Persius/hicric huggingface dataset:
DMRT1
Doublesex and mab-3 related transcription factor 1, also known as DMRT1, is a protein which in humans is encoded by the DMRT1 gene.

# Function
This gene is found in a cluster with two other members of the gene family, having in common a zinc finger-like DNA-binding motif (DM domain). The DM domain is an ancient, conserved component of the vertebrate sex-determining pathway that is also a key regulator of male development in flies and nematodes, and is found to be the key sex-determining factor in chickens. 
This gene exhibits a gonad-specific and sexually dimorphic expression pattern, just like the related doublesex gene in fruit flies. Defective testicular development and XY feminization occur when this gene is hemizygous.
The DMRT1 gene is located at the end of the 9th chromosome. This gene is a dose sensitive transcription factor protein that regulates Sertoli cells and germ cell. The majority DMRT1 protein is located in the testicular cord and Sertoli cells, with a small amount in the germ cells. Two copies of the DMRT1  gene are required for normal sexual development. When a DMRT1 gene is lost the most common disease is chromosome 9p deletion, which causes abnormal testicular formation and feminization. The DMRT1 gene is critical in the male sex determination and without this gene the default female characteristic takes over and male characteristic is slight or non-existent. In the knockout model of this gene, the mice showed changes in both Sertoli and germ cells soon after the gonadal ridge was formed. The main defects associated with this knockout gene were developmental arrest, excess proliferation of germ cells, and failure to undergo meiosis, mitosis, or migration. Thus, the knockout model shows that loss of the DMRT1 gene is associated with incomplete germ cell development leading to infertility, abnormal testicular formation, and/or feminization of the affected individual.
DMXL2
Dmx-like 2 is a protein that in humans is encoded by the DMXL2 gene.

# Function
This gene encodes a protein with 12 WD domains. Proteins with WD domains are involved in many functions including participation in signal transduction pathways. Participation of the encoded protein in regulation of the Notch signaling pathway has been demonstrated in vitro using several human cell lines (.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}PMID 20810660). A gene encoding a similar protein is located on chromosome 5. Multiple transcript variants encoding different isoforms have been found for this gene.

# Clinical relevance
Haplosufficiency of Dmxl2 has been identified as the cause of Polyendocrine-polyneuropathy syndrome, and delayed puberty. Research has indicated that this is a result of altered function of CNS synapses (in which the protein product of Dmxl2 is expressed) causing altered activation of the GnRH neurons of the hypothalamus.
DNAI2
Dynein intermediate chain 2, axonemal, also known as axonemal dynein intermediate chain 2, is a protein that in humans is encoded by the DNAI2 gene.

# Function
The protein encoded by this gene belongs to the dynein intermediate chain family, and is part of the dynein complex of respiratory cilia and sperm flagella.

# Clinical significance
Mutations in the DNAI2 gene are associated with primary ciliary dyskinesia.
DNAL1
Dynein light chain 1, axonemal is a protein that in humans is encoded by the DNAL1 gene.

# Function
DNAL1 is a component of outer dynein arms, which contain the molecular motors for ATP-dependent cilia movement.

# Clinical significance
Mutations in the DNAL1 gene are associated with primary ciliary dyskinesia.
DNPEP
Aspartyl aminopeptidase is an enzyme that in humans is encoded by the DNPEP gene.

# Function
The protein encoded by this gene is an aminopeptidase which prefers acidic amino acids, and specifically favors aspartic acid over glutamic acid. It is thought to be a cytosolic protein involved in general metabolism of intracellular proteins.

# Model organisms
Model organisms have been used in the study of DNPEP function. A conditional knockout mouse line called Dnpeptm1e(EUCOMM)Wtsi was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Additional screens performed:  - In-depth immunological phenotyping
DORN1
DORN1 refers to a purinergic receptor found in green plants, which is involved in extracellular ATP detection. Through the process of signal transduction, DORN1 couples ATP binding (which occurs during cellular stress) to downstream signalling and ultimately gene expression, which is thought to aid in plant survival. 

# Molecular properties
In contrast to animal purinergic receptors (which are G protein-coupled receptors), DORN1 is a lectin receptor kinase (LecRK), and is part of the L type lectin receptor kinases, due to its legume-like extracellular domain. 
In green plants such as Arabidopsis thaliana, several mutants lacking the DORN1 receptors are unable to phosphorylate mitogen-activated protein kinases after ATP stimulation.

