PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23709226-6 2013 Our structural data, combined with mutagenesis and in vitro binding assays, define the central mannose-binding site on LMAN1 and pinpoint histidine 178 and glycines 251/252 as critical residues for FV/FVIII binding. Mannose 95-102 lectin, mannose binding 1 Homo sapiens 119-124 32806600-4 2020 Deploying biochemical-silencing methods and molecular interaction studies in HBV-expressing liver cells, we herein identified the cellular ERGIC-53, a high-mannose-specific lectin, and distinct components of the endoplasmic reticulum (ER) export machinery COPII as crucial factors of viral trafficking and egress. Mannose 156-163 lectin, mannose binding 1 Homo sapiens 139-147 24498414-3 2014 VIP36 specifically interacts with the alpha1,2-linked D1 mannosyl arm without terminal glucosylation, while ERGIC-53 shows a broader specificity and lower binding affinity to the high-mannose-type oligosaccharides, irrespective of the presence or absence of the non-reducing terminal glucose residue at the D1 arm. Mannose 184-191 lectin, mannose binding 1 Homo sapiens 108-116 24498414-4 2014 In this study, we determined the crystal structure of ERGIC-53-CRD in complex with their binding partner, MCFD2 and the alpha1,2 mannotriose which corresponds to the trisaccharide of the D1 arm of high-mannose-type glycans. Mannose 202-209 lectin, mannose binding 1 Homo sapiens 54-62 23852824-9 2013 FV and FVIII likely bind LMAN1 through the high-mannose N-linked glycans under the higher Ca2+ conditions in the ER and dissociate in the lower Ca2+ environment of the ER-Golgi intermediate compartment. Mannose 48-55 lectin, mannose binding 1 Homo sapiens 25-30 23709226-5 2013 To understand the biochemical basis and regulation of LMAN1 binding to glycoprotein cargo, we solved crystal structures of the LMAN1-CRD bound to Man-alpha-1,2-Man, the terminal carbohydrate moiety of high mannose glycans. Mannose 206-213 lectin, mannose binding 1 Homo sapiens 54-59 20817851-1 2010 The LMAN1-MCFD2 (lectin, mannose binding 1/multiple coagulation factor deficiency protein 2) cargo receptor complex transports coagulation factors V (FV) and VIII (FVIII) from the endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC). Mannose 25-32 lectin, mannose binding 1 Homo sapiens 4-9 15886209-2 2005 LMAN1 is a type 1 transmembrane protein with homology to mannose-binding lectins. Mannose 57-64 lectin, mannose binding 1 Homo sapiens 0-5 19787799-6 2009 In addition, a Myc/6xHis-tagged recombinant form of wild-type LMAN1 could bind to D-mannose, but that of the mutant could not. Mannose 82-91 lectin, mannose binding 1 Homo sapiens 62-67 19787799-7 2009 The p.Trp67Ser mutation was located in the carbohydrate recognition domain (CRD), which is thought to participate in the selective binding of LMAN1 to the D-mannose of glycoproteins as well as the EF-motif of MCFD2. Mannose 155-164 lectin, mannose binding 1 Homo sapiens 142-147 19787799-8 2009 Taken together, it was suggested that the p.Trp67Ser mutation might affect the molecular chaperone function of LMAN1, impairing affinity for D-mannose as well as for MCFD2, which may be responsible for F5F8D in the patient. Mannose 141-150 lectin, mannose binding 1 Homo sapiens 111-116 19183188-4 2009 LMAN1 is a mannose-specific lectin that cycles between the endoplasmic reticulum (ER) and the ER-Golgi intermediate compartment. Mannose 11-18 lectin, mannose binding 1 Homo sapiens 0-5 18590741-3 2008 While ERGIC-53 is known to be a lectin-type mannose binding protein, the role of MCFD2 in the secretory pathway is comparatively unclear. Mannose 44-51 lectin, mannose binding 1 Homo sapiens 6-14 18577465-9 2008 In addition, it shows that both wild type and TDII FGFR3 interact with the mannose-specific lectin ERGIC-53. Mannose 75-82 lectin, mannose binding 1 Homo sapiens 99-107 16691507-4 2006 The three-dimensional structure of such a receptor, p58/ERGIC-53, has been recently solved by x-ray crystallography, which is a mannose-selective lectin and contains two Ca(2+) ions. Mannose 128-135 lectin, mannose binding 1 Homo sapiens 52-55 16691507-4 2006 The three-dimensional structure of such a receptor, p58/ERGIC-53, has been recently solved by x-ray crystallography, which is a mannose-selective lectin and contains two Ca(2+) ions. Mannose 128-135 lectin, mannose binding 1 Homo sapiens 56-64 16691507-9 2006 Properties of these modeled complexes were studied to examine the nature of physicochemical forces involved in the complex formation and compared with p58/ERGIC-53-mannose complex. Mannose 164-171 lectin, mannose binding 1 Homo sapiens 151-154 16691507-9 2006 Properties of these modeled complexes were studied to examine the nature of physicochemical forces involved in the complex formation and compared with p58/ERGIC-53-mannose complex. Mannose 164-171 lectin, mannose binding 1 Homo