Persius/hicric huggingface dataset:
Calmodulin

# Overview
Calmodulin (CaM) (an abbreviation for CALcium MODULated proteIN) is a calcium-binding protein expressed in all eukaryotic cells.  It can bind to and regulate a number of different protein targets, thereby affecting many different cellular functions.

# Function
CaM mediates processes such as inflammation, metabolism, apoptosis, muscle contraction, intracellular movement, short-term and long-term memory, nerve growth and the immune response.  CaM is expressed in many cell types and can have different subcellular locations, including the cytoplasm, within organelles, or associated with the plasma or organelle membranes.  Many of the proteins that CaM binds are unable to bind calcium themselves, and as such use CaM as a calcium sensor and signal transducer.  CaM can also make use of the calcium stores in the endoplasmic reticulum, and the sarcoplasmic reticulum.  CaM undergoes a conformational change upon binding to calcium, which enables it to bind to specific proteins for a specific response. CaM can bind up to four calcium ions, and can undergo post-translational modifications, such as phosphorylation, acetylation, methylation and proteolytic cleavage, each of which can potentially modulate its actions. Calmodulin can also bind to edema factor toxin from the anthrax bacteria.

# Structure
Calmodulin is a small, acidic protein approximately 148 amino acids long (16706 Dalton) and, as such, is a favorite for testing protein simulation software. It contains four EF-hand "motifs", each of which binds a Ca2+ ion. The protein has two approximately symmetrical domains, separated by a flexible "hinge" region.

# Mechanism
Calcium is bound via the use of the EF hand motif, which supplies an electronegative environment for ion coordination. After calcium binding, hydrophobic methyl groups from methionine residues become exposed on the protein via conformational change. This presents hydrophobic surfaces, which can in turn bind to Basic Amphiphilic Helices (BAA helices) on the target protein. These helices contain complementary hydrophobic regions. The flexibilily of Calmodulin's hinged region allows the molecule to "wrap around" its target. This property allows it to tightly bind to a wide range of different target proteins.

# Family members
- Calmodulin 1 (CALM1)
- Calmodulin 2 (CALM2)
- Calmodulin 3 (CALM3)
- Calmodulin-like 1 (CALML1)
- Calmodulin-like 3 (CALML3)
- Calmodulin-like 4 (CALML4)
- Calmodulin-like 5 (CALML5)
- Calmodulin-like 6 (CALML6)

# Other calcium-binding proteins
Calmodulin belongs to one of the two main groups of calcium-binding proteins, called EF hand proteins. The other group, called annexins, bind calcium and phospholipid (e.g., lipocortin). Many other proteins bind calcium, although binding calcium may not be considered their principal function in the cell.
Calretinin
Calretinin also known as 29 kDa calbindin is a calcium-binding protein involved in calcium signaling.  In humans, the calretinin protein is encoded by the CALB2 gene.

# Function
This gene encodes an intracellular calcium-binding protein belonging to the troponin C superfamily. Members of this protein family have six EF-hand domains which bind calcium. This protein plays a role in diverse cellular functions, including message targeting and intracellular calcium buffering.
Calretinin is abundantly expressed in neurons including retina (which gave it the name) and cortical interneurons. Expression was found in different neurons than that of the similar vitamin D-dependent calcium-binding protein, calbindin-28kDa.
Calretinin has an important role as a modulator of neuronal excitability including the induction of long-term potentiation.  Loss of expression of calretinin in hippocampal interneurons has been suggested to be relevant in temporal lobe epilepsy.
It is expressed in a number of other locations including hair follicles.

# Clinical significance
Calretinin is a diagnostic marker for some human diseases, including Hirschsprung disease and some cancers.

## Mesothelioma
Using immunohistochemistry, calretinin can be demonstrated in both benign mesothelium and in malignant mesothelioma and can be used to help differentiate different lung tumours. Antibodies to calretinin can also be used to distinguish between different types of brain tumour, demonstrating only those with neuronal rather than glial, differentiation. Furthermore, the essential function of calretinin in mesothelioma cell lines has been demonstrated in vitro and may be an interesting target for therapeutical approaches.

