Persius/hicric huggingface dataset:
Sue Bale
Professor Sue Bale FRCN, PhD, BA, RGN, NDN, RHV, PG Dip, Dip N is a UK nurse with a special interest in wound healing. She received her Ph D from the University of Glamorgan in 2003.

# Work in wound healing
She was part of the original team that established a unique wound healing service in The Wound Healing Research Unit, Cardiff, based in the University of Wales College of Medicine. She is author of a wide range of books and articles on wound care.
Sue is a founder member of the Wound Care Society (1985); the European Wound Management Association; (1991); the Journal of Wound Care (1992); the European Pressure Ulcer Advisory Panel (1996). 

# Work
She works as Associate Director of Nursing (R&D) in Gwent Healthcare NHS Trust and lives in Monmouthshire.

# Fellowship
She is a fellow of the Royal College of Nursing.

# Recent publications:
Bale, Sue (2004). Wound Care Nursing, 2nd Edition - A Patient-Centered Approach. Mosby Ltd. ISBN 0-7234-3344-5. Unknown parameter |coauthors= ignored (help).mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"\"""\"""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{display:none;font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
Bale, Sue (2004). "The benefits of implementing a new skin care protocol in nursing homes". Journal of Tissue Viability. 14(2): 4450. Unknown parameter |coauthors= ignored (help)
Bale, Sue (2004). "A topical metronidazole gel used to treat malodorous wounds". British Journal of Nursing. 13(11). Unknown parameter |coauthors= ignored (help)
Jones, V. (2004). Acute and chronic wound healing. In "Wound Care Essentials Practice" (Baronowski S, and E. A. Ayello, Eds. Lippincott Williams and Wilkins. ISBN 1-58255-274-6. Unknown parameter |coauthors= ignored (help)
Sulfiram

# Overview
Sulfiram (INN) or monosulfiram, trade name Tetmosol, is an ectoparasiticide used in the treatment and prevention of scabies. It is usually sold as a solution or medicated soap, sometimes in combination with benzyl benzoate.
Sulfiram is now rarely used, but, as of  2010, is still available in Brazil, India, and South Africa (as monotherapy) and  France (with benzyl benzoate).

# Adverse effects
Dizziness, headache, fatigue and erythematous rash may occur. A single case of toxic epidermal necrolysis was reported in 1968.
Sulfiram is structurally related to disulfiram (Antabuse), and readily converts to disulfiram when exposed to light. Like disulfiram, it can produce an unpleasant reaction when consumed with alcohol.
Sultiame

# Overview
Sultiame (rINN, also known as sulthiame) is a sulfonamide and inhibitor of the enzyme carbonic anhydrase. It is used as an anticonvulsant.

# History
Sultiame was first synthesised in the laboratories of Bayer AG in the mid 1950s and eventually launched as Ospolot in Europe and other markets the early 1960s. It never became a registered drug in the USA. The brand was transferred to Desitin GmbH in 1993 and is sold in several European countries, in Israel, Japan, and Australia.
Sultiame became established as a second-line drug for treatment of partial epilepsy in the 1960s and 1970s and was often used in combination with the established anticonvulsant phenytoin. Temporal lobe seizures appeared particularly responsive to sultiame. Doubts subsequently arose as to whether sultiame has intrinsic anticonvulsant properties. After discovering sultiame's ability to raise the blood levels of phenytoin, it was assumed that sultiame would only act in combination with phenytoin. This finding, together with the equivocal results of a study in the US, resulted in a quick decline of sultiame's use. It was only in 1988, that the German child neurologist Hermann Doose discovered its specific effects in benign focal epilepsies of childhood. Today,  sulthiame is the drug of choice for benign focal epilepsies of childhood (such as benign rolandic epilepsy) in the German-speaking countries and Israel. There is renewed interest in sultiame's other potential uses, e.g., in West syndrome and other refractory epilepsies

# Indications
Historically, sultiame has been used to treat partial seizures. In Australia, it is currently registered for behavioural disorders associated with epilepsy; hyperkinetic behaviour; temporal lobe epilepsy; myoclonic seizures; grand mal attacks; and Jacksonian seizures. In contrast to other sulfonamide drugs, sultiame is devoid of antibacterial activity.

