Persius/hicric huggingface dataset:
Lesser sac
The lesser sac, also known as the omental bursa, is the cavity in the abdomen that is formed by the lesser and greater omentum.  Usually found in mammals, it is connected with the greater sac via the epiploic foramen (also known as the Foramen of Winslow).  In mammals, it is not uncommon for the lesser sac to contain considerable amounts of fat.
In human anatomy, the wall of the stomach, pancreas and splenic artery are a part of the wall of the lesser sac.  If these structures rupture they may leak into the lesser sac. For the stomach, which lies anterior to the omental bursa, the rupture must be on the posterior side, as if it were anteriorly located, the leak would collect in the greater sac.
The lesser sac is embryologically formed from an infolding of the greater omentum.  The open end of the infolding, known as the epiploic foramen, is usually proximal to the stomach.

# Additional images
- Upper part of celom of human embryo of 6.8 mm., seen from behind.
- Schematic figure of the bursa omentalis, etc. Human embryo of eight weeks.
- Diagrams to illustrate the development of the greater omentum and transverse mesocolon.
Malar rash
Malar rash, also called butterfly rash, is a medical sign consisting of a characteristic form of facial rash. It is often seen in Lupus erythematosus. Malar is the Latin for "cheek".
The malar rash of lupus is red or purplish and mildly scaly.  Characteristically, it has the shape of a butterfly and involves the bridge of the nose.

# Epidemiology and Demographics
A malar rash is present in approximately 46-65% of lupus sufferers and varies between different populations.

# Diagnosis

## Common Causes
There are numerous other conditions which can cause rashes with a similar appearance. Where lupus is suspected further medical tests (usually an ANA) and a detailed history are necessary to differentiate it from other conditions.
By-product
A by-product is a secondary or incidental product deriving from a manufacturing process, a chemical reaction or a biochemical pathway, and is not the primary product or service being produced.  A by-product can be useful and marketable, or it can have severe ecological consequences.

# Major by-products

## Animal sources
- dried blood and blood meal - from slaughterhouse operations
- chicken by-product meal - clean parts of the carcass of slaughtered chicken, such as necks, feet, undeveloped eggs, and intestines.
- chrome shavings - from a stage of leather manufacture
- collagen and gelatin - from the boiled skin and other parts of slaughtered livestock
- feathers - from poultry processing
- lanolin - from the cleaning of wool
- manure - from animal husbandry
- meat and bone meal - from the rendering of animal bones and offal
- poultry byproduct and poultry meal - made from unmarketable poultry bones and offal
- poultry litter - swept from the floors of chicken coops]
- whey - from cheese manufacturing
- fetal pigs

## Vegetation
- acidulated soap stock - from the refining of vegetable oil
- bran and germ - from the milling of whole grains into refined grains
- brewer's yeast - from ethanol fermentation
- corn stover - residual plant matter after harvesting of cereals
- distillers grains - from ethanol fermentation
- glycerol - from the production of biodiesel
- grape seed oil - recovered from leftovers of the winemaking process
- molasses - from sugar refining
- orange oil and other citrus oils - recovered from the peels of processed fruit
- pectin - recovered from the remains of processed fruit
- sawdust and bark- from the processing of logs into lumber
- straw- from grain harvesting

## Minerals and petro chemicals
- asphalt - from the refining of crude oil
- fly ash - from the combustion of coal
- slag - from ore refining
- gypsum - from Flue gas desulfurization
- ash and smoke - from the combustion of fuel
- mineral oil - from refining crude oil to produce gasoline
- salt - from desalination

## Other
- sludge - from wastewater treatment
C-terminus
The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal end, or COOH-terminus) of a protein or polypeptide is the end of the amino acid chain terminated by a free carboxyl group (-COOH). The convention for writing peptide sequences is to put the C-terminal end on the right and write the sequence from N- to C-terminus.

# Chemistry
Each amino acid has a carboxyl group and an amine group, and amino acids link to one another to form a chain by a dehydration reaction by joining the amine group of one amino acid to the carboxyl group of the next. Thus polypeptide chains have an end with an unbound carboxyl group, the C-terminus, and an end with an amine group, the N-terminus. Proteins are synthesized starting from the N-terminus and ending at the C-terminus.