## Hirschsprung disease
In Hirschsprung disease, calretinin immunohistochemistry offers additional diagnostic value in specimens with inadequate amount of submucosa and rarely seen ganglion cells.  The presence of ganglion cells consistently correlated with calretinin-positive thin nerve fibrils in the lamina propria, muscularis mucosae and superficial submucosa.  These calretinin-positive thin neurofibrils are absent in the aganglionic segments of bowel and in the areas without ganglion cells from the junction of normal with diseased rectum.  Calretinin is strongly expressed in the submucosal and subserosal nerve trunks in the ganglionic segment.  No calretinin expression is seen in the nerve trunks in the rest of the aganglionic segment.  It has faint expression in the thick nerve trunks from the areas without ganglion cells.  Faint positivity of the thick submucosal and subserosal nerves in the absence of ganglion cells and calretinin positive nerve fibrils, is characteristic of the junction of the aganglionic-to-normal rectum.
Intertrigo
An intertrigo is an inflammation (rash) of the body folds (adjacent areas of skin).
An intertrigo sometimes refers to a bacterial, fungal, or viral infection that has developed at the site of broken skin due to such inflammation.
An intertrigo usually develops from the chafing of warm, moist skin in the areas of the inner thighs and genitalia, the armpits, under the breasts, the underside of the belly, behind the ears, and the web spaces between the toes and fingers. An intertrigo usually appears red and raw-looking, and may also itch, ooze, and be sore. Intertrigos occur more often among overweight individuals, those with diabetes, those restricted to bed rest or diaper use, and those who use medical devices, like artificial limbs, that trap moisture against the skin.  Also, there are several skin diseases that can cause an intertrigo to develop, such as dermatitis or inverse psoriasis.

# Differentiating intertrigo from other diseases
Intertrigo should be differentiated from other diseases causing papulosquamous or erythmatosquamous rash. The differentials include:

# Treatments
In general, treatment for all skin rashes, less is more, and consult a dermatologist if it persists for more than a week.  Infections can be treated with a topical and/or oral medication(s).  The most common treatment being a baby diaper rash ointment such as a topical zinc oxide cream.  Some commonly available over the counter brand names: Sudocrem, Desitin, Butt Paste, and Balmex.  There are also many other generic diaper rash creams that may work.  Also for a persistent intertrigo infection it is common for an anti-fungal cream, most commonly clotrimazole 1%, to be used in conjunction with a diaper rash ointment.
It is suggested to use a paper towel to apply the zinc oxide cream and/or anti-fungal ointment(s) to avoid excessive hand washing, as it is very difficult to wash zinc oxide ointment from the hands because it resists water.  Other ingredients in baby rash ointments that are beneficial to relief of intertrigo is cod liver oil and shark liver oil.  These oils are also available in pill forms that may also help the infection (see links).
Hydrocortisone available at drug stores and over the counter in low dosages is beneficial in relieving the pain and symptoms of the infection but does not cure the infection.
Keeping the area of the intertrigo dry and exposed to the air can help prevent recurrences. If the individual is overweight, losing weight can help. Using antibacterial soap, surrounding the skin with absorbent cotton or a band of cotton fabric, and treating the skin with absorbent body powders and even antiperspirants will all help prevent future occurrences. Relapses of intertrigos are common, however, and require periodic care from a dermatologist.

# Prescription Medicines
These prescriptions are very dangerous and are usually only prescribed by a doctor for extreme cases.
- Grifulvin V
- Griseofulvin
Captodiame

