PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17326675-4 2007 The binding of both mAbs to their epitopes on the N-domain of ACE is significantly diminished by the presence of the C-domain in the two-domain somatic tissue ACE and further diminished by the presence of sialic acid residues on the surface of blood ACE. N-Acetylneuraminic Acid 205-216 angiotensin I converting enzyme Homo sapiens 62-65 17326675-7 2007 As a result, the regions of the epitopes for mAb 1G12 and 6A12 on the N-domain, shielded in somatic ACE by the C-domain globule and additionally shielded in blood ACE by sialic acid residues in the oligosaccharide chains localized on Asn289 and Asn416, become unmasked. N-Acetylneuraminic Acid 170-181 angiotensin I converting enzyme Homo sapiens 100-103 17326675-7 2007 As a result, the regions of the epitopes for mAb 1G12 and 6A12 on the N-domain, shielded in somatic ACE by the C-domain globule and additionally shielded in blood ACE by sialic acid residues in the oligosaccharide chains localized on Asn289 and Asn416, become unmasked. N-Acetylneuraminic Acid 170-181 angiotensin I converting enzyme Homo sapiens 163-166 6320726-4 1983 These data indicate that ACE in the circulation contains a greater amount of sialic acid than purified ACE. N-Acetylneuraminic Acid 77-88 angiotensin I converting enzyme Homo sapiens 25-28 6320726-5 1983 The implication is that purified ACE isoenzymes which differ in sialic acid content may not reflect tissue-specific isoenzymes but rather artifacts of purification. N-Acetylneuraminic Acid 64-75 angiotensin I converting enzyme Homo sapiens 33-36 11114069-4 2000 ACE-ACE interaction was competitively inhibited by Neu5Ac- or Gal-terminated saccharides. N-Acetylneuraminic Acid 51-57 angiotensin I converting enzyme Homo sapiens 0-3 11114069-4 2000 ACE-ACE interaction was competitively inhibited by Neu5Ac- or Gal-terminated saccharides. N-Acetylneuraminic Acid 51-57 angiotensin I converting enzyme Homo sapiens 4-7