# Function

## C-terminal retention signals
While the N-terminus of a protein often contains targeting signals, the C-terminus can contain retention signals for protein sorting. The most common ER retention signal is the amino acid sequence -KDEL (or -HDEL) at the C-terminus, which keeps the protein in the endoplasmic reticulum and prevents it from entering the secretory pathway.

## C-terminal modifications
The C-terminus of proteins can be modified posttranslationally, most commonly by the addition of a lipid anchor to the C-terminus that allows the protein to be inserted into a membrane without having a transmembrane domain.
- Prenylation
One form of C-terminal modification is prenylation. During prenylation, a farnesyl- or geranylgeranyl-isoprenoid membrane anchor is added to a cysteine residue near the C-terminus. Small, membrane-bound G proteins are often modified this way.
- GPI anchors
Another form of C-terminal modification is the addition of a phosphoglycan, glycosylphosphatidylinositol (GPI), as a membrane anchor. The GPI anchor is attached to the C-terminus after proteolytic cleavage of a C-terminal propeptide. The most prominent example for this type of modification is the prion protein.

## C-terminal domain
The C-terminal domain (CTD) of some proteins has specialized functions.
- CTD of RNA polymerase
The carboxy-terminal domain of RNA polymerase II typically consists of up to 52 repeats of the sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser . Other proteins often bind the C-terminal domain of RNA polymerase in order to activate polymerase activity. It is the protein domain which is involved in the initiation of DNA transcription, the capping of the RNA transcript, and attachment to the spliceosome for RNA splicing.
C8 complex
Complement component 8 is a protein involved in the complement system. It is part of the membrane attack complex (MAC).
A hereditary deficiency of C8 can result in increased susceptibility to Neisseria infections, such as meningitis and gonorrhea.

# Structure
C8 is a heterotrimer; it consists of three different subunits. These are called C8 alpha, beta and gamma chains, encoded by the genes C8A, C8B and C8G respectively.
CARE Trial

# Objective
To assess if pravastatin would reduce the sum of fatal coronary artery disease (CAD) and nonfatal myocardial infarction (MI) in patients who had a previous MI and a total cholesterol value < 240 mg/dl.

# Methods
Cholesterol and Recurrent Events trial was a double blinded, randomized study wherein 4159 patients with a history of a myocardial infarction in the previous two years who had a total cholesterol value < 240 mg/dl were enrolled and treated with either 40 mg pravastatin or a placebo.

# Results
The following results were obtained after a median follow-up time of 5 years:
- Reduced combined end point of coronary death and nonfatal MI (10.2 versus 13.2 percent)
- Reduced need for revascularization with CABG or PTCA (14.1 versus 18.8 percent)
- Reduced frequency of stroke (2.6 versus 3.8 percent) and of stroke plus transient ischemic attacks (4.4 versus 6.0 percent)
Caspase 10
Caspase-10 is an enzyme that, in humans, is encoded by the CASP10 gene.
This gene encodes a protein that is 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 that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 3 and 7, and the protein itself is processed by caspase 8. Mutations in this gene are associated with apoptosis defects seen in type II autoimmune lymphoproliferative syndrome. Three alternatively spliced transcript variants encoding different isoforms have been described for this gene.

# Interactions
Caspase 10 has been shown to interact with FADD, CFLAR, Caspase 8, Fas receptor, RYBP, TNFRSF1A and TNFRSF10B.
Caveolin 1
Caveolin-1 is a protein that in humans is encoded by the CAV1 gene.

# Function
The scaffolding protein encoded by this gene is the main component of the caveolae plasma membranes found in most cell types. The protein links integrin subunits to the tyrosine kinase FYN, an initiating step in coupling integrins to the Ras-ERK pathway and promoting cell cycle progression. The gene is a tumor suppressor gene candidate and a negative regulator of the Ras-p42/44 MAP kinase cascade. CAV1 and CAV2 are located next to each other on chromosome 7 and express colocalizing proteins that form a stable hetero-oligomeric complex. By using alternative initiation codons in the same reading frame, two isoforms (alpha and beta) are encoded by a single transcript from this gene.

