What is the name of the tough fibrous structural protein found in fingernails and toenails?
"or the physical region of the protein that participates in chemical catalysis. In solution proteins also undergo variation in structure through thermal vibration and the collision with other molecules. Proteins can be informally divided into three main classes, which correlate with typical tertiary structures: globular proteins, fibrous proteins, and membrane proteins. Almost all globular proteins are soluble and many are enzymes. Fibrous proteins are often structural, such as collagen, the major component of connective tissue, or keratin, the protein component of hair and nails. Membrane proteins often serve as receptors or provide channels for polar or charged molecules to pass"
"Tavaborole Tavaborole (trade name Kerydin) is a topical antifungal medication for the treatment of onychomycosis, a fungal infection of the nail and nail bed. Tavaborole began its Phase 3 trials in December 2010 and was approved by the US FDA in July 2014. Tavaborole inhibits an essential fungal enzyme, leucyl-tRNA synthetase, that is required for protein synthesis. The inhibition of protein synthesis leads to termination of cell growth and then cell death, eliminating the fungal infection. Tavaborole, when prepared with a 1:1 mixture of ethyl acetate and propylene glycol, has the ability to fully penetrate through the human nail. In"
"Three-finger protein Three-finger proteins or three-finger protein domains (3FP or TFPD) are a protein superfamily consisting of small, roughly 60-80 amino acid residue protein domains with a common tertiary structure: three beta strand loops extended from a hydrophobic core stabilized by disulfide bonds. The family is named for the outstretched ""fingers"" of the three loops. Members of the family have no enzymatic activity but are capable of forming protein-protein interactions with high specificity and affinity. The founding members of the family, also the best characterized by structure, are the three-finger toxins found in snake venom, which have a variety of"
"SNAI1 Zinc finger protein SNAI1 (sometimes referred to as Snail) is a protein that in humans is encoded by the ""SNAI1"" gene. Snail is a family of transcription factors that promote the repression of the adhesion molecule E-cadherin to regulate epithelial to mesenchymal transition (EMT) during embryonic development. The Drosophila embryonic protein SNAI1, commonly known as Snail, is a zinc finger transcriptional repressor which downregulates the expression of ectodermal genes within the mesoderm. The nuclear protein encoded by this gene is structurally similar to the Drosophila snail protein, and is also thought to be critical for mesoderm formation in the"
"Zinc finger A zinc finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions (Zn) in order to stabilize the fold. Originally coined to describe the finger-like appearance of a hypothesized structure from ""Xenopus laevis"" transcription factor IIIA, the zinc finger name has now come to encompass a wide variety of differing protein structures. ""Xenopus laevis"" TFIIIA was originally demonstrated to contain zinc and require the metal for function in 1983, the first such reported zinc requirement for a gene regulatory protein. Proteins that contain zinc fingers (""zinc finger proteins"") are"
"Osteonectin Osteonectin (ON) also known as secreted protein acidic and rich in cysteine (SPARC) or basement-membrane protein 40 (BM-40) is a protein that in humans is encoded by the ""SPARC"" gene. Osteonectin is a glycoprotein in the bone that binds calcium. It is secreted by osteoblasts during bone formation, initiating mineralization and promoting mineral crystal formation. Osteonectin also shows affinity for collagen in addition to bone mineral calcium. A correlation between osteonectin over-expression and ampullary cancers and chronic pancreatitis has been found. The human SPARC gene is 26.5 kb long, and contains 10 exons and 9 introns and is located"
"specificity profiles of proteins generated by the OPEN method have never been reported. This entry represents the CysCysHisCys (C2HC) type zinc finger domain found in eukaryotes. Proteins containing these domains include: Zinc finger A zinc finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions (Zn) in order to stabilize the fold. Originally coined to describe the finger-like appearance of a hypothesized structure from ""Xenopus laevis"" transcription factor IIIA, the zinc finger name has now come to encompass a wide variety of differing protein structures. ""Xenopus laevis"" TFIIIA was originally demonstrated"
"been constructed. Zinc finger (Znf) domains are relatively small protein motifs that contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not, instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from ""Xenopus laevis"" (African clawed frog), however they are now recognised to bind DNA, RNA, protein, and/or lipid substrates. Their binding properties depend on the amino acid sequence of"
"Tooth enamel Tooth enamel is one of the four major tissues that make up the tooth in humans and many other animals, including some species of fish. It makes up the normally visible part of the tooth, covering the crown. The other major tissues are dentin, cementum, and dental pulp. It is a very hard, white to off-white, highly mineralised substance that acts as a barrier to protect the tooth but can become susceptible to degradation, especially by acids from food and drink. Enamel is the hardest substance in the human body and contains the highest percentage of minerals, 96%,"
"incisors, decreased bone mineral density, abnormal lens morphology, cataracts and a decreased length of long bones. Osteonectin Osteonectin (ON) also known as secreted protein acidic and rich in cysteine (SPARC) or basement-membrane protein 40 (BM-40) is a protein that in humans is encoded by the ""SPARC"" gene. Osteonectin is a glycoprotein in the bone that binds calcium. It is secreted by osteoblasts during bone formation, initiating mineralization and promoting mineral crystal formation. Osteonectin also shows affinity for collagen in addition to bone mineral calcium. A correlation between osteonectin over-expression and ampullary cancers and chronic pancreatitis has been found. The human"
