Persius/hicric huggingface dataset:
Rouleaux

# Overview
Rouleaux (singular is rouleau) are stacks of red blood cells formed because of the unique discoid shape of these cells in vertebrate body. The flat surface of the discoid RBCs give them a large surface area to make contact and stick to each other forming rouleux. They occur when the plasma protein concentration is high, and because of them the ESR (erythrocyte sedimentation rate) is also increased. Conditions which do this include infections, inflammatory and connective tissue disorders, and cancers. It also occurs in diabetics and is one of the causative factors for microvascular occlusion in diabetic retinopathy.
1. Rouleaux refers to the stacking of RBC
2. The presence of acute phase proteins particularly fibrinogen interacts with sialic acid on the surface of RBC and allows the formation of rouleaux
3. Anaemia by altering the ratio of RBC to plasma increases rouleaux formation and accelerates sedimentation
4. Rouleaux formation is retarded by albumin proteins

# Kinetics of Linear Rouleaux Formation
According to Smoluchowski, the kinetics of aggregation of colloids is based on the assumption that each particle is surrounded by a "sphere influence. Single spherical particles, which undergo Brownian motion collide and sticking of particles. As aggregation proceeds, the average diffusion constant of the aggregate population decreases. The aggregation of red blood cells prgresses in the same manner except that cells are biconcave rather than spherical.
Ryegrass

# Overview
Ryegrass (Lolium) is a genus of nine species of tufted grasses in the Pooideae subfamily of the Poaceae family. They are characterized by bunch-like growth habits. Also called tares (even though there is no firm evidence that this is the same as the plant given that name in English language translations of the Bible (as in the "Parable of the Tares") - vetches are another candidate), these plants are native to Europe, Asia and northern Africa, but are widely cultivated and naturalized elsewhere. Ryegrasses are naturally diploid, with 2n = 14, and are closely related to the fescues Festuca.
Ryegrass should not be confused with rye, which is a grain crop.

# Species
The following are accepted as distinct species:
- Lolium canariense Steud. - Canary Islands ryegrass
- Lolium edwardii H.Scholz, Stierst. & Gaisberg
- Lolium multiflorum Lam. - Italian ryegrass
- Lolium perenne L. - Perennial ryegrass
- Lolium persicum - Persian ryegrass or Persian darnel
- Lolium remotum Schrank
- Lolium rigidum Gaudin - Stiff darnel, Wimmera ryegrass
- Lolium temulentum L. - Darnel, poison darnel

# Cultivation and uses
Ryegrasses contain some species which are important grasses for both lawns, and as pasture and for grazing and hay for livestock, being a highly nutritious stock feed. Ryegrasses are also used in soil erosion control programs. It is the principal grazing grass in New Zealand where some 10 million kilograms of certified seed are produced every year. There is a  large range of cultivars.  The primary species found worldwide and used for both lawns and as a forage crop is perennial ryegrass (Lolium perenne). Like many cool-season grasses of the family Poaceae, it harbors a symbiotic fungal endophyte, either Epichloe or its close relative Neotyphodium, of which both are of the fungal family Clavicipitaceae
Some species, particularly L. temulentum, are weeds which can have a severe impact on the production of wheat and other crops. Ryegrass pollen is also one of the major causes of hay fever.
Many grass tennis courts including Wimbledon are planted in ryegrass in different compositions, depending on the tournament.

# Synonyms
- L. ambiguum = Lolium multiflorum
- L. annuum = Lolium temulentum
- L. arundinaceum = Festuca arundinacea
- L. berteronianum = Lolium temulentum
- L. brasilianum = Lolium perenne
- L. canadense = Lolium perenne
- L. crassiculme = Lolium rigidum
- L. cuneatum = Lolium temulentum
- L. dorei = Lolium persicum
- L. giganteum = Festuca gigantea
- L. gracile = Lolium temulentum
- L. lepturoides = Lolium rigidum subsp. lepturoides
- L. marschallii = Lolium perenne
- L. parabolicae = Lolium rigidum
- L. pratense = Festuca pratensis
- L. remotum = Lolium temulentum subsp. remotum
- L. romanum = Lolium multiflorum
- L. scabrum = Lolium multiflorum
- L. siculum = Lolium multiflorum
- L. subulatum = Lolium rigidum subsp. lepturoides
- L. teres = Lolium rigidum subsp. lepturoides
- L. trabutii = Lolium rigidum
SAPS III

