PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10026209-4 1999 Altered sedimentation of intracellular complexes following treatment with the specific proteasome inhibitor lactacystin, and in combination with mannosidase inhibition, revealed that the removal of mannose from attached oligosaccharides abrogates the release of misfolded alpha1-antitrypsin from calnexin prior to proteasomal degradation. Mannose 198-205 serpin family A member 1 Homo sapiens 272-290 20477988-7 2010 In the living cell, VIP36 bound exclusively to the high-mannose form of alpha1-AT. Mannose 56-63 serpin family A member 1 Homo sapiens 72-81 12736254-4 2003 We also show that misfolded alpha1-antitrypsin NHK contains labeled Glc1Man9GlcNAc and Man5-9GlcNAc released by endo-beta-N-acetylglucosaminidase H in pulse-chase experiments with [2-3H]mannose. Mannose 186-193 serpin family A member 1 Homo sapiens 28-46 10026209-7 1999 A model is proposed in which the removal of mannose from multiple attached oligosaccharides directs calnexin in the selection of misfolded alpha1-antitrypsin for degradation by the proteasome. Mannose 44-51 serpin family A member 1 Homo sapiens 139-157 3315863-7 1987 Human alpha-AT secreted into the culture broth contains, in addition to core carbohydrate, variable numbers of mannose outer chains, typical of secreted yeast proteins such as invertase. Mannose 111-118 serpin family A member 1 Homo sapiens 6-14 9569229-3 1998 The gene encoding human alpha1-antitrypsin (A1AT) was delivered to macrophages in vitro and in vivo by targeting the mannose receptor with mannose-terminal molecular conjugates. Mannose 117-124 serpin family A member 1 Homo sapiens 24-42 9569229-3 1998 The gene encoding human alpha1-antitrypsin (A1AT) was delivered to macrophages in vitro and in vivo by targeting the mannose receptor with mannose-terminal molecular conjugates. Mannose 117-124 serpin family A member 1 Homo sapiens 44-48 9559545-4 1998 Besides the core carbohydrates, variable numbers of mannose outer chains were also added to some of the secreted alpha 1-AT. Mannose 52-59 serpin family A member 1 Homo sapiens 113-123 9559545-5 1998 The human alpha 1-AT secreted in both methylotrophic yeasts was also heterogeneous and hypermannosylated as observed in S. cerevisiae, although the overall length of mannose outer chains of alpha 1-AT in the methylotrophic yeasts appeared to be relatively shorter than those of alpha 1-AT in S. cerevisiae. Mannose 166-173 serpin family A member 1 Homo sapiens 10-20 7576538-4 1995 Unlike plasma alpha 1AT, however, treatment of the yeast-produced alpha 1AT with endoglycosidase H decreased the molecular mass to that of recombinant alpha 1AT produced in Escherichia coli, indicating the high-mannose type N-linked glycosylation of the secreted alpha 1AT. Mannose 211-218 serpin family A member 1 Homo sapiens 66-75 7576538-4 1995 Unlike plasma alpha 1AT, however, treatment of the yeast-produced alpha 1AT with endoglycosidase H decreased the molecular mass to that of recombinant alpha 1AT produced in Escherichia coli, indicating the high-mannose type N-linked glycosylation of the secreted alpha 1AT. Mannose 211-218 serpin family A member 1 Homo sapiens 66-75 7576538-4 1995 Unlike plasma alpha 1AT, however, treatment of the yeast-produced alpha 1AT with endoglycosidase H decreased the molecular mass to that of recombinant alpha 1AT produced in Escherichia coli, indicating the high-mannose type N-linked glycosylation of the secreted alpha 1AT. Mannose 211-218 serpin family A member 1 Homo sapiens 66-75 8380585-2 1993 This study explores the mechanism whereby ionomycin, a Ca2+ ionophore, and thapsigargin, an ER Ca(2+)-ATPase inhibitor, promote retention of alpha 1-antitrypsin (alpha 1-AT) bearing high mannose, endoglycosidase H (Endo H)-sensitive oligosaccharide side chains within the ER of HepG2 cells. Mannose 187-194 serpin family A member 1 Homo sapiens 141-160 8380585-2 1993 This study explores the mechanism whereby ionomycin, a Ca2+ ionophore, and thapsigargin, an ER Ca(2+)-ATPase inhibitor, promote retention of alpha 1-antitrypsin (alpha 1-AT) bearing high mannose, endoglycosidase H (Endo H)-sensitive oligosaccharide side chains within the ER of HepG2 cells. Mannose 187-194 serpin family A member 1 Homo sapiens 162-172 1740441-5 1992 Ionomycin blocked processing of alpha 1-antitrypsin at the conversion from the high mannose to the complex glycosylated form without affecting ATP or GTP contents. Mannose 84-91 serpin family A member 1 Homo sapiens 32-51 1650361-3 1991 Inhibition of endoplasmic reticulum glucosidase I and II by dNM and its derivatives resulted in an intracellular accumulation of alpha 1-antitrypsin with glucose-containing high mannose type oligosaccharides (precursor). Mannose 178-185 serpin family A member 1 Homo sapiens 129-148 2111144-4 1990 Two molecular forms of alpha 1-antitrypsin could be identified: a 51-kDa intracellular form, susceptible to endoglucosaminidase H, thus representing the high-mannose type precursor form and a 56-kDa form resistant to endoglucosaminidase H which was secreted into the medium. Mannose 158-165 serpin family A member 1 Homo sapiens 23-42 8428908-5 1993 In accordance with this, "high mannose"-glycosylated alpha 1-antitrypsin was retained in or transported back to the ER. Mannose 31-38 serpin family A member 1 Homo sapiens 53-72 2579069-6 1985 When alpha 1-antitrypsin was immunoprecipitated from the cell lysates, sodium dodecyl sulfate-polyacrylamide gel electrophoresis fluorographic analysis demonstrated that the conversion of the high-mannose precursor to the hybrid form in swainsonine-treated cells occurred more rapidly (by about 10 min) than the conversion to the complex form in control cells. Mannose 197-204 serpin family A member 1 Homo sapiens 5-24 6790534-6 1981 Rat alpha-1-antitrypsin contains 14.3 residues/mol of N-acetylglucosamine, 5.0 residues/mol of mannose, 4.2 residues/mol of galactose, and 5.8 residues/mol of sialic acid. Mannose 95-102 serpin family A member 1 Homo sapiens 4-23 6223177-2 1983 The results suggest normal oligosaccharide side chains of high mannose type on lysosomal enzymes in alpha 1-antitrypsin (AAT) deficiency. Mannose 63-70 serpin family A member 1 Homo sapiens 100-119 1084886-7 1976 Specifically, the Z-type alpha-1-AT is deficient in 1 glucosamine residue, 3 neutral sugar residues (1 mannose and 2 galactose), and 2 sialic acid residues. Mannose 103-110 serpin family A member 1 Homo sapiens 25-35 308696-0 1978 alpha1-Antitrypsin: the presence of excess mannose in the Z variant isolated from liver. Mannose 43-50 serpin family A member 1 Homo sapiens 0-18