collagen-like

19 examples (0.04 sec)
  • C-mannosylation is also abundant and can be found in collagen-like regions.
  • Since the editing sites are located just before a collagen like trimerization domain, editing may effect protein oligomerization.
  • It is water soluble and has collagen-like domains similar to SP-D.
  • They have a collagen-like domain, which is essential for ligand binding.
  • The latter silenced eventually by mutations in the glycine residues of the collagen-like region.
  • The skeleton of the Venus sea fan is composed of calcite and a collagen-like substance.
  • Rather than forming collagen-like fibers, laminins form networks of web-like structures that resist tensile forces in the basal lamina.
  • The amino acid differences that distinguish among SFTPA2 variants are located both at the carbohydrate recognition and the collagen-like domains.
  • The amino acid differences that distinguish among SFTPA1 variants are located both at the carbohydrate recognition and the collagen-like domains.
  • Some snail poisons, conotoxins, contain hydroxyproline, but lack collagen-like sequences.
  • The skeleton is composed of calcite and gorgonion, a collagen-like compound.
  • The amino acid differences that distinguish between SFTPA2 and SFTPA1 genes and between their corresponding variants are located at the collagen-like domain.
  • This gene encodes the subunit of a collagen-like molecule associated with acetylcholinesterase in skeletal muscle.
  • The structure of SP-A1 monomers consists of four domains: an N-terminal, a collagen-like domain, a neck region, and a carbohydrate recognition domain.
  • The structure of SP-A2 monomers consists of four domains: an N-terminal, a collagen-like domain, a neck region, and a carbohydrate recognition domain.
  • The amino acid differences that distinguish between SP-A1 and SP-A2 genes and between their corresponding variants are located at the collagen-like domain.
  • In addition to collagen, the mammalian proteins elastin and argonaute 2 have collagen-like domains in which hydroxyproline is formed.
  • These share the same topology, each possessing a small, globular N-terminal domain, a collagen-like Gly/Pro-rich central region, and a conserved C-terminal region, the C1q domain.
  • It is found in association with other domains, such as C1q, laminin-type EGF-like, collagen-like, FN3, WAP, ZP or FAS1.