# Overview
SAPS III is a system for predicting mortality, one of several ICU scoring systems. Its name stands for "Simplified Acute Physiology Score" and is a supplement to the SAPS II scoring system. It has been designed to provide a real-life predicted mortality for a patient by following a well defined procedure, based on a mathematical model that needs calibration. Predicted mortalities are good when comparing groups of patients, and having near-real-life mortalities means, that this scoring system can answer questions like "if the patients from hospital A had been in hospital B, what would their mortality have been?".
However, in order to achieve this great functionality, you must calibrate the system, which is additional effort, and it is difficult to compare two groups of patients if they weren't scored using the same calibration. SAPS III is therefore not suitable for publishing data about the morbidity of a single group of patients.
The SAPS III project is conducted by the SAPS III Outcomes Research Group (SORG).
SECISBP2
SECIS-binding protein 2 (commonly referred to as SBP2) is a protein that in humans is encoded by the SECISBP2 gene.

# Function
The incorporation of selenocysteine into a protein requires the concerted action of an mRNA element called a sec insertion sequence (SECIS), a selenocysteine-specific translation elongation factor and a SECIS binding protein. With these elements in place, a UGA codon can be decoded as selenocysteine. SBP2 is a nuclear protein that functions as a SECIS binding protein, but experimental evidence indicates that SBP2 is cytoplasmic.

# Clinical significance
Mutations in this gene have been associated with a reduction in activity of a specific thyroxine deiodinase, a selenocysteine-containing enzyme, and abnormal thyroid hormone metabolism.
SERPINB1
Leukocyte elastase inhibitor (LEI) also known as serpin B1 is a protein that in humans is encoded by the SERPINB1 gene. It is a member of the clade B serpins or ov-serpins (ovalbumin related serpins) founded by ovalbumin.
MNEI (monocyte/neutrophil elastase inhibitor) is the mouse orthologue of human SerpinB1.

# Function
SerpinB1 is a cytoplasmic serine protease inhibitor of  polymorphonuclear neutrophils. Among other serine proteases, it specifically inhibits  neutrophil elastase, PR3 and cathepsin G, all found in neutrophil granules, by a suicide inhibition mechanism. SerpinB1 was found to reduce tissue damage caused by the mentioned proteases during inflammation and has a role in neutrophil homeostasis in mice. In various infection models (e.g. pneumonia) correlation of SerpinB1 absence and lack of microbial clearance have been shown. Different knockout strains serve as model to investigate the role of SerpinB1 in vivo.
SH3BGRL3
SH3 domain-binding glutamic acid-rich-like protein 3 is a protein that in humans is encoded by the SH3BGRL3 gene.
The 10.5kDa protein SH3 binding glutamic acid-rich protein-like 3 has an isoelectric point of 5.0. SH3 binding glutamic acid-rich (SH3BGR) gene is located to human chromosome 21. Two homologous genes, SH3BGRL and SH3BGRL3 are located to chromosome Xq13.3 and 1p34.3-35, respectively and code for small proteins similar to the N-terminal region of the SH3BGR protein. SH3BGRL3 protein shows a significant similarity to glutaredoxin 1 of E. coli, and all the three proteins are predicted to belong to thioredoxin-like protein family. Glutaredoxins (GRXs) are ubiquitous oxidoreductases, which catalyze the reduction of many intra-cellular protein disulfides and play an important role in many redox pathways. However, the SH3BGRL3 protein lacks the enzymatic function of glutaredoxins and may have a role as a regulator of redox activity.