# Adverse effects
The more common adverse effects are ataxia, paraesthesia of face and limbs, hyperpnoea, dyspnoea, and anorexia. Less common adverse effects include giddiness, rash, StevensJohnson syndrome, nausea, weight loss, leukopenia, headache, psychic changes, depression, drooling, increased pain, frequency of fits, insomnia, status epilepticus. Disturbances in calcium and vitamin D metabolism have been occasionally reported after long-term use.

# Interactions
Sultiame taken together with primidone may lead to severe side-effects, including psychotic reactions. The addition of sulthiame to phenytoin therapy has shown to be followed by a rise in the serum levels of phenytoin. Sultiame may also lead to a rise of phenobarbitone blood levels. Alcohol must not be consumed during treatment.

# Overdose
Vomiting, hypotension, headache, vertigo, ataxia, metabolic acidosis with hyperpnoea and catatonic state may occur. There is no specific antidote. It is not known whether dialysis may help in case of overdose.

# Synthesis
p-Aminobenzenesulfonamide can be alkylated by -chlorobutylsulfonyl chloride in base via presumed intermediate, which spontaneously cyclizes to give sulthiame.
Sushruta

# Overview
Sushruta (also spelt Susruta or Sushrutha) (c. 6th century BC) was the first surgeon in the world who lived in ancient India and is the author of the book Sushruta Samhita, in which he describes over 120 surgical instruments, 300 surgical procedures and classifies human surgery in 8 categories. He lived and taught and practiced his art on the banks of the Ganga in the area that corresponds to the present day city of Varanasi in North India.
In the Sushruta school, the first person to expound Ayurvedic knowledge was Dhanvantari who then taught it to Divodasa who, in turn, taught it to Sushruta, Aupadhenava, Aurabhra, Paushakalavata, Gopurarakshita, and Bhoja.
Because of his seminal and numerous contributions to the science and art of surgery he is also known by the title "Father of Surgery." Much of what is known about this inventive surgeon is contained in a series of volumes he authored, which are collectively known as the Susrutha Samhita. The "Samhita" has some writings that date as late as the 1st century, and some scholars believe that there were contributions and additions to his teachings from generations of his students and disciples. Susrutha is also the father of Plastic Surgery and Cosmetic Surgery since his technique of forehead flap rhinoplasty (repairing the disfigured nose with a flap of skin from the forehead),that he used to reconstruct noses that were amputated, is practiced almost unchanged in technique to this day. The Susrutha Samhita contains the first known description of several operations, including the uniting of bowel, the removal of the prostate gland, the removal of cataract lenses and the draining of abscesses. Susrutha was also the first surgeon to advocate the practice of operations on inanimate objects such as watermelons, clay plots and reeds; thus predating the modern practice of the surgical workshop by half a millennium.
Sushruta was also a notable teacher. He told his pupils that one could become a good physician only if one knew both theory and practice. He advised his pupils to use carcases and models for practice before surgery.In addition to classifying worms that infect the human body, leeches for bloodletting, medicinal herbs, alkalies and metals, Sushruta gave a vague classification of animals.
Swelling
- Edema
Swelling can mean:
- In medicine:
Swelling (medical) is the enlargement of organs caused by accumulation of excess fluid in tissues, called edema.
- Swelling (medical) is the enlargement of organs caused by accumulation of excess fluid in tissues, called edema.
- In engineering:
Increase of volume of material, due to absorption of a solvent (common for plastic polymers)
Neutron-induced swelling caused by neutron radiation.
- Increase of volume of material, due to absorption of a solvent (common for plastic polymers)
- Neutron-induced swelling caused by neutron radiation.
Sylvatic
Sylvatic is a scientific term referring to diseases or pathogens affecting only wild (sylvan means forest-dwelling) animals.  In the context of animal research, its opposite is domestic, which refers to pets, farm animals or other animals which do not dwell in the wild.
- Examples: sylvatic rabies; sylvatic and domestic bacterial strains; sylvatic yellow fever
The word "sylvatic" is also simply a synonym for "sylvan" (or "silvan") = "of the forest".
Symplast
The symplast of a plant is the inner side of the plasma membrane in which water (and low molecular solutes) can freely diffuse.
The plasmodesmata allow the direct flow of small molecules such as sugars, amino acids and ions between cells. Larger molecules can also be transported through with the help of actin structures.
This allows direct cytoplasm to cytoplasm flow of water and other nutrients allow concentration gradients. It is particularly used in the root systems to bring in nutrients from soil. It moves these solutes from epidermis cells through the cortex into the endodermis and eventually the pericycle where it can be moved into the xylem for long distance transport.
It is contrasted with the apoplastic flow which uses cell wall transport.
T-tubule

