Persius/hicric huggingface dataset:
HOSxP
HOSxP is a hospital information system, including Electronic health record (EHR), in use in over 70 hospitals across Thailand. The software aims to ease the healthcare workflow of health centers, for small sanitariums to central hospitals.
Before becoming HOSxP, the software was called KSK-HDBMS. Seeking a more friendly name, the development team opted for the name HOSxP, which comes from Hospital and Experience. The name also reflects the software's graphical user interface, which mimic the theme of Windows XP, no matter what actually the underlying operating system.
Distributed under GNU General Public License (GPL), HOSxP is free software.

# History
The development started in 1999. Emerged from a solo project by Chaiyaporn Suratemekul, a pharmacist by training, now main developers of the software are staffs from Bangkok Medical Software Co., Ltd., a company lead by Chaiyaporn. The development infrastructure, including source code repository, is hosted by SourceForge.net.

# Architecture and technical information
HOSxP uses a client-server architecture. For the database server, it is claimed to run on many RDBMS, like MySQL, Microsoft SQL Server, PostgreSQL, and Interbase/Firebird.
- Client-server (two-tier)
a server software can run on either Linux or Microsoft Windows
a client software can run only on Microsoft Windows
- a server software can run on either Linux or Microsoft Windows
- a client software can run only on Microsoft Windows
- Multi-tier technology (Borland DataSnap)
- Distributed Component Object Model (DCOM)
Borland Delphi and its Linux counterpart Kylix are the integrated development environments of choice in the project.
A user is allowed to write scripts in the Pascal programming language to automate tasks in HOSxP.

# Awards
- Thailand ICT Award 2004 2nd Healthcare Application
- Thailand ICT Award 2005 1st Healthcare Application
- Thailand ICT Award 2005 Popular Award
HOT-2
HOT-2, or 2,5-dimethoxy-4-(-ethylthio)-N-hydroxyphenethylamine is a psychedelic phenethylamine of the 2C family.  It was presumably first synthesized by Alexander Shulgin and reported in his book PIHKAL.

# Chemistry
HOT-2's full chemical name is 2-[4-(2-ethylthio)-2,5-dimethoxyphenyl-N-hydroxyethanamine.  It has structural properties similar to 2C-T-2 and to other drugs in the HOT- series, with the most closely related compounds being HOT-7 and HOT-17.

# General Information
The dosage range of HOT-2 is typically 10-18 mg and its duration is approximately 6-10 hours according to Shulgin.  HOT-2 produces visuals and moving, flowing lights.  It also causes euphoria and increases blood pressure.

# Categorization
HOT-7
HOT-7, or 2,5-dimethoxy-4-(-propylthio)-N-hydroxyphenethylamine, is a psychedelic phenethylamine of the 2C family.  It was presumably first synthesized by Alexander Shulgin and reported in his book, PIHKAL.

# Chemistry
HOT-7's full chemical name is 2-[4-(2-propylthio)-2,5-dimethoxyphenyl-N-hydroxyethanamine.  It has structural properties similar to 2C-T-7 and to other drugs in the HOT- series, with the most closely related compounds being HOT-2 and HOT-17.

# General Information
The dosage range of HOT-7 is typically 15-25 mg and its duration is approximately 6-8 hours according to Shulgin.  HOT-7 produces closed-eye and open-eye visuals.  It also induces a feeling similar to that of being drunk.

# Categorization
HOXA2
Homeobox protein Hox-A2 is a protein that in humans is encoded by the HOXA2 gene.

# Function
In vertebrates, the genes encoding the class of transcription factors called homeobox genes are found in clusters named A, B, C, and D on four separate chromosomes. Expression of these proteins is spatially and temporally regulated during embryonic development. This gene is part of the A cluster on chromosome 7 and encodes a DNA-binding transcription factor which may regulate gene expression, morphogenesis, and differentiation. The encoded protein may be involved in the placement of hindbrain segments in the proper location along the anterior-posterior axis during development. Two transcript variants encoding two different isoforms have been found for this gene, with only one of the isoforms containing the homeodomain region.
HOXA2 controls the embryonic development of the lower and middle part of the face and of the middle ear. Mutations in it are known to cause microtia, hearing impairment, and cleft palate.
HOXA3
Homeobox protein Hox-A3 is a protein that in humans is encoded by the HOXA3 gene.