# Overview
Captodiame (INN), also known as captodiamine, is an antihistamine sold under the trade names Covatine, Covatix, and Suvren which is used as a sedative and anxiolytic. It is a derivative of diphenhydramine.
A 2004 study suggested captodiame may be helpful in preventing benzodiazepine withdrawal syndrome in people discontinuing benzodiazepine treatment.
In addition to its actions as an antihistamine, captodiamine has been found to act as a 5-HT2C receptor antagonist and 1 receptor and D3 receptor agonist. It produces antidepressant-like effects in rats. However, captodiamine is unique among antidepressant-like drugs in that it increases brain-derived neurotrophic factor (BDNF) levels in the hypothalamus but not in the frontal cortex or hippocampus. This unique action may be related to its ability to attenuate stress-induced anhedonia and corticotropin-releasing factor (CRF) signaling in the hypothalamus.
Carbapenem
Carbapenems are a class of beta-lactam antibiotics with a broad spectrum of antibacterial activity, and have a structure which renders them highly resistant to beta-lactamases. Carbapenem antibiotics were originally developed from thienamycin, a naturally-derived product of Streptomyces cattleya.
The following drugs belong to the carbapenem class:
- Imipenem (often given as part of Imipenem/cilastatin)
Imipenem can be hydrolysed in the mammalian kidney by a dehydropeptidase enzyme, and so is given with a dehydropeptidase inhibitor, cilastatin
- Imipenem can be hydrolysed in the mammalian kidney by a dehydropeptidase enzyme, and so is given with a dehydropeptidase inhibitor, cilastatin
- Meropenem
- Ertapenem
- Faropenem
- Doripenem
- Panipenem/betamipron
These agents have the broadest antibacterial spectrum compared to other beta-lactam classes such as penicillins and cephalosporins. Additionally they are generally resistant to the typical bacterial beta-lactamase enzymes which are one of the principal resistance mechanisms of bacteria.  They are active against both Gram positive and gram negative bacteria, with the exception of intracellular bacteria, such as the Chlamydiae.
The carbapenems are structurally very similar to the penicillins, but the sulfur atom in position 1 of the structure has been replaced with a carbon atom, and hence the name of the group, the carbapenems.
Due to their expanded spectra, the desire to avoid generation of resistance and the fact that they have generally poor oral bioavailability, they are administered intravenously in hospital settings for more serious infections. However, research is underway to develop an effective oral carbapenem.
Carol Cass

# Overview
Carol Cass is an Canadian research scientist. She is internationally recognized as an expert on nucleosides, an important class of anti-cancer drugs.  Her research has led to the more effective use of nucleoside drugs and the development of new treatments for patients with acute and chronic leukemias, lymphomas, and cancers of the lung, bladder, breast and pancreas.
She determined that nucleoside-based drugs are able to cross cell membranes by binding to specialized transporter proteins. The drugs are able to enter and directly attack cancer cells during the binding process.
Since 2003, Cass has been director of Albertas Cross Cancer Institute. She is Canada research chair in oncology at the University of Alberta.

# Awards
- 2006, awarded the Robert L. Noble Prize by the National Cancer Institute of Canada for her contributions to cancer research.
Carr index
The Carr index is an indication of the compressibility of a powder.  It is calculated by the formula C=100\frac{V_B-V_T}{V_B}, where V_B is the freely settled volume of a given mass of powder, and V_T is the tapped density of the same mass of powder.  It can also be expressed as C=100\times(1-\frac{\rho_B}{\rho_T}), where \rho_B is the freely settled bulk density of the powder, and \rho_T is the tapped density of the powder.
The Carr index is frequently used in pharmaceutics as an indication of the flowability of a powder.  A Carr index greater than 25% is considered to be an indication of poor flowability, and below 15%, of good flowability.
The Carr index is related to the Hausner ratio, another indication of flowability, by the formula C=100\times(H-1).
Caspase 12
Caspase 12 is a protein that belongs to a family of enzymes called caspases which cleave their substrates at C-terminal aspartic acid residues.  It is closely related to caspase 1 and other members of the caspase family, known as inflammatory caspases, which process and activate inflammatory cytokines such as interleukin 1 and interleukin 18.

# Gene
It is found on chromosome 11 in humans in a locus with other inflammatory caspases.
CASP12 orthologs have been identified in numerous mammals for which complete genome data are available.