# Overview
A T-tubule (or transverse tubule), is a deep invagination of the plasma membrane found in skeletal and cardiac muscle cells.  These invaginations allow depolarization of the membrane to quickly penetrate to the interior of the cell.

# Structure
Each muscle fiber consists of T-tubules which run perpendicularly (transversely) to the long axis of the fiber. As they are invaginations of the plasma membrane, each T-tubule is composed of a phospholipid bilayer in which are embedded a large number of L-type calcium channels. The T-tubule extends from the surface of the muscle fiber into its interior, effectively bringing the extracellular environment in proximity to the innermost confines of the cell.
In skeletal and cardiac muscle, the T-tubules are adjacent to the terminal sacs (or terminal cisternae) of the fiber's sarcoplasmic reticulum. In skeletal muscle, the T-tubule is surrounded by a pair of terminal cisternae in an arrangement called a triad that is found at the junction of the A and I bands. Cardiac muscle has a similar structure, the diad, which is composed of a T-tubule and a single terminal cisterna; it occurs at the Z line.

# Excitation-contraction coupling
T-tubules are the major sites for the coupling of excitation and contraction, which is the process whereby the spreading depolarization is converted into force production by muscle fibers. The L-type calcium channels in T-tubules activate in response to electrical stimulation; their opening allows calcium to flow down its electrochemical gradient and into the cell. Activation of the L-type channel also causes a mechanical interaction between it and calcium-release channels located on the adjacent sarcoplasmic reticulum membrane.
In skeletal muscle, the influx of calcium through the L-type calcium channel on the T-tubule contributes little to excitation-contraction coupling, whereas it is crucial to the proper function of cardiac muscle (see Cardiac action potential). Conversely, the mechanical interaction between the T-tubule's L-type calcium channel and the calcium-release channel is critical to proper skeletal muscle contraction, whereas it contributes little to the contraction of cardiac muscle.

# Detubulation
It is possible to physically and functionally uncouple T-tubules from the surface membrane using a technique known as detubulation. This relies on osmotically active chemicals, such as glycerol (for skeletal muscle) or formamide (mainly for cardiac muscle). Addition of these chemicals to the solution surrounding muscle cells causes the cells to shrink; when the chemical is withdrawn the cells rapidly expand before returning to their normal size. The rapid expansion is thought to cause the t-tubules to detach from the surface membrane, which reseals, and to reseal within the cell. This technique can be used to investigate the function of the t-tubules.
There is some evidence that heart failure precipitates the loss of the T-tubule network, again indicating their importance.
T.O.T.E.
T.O.T.E., standing for "Test - Operate - Test - Exit", is an iterative problem solving strategy based on feedback loops.
The self-control mechanisms in human tasking have been explained in terms of both operations and monitoring processes (Miller, Gallanter, and Pibram, 1960). Each recurring operation would be associated to a monitoring process, to test if the intended control was met or not.
Its premise is that a common algorithm for solving non-deterministic problems in a complex system, is to test where the system is currently, then perform some operation that makes a change, then retest again, and to repeat this until the answer is satisfactory, at which point the process is complete and ends (or exits).
TOTEs are often nested within other TOTEs, since as a means to meet a goal, they are applicable to sub-goals too.
It is commonly used in many disciplines where iterative methods are applicable, such as engineering, artificial intelligence, and cybernetics. In psychology, it is explicitly used as a key strategy within neuro-linguistic programming.