# Function
In vertebrates, the genes encoding the class of transcription factors called homeobox genes are found in clusters named A, B, C, and D on four separate chromosomes. Expression of these proteins is spatially and temporally regulated during embryonic development. This gene is part of the A cluster on chromosome 7 and encodes a DNA-binding transcription factor which may regulate gene expression, morphogenesis, and differentiation. Three transcript variants encoding two different isoforms have been found for this gene.
During normal fetal development, HoxA3 is expressed in mesenchymal neural crest cells and endodermal cells found in the third pharyngeal pouch. Expression of HoxA3 in these cells affects the proper formation of the thymus, thyroid, and parathyroid organs. While the gene does not seem to affect the proliferation or migration of the pharyngeal neural crest cells, it does appear to trigger cellular differentiation events required to form these organs. Knockout of HoxA3 leads to failure in forming the thymus (athymia) and parathyroid gland (aparthyroidism). Mutant HoxA3 also causes a reduction in thyroid size. While the follicular and parafollicular cells still differentiate, their numbers are reduced and they are not evenly distributed throughout the gland. Mutant HoxA3 models show similar phenotypes as those seen in DiGeorges Syndrome, and it is possible that the two are linked.

# Regulation
The HOXA3 gene is repressed by the microRNA miR-10a.
HOXA5
Homeobox protein Hox-A5 is a protein that in humans is encoded by the HOXA5 gene.

# Function
In vertebrates, the genes encoding the class of transcription factors called homeobox genes are found in clusters named A, B, C, and D on four separate chromosomes. Expression of these proteins is spatially and temporally regulated during embryonic development. This gene is part of the A cluster on chromosome 7 and encodes a DNA-binding transcription factor which may regulate gene expression, morphogenesis, and differentiation. Methylation of this gene may result in the loss of its expression and, since the encoded protein upregulates the tumor suppressor p53, this protein may play an important role in tumorigenesis.
HoxA5 is controlled, at least in part, by DNA methylation. HoxA5 has been shown to upregulate the tumor suppressor p53 and AKT1 by downregulation of PTEN. Suppression of HoxA5 has been shown to attenuate hemangioma growth. HoxA5 has far-reaching effects on gene expression, causing ~300 genes to become upregulated upon its induction in breast cancer cell lines.  HoxA5 protein transduction domain overexpression prevents inflammation shown by inhibition of TNF-inducible monocyte binding to HUVECs.
Comparison of the HoxA5 promoter methylation profile across cell types from the least differentiated (human embryonic stem cells) to the most endothelial-like (human umbilical vein endothelial cells, or HUVECs) shows that the HoxA5 promoter is normally heavily methylated in non-differentiated cells and becomes demethylated as cells differentiate down the endothelial lineage. HoxA5 contains a C-Amp Response Elements (CRE) in its promoter.  POL2 and CTCF binding are enriched at the CpG-dense HoxA5 promoter in HUVECs, demonstrating transcriptional activity.

# Clinical significance
HoxA5 is suppressed in acute myeloid leukemia (AML), and the DNMT inhibitor decitabine (5Aza) is used to treat this disease. While HoxA5 is known to be hypermethylated in AML, it has not yet been shown whether decitabine directly targets these genes for demethylation.
HOXA6
Homeobox protein Hox-A6 is a protein that in humans is encoded by the HOXA6 gene.

# Function
In vertebrates, the genes encoding the class of transcription factors called homeobox genes are found in clusters named A, B, C, and D on four separate chromosomes. Expression of these proteins is spatially and temporally regulated during embryonic development. This gene is part of the A cluster on chromosome 7 and encodes a DNA-binding transcription factor which may regulate gene expression, morphogenesis, and differentiation.