"Matrix (biology) In biology, matrix (plural: matrices) is the material (or tissue) in animal or plant cells, in which more specialized structures are embedded, and a specific part of the mitochondrion. The internal structure of connective tissues is an extracellular matrix. Finger nails and toenails grow from matrices. It is found in various connective tissue. It is generally used as a jelly like structure instead of cytoplasm in connective tissue. The main ingredients of the extracellular matrix are glycoproteins secreted by the cells. (Recall that glycoproteins are proteins with covalently bound carbohydrates, usually short chains of sugars.) The most abundant"
"projecting edge of the eponychium covering the proximal strip of the lunula. The nail wall (""vallum unguis"") is the cutaneous fold overlapping the sides and proximal end of the nail. The lateral margin (""margo lateralis"") lies beneath the nail wall on the sides of the nail, and the nail groove or fold (""sulcus matricis unguis"") are the cutaneous slits into which the lateral margins are embedded. The paronychium is the soft tissue border around the nail, and paronychia is an infection in this area. A healthy fingernail has the function of protecting the distal phalanx, the fingertip, and the surrounding"
"the nail bed forms a germinal layer which hardens as the cells acquire keratin and becomes a new nail. Until this layer has formed, the exposed nail bed is highly sensitive, and is typically covered with a non-adherent dressing, as an ordinary dressing will stick to the nail bed and cause pain upon removal. In the average person, fingernails require 3 to 6 months to regrow completely, while toenails require 12 to 18 months. In brachial plexus avulsions, the brachial plexus (a bundle of nerves that communicates signals between the spine and the arms, shoulders, and hands) is torn from"
"RING finger domain In molecular biology, a RING (Really Interesting New Gene) finger domain is a protein structural domain of zinc finger type which contains a CHC amino acid motif which binds two zinc cations (seven cysteines and one histidine arranged non-consecutively). This protein domain contains from 40 to 60 amino acids. Many proteins containing a RING finger play a key role in the ubiquitination pathway. Zinc finger (Znf) domains are relatively small protein motifs that bind one or more zinc atoms, and which usually contain multiple finger-like protrusions that make tandem contacts with their target molecule. They bind DNA,"
"telangiectasia.) Sclerodactyly Sclerodactyly is a localized thickening and tightness of the skin of the fingers or toes. Sclerodactyly often leads to ulceration of the skin of the distal digits and is commonly accompanied by atrophy of the underlying soft tissues. The term ""sclerodactyly"" is made up from the Greek ""skleros"" meaning hard and ""daktylos"" meaning a finger or toe – ""hard fingers or toes"". It is sometimes associated with scleroderma and mixed connective tissue disease, auto-immune disorders. Sclerodactyly is a component of the CREST variant of scleroderma (CREST is an acronym that stands for calcinosis, Raynaud's phenomenon, esophageal dysmotility, sclerodactyly,"
"beneath the nail plate, which moves toward the finger tip with the plate. The epidermis is attached to the dermis by tiny longitudinal ""grooves"" called matrix crests (""cristae matricis unguis""). In old age, the nail plate becomes thinner, and these grooves become more visible. The nail sinus (""sinus unguis"") is where the nail root is; i.e. the base of the nail underneath the skin. It originates from the actively growing tissue below, the matrix. The nail plate (""corpus unguis"") is the hard part of the nail, made of translucent keratin protein. Several layers of dead, compacted cells cause the nail"
"vitamin A and B results in fragile nails with horizontal and vertical ridges. Some over-the-counter vitamin supplements such as certain multivitamins and biotin may help in growth of strong nails, although this is quite subjective. Protein is a building material for new nails; therefore, low dietary protein intake may cause anemia and the resultant reduced hemoglobin in the blood filling the capillaries of the nail bed reflects varying amounts of light incident on the nail matrix resulting in lighter shades of pink ultimately resulting in white nail beds when the hemoglobin is very low. When hemoglobin is close to 15"
"Hapalonychia Hapalonychia, also known as egg-shell nail, is a condition in which the top of a toe or finger nail becomes soft and thin, causing it to bend or break. This condition can manifest as a result of genetic discrepancy and may also occur due to malnutrition and debility. Nails are often a representation of the internal nutritional of health. Although overall well-being is not typically determined by nail health, fissures, breaks and calcium spots are minor indications of inner health. Hapalonychia may also be attributed to myxedema, rheumatoid arthritis, anorexia, bulimia, Hansen's disease, Raynaud phenomenon, oral retinoid therapy, or"
"osteonectin. It binds collagen and hydroxyapatite in separate domains, is found in relatively large amounts in immature bone, and promotes mineralization of collagen. Fibroblasts, including periodontal fibroblasts, synthesize osteonectin. This protein is synthesized by macrophages at sites of wound repair and platelet degranulation, so it may play an important role in wound healing. SPARC does not support cell attachment, and like thrombospondin and tenascin, is anti-adhesive and an inhibitor of cell spreading. It disrupts focal adhesions in fibroblasts. It also regulates the proliferation of some cells, especially endothelial cells, mediated by its ability to bind to cytokines and growth factors."
