collagen (Also collagens) : Related Words Words similar in meaning to collagen
- protein«
- collagen«
- trout pout«
- proline«
- collagenous«
- scleroprotein«
- tropocollagen«
- procollagen«
- collagenic«
- albuminoid«
- semiglutin«
- alpha peptide«
- scleroderma«
- scar tissue«
- bone«
- reticulin«
- hydroxyproline«
- proximate principle«
- amino acid«
- collagen fibril«
- prolidase«
- type«
- triple helix«
- picrosirius red«
- fibroblast«
- osteonectin«
- peptide«
- osteolathyrism«
- lysine«
- ossein«
- glycine«
- neurothekeoma«
- collagen fiber«
- matrix«
- vitamin c«
- hyalocyte«
- cartilage«
- glycoprotein«
- skin«
- gelatine«
- formation«
- gelatin«
- enzyme«
- ficolin«
- mutation«
- fibrocyte«
- proteolysis map)—animation«
- cell«
- fiber«
- extracellular«
- entactin«
- hydroxyproline content«
- endotendineum«
- molecule«
- elastoidin«
- fibril«
- elastin«
- microfibril«
- dispase«
- glue«
- deoxypyridinoline«
- tissue«
- decorin«
- lysyl oxidase«
- cuticulin«
- collagen molecule«
- connective tissue«
- hydroxylysine«
- collectin«
- endoplasmic reticulum«
- handed helix«
- collagenopathy«
- collagen type«
- collagenolytic«
- pro«
- collagenolysis«
- cofactor«
- collagenized«
- collagenization«
- tendon«
- collageneous«
- main component«
- collagenated«
- signal peptide«
- collagenase«
- registration peptide«
- chondronectin«
- lower proline«
- chondromucoid«
- step«
- extracellular space«
- atelocollagen«
- hydroxylation«
- glycosylation«
- microfibrillar structure«
- hydroxylysines«
- alpha-2 chain«
- golgi apparatus«
- triple helical structure«
- interrupted triple helix«
- glycine content«
- lower thermal stability«
- covalent crosslinking«
- collagen structure«
- collagen scaffold«
- fibrous structural protein«
- collagen formation«
- process«
- cornea«
- fibrillar collagen«
- food«
- disorder«
- conformation«
- overlap region«
- propeptide«
- collagen synthesis«
- blood«
- type i.«
- fibrous protein«
- hyp«
- alpha chain«
- abundant protein«
- animal glue«
- signal sequence«
- tissue regeneration«
- danlos syndrome«
- water fish«
- type i«
- type iv«
- gly«
- basement membrane«
- ehlers«
- ramachandran«
- rer«
- type iii«
- pre«
- sinew«
- muscle tissue«
- extracellular matrix«
- cosmetic surgery«
- bse«
- tensile strength«
- scurvy«
- animal«
- amino«
- wound«
- hydroxyl«
- lumen«
- wrinkle«
- model«
- helix«
- ligament«
- gap«
- sequence«
- major component«
- |journal=j mol biol |volume=152«
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- wound sterile«
- wound deterioration«
- vitamin result«
- vascular ligature«
- unusual gx1x2 character«
- unusual amino acid composition«
- uncommon derivative amino acid«
- typical physiological mean«
- tropocollogen«
- tropocollagen subunit«
- tropocollagen strand«
- tropocollagen helix«
- triple alpha helical structure«
- transfer vesicle«
- toxic pentanedial«
- tough bundle«
- topological progression«
- tendinous muscle«
- synthetic plastic adhesive«
- synthetic pathogenesis«
- super helix«
- suffix -γέν«
- sufficient denaturation«
- strong molecule«
- strong connective tissue«
- staggered array«
- stagger distance d«
- specific mrna sequence«
- specific location relative«
- specific hydroxylysine residue«
- skin strength«
- skin discolors«
- single collagen molecule«
- similar proline«
- repairs—an application incompatible«
- reconstructive surgical uses«
- quasihexagonal array«
- prolyl-4-hydroxylase«
- potassium embelate«
- periodic pentameric arrangement«
- period repeat«
- pattern gly«
- osteogenesis imperfecta –«
- normal collagen production«
- normal collagen polyproline ii«
- neutral salt molecule«
- neighboring microfibrils«
- natural wound dressing«
- multiple tropocollagen molecule«
- multiple triple helix«
- multiple collagen fibril form«
- most medical collagen«
- most collagen form«
- monomeric collagen«
- methyl embelin«
- meshwork collagen«
- membrane associated collagen«
- matrix association«
- main collagenous component«
- loxl4«
- loxl3«
- looser triple helix«
- linking/stabilization agent«
- larger fibrillar bundle«