# Role in cancer
Proteins such as glutaredoxin and thioredoxin are reported as up-regulated in many cancers such as lung and pancreatic; they have been implicated in increased resistance of cancer cells to free-radicals. There is little current evidence which directly links SH3GRPL3 with survival in cancer cells, however the protein has recently been identified as up-regulated in glioblastoma multiforme compared to normal cerebral tissue on proteomic analysis. Studies of acute promyelocytic leukemia cell line NB4 have also reported up-regulation of the protein. Conversely, the related protein SH3BGRL is reported to be downregulated in fibroblasts, lymphoid cells, and splenic tumor cells transformed by the viral oncogene v-Rel. Co-expression of SH3BGRL with v-Rel in primary splenic lymphocytes reduced the number of colonies formed by 76%.  Xu et al. reported SH3BGRPL3 protein as a post-translational modification of the 27kDa tumor necrosis factor alpha (TNF-) inhibitory protein, TIP-B1. This protein is potentially involved in resistance of cells to the apoptosis-inducing affect of TNF-.
SIGLEC10
Sialic acid-binding Ig-like lectin 10 is a protein that in humans is encoded by the SIGLEC10 gene.  The mouse orthologue is Siglec G.

# Structure and Function
Like most but not all other Siglecs, Siglec-10 bears an ITIM (Immunoreceptor tyrosine-based inhibitory motif) within its cytoplasmic domain. Siglec-10 is a ligand for CD52, the target of the therapeutic monoclonal antibody Alemtuzumab. It is also reported to bind to Vascular adhesion protein 1 (VAP-1) and to the co-stimulatory molecule CD24 also known as HSA (Heat-stable antigen).

# Gene Family summary
SIGLECs are members of the immunoglobulin superfamily that are expressed on the cell surface. Most SIGLECs have 1 or more cytoplasmic immune receptor tyrosine-based inhibitory motifs, or ITIMs. SIGLECs are typically expressed on cells of the innate immune system, with the exception of the B-cell expressed SIGLEC6 (MIM 604405).
SLC22A12
Solute carrier family 22 (organic anion/cation transporter), member 12, also known as SLC22A12 and URAT1, is a protein which in humans is encoded by the SLC22A12 gene.

# Function
The protein encoded by this gene is a urate transporter and urate-anion exchanger which regulates the level of urate in the blood. This protein is an integral membrane protein primarily found in kidney. Two transcript variants encoding different isoforms have been found for this gene.

# Clinical significance
Numerous single nucleotide polymorphisms of this gene are significantly associated with altered (increased or decreased) reabsorption of uric acid by the kidneys. Respectively, these altered rates of reabsorption contribute to hyperuricemia and hypouricemia.

# Interactions
SLC22A12 has been shown to interact with PDZK1.

# Inhibition
Lesinurad is a urate transporter inhibitor that has been approved to treat gout. Lesinurad enhances urate excretion by inhibition the tubular re-absorption. Probenecid also facilitates uric acid secretion.
SLC25A21
Mitochondrial 2-oxodicarboxylate carrier also known as solute carrier family 25 member 21 (SLC25A21) is a protein that in humans is encoded by the SLC25A21 gene.
It is a homolog of the S. cerevisiae ODC proteins, mitochondrial carriers that transport C5-C7 oxodicarboxylates across inner mitochondrial membranes. One of the species transported by ODC is 2-oxoadipate, a common intermediate in the catabolism of lysine, tryptophan, and hydroxylysine in mammals. Within mitochondria, 2-oxoadipate is converted into acetyl-CoA.

# Model organisms
Model organisms have been used in the study of SLC25A21 function. A conditional knockout mouse line, called Slc25a21tm1a(KOMP)Wtsi was generated as part of the International Knockout Mouse Consortium program  a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty one tests were carried out on homozygous mutant mice and ten significant abnormalities were observed, including sub-viability at weaning, decreased body weight, absent pinna reflex, abnormal snout, skull, spine and tooth morphology, atypical indirect calorimetry, body composition and plasma chemistry data, increased mean platelet volume and moderate elevations in auditory thresholds.
SLC25A46
Solute carrier family 25 member 46 is a protein that in humans is encoded by the SLC25A46 gene. This protein is a member of the SLC25 mitochondrial solute carrier family. It is a transmembrane protein located in the mitochondrial outer membrane involved in lipid transfer from the endoplasmic reticulum (ER) to mitochondria. Mutations in this gene result in neuropathy and optic atrophy.

# Structure
The SLC25A46 gene is located on the q arm of chromosome 5 in position 22.1 and spans 27,039 base pairs. The gene produces a 46.2 kDa protein composed of 418 amino acids. This gene has 8 exons and encodes a multi-pass integral membrane protein localized to the mitochondrial outer membrane.