# Clinical significance

## Leukemia
HOXA6 was examined to be preferentially expressed in primitive cells (e.g. hematopoietic progenitor cells), under the regulation of growth factors and cell cycles. Interleukin 3 and all-trans retinoic acid were found to be the inducing factors that can stimulate the expression of HOXA6. In mitotic process, HOXA6 was mainly expressed in S-phase and G2M phase cells. Overexpression of HoxA6 increased proliferation but inhibited differentiation of multipotential stem cells in the process of hemopoiesis, even had the capacity to transform primary hematopoietic cells into immortal cell lines. Transplantation of these cell lines may cause acute myeloid leukemia in recipient animals.Also in patients with acute myeloid leukemia, HOXA6 expression was upregulated. The comethylation of HOX genes, including HOXA6, leads to the dysfunction of tumor suppression genes by reducing gene expression. The methylation processes can be identified in adult chronic lymphocytic leukemia and childhood acute lymphocytic leukemia.

## Glioblastoma
HOXA6 may also contribute to the invasive tendency of glioblastoma multiforme cells. Suppressed expression of HOXA6 by introducing its antisense fragments can reduce the invasion of glioblastoma multiforme cells.
HOXB6
Homeobox protein Hox-B6 is a protein that in humans is encoded by the HOXB6 gene.

# Function
This gene is a member of the Antp homeobox family and encodes a protein with a homeobox DNA-binding domain. It is included in a cluster of homeobox B genes located on chromosome 17. The encoded protein functions as a sequence-specific transcription factor that is involved in development, including that of lung and skin, and has been localized to both the nucleus and cytoplasm. Altered expression of this gene or a change in the subcellular localization of its protein is associated with some cases of acute myeloid leukemia and colorectal cancer.

# During development
HOX B6 gene is only expressed in erythoid progenitor cells, which are the precursor to red blood cells used for transport of oxygen and carbon dioxide throughout the body. During development, the formation of the HOX gene factor happens in the first stages of fetal development, namely soon after the establishment of the mesoderm, which is the middle layer of the future embryo. However, HOX B6 is only expressed once the undifferentiated stem cells of the embryo distinguish themselves into the erythpoietic phase. The research has shown that HOX B6 is not expressed in hematopoietic stem cells located in the red bone marrow, which are the precursor cells to all types of blood cells, or primordial germ cells (PGCs), the precursor to cells passed on in each generation.  Since it is a transcriptional factor, HOX B6 regulates erythpoigenesis (red blood cell formation) using mRNA as the basis for certain protein productions.  The specific gene factor for erytopoigenesis has relatively been unobserved in the scientific community, and no known diseases have been associated with a defect HOX B6 gene. However, it has been shown in correlation with major skeletal deformations.
HOXB6 is a structural protein that has been shown to influence the growth and differentiation of the different blood lineages. This gene has also been shown to encourage the growth of granulocytes and monocytes, but at the cost of other blood cells. HOXB6 has the ability to cause the indefinite proliferation of murine marrow cells, as well as expand hematopoietic stem cells. When expressed abnormally, HOXB6 displays many characteristics of a potent oncoprotein. An oncoprotein can cause the transformation of a normal cell into a tumor cell. Overexpression of HOXB6, along with the addition of MEIS1 protein, has been implicated in the development of acute myeloid leukemia (AML). Acute myeloid leukemia is a cancer of the blood cells, specifically the leukocytes. The chromosomal irregularity most frequently seen in HOXB6 AML is a reappearing interstitial deletion of chromosome 2. Fundamental HOXB6 expression stops myeloid differentiation and debilitates erythropoiesis, megakaryopoiesis, and lymphopoiesis.
HOXB7
Homeobox protein Hox-B7 is a protein that in humans is encoded by the HOXB7 gene.

# Function
This gene is a member of the Antp homeobox family and encodes a protein with a homeobox DNA-binding domain. It is included in a cluster of homeobox B genes located on chromosome 17. The encoded nuclear protein functions as a sequence-specific transcription factor that is involved in cell proliferation and differentiation. Increased expression of this gene is associated with some cases of melanoma and ovarian carcinoma.

# Interactions
HOXB7 has been shown to interact with PBX1 and CREB-binding protein.
HOXB8
Homeobox protein Hox-B8 is a protein that in humans is encoded by the HOXB8 gene.

