any effect on itching , although other research indicates it has some antipruritic qualities
- Burow's solution (aluminium acetate)
- Olive oil
- Jewelweed, has been shown to be devoid of any anti-itch activity in several controlled studies 
- SSRIs (selective serotonin reuptake inhibitors) comprise a class of medicines commonly used for depression, and are also said to be effective in controlling pruritus in a small number of refractory cases.

# Home remedies
- Cooling with ice or cold water
- Heat, for example by a hot shower.  Dabbing with a cloth dipped in boiling water can be very effective, as it causes the cells to release all their histamine.
- Soft rubbing, which activates fast-conducting, low-threshold neurons
- Slightly painful stimulation like scratching, based on a spinal antagonism between pain- and itch-processing neurons
- Mixture of Rose water and starch can have an itch-calming effect
Glycoprotein

# Overview
Glycoproteins are proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbones. Basically, glycoprotein is a biomolecule composed of a protein and a carbohydrate (an oligosaccharide). The carbohydrate is attached to the protein in a cotranslational or posttranslational modification.
In proteins that have segments extending extracellularly, the extracellular segments are often glycosylated.

# N-glycosylation and O-glycosylation
There are two types of glycosylation:
- In N-glycosylation (see on the right), the addition of sugar chains can happen at asparagine.
- In O-glycosylation, the addition of sugar chains can happen at hydroxylysine, hydroxyproline, serine, or threonine.

# Monosaccharides
Monosaccharides commonly found in eukaryotic glycoproteins include:
The sugar group(s) can assist in protein folding or improve proteins' stability.

# Examples
One example of glycoproteins found in the body are mucins, which are secreted in the mucus of the respiratory and digestive tracts. The sugars attached to mucins give them considerable water-holding capacity and also make them resistant to proteolysis by digestive enzymes.
Glycoproteins are important for immune cell recognition, especially in mammals. Examples of glycoproteins in the immune system are:
- molecules such as antibodies (immunoglobulins), which interact directly with antigens
- molecules of the major histocompatibility complex (or MHC), which are expressed on the surface of cells and interact with T-cells as part of the adaptive immune response.
Other examples of glycoproteins include:
- components of the zona pellucida, which surrounds the oocyte, and is important for sperm-egg interaction.
- structural glycoproteins, which occur in connective tissue. These help bind together the fibers, cells, and ground substance of connective tissue. They may also help components of the tissue bind to inorganic substances, such as calcium in bone.
Soluble glycoproteins often show a high viscosity, for example, in egg white and blood plasma.

# Hormones
Hormones that are glycoproteins include:
- Follicle stimulating hormone
- Luteinizing hormone
- Thyroid stimulating hormone
- human chorionic gonadotropin
- Alpha-fetoprotein
- Erythropoietin (EPO)

# Functions

# Analysis
A variety of methods used in detection, purification, and structural analysis of glycoproteins are