# Function
The encoded protein is an orphan transporter involved in lipid transfer from the endoplasmic reticulum to mitochondria. It promotes mitochondrial fission and prevents the formation of hyperfilamentous mitochondria. This protein forms a complex with mitofilin (IMMT) on the inner mitochondrial membrane, independent of MFN2.

# Clinical Significance
Mutations in the SLC25A46 gene, inherited in an autosomal recessive manner, cause type 6B hereditary motor and sensory neuropathy. Symptoms include early-onset optic atrophy, progressive visual loss, and peripheral sensorimotor neuropathy manifesting as axonal Charcot-Marie-Tooth disease, with variable age at onset and severity.
Overexpression of this protein causes mitochondrial fragmentation while knockdown of this protein causes mitochondrial hyperfusion and hyperfilamentous mitochondria due to decreased mitochondrial fission. Loss of this gene also has many other effects: premature cellular senescence, impaired cellular respiration, destabilization of the MICOS (mitochondrial contact site and cristae organizing system) complex, loss of and shortened cristae, altered ER morphology, impaired cell migration, and changes in mitochondrial phospholipid composition.

# Interactions
This protein interacts with IMMT, a component of the MICOS complex, along with other components of this complex and components of an ER membrane protein complex involved in transferring lipids to mitochondria. Additionally, this protein interacts with SLC7A8, SLC10A1, SLC10A6, FHL3, FUNDC1, linc01142, LEPROTL1, ODF4, VMA21, MFSD14B, PQLC1, HSD17B11, REEP2, REEP4, and TOMM22. This protein possibly interacts with OPA1 and MFN2.
SLC38A10
Sodium-coupled neutral amino acid transporter 10 also known as solute carrier family 38, member 10 is a protein that in humans is encoded by the SLC38A10 gene.

# Model organisms
Model organisms have been used in the study of SLC38A10 function. A conditional knockout mouse line, called Slc38a10tm1a(EUCOMM)Wtsi was generated as part of the International Knockout Mouse Consortium program  a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty four tests were carried out on mutant mice and four significant abnormalities were observed. Homozygous animals of both sex had decreased body weights, and DEXA analysis showed that this correlated with decreased bone mineral content and decreased body length. Indirect calorimetry analysis showed that males displayed increased oxygen consumption and energy expenditure, while clinical chemistry tests found that females had decreased circulating amylase levels and males had hypoalbuminemia and increased circulating creatinine levels.
SMARCAL1
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1 is a protein that in humans is encoded by the SMARCAL1 gene.

# Function
The protein encoded by this gene is a member of the SWI/SNF family of proteins. Members of this family have helicase and ATPase activities and are thought to regulate transcription of certain genes by altering the chromatin structure around those genes. The SMARCAL1 protein convert RPA-bound, single stranded DNA into double-stranded DNA, an enzyme activity termed "annealing helicase".
The encoded protein shows sequence similarity to the E. coli RNA polymerase-binding protein HepA. Mutations in this gene are a cause of Schimke immunoosseous dysplasia (SIOD), an autosomal recessive disorder with the diagnostic features of spondyloepiphyseal dysplasia, renal dysfunction, and T-cell immunodeficiency.

# Model organisms
Model organisms have been used in the study of SMARCAL1 function. A conditional knockout mouse line, called Smarcal1tm1a(EUCOMM)Wtsi was generated as part of the International Knockout Mouse Consortium program  a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty tests were carried out and one significant phenotype was observed: homozygous mutant mice had abnormal brain histopathology, including an enlarged hippocampus and a thickened hippocampus stratum oriens.
Sapience

# Overview
Sapience is often defined as wisdom, or the ability of an organism or entity to act with judgment. Judgment is a mental facility that is a particular form of intelligence or
may be considered an additional facility, above intelligence, with its own properties. Robert Sternberg  has segregated the capacity for judgment from ordinary meanings of intelligence, which is closer to the sense of clever than to wisdom. Good judgment in making decisions about complex life or social decisions is a hallmark of being wise.
The word sapience is derived from the Latin word for wisdom, sapientia.  Both are related to the Latin verb sapere, which means "to taste, to be wise, to know ;" the present participle of sapere forms part of Homo sapiens, the Latin binomial nomenclature created by Carolus Linnaeus to describe the human species. Linnaeus had originally given humans the species name of diurnus, meaning man of the day. But he later decided that the dominating feature of humans was wisdom, hence application of the name sapiens. His chosen biological name was intended to emphasize man's uniqueness and separation from the rest of the animal kingdom.
Sedation

# Overview
Sedation is a medical procedure involving the administration of sedative drugs, generally to facilitate a medical procedure with local anaesthesia.