# More
Generic TOTE structure:
- Test to obtain some representation of the problem state
- Operate - intervene in some way
- Test again to see if the problem state is the same - if it is loop back to operate if it isn't
- Exit - problem solved

## Simple example
When driving a car and looking for the appropriate turn off.
- Test - is this the turnoff? - No
- Operate - keep driving
- Test - is this the turnoff? - No
- Operate - keep driving
- Test - is this the turnoff? - Yes
- Exit
(this only finds the correct turnoff, and would be embedded in a larger TOTE)

## Examples of nested TOTEs
Cooking a meal:
- The top level TOTE for "testing if meal is cooked" is:
Check meal -- leave a while -- recheck meal - take out of oven.
- As part of the "leave a while" part, there is a nested TOTE:
Check 5 minutes is up -- wait a while -- recheck 5 minutes is up -- exit (ie "leave a while" subgoal is achieved)

# Principles
- Working memory is limited to 72 chunks of information.
- Planning, consisting of TOTE units, is essential in cognitive process.
- Control of behavior exposes a set of chunks and TOTE units
TMEM106A
TMEM106A is a gene that encodes the transmembrane protein 106A (TMEM106A) in Homo sapiens. It is located at 17q21.31 on the plus strand next to cancer-related genes NBR1 and BRCA1. The TMEM106A gene contains a domain of unknown function, DUF1356.

# Protein structure
The TMEM106A protein has a molecular weight of 28.9 kdal. It has 262 amino acids, 240 of which are in the domain of function. The protein has a transmembrane region. There is evidence for a secondary transmembrane region in humans but this region is not conserved in related orthologs.  The protein does not contain a peptide signal protein. The protein structure contains a similar proportion of  alpha-helix and beta-strand secondary structures (this does not include transmembrane structures).
There are several areas for post-translational modification for TMEM106A including:
- Phosphorylation,
- N-glycosylation 
- Lysine glycosylation 

# Homology

## Paralogs
The TMEM106A gene has two paralogs: TMEM106B and TMEM106C. These paralogs belong to the gene family pfam07092, which belongs to the DUF1356 superfamily. This family consists of several mammalian proteins that are around 250 amino acids in length. TMEM106B and TMEM106C are conserved in invertebrates to mammals.

## Orthologs
The TMEM106A gene has been found in only the Chordate phylum. Of the three subphyla, TMEM106A is most commonly found in Vertebrata and has also been found in select members of Tunicata, which are invertebrate marine filter feeders. This phylum split occurred 722.5 million years ago. TMEM106A has not been seen in bacteria, plants, or fungi.

# Expression
TMEM106A is expressed in several human tissues. The tissues with highest expression are uterus, kidneys, small intestine, and stomach. EST profiles for orthologs show expression is conserved with greatest expression in kidneys and lesser expression in several other areas. Some tissues never show expression including: muscle, adipose tissue, and bone.

# Gene neighborhood
In Homo sapiens, TMEM106A is located next to NBR1, a gene identified as an ovarian tumor antigen monitored in ovarian cancer.  It is also located near BRCA1, a breast cancer tumor suppressor gene. The first 140 amino acids of the TMEM106A protein, including portions of DUF1356 and a transmembrane region, are deleted along with BRCA1 during early-onset breast cancer.
TMEM106C
TMEM106C is a gene that encodes the transmembrane protein 106C (TMEM106C) in Homo sapiens It has been found to be overexpressed in cancer cells and also is related to distal arthrogryposis, a condition of stiff joints and irregular muscle development. The TMEM106C gene contains a domain of unknown function, DUF1356, that spans most of the protein. Transmembrane protein 106C also goes by the aliases MGC5576 or MGC111210, LOC79022.

# Location and gene neighborhood
The TMEM106C gene is located on the long arm of the 12th chromosome. It is found at position 12q13.1. This gene spans from 48357225 to 48362667  on chromosome 12. This gene is in between COL2A1, the human type II collagen gene, and VDR, the human Vitamin D Receptor gene.
This protein is found to be an integral part of the endoplasm reticulum membrane.