# Clinical significance
The CASP12 gene is subject to polymorphism, which can generate a full length caspase protein (Csp12L) or an inactive truncated form (Csp12S). The functional form appears to be confined to people of African descent and is linked with susceptibility to sepsis; people carrying the functional gene have decreased responses to bacterial molecules such as lipopolysaccharide (LPS).
A study in May 2009 by McGill University Health Centre has suggested that estrogen may serve to block the production of caspase-12, resulting in a stronger inflammatory reaction to bacterial pathogens. The trials were carried out on laboratory mice which had been implanted with the human caspase-12 gene.
The inactive truncated form (Csp12S) of the CASP12 gene was spread and nearly fixed in non-African populations due to positive selection beginning perhaps 60100 thousand years ago. Its selective advantage is thought to be sepsis resistance in populations that experienced more infectious diseases as population sizes and densities increased.
Caspase 14
Caspase 14 is an enzyme that in humans is encoded by the CASP14 gene.
The CASP14 gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This caspase has been shown to be processed and activated by caspase 8 and caspase 10 in vitro, and by anti-Fas agonist antibody or TNF-related apoptosis inducing ligand in vivo. The expression and processing of this caspase may be involved in keratinocyte terminal differentiation, which is important for the formation of the skin barrier.
According to the Human Protein Atlas, the CASP14 protein is enriched human skin and mainly expressed in the upper layers of the epidermis.The protein is mainly localised to the cytosol according to the Cell Atlas.
Catabiosis
Catabiosis - the process of growing older, aging and physical degradation.
The word comes from Greek 'kata' - down, against, reverse and 'biosis' -  way of life and is generally used to describe senscence and degeneration in living organisms and biophysics of aging in general.
One of the popular catabiotic theories is the entropy theory of aging, where aging is characterized by thermodynamically favourable increase in structural disorder. Living organisms are not closed systems that take free energy from the environment and offload their entropy as waste. However, basic components of living systems: DNA, proteins, lipids and sugars tend towards the state of maximum entropy while continuously accumulating damages causing catabiosis of the living structure.
Catabiotic force on the contrary is the influence exerted by living structures on adjoining cells, by which the latter are developed in harmony with the primary structures.
Catabolism
Catabolism is the set of metabolic pathways that break down molecules into smaller units and release energy. In catabolism, large molecules such as polysaccharides, fatty acids, nucleic acids and proteins are broken down into smaller units such as monosaccharides, fatty acids, nucleotides and amino acids, respectively. As molecules such as polysaccharides, proteins and nucleic acids are made from long chains of these small monomer units, the large molecules are called polymers.
Cells use the monomers released from breaking down polymers to either construct new polymer molecules, or degrade the monomers further to simple waste products, releasing energy. Cellular wastes include lactic acid, acetic acid, carbon dioxide, ammonia, and urea. The creation of these wastes is usually an oxidation process involving a release of chemical free energy, some of which is lost as heat, but the rest is used to drive the synthesis of adenosine triphosphate (ATP). This molecule acts as a way for the cell to transfer the energy released by catabolism to the energy-requiring reactions that make up anabolism. Catabolism therefore provides the chemical energy necessary for the maintenance and growth of cells. Examples of catabolic processes include glycolysis, the citric acid cycle, the breakdown of muscle protein in order to use amino acids as substrates for gluconeogenesis and breakdown of fat in adipose tissue to fatty acids.
There are many signals that control catabolism. Most of the known signals are hormones and the molecules involved in metabolism itself. Endocrinologists have traditionally classified many of the hormones as anabolic or catabolic, depending on which part of metabolism they stimulate. The "classic" catabolic hormones known since the early 20th century are cortisol, glucagon, and adrenaline (and other catecholamines). In recent decades, many more hormones with at least some catabolic effects have been discovered, including cytokines, orexin and hypocretin (a hormone pair), and melatonin.
Categories

# Why put an article in a category?
- At some point it becomes useful to classify the information according to categories. For instance, you might want to add an article on acute MI to the category of cardiology. Acute MI would then be included with all the other articles related to the subject of cardiology in this category. All the articles in a category can come together to forming a living textbook of a given topic.
- Categories are also used to list all the articles that need work for instance, like the addition of an overview statement.