# Function
DORN1 receptors may play a role in mediating wound-induced inflammatory responses in green plants, with ATP acting as a damage-associated molecular pattern molecule. In response to cell lysis, ATP is discharged and binds onto the extracellular lectin domain of the DORN1 receptor. The intracellular DORN1 kinase domain is subsequently activated, resulting in several cellular responses such as mitogen-activated protein kinase activation, increased cytosolic calcium concentration and reactive oxygen species (ROS) production,  ultimately leading to the induction of defence gene expression.
DOT1L
DOT1-like (Disruptor of telomeric silencing 1-like), histone H3K79 methyltransferase (S. cerevisiae), also known as DOT1L, is a protein found in humans, as well as other eukaryotes.
The methylation of histone H3 lysine 79 (H3K79) by DOT1L which is a conserved epigenetic mark in many eukaryotic epigenomes, increases progressively along the aging process, suggesting that "DOT1L might function as a vital clock, ticking the hours impassively".
DOT1L has been reported to play an important role in the processes of mixed-lineage leukemia (MLL)-rearranged leukemias
Small molecule inhibitors of Dot1L catalytic activity have been developed.
DPP10
Inactive dipeptidyl peptidase 10 is a protein that in humans is encoded by the DPP10 gene. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

# Function
This gene encodes a single-pass type II membrane protein that is a member of the S9B family in clan SC of the serine proteases. This protein has no detectable protease activity, most likely due to the absence of the conserved serine residue normally present in the catalytic domain of serine proteases. However, it does bind specific voltage-gated potassium channels and alters their expression and biophysical properties.

# Clinical significance
Mutations in this gene have been associated with asthma and autism spectrum disorders.
DUSP1
Dual specificity protein phosphatase 1 is an enzyme that in humans is encoded by the DUSP1 gene.

# Function
The expression of DUSP1 gene is induced in human skin fibroblasts by oxidative/heat stress and growth factors.  It specifies a protein with structural features similar to members of the non-receptor-type protein-tyrosine phosphatase family, and which has significant amino-acid sequence similarity to a Tyr/Ser-protein phosphatase encoded by the late gene H1 of vaccinia virus.  The bacterially expressed and purified DUSP1 protein has intrinsic phosphatase activity, and specifically inactivates mitogen-activated protein (MAP) kinase in vitro by the concomitant dephosphorylation of both its phosphothreonine and phosphotyrosine residues.  Furthermore, it suppresses the activation of MAP kinase by oncogenic ras in extracts of Xenopus oocytes.  Thus, DUSP1 may play an important role in the human cellular response to environmental stress as well as in the negative regulation of cellular proliferation.

# Interactions
DUSP1 has been shown to interact with MAPK14, MAPK1 and MAPK8.
DUSP3
Dual specificity protein phosphatase 3 is an enzyme that in humans is encoded by the DUSP3 gene.
The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene maps in a region that contains the BRCA1 locus which confers susceptibility to breast and ovarian cancer. Although DUSP3 is expressed in both breast and ovarian tissues, mutation screening in breast cancer pedigrees and in sporadic tumors was negative, leading to the conclusion that this gene is not BRCA1.

# Model organisms
Model organisms have been used in the study of DUSP3 function. A conditional knockout mouse line, called Dusp3tm1a(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 five tests were carried out on mutant mice and four significant abnormalities were observed. Homozygous mutants had an increased percent of body fat, abnormal humerus morphology and an increased susceptibility to bacterial infection. Corpus callosum area, hippocampus area and total brain section area was increased, while length of pyramidal cell layer was reduced.

# Interactions
DUSP3 has been shown to interact with MAPK3 and MAPK1.
DUSP4
Dual specificity protein phosphatase 4 is an enzyme that in humans is encoded by the DUSP4 gene.

# Function
The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product inactivates ERK1, ERK2 and JNK, is expressed in a variety of tissues, and is localized in the nucleus. Two alternatively spliced transcript variants, encoding distinct isoforms, have been observed for this gene. In addition, multiple polyadenylation sites have been reported.
In melanocytic cells DUSP4 gene expression may be regulated by MITF.
DUSP5
Dual specificity protein phosphatase 5 is an enzyme that in humans is encoded by the DUSP5 gene.

# Function
The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily.  These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues.  They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation.  Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli.  This gene product inactivates ERK1/2, is expressed in a variety of tissues with the highest levels in pancreas and brain, and is localized in the nucleus.

