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12 relations: Actin, Bullous pemphigoid, Collagen, type XVII, alpha 1, Cytoskeleton, DCTN1, Erbin (protein), Gene, Hemidesmosome, Intermediate filament, Plakin, Protein, Protein–protein interaction.
Actin
Actin is a family of globular multi-functional proteins that form microfilaments.
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Bullous pemphigoid
Bullous pemphigoid is an acute or chronic autoimmune skin disease, involving the formation of blisters, more appropriately known as bullae, at the space between the epidermis and dermis skin layers.
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Collagen, type XVII, alpha 1
Collagen XVII, previously called BP180, is a transmembrane protein which plays a critical role in maintaining the linkage between the intracellular and the extracellular structural elements involved in epidermal adhesion.
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Cytoskeleton
A cytoskeleton is present in all cells of all domains of life (archaea, bacteria, eukaryotes).
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DCTN1
Dynactin subunit 1 is a protein that in humans is encoded by the DCTN1 gene.
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Erbin (protein)
Erbb2 interacting protein (ERBB2IP) also known as Erbin is a protein which in humans is encoded by the ERBB2IP gene.
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Gene
In biology, a gene is a sequence of DNA or RNA that codes for a molecule that has a function.
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Hemidesmosome
Hemidesmosomes (HD) are very small stud-like structures found in keratinocytes of the epidermis of skin that attach to the extracellular matrix (ECM).
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Intermediate filament
Intermediate filaments (IFs) are cytoskeletal components found in the cells of vertebrate animal species, and perhaps also in other animals, fungi, plants, and unicellular organisms.
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Plakin
A plakin is a protein that associates with junctional complexes and the cytoskeleton.
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Protein
Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues.
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Protein–protein interaction
Protein–protein interactions (PPIs) are the physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by electrostatic forces including the hydrophobic effect.
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BPAG1, BPAg1, DST (gene).