# Interactions
Caveolin 1 has been shown to interact with heterotrimeric G proteins,
Src tyrosine kinases (Src, Lyn) and H-Ras, 
cholesterol,
TGF beta receptor 1, 
endothelial NOS, 
androgen receptor, 
amyloid precursor protein, 
gap junction protein, alpha 1,
nitric oxide synthase 2A, epidermal growth factor receptor, endothelin receptor type B, PDGFRB, PDGFRA, PTGS2, TRAF2, estrogen receptor alpha, caveolin 2, PLD2, Bruton's tyrosine kinase and SCP2. All these interactions are through a caveolin-scaffolding domain (CSD) within caveolin-1 molecule. Molecules that interact with caveolin-1 contain caveolin-binding motifs (CBM).
CCS (gene)
Copper chaperone for superoxide dismutase is a metalloprotein that is responsible for the delivery of Cu to superoxide dismutase (SOD1). CCS is a 54kDa protein that is present in mammals and most eukaryotes including yeast. The structure of CCS is composed of three distinct domains that are necessary for its function. Although CCS is important for many organisms, there are CCS independent pathways for SOD1, and many species lack CCS all together, such as C. elegans. In humans the protein is encoded by the CCS gene.

# Structure and function
CCS is composed of three domains. Domain I is located on the N-terminus and contains the MXCXXC Cu binding sequence. It has been determined to be necessary for function of CCS but its specific role is currently unknown. The structure of domain II greatly resembles that of SOD1 which allows it to perform the function of binding to SOD1. Domain III contains a CXC Cu binding motif and performs the Cu insertion and subsequent disulfide oxidation of SOD1.
When CCS docks to SOD1, cysteine 244 of CCS and 57 of SOD1 form a disulfide linkage. This disulfide bond is then transferred to form a disulfide bridge between cysteine 57 and 146 of SOD1. CCS's catalytic oxidation of SOD1's disulfide bridge can only be performed in the presence of oxygen. Furthermore, the disulfide linkage of SOD1 can be performed without the presence of CCS but requires oxygen and is much slower. Additionally, CCS is proposed to help the proper folding of SOD1 by binding in the apo-state.
As well as SOD1, CCS (gene) has been shown to interact with APBA1.

# Localization
CCS is localized in the nucleus, cytosol, and mitochondrial intermembrane space. CCS is imported to the mitochondria by Mia40 and Erv1 disulfide relay system. The cysteine 64 of CCS Domain I generates a disulfide intermediate with Mia40. This disulfide bond is transferred to link cysteine 64 and 27 of CCS, stabilizing the protein in the mitochondrial intermembrane space where it delivers Cu to the Cu-less apo-SOD1.

# Role in copper homeostasis
In mammals cellular Cu levels are regulated by CCS's interaction with the 26S proteasome. During times of Cu excess CCS delivers Cu to XIAP and primes the complex for auto-ubiquitination and subsequent degradation. Expression of SOD1 is not modified by Cu availability but by CCS ability to deliver Cu. Knockouts of CCS (ccs) show 70-90% decrease in SOD1 activity as well as increased expression of Cu binding proteins, namely, MT-I, MT-II, ATOX1, COX17, ATP7A to, presumably, reduce the amount of free Cu.
Cells with CCS mutants have been shown to display ALS like symptoms. Moreover, SOD1 mutants that have altered interactions with CCS have been shown to display misfolding and aggregation.
Syndecan 1
Syndecan 1 is a protein which in humans is encoded by the SDC1 gene.

# Function
The protein encoded by this gene is a transmembrane (type I) heparan sulfate proteoglycan and is a member of the syndecan proteoglycan family. The syndecans mediate cell binding, cell signaling, and cytoskeletal organization and syndecan receptors are required for internalization of the  HIV-1 tat protein. The syndecan-1 protein functions as an integral membrane protein and participates in cell proliferation, cell migration and cell-matrix interactions via its receptor for extracellular matrix proteins. Syndecan-1 is a sponge for growth factors, with binding largely via heparan sulfate chains.
An exception is the prosecretory mitogen lacritin that binds syndecan-1 only after heparanase modification. Binding utilizes an enzyme-regulated 'off-on' switch in which active epithelial heparanase (HPSE) cleaves off heparan sulfate to expose a binding site in the N-terminal region of syndecan-1's core protein. Three SDC1 elements are required.  (1) The heparanase-exposed hydrophobic sequence GAGAL that promotes the alpha helicity of lacritin's C-terminal amphipathic alpha helix form and likely binds to the hydrophobic face.  (2) Heparanase-cleaved heparan sulfate that is 3-O sulfated.  This likely interacts with the cationic face of lacritin's C-terminal amphipathic alpha helix.  (3) An N-terminal chondroitin sulfate chain that also likely binds to the cationic face.  Point mutagenesis of lacritin has narrowed the ligation site.
While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. These two represent the major variants of this gene and encode the same protein.