# Model organisms
Model organisms have been used in the study of DUSP5 function. A conditional knockout mouse line called Dusp5tm1a(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Additional screens performed:  - In-depth immunological phenotyping
DUSP7
Dual specificity protein phosphatase 7 is an enzyme that in humans is encoded by the DUSP7 gene.

# Function
Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to de-phosphorylate both tyrosine (EC 3.1.3.48) and serine / threonine (EC 3.1.3.16) residues. DUSP7 belongs to a class of DUSPs, designated MKPs, that dephosphorylate MAPK (mitogen-activated protein kinase) proteins ERK, JNK, and p38 with specificity distinct from that of individual MKP proteins. MKPs contain a highly conserved C-terminal catalytic domain and an N-terminal Cdc25-like (CH2) domain. MAPK activation cascades mediate various physiologic processes, including cellular proliferation, apoptosis, differentiation, and stress responses.
It is known to bind and dephosphorylate ErkII, and as it, along with the other members of the DUSP family expresses high selectively for MAP kinases, it has been suggested that it functions as a method for selectively activating/deactivating different members of that family.
LRRK2
Leucine-rich repeat kinase 2 (LRRK2), also known as dardarin (from the Basque word "dardara" which means trembling), is an enzyme that in humans is encoded by the PARK8 gene. LRRK2 is a member of the leucine-rich repeat kinase family. Variants of this gene are associated with an increased risk of Parkinson's disease and also Crohn's disease.

# Function
The LRRK2 gene encodes a protein with an armadillo repeats (ARM) region, an ankyrin repeat (ANK) region, a leucine-rich repeat (LRR) domain, a kinase domain, a RAS domain, a GTPase domain, and a WD40 domain. The protein is present largely in the cytoplasm but also associates with the mitochondrial outer membrane.
LRRK2  interacts with the C-terminal R2 RING finger domain of parkin, and parkin interacted with the COR domain of LRRK2. Expression of mutant LRRK2 induced apoptotic cell death in neuroblastoma cells and in mouse cortical neurons.
Expression of LRRK2 mutants implicated in autosomal dominant Parkinson's disease causes shortening and simplification of the dendritic tree in vivo and in cultured neurons. This is mediated in part by alterations in macroautophagy, and can be prevented by protein kinase A regulation of the autophagy protein LC3. The G2019S and R1441C mutations elicit post-synaptic calcium imbalance, leading to excess mitochondrial clearance from dendrites by mitophagy.  LRRK2 is also a substrate for chaperone-mediated autophagy.

# Clinical significance
Mutations in this gene have been associated with Parkinson's disease type 8.
The Gly2019Ser mutation in LRRK2 is a relatively common cause of familial Parkinson's disease in Caucasians. It may also cause sporadic Parkinson's disease. The mutated Gly amino acid is conserved in all kinase domains of all species.
The Gly2019Ser mutation is one of a small number of LRRK2 mutations proven to cause Parkinson's disease. Of these, Gly2019Ser is the most common in the Western World, accounting for ~2% of all Parkinson's disease cases in North American Caucasians. This mutation is enriched in certain populations, being found in approximately 20% of all Ashkenazi Jewish Parkinson's disease patients and in approximately 40% of all Parkinson's disease patients of North African Berber Arab ancestry.
Unexpectedly, genomewide association studies have found an association between LRRK2 and Crohn's disease as well as with Parkinson's disease, suggesting that the two diseases share common pathways.
Attempts have been made to grow crystals of the LRRK2 aboard the International Space Station, as the low-gravity environment renders the crystals less susceptible to sedimentation and convection, and thus easier to map.
Mutations in the LRRK2 gene is the main factor in contributing to the genetic development of Parkinson's disease, and over 100 mutations in this gene have been shown to increase the chance of PD development. These mutations are most commonly seen in Jewish, North African Arab Berber, Chinese, and Japanese populations
Debye