"and type II keratin proteins in a tissue-specific and cellular differentiation-specific manner. The keratin proteins of epithelial tissues are commonly known as ""keratins"" or are sometimes referred to as ""epithelial keratins"" or ""cytokeratins"". The specialized keratins of hair and nail are known as ""hard keratins"" or ""trichocyte keratins"". Trichocytes are the specialized epithelial cells from which hair and nail are composed. Trichocyte keratins are similar in their gene and protein structure to keratins except that they are especially rich in the sulfur-containing amino acid cysteine, which facilitates chemical cross-linking of the assembled hard keratins to form a more structurally resilient"
"radiodermatitis. Hapalonychia Hapalonychia, also known as egg-shell nail, is a condition in which the top of a toe or finger nail becomes soft and thin, causing it to bend or break. This condition can manifest as a result of genetic discrepancy and may also occur due to malnutrition and debility. Nails are often a representation of the internal nutritional of health. Although overall well-being is not typically determined by nail health, fissures, breaks and calcium spots are minor indications of inner health. Hapalonychia may also be attributed to myxedema, rheumatoid arthritis, anorexia, bulimia, Hansen's disease, Raynaud phenomenon, oral retinoid therapy,"
"Sclerodactyly Sclerodactyly is a localized thickening and tightness of the skin of the fingers or toes. Sclerodactyly often leads to ulceration of the skin of the distal digits and is commonly accompanied by atrophy of the underlying soft tissues. The term ""sclerodactyly"" is made up from the Greek ""skleros"" meaning hard and ""daktylos"" meaning a finger or toe – ""hard fingers or toes"". It is sometimes associated with scleroderma and mixed connective tissue disease, auto-immune disorders. Sclerodactyly is a component of the CREST variant of scleroderma (CREST is an acronym that stands for calcinosis, Raynaud's phenomenon, esophageal dysmotility, sclerodactyly, and"
"finger proteins. In humans, there are no other aliases, and its neighboring genes are MIR4754, A1BG, and RPS5. ZNF837 mRNA that is made into function protein contains 1921 nucleotides, of which 222-1817 are translated to a protein containing 3 exons. The protein consists of 531 amino acids with a weight of 58,078 Da with an isoelectric point at 9.525. There are 2 transcript variants. Transcript variant 1, 2050 base pairs in length, is non-coding due to a nonsense-mediated mRNA decay . Transcript variant 2 is made into the functional protein due to an alternate splice site It is predicted via"
"Tinea nigra Tinea nigra (also known as ""superficial phaeohyphomycosis,"" and ""Tinea nigra palmaris et plantaris"") is a superficial fungal infection that causes dark brown to black painless patches on the palms of the hands and the soles of the feet. This infection is caused by the fungus formerly classified as ""Exophiala werneckii"", but more recently classified as ""Hortaea werneckii"". The causative organism has also been described as ""Phaeoannellomyces werneckii"". Diagnosis of tinea nigra causing fungus is made on microscopic examination of skin scrapings, mixed with potassium hydroxide (KOH). The KOH lyses the nonfungal debris. Treatment consists of topical application of"
"date. Zinc fingers were first identified in a study of transcription in the African clawed frog, ""Xenopus laevis"" in the laboratory of Aaron Klug. A study of the transcription of a particular RNA sequence revealed that the binding strength of a small transcription factor (transcription factor IIIA; TFIIIA) was due to the presence of zinc-coordinating finger-like structures. Amino acid sequencing of TFIIIA revealed nine tandem sequences of 30 amino acids, including two invariant pairs of cysteine and histidine residues. Extended x-ray absorption fine structure confirmed the identity of the zinc ligands: two cysteines and two histidines. The DNA-binding loop formed"
"blood vessels. The lunula is most noticeable on the thumb; however, not everyone's lunulae are visible. In some cases, the eponychium may partially or completely cover the lunula. Lunula (anatomy) The lunula, or lunulae (pl.) (), is the crescent-shaped whitish area of the bed of a fingernail or toenail. The lunula is the visible part of the root of the nail. In humans, it appears by week 14 of gestation, and has a primary structural role in defining the free edge of the distal nail plate (the part of the nail that grows outward). It is located at the end"