- larger collagen aggregate«
- kólla«
- individual polypeptide strand«
- individual peptide chain«
- individual cardiac valvular leaflet«
- individual amino acid supplementation«
- inconspicuous patch testing«
- hydroxyproline ring«
- hydroxproline content«
- heart valve ring«
- healthy collagen fiber«
- handed triple helix«
- growth hormone injection«
- gradual calcium deposition«
- golgi apparatus modification«
- glycine ’s single hydrogen atom«
- glycine accounting«
- glue producer«
- galactose monomer«
- fraction collagen molecule«
- form basal lamina«
- fish collagen«
- final mrna exit«
- fibrogenic cell«
- fibripositors«
- fibrillary collagen«
- fibrillar collagen type«
- fibrilar collagen«
- experimental incision«
- ethanedial«
- entire collagen triple helix«
- embeline«
- duration military«
- dominant autosomal disorder«
- discontinuous d«
- dimensional stranded structure«
- crisscross decoration«
- cooperative quaternary structure«
- continuous torsional force«
- collagenous cardiac skeleton«
- collagen xviii. patient«
- collagen underpinning«
- collagen synthesis pathway«
- collagen supplementation«
- collagen preparation«
- collagen microfibril«
- collagen fibrils/aggregates«
- collagen contribution«
- collagen alpha«
- collagen adhesive«
- cell–matrix communication«
- cardiac muscle mass«
- cardiac imaging technology«
- ca10(oh)2(po4)6«
- bone grafts«
- body protein content«
- artificial wound dressing«
- afm–based nanoindentation«
- sponge«
- chain«
- blood vessel«
- residue«
- common form«
- various cross«
- tissue regulation«
- tail tendon«
- soft keratin«
- rope basket«
- preprocollagen«
- postranslational modification«
- polypeptide strand«
- peptide formation«
- organized aggregate«
- multiplexin«
- mammalian collagen«
- loxl2«
- intrachain hydrogen bonding«
- intermolecular cross«
- helix associate«
- healing aid«
- fibrillar structure«
- fibril associated collagen«
- elongated fibril«
- collagenopathies«
- collagen peptidase«
- collagen monomer«
- collagen breakdown«
- chondrodysplasias«
- capillary growth«
- average amino acid composition«
- artificial skin substitute«
- alpha-1 chain«
- translation«
- single collagen fibril«
- poikilotherm animal«
- packing structure«
- irregular connective tissue«
- hemostatic property«
- hemostatic plug«
- defective collagen«
- collagen subunit«
- collagen casing«
- col18a1 gene«
- burn dressing«
- alternate combination«
- disease«
- body«
- degradation«
- tropocollagen molecule«
- regulation role«
- rabbit lung«
- procollagen peptidase«
- procollagen molecule«
- packing arrangement«
- loxl1«
- hydroxylase enzyme«
- healthy granulation tissue«
- handed alpha helix«
- formaldehyde glue«
- enzyme collagenase«
- collagenous structure«
- collagen tissue«
- chemotactic property«
- cardiac input«
- deposition«
- microfibrillar«
- main structural protein«
- disease scurvy«
- connective tissue matrix«
- closed herd«
- yonath«
- tissue property«
- osteoarthritis pain«
- observed structure«
- musical string«
- mmp inhibitor«
- macit«
- hereditary link«
- excessive deposition«
- covalent cross«
- collagen sequence«
- cell–cell«
- type xv«
- total sequence«
- silk fibroin«
- scientific research application«
- protective lining«
- prolyl hydroxylase«
- ppii«
- knobloch syndrome«
- key natural resource«
- identical chain«
- dopaquinone«
- bovine collagen«
- healing«
- triple helix structure«
- surgical purpose«
- gap region«
- collagen helix«
- additional assembly«
- skeleton«
- combination«
- lysyl hydroxylase«
- impermeable membrane«
- hypermobility syndrome«
- hydroxylation reaction«
- additional chain«
- supplement«
- cross«
- wound bed«
- type xiii«
- monomeric structure«
- mature tissue«
- mammal skin«
- donor animal«
- cardiac skeleton«
- atrioventricular septum«
- -gen«
- function«
- correct property«
- weak bone«
- propeptides«
- osteoid«
- free animal«
- fine violin«
- cardiac performance«
- regular repetition«
- adhesiveness«
- keratin«
- chondrin«
- ceratin«
- Ehlers-Danlos syndrome«
- 40nm gap«
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