# How to put an article in a category
To add an article to a category, simply add (for each category) a line as follows:
Note (1): The absent space between the colon (:) and the words before it and after it
Note (2): Only the letter  in "Category" and the first letter in the category name are capitalized
Typing this:
Note: Only the first letter in the first word is capitalized , but the first letter in the second word is not capitalized 
Adds the page to the Category of Cardiology chapters and Vascular medicine chapters, respectively.
It is convention to insert these lines near the bottom of the wiki page. Once your edit is saved, the category will exist and add the article you just edited will be added to it.

# Approved Categories for Tagging Chapter Pages
Causticity
A corrosive substance is one that will destroy or irreversibly damage another substance with which it comes in contact. The main hazards to people include damage to eyes, skin and tissue under the skin, but inhalation or ingestion of a corrosive substance can damage the respiratory and gastrointestinal tracts.
A low concentration of a corrosive substance is usually an irritant. Corrosion of non-living surfaces such as metals is a distinct process. For example, a water/air electrochemical cell corrodes iron to rust. In the Globally Harmonized System, both rapid corrosion of metals and chemical corrosion of skin qualify for the "corrosive" symbol.
Common corrosives are strong acids and strong bases, or concentrated solutions of certain weak acids and weak bases. Their action on living tissue is based on acid-base catalysis of ester and amide hydrolysis. Both corrosive acids and corrosive bases are able to defat skin by catalyzing the hydrolysis of fats, which are chemically esters). Proteins are chemically amides, which can also be hydrolyzed by acid-base catalysis. Strong acids and bases denature proteins  and also hydrate easily.  Hydration removes water from the tissue and is significantly exothermic. For example, concentrated sulfuric acid causes thermal burns in addition to chemical burns.
There are also more specific corrosives. Hydrofluoric acid, for example, is initially painless but easily permeates tissue to selectively attack bone. Although zinc chloride solutions are also regularly acidic (by the Brnsted definition), the zinc cation also specifically attacks hydroxyl groups as a Lewis acid. This explains the ability of zinc chloride solutions to react with cellulose and corrode through paper and silk.
The word 'corrosion' is derived from the latin verb corrode which means 'to gnaw' indicating how these substance seem to 'gnaw' their way through the flesh.

# Corrosive substances
Common corrosive chemicals are classified into:
- Acids
- Strong acids  the most common are sulfuric acid, nitric acid and hydrochloric acid (H2SO4, HNO3 and HCl, respectively).
- Some concentrated weak acids, for example acetic acid
- Solutions of Lewis acids with specific reactivity, e.g. solutions of zinc chloride
- Bases
- Caustics or alkalis, such as sodium hydroxide (NaOH) and potassium hydroxide (KOH); also, alkali metals in the metallic form hydrate to give caustics
- Some concentrated weak bases, such as ammonia when anhydrous or in a concentrated solution
- Dehydrating agents such as phosphorus pentoxide, calcium oxide, anhydrous zinc chloride, also elemental alkali metals
- Electrophilic halogens: elemental fluorine, chlorine, bromine and iodine, and electrophilic salts such as sodium hypochlorite or N-chloro compounds such as chloramine-T; anionic halogens as in chlorides are not corrosive
- Organic halides and organic acid halides such as acetyl chloride and benzyl chloroformate
- Acid anhydrides
- Some organic materials such as phenol ("carbolic acid")
- Extremely electrophilic reagents such as dimethyl sulfate
Caveolin 2
Caveolin-2 is a protein that in humans is encoded by the CAV2 gene.
The protein encoded by this gene is a major component of the inner surface of caveolae, small invaginations of the plasma membrane, and is involved in essential cellular functions, including signal transduction, lipid metabolism, cellular growth control and apoptosis. This protein may function as a tumor suppressor. CAV1 and CAV2 are located next to each other on chromosome 7 and express colocalizing proteins that form a stable hetero-oligomeric complex. Two transcript variants encoding distinct isoforms have been identified for this gene. By using alternative initiation codons in the same reading frame, two isoforms (alpha and beta) are encoded by one transcript.

# Interactions
Caveolin 2 has been shown to interact with Caveolin 1 and RAS p21 protein activator 1.