# Clinical significance
Altered syndecan-1 expression has been detected in several different tumor types.
It is a specific antigen on multiple myeloma cells.
Indatuximab ravtansine targets this protein.

# Application
It is a useful marker for plasma cells, but only if the cells tested are already known to be derived from blood.
Chimerin 1
Chimerin 1, (CHN1) also known as alpha-1-chimerin, n-chimerin is a protein which in humans is encoded by the CHN1 gene.
Chimerin 1 is a GTPase activating protein specific for RAC GTP-binding proteins. It is expressed primarily in the brain and may be involved in signal transduction.
This gene encodes GTPase-activating protein for p21-rac and a phorbol ester receptor. It plays an important role in ocular motor axon pathfinding.

# Function
CHN1 is a three-domain protein with the N-terminal SH2 domain, the C-terminal RhoGAP domain and the central C1 domain similar to protein kinase C. When lipid diacylglycerol (DAG) binds to the C1 domain, CHN1 is transferred to the plasma membrane and negatively regulates Rho-family small GTPases RAC1 and CDC42, thus causing the morphological change of axons by pruning the ends of axon dendrites.
Mutational analysis suggests that un-overlapping residues of the RhoGAP domain are involved in RAC1-binding and the RAC1-GAP activity. Regulation of the RhoGAP activity of CHN1 by phorbol esters, natural compounds mimic of the lipid second messenger DAG, presents a possible way of designing agents for therapeutics.

# Clinical significance
Heterozygous missense mutations in this gene cause Duane's retraction syndrome 2 (DURS2).
CKB (gene)
Brain-type creatine kinase also known as CK-BB is a creatine kinase that in humans is encoded by the CKB gene.

# Function
The protein encoded by this gene, CK-BB, consists of a homodimer of two identical brain-type CK-B subunits. BB-CK is a cytoplasmic enzyme involved in cellular energy homeostasis, with certain fractions of the enzyme being bound to cell membranes, ATPases, and a variety of ATP-requiring enzymes in the cell. There, CK-BB forms tightly coupled microcompartments for in situ regeneration of ATP that has been used up. The encoded protein reversibly catalyzes the transfer of "energy-rich" phosphate between ATP and creatine or between phospho-creatine (PCr) and ADP. Its functional entity is a homodimer (CK-BB) in brain and smooth muscle as well as in other tissues and cells such as neuronal cells, retina, kidney, bone, etc.  In heart, a heterodimer (CK-MB) shahil consisting of one CK-B brain-type CK subunit and one CK-M muscle-type CK subunit is prominently expressed.  The encoded CK-BB and CK-MB proteins are members of the ATP:guanido phosphotransferase protein family.

# Ectopic expression
Ectopic expression (CKBE) of the B (brain) type of creatine kinase (CK-BB) in red cells and platelets is a rare, benign anomaly detected during a newborn screening program for Duchenne muscular dystrophy.
CKM (gene)
Creatine kinase, muscle also known as CKM is a creatine kinase that in humans is encoded by the CKM gene.

# Structure
In the figure to the right, the crystal structure of the muscle-type M-CK monomer is shown.  In vivo, two such monomers arrange symmetrically to form the active MM-CK enzyme.

# Function
The protein encoded by this gene is a cytoplasmic enzyme involved in cellular energy homeostasis. The encoded protein reversibly catalyzes the transfer of "energy-rich" phosphate between ATP and creatine and between phospho-creatine and ADP. Its functional entity is a MM-CK homodimer in striated (sarcomeric) skeletal and cardiac muscle.

# Clinical significance
In heart, in addition to the MM-CK homodimer, also the heterodimer MB-CK consisting of one muscle (M-CK) and one brain-type (B-CK) subunit is expressed. The latter may be an important serum marker for myocardial infarction, if released from damaged myocardial cells into the blood where it can be detected by clinical chemistry.
CLAS Trial

# Objective
To determine whether combined therapy with the lipid lowering agents colestipol hydrochloride (30g daily) plus niacin (3-12g daily) would produce significant change in coronary, carotid, and femoral artery atherosclerosis and coronary bypass graft lesions as determined by angiography.  Also, to determine possible correlations between lesion changes and plasma lipid and lipoprotein cholesterol levels and to explore interrelationships of atherosclerosis change in femoral, coronary, and carotid arteries.