"PHD finger The PHD finger was discovered in 1993 as a Cys-His-Cys motif in the plant homeodomain (hence PHD) proteins HAT3.1 in ""Arabidopsis thaliana"" and maize ZmHox1a. The PHD finger motif resembles the metal binding RING domain (Cys-His-Cys) and FYVE domain. It occurs as a single finger, but often in clusters of two or three, and it also occurs together with other domains, such as the chromodomain and the bromodomain. The PHD finger, approximately 50-80 amino acids in length, is found in more than 100 human proteins. Several of the proteins it occurs in are found in the nucleus, and"
"SNAI2 Zinc finger protein SNAI2 is a protein that in humans is encoded by the ""SNAI2"" gene. This gene encodes a member of the Snail superfamily of C2H2-type zinc finger transcription factors. The encoded protein acts as a transcriptional repressor that binds to E-box motifs and is also likely to repress E-cadherin transcription in breast carcinoma. This protein is involved in epithelial-mesenchymal transitions and has antiapoptotic activity. It regulates differentiation and migration of neural crest cells along with other genes (e.g. FOXD3, SOX9 and SOX10, BMPs) in embryonic life. Mutations in this gene may be associated with sporadic cases of"
"be used as a therapeutic measure for the treatment of breast cancer before chemotherapy treatment. SNAI1 has been shown to interact with CTDSPL, CTDSP1 and CTDSP2. SNAI1 Zinc finger protein SNAI1 (sometimes referred to as Snail) is a protein that in humans is encoded by the ""SNAI1"" gene. Snail is a family of transcription factors that promote the repression of the adhesion molecule E-cadherin to regulate epithelial to mesenchymal transition (EMT) during embryonic development. The Drosophila embryonic protein SNAI1, commonly known as Snail, is a zinc finger transcriptional repressor which downregulates the expression of ectodermal genes within the mesoderm. The"
"can pose a risk. Water can penetrate the nail as can many other substances including paraquat, a fast acting herbicide that is harmful to humans, urea which is often an ingredient in creams and lotions meant for use on hands and fingers, and several fungicidal agents such as salicylic acid, miconazole branded Monistat, natamycin; and sodium hypochlorite which is the active ingredient in common household bleach (but usually only in 2–3% concentration). Healthcare and pre-hospital-care providers (EMTs or paramedics) often use the fingernail beds as a cursory indicator of distal tissue perfusion of individuals who may be dehydrated or in"
"Lunula (anatomy) The lunula, or lunulae (pl.) (), is the crescent-shaped whitish area of the bed of a fingernail or toenail. The lunula is the visible part of the root of the nail. In humans, it appears by week 14 of gestation, and has a primary structural role in defining the free edge of the distal nail plate (the part of the nail that grows outward). It is located at the end of the nail (that is closest to the skin of the finger), but it still lies under the nail. It is not actually white but only appears so"
"most conservation in mammals. The table above displays the results of an NCBI Blast from 2015 with selected taxa from main branches of vertebrates and invertebrates. This is not a complete list. RNF113A Ring Finger Protein 113A is a protein that in humans is encoded by the RNF113A gene. It is found in humans on the X Chromosome. RNF113A contains two highly conserved domains, the RING (Really Interesting New Gene) finger domain and Zinc finger domain. RING finger domains have been associated with some tumor suppressors and cytokine receptor-associated molecules. These domains also act in DNA repair and mediating protein-protein"
"near the ends of the nails. The recognition of characteristic nail patterns, such as Terry’s nails, may be a helpful herald for early diagnosis of systemic diseases. This was named for Dr. Richard Terry. Terry's nails Terry's nails is a physical condition in which a person's fingernails or toenails appear white with a characteristic ""ground glass"" appearance without any lunula. The condition is thought to be due to a decrease in vascularity and an increase in connective tissue within the nail bed. It frequently occurs in the setting of liver failure, cirrhosis, diabetes mellitus, congestive heart failure, hyperthyroidism, or malnutrition."