LinkDB: 116 24347 25654 32452 3373 38424 43937
CC: CCSD:116 AU: Vliegenthart JFG; Dorland L; van Halbeek H TI: High-resolution, 1H-nuclear magnetic resonance spectroscopy as a tool in the structural analysis of carbohydrates related to glycoproteins CT: Adv Carbohydr Chem Biochem (1983) 41: 209-374 SC: 55 BS: (CN) human, (OT) urine, (disease) aspartylglucosaminuria MT: N-linked glycoprotein AM: 1H-NMR SB: van Halbeek H DA: 22-04-1989 FC: f66294b1 SI: CBank:5426 ---------------- structure: b-D-Galp-(1-4)-b-D-GlcpNAc-(1-4)-Asn ================end of record
CC: CCSD:24347 AU: Auge C; Gautheron C; Pora H TI: Enzymic synthesis of the sialylglycopeptide, .alpha.-D-NeupAc-(2-6)-.beta.-D- Galp-(1-4)-.beta.-D-GlcpNAc-(1-4N)-L-Asn CT: Carbohydr Res (1989) 193: 288-293 SC: 7 ST: synthetic MT: N-linked glycoprotein AM: 13C-NMR AM: 1H-NMR SB: Kleen A DA: 22-04-1992 FC: f66294b1 SI: CBank:5426 ---------------- structure: b-D-Galp-(1-4)-b-D-GlcpNAc-(1-4)-Asn ================end of record
CC: CCSD:25654 AU: Kaartinen V; Mononen T; Laatikainen R; Mononen I TI: Substrate specificity and reaction mechanism of human glycoasparaginase. The N-glycosidic linkage of various glycoasparagines is cleaved through a reaction mechanism similar to L-asparaginase CT: J Biol Chem (1992) 267: 6855-6858 [PMID:1551892] SC: II MT: N-linked glycoprotein SB: Doubet S DA: 13-01-1993 FC: f66294b1 SI: CBank:5426 ---------------- structure: b-D-Galp-(1-4)-b-D-GlcpNAc-(1-4)-Asn ================end of record
CC: CCSD:32452 AU: David S; Auge C; Gautheron C TI: Enzymic methods in preparative carbohydrate chemistry CT: Adv Carbohydr Chem Biochem (1991) 49: 175-237 [PMID:1814172] SC: 58 ST: synthetic MT: N-linked glycopeptide SB: Kleen A DA: 28-09-1994 FC: f66294b1 SI: CBank:5426 ---------------- structure: b-D-Galp-(1-4)-b-D-GlcpNAc-(1-4)-Asn ================end of record
CC: CCSD:3373 AU: Breg J; Kroon-Batenburg LMJ; Strecker G; Montreuil J; Vliegenthart JFG TI: Conformational analysis of the sialyl.alpha.(2-3/6)N-acetyllactosamine structural element occurring in glycoproteins, by two-dimensional NOE 1H- NMR spectroscopy in combination with energy calculations by hard-sphere exo-anomeric and molecular mechanics force-field with hydrogen-bonding potential CT: Eur J Biochem (1989) 178: 727-739 [PMID:2912732] SC: I BS: (CN) human, (OT) urine, (disease) aspartylglucosaminuria MT: N-linked glycoprotein AM: 13C-NMR AM: 1H-NMR AM: 2D-NMR AM: HSEA AM: MM2 AM: MM2HB SB: van Kuik A DA: 01-02-1990 FC: f66294b1 SI: CBank:5426 ---------------- structure: b-D-Galp-(1-4)-b-D-GlcpNAc-(1-4)-Asn ================end of record
CC: CCSD:38424 AU: Mononen I; Fisher KJ; Kaartinen V; Aronson NN TI: Aspartylglycosaminuria: protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation CT: FASEB J (1993) 7: 1247-1256 [PMID:8405810] SC: II MT: N-linked glycopeptide SB: Westra B DA: 12-06-1995 FC: f66294b1 SI: CBank:5426 ---------------- structure: b-D-Galp-(1-4)-b-D-GlcpNAc-(1-4)-Asn ================end of record
CC: CCSD:43937 AU: Garg HG; Von dem Bruch K; Kunz H TI: Developments in the synthesis of glycopeptides containing glycosyl L- asparagine, L-serine, and L-threonine CT: Adv Carbohydr Chem Biochem (1994) 50: 277-310 [PMID:7942256] SC: 185 ST: synthetic MT: N-linked glycopeptide SB: Westra B DA: 06-12-1995 FC: f66294b1 SI: CBank:5426 ---------------- structure: b-D-Galp-(1-4)-b-D-GlcpNAc-(1-4)-Asn ================end of record