glycosylation

navigate by keyword : rage membrane receptor advanced glycosylation immunoglobulin diabetes inflammation tumour invasion cancer aggregation alzheimer 039 disease dementia amyloid plaque biological degenerative plaques aging cell protein molecules degeneration attached product specific belongs superfamily involved conformations transmembrane intracellular domains assumed

RAGE receptor (mouse) hexamer, active form after ligand binding Royalty Free Stock Photo
Structure of human Macrophage Migration Inhibitory Factor (glycosylation-inhibiting factor) homotrimer Royalty Free Stock Photo
Hemoglobin molecule Royalty Free Stock Photo
Golgi apparatus or Golgi body Royalty Free Stock Photo
Blood - Hemoglobin Molecule Royalty Free Stock Photo
Structure of triple ACE2-bound SARS-CoV-2 trimer spike Royalty Free Stock Photo
Mannose molecular structure on white Royalty Free Stock Photo
The RAGE receptor attached to a cell membrane
Vector types of N-glycans. Oligomannose, complex and hybrid. Royalty Free Stock Photo
Structure of human hemoglobin molecule Royalty Free Stock Photo
Ricin castor bean plant poisonous protein, chemical structure Royalty Free Stock Photo
Threonine (Thr, T) molecule Royalty Free Stock Photo
Ricin castor bean plant poisonous protein, chemical structure. Royalty Free Stock Photo
Golgi apparatus vector illustration. Labeled microscopic scheme and diagram with cisternae, lumen, secretory forming vesicle. Royalty Free Stock Photo
Mucin structure as chemical glycosylated proteins closeup outline diagram Royalty Free Stock Photo
RAGE (Advanced glycosylation end product-specific receptor) belongs to the immunoglobulin superfamily and is involved in diabetes, Alzheimer's disease, inflammation and tumour invasion. The conformations of the transmembrane and intracellular domains are assumed


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