# Overview
The debye (symbol: D) is a non-SI, CGS unit of electrical dipole moment. It is defined as 1Template:E statcoulomb centimeter (or 1Template:E esu m, or 1Template:E Fr cm). In SI units, 1 D equals approximately 3.33564Template:E coulomb-meter (exactly 1Template:E C m2/s divided by c, the speed of light in vacuum).  Conversely 1 C m = 2.9979Template:E D. 
It is named after the physicist Peter J. W. Debye.
Historically the debye was defined as the dipole moment resulting from two charges of opposite sign but an equal magnitude of 10-10 statcoulomb (generally called esu in older literature), which were separated by 1 angstrom (10-8 cm or 10-10m).
Note that 
10-10 statcoulomb is 0.48 units of elementary charge.
This gave a convenient unit for molecular dipole moments. Typical dipole moments for  simple diatomic molecules are in the range of 0 - 11D, where symmetric homoatomic species, e.g. chlorine, Cl2,  have a dipole moment of 0D and highly ionic molecular species such as gas phase potassium bromide, KBr have a dipole moment of 10.5D. 
The debye is still used in atomic physics and chemistry because SI units are inconveniently large, particularly since the smallest prefix is Template:E (e.g., 2.54 D = 8.47Template:E yCm). Note that SI disallows the application of prefixes to both members of a compound unit (e.g., 2.54 D = 8.47 fCfm) or the compounding of prefixes (e.g., 2.54 D = 8.47 yCm), so there is currently no satisfactory solution to this problem of notation.
Densa
Densa is a fictional parody association of Mensa International. "Densa" is a play on the words: "Mensa" and "dense." It is a fictional society analgous to Mensa.  Just as Mensa is a society for people who have an exceptionally high IQ, Densa would be a society for people with an exceptionally low IQ. The word is usually used for comical or satirical effect.  For example, some one might say a member of Mensa is a member of Densa or should be a member of Densa for doing something dumb. It is almost always used in a light-hearted manner with a wink and a nod. 
The concept of an organization for the mentally dense originated in "Boston & Outskirts Mensa Bulletin (BOMB)", August, 1974, in "A-Bomb-inable Puzzle II" by John D. Coons. The puzzle involved "The Boston chapter of Densa, the low IQ society." Subsequent issues had additional puzzles with gags about the group, and were widely reprinted by the bulletins of other Mensa groups, before the concept of a low IQ group gained wider circulation in the 1970s, with other people creating quizzes, etc.
A humor book called the The Densa Quiz: The Official & Complete Dq Test of the International Densa Society was written in 1983 by  Stephen Price and J. Webster Shields. 
cite news | last = McGowan | first = William | title = A Sense of Belonging | publisher = The New York Times | date = 1987-08-23 | url =  | accessdate = 2007-06-28 }}
Not available through New York Times archival service, but available through Proquest.
Dimer
A dimer is a chemical or biological entity consisting of two subunits called monomers, which are held together by either intramolecular forces (covalent bonds) or weaker intermolecular forces.

# Chemistry
An example of a molecular dimer (i.e. held together by intramolecular forces) is dicyclopentadiene, wherein two cyclopentadiene molecules have reacted to give the product.
Molecular dimers are often formed by the reaction of two identical compounds e.g.: 2A  A-A.
In this example, monomer "A" is said to dimerise to give the dimer "A-A". Diaminocarbenes are another example which dimerise, to give tetraaminoethylenes.
An example of an intermolecular or physical dimer is acetic acid wherein hydrogen bonds hold the two molecules together. The water dimer is another such dimer.
The term homodimer is used when the two molecules are identical (e.g. A-A) and heterodimer when they are not (e.g. A-B).
The reverse of dimerisation is often called disassociation.

# Biochemistry
In biochemistry and molecular biology, dimers of macromolecules like proteins and nucleic acids are often observed. The dimerization of identical subunits is called homodimerization; the dimerization of different subunits or unrelated monomers is called heterodimerization. Most dimers in biochemistry are not connected by covalent bonds with the exception of disulfide bridges.
An example of this would be the enzyme reverse transcriptase, which is made of two different amino acid chains.

## Examples
- Nucleic acids:
DNA
- DNA
- DNA Polymerase
- Proteins:
Antibodies
Protein kinases:
Receptor tyrosine kinases
Transcription factors
Leucine zipper motif proteins
Nuclear receptors
14-3-3 proteins
G protein-coupled receptors
G protein -subunit dimer
Kinesin
Triosephosphateisomerase (TIM)
Alcohol dehydrogenase
Factor XI
Factor XIII
Toll-like receptor
Fibrinogen
- Antibodies
- Protein kinases:
Receptor tyrosine kinases
- Receptor tyrosine kinases
- Transcription factors
Leucine zipper motif proteins
Nuclear receptors
- Leucine zipper motif proteins
- Nuclear receptors
- 14-3-3 proteins
- G protein-coupled receptors
- G protein -subunit dimer
- Kinesin
- Triosephosphateisomerase (TIM)
- Alcohol dehydrogenase
- Factor XI
- Factor XIII
- Toll-like receptor
- Fibrinogen