# Uses
Sedation is typically used in procedures such as endoscopy, vasectomy, or minor surgery and in dentistry for reconstructive surgery, some cosmetic surgeries, removal of impacted wisdom teeth, or for high-anxiety patients. Sedation methods in dentistry include inhalation sedation (using nitrous oxide), oral sedation, and intravenous (IV) sedation. Inhalation sedation is also sometimes referred to as Relative Analgesia.
Sedation is also used extensively in the intensive care unit so that patients who are being ventilated tolerate having an endotracheal tube in their trachea.

# Risks
Airway obstruction, apnoea and hypotension are not uncommon during sedation and require the presence of health professionals who are suitably trained to detect and manage these problems.

# Causes
- Drug side effect:
Butorphanol
Carbinoxamine
Clobazam
Diphenhydramine
Hydrocodone bitartrate and acetaminophen
Metyrapone
Metirosine
Nabilone
Oxaprozin
Papaverine
Sodium oxybate
- Butorphanol
- Carbinoxamine
- Clobazam
- Diphenhydramine
- Hydrocodone bitartrate and acetaminophen
- Metyrapone
- Metirosine
- Nabilone
- Oxaprozin
- Papaverine
- Sodium oxybate

# Levels of sedation
Sedation scales are used in medical situations in conjunction with a medical history in assessing the applicable degree of sedation in patients in order to avoid under-sedation (the patient risks experiencing pain or distress) and over-sedation (the patient risks side effects such as suppression of breathing, which might lead to death). Typically, levels are (i) agitation, (ii) calm, (iii) responsive to voice only, (iv) responsive to shaking only, (v) responsive to pain only,  and (vi) not responsive.
Examples of sedation scales include: MSAT (Minnesota Sedation Assessment Tool) and the Ramsay Scale (Ramsay, et al. 1974)
Selectin
Selectins are a family of cell adhesion molecules (or CAM's). All selectins are single-chain transmembrane glycoproteins which share similar properties to C-type lectins due to a related amino terminus and calcium-dependent binding.

# Types
There are three subsets of selectins:
- E-selectin (in endothelial cells)
- L-selectin (in leukocytes)
- P-selectin (in platelets and endothelial cells)

# Etymology
The name selectin comes from the words "selected" and "lectins" which are a type of carbohydrate recognizing proteins.

# Function
During an inflammatory response stimuli such as histamine and thrombin cause endothelial cells to mobilize P-selectin from stores inside the cell to the cell surface. In addition, cytokines such as TNF-alpha stimulate the expression of E-selectin and additional P-selectin a few hours later.
As the leukocyte rolls along the blood vessel wall, the distal lectin-like domain of the selectin binds to certain carbohydrate groups presented on proteins (such as PSGL-1) on the leukocyte, which slows the cell and allows it to leave the blood vessel and enter the site of infection. The low-affinity nature of selectins is what allows the characteristic "rolling" action attributed to leukocytes during the leukocyte adhesion cascade.
The best-characterized ligand for the three selectins is P-selectin glycoprotein ligand-1 (PSGL-1), which is a mucin-type glycoprotein expressed on all white blood cells.
Neutrophils and eosinophils bind to E-selectin. One of the reported ligands for E-selectin is the sialylated Lewis X Ag (sLe(x)). Eosinophils, like neutrophils, use sialylated, protease-resistant structures to bind to E-selectin, although the eosinophil expresses much lower levels of these structures on its surface. 
Ligands for P-selectin on eosinophils and neutrophils are similar sialylated, protease-sensitive, endo-beta-galactosidase-resistant structures, clearly different than those reported for E-selectin, and suggest disparate roles for P-selectin and E-selectin during recruitment during inflammatory responses.