The N-terminal domain of chromogranin A (CgA1-40) interacts with monolayers of membrane lipids of fungal and mammalian compositions.
Maget-Dana
R
R
Centre de Biophysique Moleculaire, CNRS, 45071 Orleans, France.
Metz-Boutigue
M-H
MH
Helle
K B
KB
D000528:Alternaria / Q000378:metabolism; D000818:Animals; D001232:Aspergillus fumigatus / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D037282:Calreticulin; D002417:Cattle; D002462:Cell Membrane / Q000378:metabolism*; D002478:Cells, Cultured; D053379:Chromogranin A; D002864:Chromogranins / Q000737:chemistry* / Q000378:metabolism*; D050356:Lipid Metabolism; D009492:Neurospora crassa / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D010743:Phospholipids / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012261:Ribonucleoproteins / Q000737:chemistry / Q000378:metabolism
D002135:Calcium-Binding Proteins; D037282:Calreticulin; D053379:Chromogranin A; D002864:Chromogranins; D010446:Peptide Fragments; D010743:Phospholipids; D012261:Ribonucleoproteins; C121986:vasostatin