# Function
This gene is a member of the Antp homeobox family and encodes a nuclear protein with a homeobox DNA-binding domain. It is included in a cluster of Homeobox B genes located on chromosome 17. The encoded protein functions as a sequence-specific transcription factor that is involved in development. Increased expression of this gene is associated with colorectal cancer. Mice that have had the murine ortholog (see Homology (biology)  Orthology) of this gene knocked out exhibit an excessive pathologic grooming behavior. This behavior is similar to the behavior of humans suffering from the obsessive-compulsive spectrum disorder trichotillomania.
Transplantation of normal (wild-type) bone marrow into a Hoxb8 mutant mouse results in a reduction of compulsive grooming.
HSPB6
Heat shock protein beta-6 is a protein that in humans is encoded by the HSPB6 gene.
HSPB6 also known as hsp20 is a 17-kDa member of the small heat shock family of proteins. HSPB6 was first identified in 1994 when it was isolated from rat and human skeletal muscle as a complex with HSPB1 (also known as HSP27) and HSPB5 (also known as B-crystallin).
HSPB6 is expressed in multiple tissues; however, HSPB6 is most highly and constitutively expressed in different types of muscle including vascular, airway, colonic, bladder, uterine smooth muscle, cardiac muscle and skeletal muscle. HSPB6 has specific functions for vasodilation, platelet function, and insulin resistance and in smooth and cardiac muscle.
HTRA1
Serine protease HTRA1 is an enzyme that in humans is encoded by the HTRA1 gene. The HTRA1 protein is composed of four distinct protein domains. They are from amino-terminus to carboxyl-terminus an Insulin-like growth factor binding domain, a kazal domain, a trypsin-like peptidase domain and a PDZ domain.
This gene encodes a member of the trypsin family of serine proteases. This protein is a secreted enzyme that is proposed to regulate the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. It has also been suggested to be a regulator of cell growth.
Mutations of this gene are responsible for the development of CARASIL, a genetic form of cerebral vasculopathy.
HVCN1
Voltage-gated hydrogen channel 1 is a protein that in humans is encoded by the HVCN1 gene.
Voltage-gated hydrogen channel 1 is a voltage-gated proton channel that has been shown to allow proton transport into phagosomes and out of many types of cells including  spermatozoa, electrically excitable cells and respiratory epithelial cells. The proton-conducting HVCN1 channel has only transmembrane domains corresponding to the S1-S4 voltage sensing domains (VSD) of voltage-gated potassium channels and voltage-gated sodium channels. Molecular simulation is consistent with a water-filled pore that can function as a "water wire" for allowing hydrogen bonded H+ to cross the membrane. However, mutation of Asp112 in human Hv1 results in anion permeation, suggesting that obligatory protonation of Asp produces proton selectivity. Quantum mechanical calculations show that the Asp-Arg interaction can produce proton selective permeation. The HVCN1 protein has been shown to exist as a dimer with two functioning pores. Like other VSD channels, HVCN1 channels conduct ions about 1000-fold slower than channels formed by tetrameric S5-S6 central pores.

# As a drug target
Small molecule inhibitors of the HVCN1 channel are being developed as chemotherapeutics and anti-inflammatory agents.
HYAL2
Hyaluronidase-2 is an enzyme that in humans is encoded by the HYAL2 gene.
This gene encodes a protein which is similar in structure to hyaluronidases. Hyaluronidases intracellularly degrade hyaluronan, one of the major glycosaminoglycans of the extracellular matrix. Hyaluronan is thought to be involved in cell proliferation, migration and differentiation. Varying functions have been described for this protein. It has been described as a lysosomal hyaluronidase which is active at a pH below 4 and specifically hydrolyzes high molecular weight hyaluronan. It has also been described as a GPI-anchored cell surface protein which does not display hyaluronidase activity but does serve as a receptor for the oncogenic virus Jaagsiekte sheep retrovirus. The gene is one of several related genes in a region of chromosome 3p21.3 associated with tumor suppression. This gene encodes two alternatively spliced transcript variants which differ only in the 5' UTR.
One study found associations between cleft lip and palate and mutations in the HYAL2 gene.
An investigation published in 2017, attributed an additional function to the Hyaluronidase 2 (HYAL2) protein. The study found interactions between HYAL2 and proteins involved in the alternative splicing of CD44 pre-mRNA, suggesting a broader regulatory role for the HYAL2 protein in cell biology.
Heave
Synonyms and Keywords: lift, parasternal heave, parasternal lift, left ventricular impulse, LV impulse

# Overview
A heave is felt as an upward displacement of the chest against the hand during palpation of the precordium. Heaves are best felt with the heel of the hand at the sternal border.