# Methods
CLAS (Cholesterol Lowering Atherosclerosis Study) was a randomized, selectively blinded study wherein 188 men, with known previous coronary artery bypass grafts, were randomized to diet plus placebo or diet plus combined lipid lowering therapy consisting of colestipol and niacin and followed up at 2 years and 4 years.

# Results
The following results were noted:
- Treatment group had a 37% raise in HDL-C levels and a 43% reduction in LDL-C levels.
- Regression of atherosclerosis, as measured by angiography, was greater with combined drug treatment at 2 years and at 4 years.
- Reduction in the percentage of subjects with new atheroma formation in native coronary arteries.
- Significantly reduced percentage of subjects with new lesions or any adverse change in bypass grafts.
- Atherosclerosis regression occurred in 16.2% of colestipol-niacin treated vs 2.4% placebo treated

# Conclusion
The benefit of combined nicotinic acid and colestipol therapy was most prominent in patients with baseline plasma cholesterol levels above 240 mg/dL.
CNO (gene)
Protein cappuccino homolog is a protein that in humans is encoded by the CNO gene.
This intronless gene encodes a protein that may play a role in organelle biogenesis associated with melanosomes, platelet dense granules, and lysosomes. A similar protein in mouse is a component of a protein complex termed biogenesis of lysosome-related organelles complex 1 (BLOC-1), and is a model for HermanskyPudlak syndrome. The encoded protein may play a role in intracellular vesicular trafficking.

# Interactions
CNO (gene) has been shown to interact with BLOC1S2 and PLDN.
CO2 sensor

# Overview
A CO2 sensor is an instrument for the measurement of carbon dioxide gas. The most common principles for CO2 sensors are infrared gas sensors (NDIR) and chemical gas sensors.

# Nondispersive Infrared (NDIR) CO2 Sensors
NDIR sensors are the simplest of the spectroscopic sensors. The key components are an infrared source, a light tube, an interference (wavelength) filter, and an infrared detector. The gas is pumped or diffuses into the light tube, and the electronics measures the absorption of the characteristic wavelength of light. NDIR sensors are most often used for measuring carbon dioxide.  The best of these have sensitivities of 20-50 PPM.  Typical NDIR sensors are still in the (US) $100 to $1000 range. Most are used for carbon dioxide, because no other sensing method works reliably for this gas. New developments include using MEMS to bring down the costs of this sensor and to create smaller devices (for example for use in air conditioning applications).

# Chemical CO2 Sensors
Chemical CO2 gas sensors with sensitive layers based on polymer- or heteropolysiloxane have the principal advantage of a very low energy consumption and can be reduced in size to fit into microelectronic-based systems. On the downside, short- and long term drift effects as well as a rather low overall lifetime are major obstacles when compared with the NDIR measurement principle.
Calcinosis
Calcinosis is the formation of calcium deposits in any soft tissue.

# Types

## Dystrophic calcification
The most common type of calcinosis is dystrophic calcification.  This type of calcification can occur as a response to any soft tissue damage, including that involved in implantation of medical devices.

## Metastatic calcification
Metastatic calcification involves a systemic calcium-phosphate mineral imbalance, which can be caused by renal failure, milk-alkali syndrome, or other etiologies.

## Tumoral calcinosis
The etiology of the rare condition of tumoral calcinosis is not entirely understood.  It is generally characterized by large, globular calcifications near joints.
Hyperphosphatemic familial tumoral calcinosis (HFTC) is a rare autosomal recessive metabolic disorder. Its principal clinical features are represented by ectopic periarticular calcifications associated with elevated levels of serum phosphate. HFTC is characterized by extensive phenotypic and genetic heterogeneity. HFTC has been shown to result from mutations in two genes: GALNT3 and FGF23. All GALNT3 mutations reported up to March 2006 were identified in patients of either Middle Eastern or African-American extraction. The secretion of FGF23 requires O-glycosylation, which is selectively directed by GALNT3, to block processing of FGF23.