sapiens 155-163 19118014-4 2009 Among 28 candidate genes, LMAN1/ERGIC53, a mannose-specific lectin mediating endoplasmatic reticulum (ER)-to-Golgi transit of glycosylated proteins, showed high mutation frequency in MSI-H colorectal cancer cell lines (52%; 12 of 23), carcinomas (45%; 72 of 161), and adenomas (40%; 8 of 20). Mannose 43-50 lectin, mannose binding 1 Homo sapiens 26-31 19118014-4 2009 Among 28 candidate genes, LMAN1/ERGIC53, a mannose-specific lectin mediating endoplasmatic reticulum (ER)-to-Golgi transit of glycosylated proteins, showed high mutation frequency in MSI-H colorectal cancer cell lines (52%; 12 of 23), carcinomas (45%; 72 of 161), and adenomas (40%; 8 of 20). Mannose 43-50 lectin, mannose binding 1 Homo sapiens 32-39 14726380-4 2004 FVIII expression is limited by unstable mRNA, interaction with endoplasmic reticulum (ER) chaperones, and a requirement for facilitated ER to Golgi transport through interaction with the mannose-binding lectin LMAN1. Mannose 187-194 lectin, mannose binding 1 Homo sapiens 210-215 14718532-4 2004 Here we report efficient binding of purified ERGIC-53 to immobilized mannose at pH 7.4, the pH of the ER, but not at slightly lower pH. Mannose 69-76 lectin, mannose binding 1 Homo sapiens 45-53 12655775-2 2002 The most prominent cycling lectin is the mannose-binding type I membrane protein ERGIC-53 (ERGIC protein of 53 kDa), a marker for the ERGIC, which functions as a cargo receptor to facilitate export of an increasing number of glycoproteins with different characteristics from the ER. Mannose 41-48 lectin, mannose binding 1 Homo sapiens 81-89 12717434-2 2003 LMAN1 is a mannose-binding type 1 transmembrane protein localized to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC; refs. Mannose 11-18 lectin, mannose binding 1 Homo sapiens 0-5 11190675-0 2001 MR60/ERGIC-53, a mannose-specific shuttling intracellular membrane lectin. Mannose 17-24 lectin, mannose binding 1 Homo sapiens 0-4 11190675-0 2001 MR60/ERGIC-53, a mannose-specific shuttling intracellular membrane lectin. Mannose 17-24 lectin, mannose binding 1 Homo sapiens 5-13 10551804-2 1999 ERGIC-53 is a homo-hexameric transmembrane lectin localized to the ERGIC that exhibits mannose-selective properties in vitro. Mannose 87-94 lectin, mannose binding 1 Homo sapiens 0-8 10652252-1 2000 The ER-Golgi intermediate compartment (ERGIC) marker ERGIC-53 is a mannose-specific membrane lectin operating as a cargo receptor for the transport of glycoproteins from the ER to the ERGIC. Mannose 67-74 lectin, mannose binding 1 Homo sapiens 53-61 10559958-3 1999 Here we show that a cathepsin-Z-related glycoprotein binds to the recycling, mannose-specific membrane lectin ERGIC-53. Mannose 77-84 lectin, mannose binding 1 Homo sapiens 110-118 10521535-0 1999 The sugar binding activity of MR60, a mannose-specific shuttling lectin, requires a dimeric state. Mannose 38-45 lectin, mannose binding 1 Homo sapiens 30-34 8868475-0 1996 ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins. Mannose 25-32 lectin, mannose binding 1 Homo sapiens 0-8 9679138-1 1998 ERGIC-53, a homo-oligomeric recycling protein associated with the ER-Golgi intermediate compartment (ERGIC), has properties of a mannose-selective lectin in vitro, suggesting that it may function as a transport receptor for glycoproteins in the early secretory pathway. Mannose 129-136 lectin, mannose binding 1 Homo sapiens 0-8 8868475-6 1996 Overexpressed ERGIC-53 binds to a mannose column in a calcium-dependent manner and also co-stains with mannosylated neoglycoprotein in a morphological binding assay. Mannose 34-41 lectin, mannose binding 1 Homo sapiens 14-22 8868475-7 1996 By using a sequential elution protocol we show that ERGIC-53 has selectivity for mannose and low affinity for glucose and GlcNAc, but no affinity for galactose. Mannose 81-88 lectin, mannose binding 1 Homo sapiens 52-60 7876089-0 1995 ERGIC-53, a membrane protein of the endoplasmic reticulum-Golgi intermediate compartment, is identical to MR60, an intracellular mannose-specific lectin of myelomonocytic cells. Mannose 129-136 lectin, mannose binding 1 Homo sapiens 0-8 7876089-0 1995 ERGIC-53, a membrane protein of the endoplasmic reticulum-Golgi intermediate compartment, is identical to MR60, an intracellular mannose-specific lectin of myelomonocytic cells. Mannose 129-136 lectin, mannose binding 1 Homo sapiens 106-110 7876089-1 1995 A mannose-specific membrane lectin (MR60) isolated from human myelomonocytic HL60 cells by affinity chromatography is expressed in intracellular organelles of immature monocytes (Pimpaneau, V., Midoux, P., Monsigny, M., and Roche, A. C. (1991) Carbohydr. Mannose 2-9 lectin, mannose binding 1 Homo sapiens 36-40 7873929-1 1994 Myelomonocytic lineage cells express an M(r) 60,000 mannose specific lectin, MR60 (Pimpaneau et al. Mannose 52-59 lectin, mannose binding 1 Homo sapiens 77-81