# Physical Examination
For more detailed information regarding the physical examination of the precordium, please consult the chapter on palpation of the precordium.
Her 3
This gene encodes a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. This membrane-bound protein has a neuregulin binding domain but not an active kinase domain. It therefore can bind this ligand but not convey the signal into the cell through protein phosphorylation. However, it does form heterodimers with other EGF receptor family members which do have kinase activity. Heterodimerization leads to the activation of pathways which lead to cell proliferation or differentiation. Amplification of this gene and/or overexpression of its protein have been reported in numerous cancers, including prostate, bladder, and breast tumors. Alternate transcriptional splice variants encoding different isoforms have been characterized. One isoform lacks the intermembrane region and is secreted outside the cell. This form acts to modulate the activity of the membrane-bound form. Additional splice variants have also been reported, but they have not been thoroughly characterized.
ErbB3 (Her-3) is a member of the epidermal growth factor receptor family of receptor tyrosine-kinases.  However, despite the namesake of the protein family to which it belongs, ErbB3 does not have kinase activity.  Rather, it is thought that ErbB3, when activated, becomes a substrate for dimerization and subsequent phosphorylation by ErbB1, ErbB2 and ErbB4.
Like many of the receptor tyrosine-kinases, ErbB3 is activated by extracellular ligand.  Ligands known to bind to ErbB3 include heregulin.
Hilum

# Overview
A hilum (formerly called a hilus) is a depression or pit at the part of an organ where structures such as blood vessels and nerves enter.
Medial depression for blood vessels and ureter to enter kidney chamber
The adjective form is "hilar", and the plural is "hila".

# Examples
- the hilum of kidney (admits the renal artery, vein, ureter, and nerves)
- splenic hilum
- hilum of lung
HslVU
The heat shock proteins hslV and hslU (also known as clpQ and clpY respectively) are expressed in many bacteria such as E. coli in response to cell stress. The hslV protein is a protease and the hslU protein is an ATPase; the two form a symmetric assembly of four stacked rings, consisting of an hslV dodecamer bound to an hslU hexamer, with a central pore in which the protease and ATPase active sites reside. The hslV protein degrades unneeded or damaged proteins only when in complex with the hslU protein in the ATP-bound state. The complex is thought to resemble the hypothetical ancestor of the proteasome, a large protein complex specialized for regulated degradation of unneeded proteins in eukaryotes, many archaea, and a few bacteria.

# Genetics
Both proteins are encoded on the same operon within the bacterial genome. Unlike many eukaryotic proteasomes, which have several different peptide substrate specificities, hslV has a specificity similar to that of chymotrypsin; hence it is inhibited by proteasome inhibitors that specifically target the chymotrypsin site in eukaryotic proteasomes. Although the HslVU complex is stable on its own, some evidence suggests that the complex is formed in vivo in a substrate-induced manner due to a conformational change in the hslU-substrate complex that promotes hslV binding.
HslV and hslU genes have also been identified in some eukaryotes, although these also require the constitutively expressed proteasome for survival. These eukaryotic HslVU complexes assemble to apparently functional units, suggesting that these eukaryotes have both functional proteasomes and functional hslVU systems.

# Motifs in peptide unfolding
A four-amino acid sequence motif - GYVG, glycine-tyrosine-valine-glycine - conserved in hslU ATPases and located on the inner surface of the assembled pore dramatically accelerates the degradation of some proteins, and is required for the degradation of others. However, these motifs are not necessary for the degradation of short peptides and play no direct role in hydrolysis, suggesting that their major role is in unfolding the native state structure of the substrate and transferring the resulting disordered polypeptide chain to the hslV subunits for degradation. These motifs also influence the assembly of the complex. Translocation is also facilitated by the C-terminal tails of the HslU subunits, which form a gate closing off the proteolytic active sites in the central pore until a substrate has been bound and unfolded.

# Mechanism
The basic mechanism by which the hslVU complex undertakes proteolytic substrate degradation is essentially the same as that observed in the eukaryotic proteasome, catalyzed by active-site threonine residues. It is inhibited by enzyme inhibitors that covalently bind the threonine. Like the proteasome, hslU must bind ATP in a magnesium-dependent manner before substrate binding and unfolding can occur.