# Protein structure
The TMEM106A protein has a molecular weight of 27.9 kdal with a PI of 6.325. It has 250 amino acids, 230 of which are in the domain of unknown function.  No signal peptide has been found for this protein but TMEM106C has transmembrane regions which gives evidence for an internal signal peptide.  This protein spans the ER membrane 2 times. There is evidence that these transmembrane regions take on helical structures. The predicted structure of the protein is shown to the left:
TMEM106C is valine-rich with no tryptophan.
There are several areas for post-translational modification for TMEM106A including:
- Phosphorylation
- Kinase-Specific Phosphoylation
- N-glycosylation

# Expression
This gene is highly expressed. TMEM106C is expressed 4.9 times the average gene.   TMEM106C has ubiquitous expression. It can be found expressed in many tissues types. Tissue types with high expression included the adrenal gland, eye, reproductive organs, cervix and blood. High expression was found using EST and GEO data.
This gene is also found overexpressed in cancer cells. This gene has found to be expressed three times more in adrenal tumor and twice more in bladder carcinoma and retinoblastoma than normal expression.
It is also found to be highly expressed in breast (mammary gland) tumor, cervical tumor, esophageal tumor, leukemia, liver tumor; lung tumor, pancreatic tumor, prostate cancer, and soft tissue/muscle tissue tumor.
TMEM106C is found in all stages of development from embryoid body, blastocyst, fetus, infant, juvenile and adult.

# Homology

## Paralogs
There are two paralogs for TMEM106C. These paralogs are TMEM106A and TMEM106B. Both genes are found highly conserved in Mammalia. TMEM106A is also found to be conserved in invertebrates as well. The protein was found in tapeworms and other invertebrate worms.

## Orthologs
TMEM106C is highly conserved in Mammalia. Links to sequences can be found in the table below:
TMEM229B
Transmembrane protein 229b is a protein that in humans is encoded by the TMEM229b gene.

# Nomenclature
The TMEM229B  gene is also known as C14orf83, FLJ33387, Q8NBD8, Hs.509707, Hs.712258, IPR010540, and CN083_HUMAN.

# Gene
The TMEM229B gene is located on the sense strand (-) of chromosome 14 at location 14q24.1 and spans the chromosomal locus 67,936,98367,982,021. Covering a total of 45,038 base pairs (bp) along the chromosome, the TMEM229B gene has a total of 3 exons in its primary unspliced transcript mRNA of 4,068 bp. There are a total of 7 transcript variants for TMEM229B ranging in mRNA size from 519 bp to 5008 bp. The TMEM229B gene is flanked by phosphatidylinotisol glycan anchor class H (PIGH), a protein associated with the endoplasmic reticulum specifically GPI-anchor biosynthesis, and PLEK2 on its left. See Figure 1.0. The gene is highly conserved in vertebrates, including portions of the approximately 3,000 base pairs of 3'UTR.

# Tissue distribution
Expressed sequence tag mapping of TMEM229B gene expression indicates that it is ubiquitously expressed throughout the body. TMEM229B is more heavily expressed in the parathyroid, skin, and thyroid tissues, and moderately expressed in bone marrow, trachea, spleen, eye, brain, pancreas, mammary gland, intestine, liver, thymus, lymph node, ovarian, muscle, lung, blood, and kidney tissues.

# Protein
The translated TMEM229B protein is a total of 167 amino acids long, with a predicted molecular weight of 19,531 Daltons. The TMEM229B protein contains a domain of unknown function, part of the domain family DUF1113, spanning from amino acids 87 to 135.
Based on predicted structure TMEM229b is highly resemblant of a connexin subunit. A highly conserved phosphorylation site exists at the Threonine-139 position. See multiple sequence alignment below.
- Annotated diagram of the TMEM229b gene (with its 3 exons), mature mRNA and protein domains. Functional peptide is predicted to take the form of a connexin 4-pass transmembrane subunit (seen below).
Annotated diagram of the TMEM229b gene (with its 3 exons), mature mRNA and protein domains. Functional peptide is predicted to take the form of a connexin 4-pass transmembrane subunit (seen below).

# Clinical relevance
Expression of the TMEM229B gene increases in several disease states including amelanotic skin melanoma, B-cell neoplasm, breast carcinoma, Burkitt's lymphoma, colorectal adenocarcinoma, carcinoma, cutaneous T cell lymphoma, esophageal carcinoma, gastric carcinoma, glioblastoma, liver carcinoma, lymphoma, melanoma, small cell lung carcinoma, T-cell acute lymphoblastic leukemia, thyroid carcinoma and Wilms' tumor as found in several microarray experiments. Over-expression of the TMEM229B gene has not been linked as a causal factor in any of these disease states.