PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25498022-2 2015 The methodology involves Corey-Link approach with suitably protected 3-oxo-D-gluco-furanose to introduce F/Cl as well as ester/amide functionalities at C-3 of glucose. Esters 121-126 complement C3 Homo sapiens 152-155 28757372-2 2017 One innovation was to couple C3b onto the magnetic agarose bead using the alternative pathway C3 convertase, which resulted in a linkage of the ligand by a covalent ester bond. Esters 165-170 complement C3 Homo sapiens 29-32 24076198-5 2013 The conjugation of GA onto chitosan probably occurred between amine (C-2), hydroxyl groups (C-3 and C-6) of chitosan and carboxyl groups of GA, forming amide and ester linkages, respectively. Esters 162-167 complement C3 Homo sapiens 92-95 24937183-0 2014 Synthesis and cytotoxic effect on cancer cell lines and macrophages of novel progesterone derivatives having an ester or a carbamate function at C-3 and C-17. Esters 81-86 complement C3 Homo sapiens 145-148 23039790-6 2012 The monoester of astaxanthin, however, allows formation of the neutral radical at C3" and prevents its formation at the opposite end where the ester group is attached. Esters 8-13 complement C3 Homo sapiens 82-84 19226157-1 2009 We report here that the monodentate complexation of Me2AlCl to an ester group significantly enhances the selectivity of hydrogen transfer on acyclic radicals flanked by both an ester functionality and a stereogenic center, leading to C-2,C-3-anti products with high diastereoselectivity. Esters 66-71 complement C3 Homo sapiens 238-241 19226157-1 2009 We report here that the monodentate complexation of Me2AlCl to an ester group significantly enhances the selectivity of hydrogen transfer on acyclic radicals flanked by both an ester functionality and a stereogenic center, leading to C-2,C-3-anti products with high diastereoselectivity. Esters 177-182 complement C3 Homo sapiens 238-241 12128171-2 2002 The esters synthesized (1 and 2) link AZT, by a succinyl linker, to the C-3 position of glucose and to C-6 of galactose. Esters 4-10 complement C3 Homo sapiens 72-75 15317455-3 2004 In contrast, ester derivatives lacking the C-3 hydroxy group were inactive to the cancer cell lines. Esters 13-18 complement C3 Homo sapiens 43-46 18524421-5 2009 Attempts to replace the ester group at C-3 position of isoxazoline with a variety of bioisosteric head groups led to significant loss of the tuberculosis inhibition indicating that an ester is required for anti-tuberculosis activity. Esters 24-29 complement C3 Homo sapiens 39-42 18524421-5 2009 Attempts to replace the ester group at C-3 position of isoxazoline with a variety of bioisosteric head groups led to significant loss of the tuberculosis inhibition indicating that an ester is required for anti-tuberculosis activity. Esters 184-189 complement C3 Homo sapiens 39-42 11791932-2 2002 A covalent amide or ester linkage is thereby supposed to form between C3b and the surface itself. Esters 20-25 complement C3 Homo sapiens 70-73 10993248-3 2000 However, replacing the ester group at C-3 in 2 and its analogues with an amido group yielded inactive or much less potent compounds against HIV replication, indicating that the ester group at C-3 in 2-4 is essential for potent anti-HIV activity. Esters 23-28 complement C3 Homo sapiens 38-41 11447230-6 2001 This region of the CH1 domain is exposed to solvent and contains a cluster of six potential acceptor sites for ester bond formation with C3b (four Ser and two Thr). Esters 111-116 complement C3 Homo sapiens 137-140 11270808-3 2001 For the carboxyheptyl glucosinolate, a novel intramolecular rearrangement reaction was observed during the final deprotection step, which generated an ester attached to the C-3 of glucose. Esters 151-156 complement C3 Homo sapiens 173-176 10993248-3 2000 However, replacing the ester group at C-3 in 2 and its analogues with an amido group yielded inactive or much less potent compounds against HIV replication, indicating that the ester group at C-3 in 2-4 is essential for potent anti-HIV activity. Esters 177-182 complement C3 Homo sapiens 38-41 10993248-3 2000 However, replacing the ester group at C-3 in 2 and its analogues with an amido group yielded inactive or much less potent compounds against HIV replication, indicating that the ester group at C-3 in 2-4 is essential for potent anti-HIV activity. Esters 177-182 complement C3 Homo sapiens 192-195 10993248-3 2000 However, replacing the ester group at C-3 in 2 and its analogues with an amido group yielded inactive or much less potent compounds against HIV replication, indicating that the ester group at C-3 in 2-4 is essential for potent anti-HIV activity. Esters 23-28 complement C3 Homo sapiens 192-195 9207914-4 1997 Oral absorption of derivatives has been optimized by modifying the C-3 ester promoiety. Esters 71-76 complement C3 Homo sapiens 67-70 10861231-1 2000 Nascent C3b can form ester bonds with various target molecules on the cell surface and in the fluid phase. Esters 21-26 complement C3 Homo sapiens 8-11 10092826-0 1999 Amplification of the antibody response by C3b complexed to antigen through an ester link. Esters 78-83 complement C3 Homo sapiens 42-45 8602875-3 1996 Activated C3b primarily forms ester bonds with hydroxyl groups of carbohydrates on complement activating surfaces, but it has also been shown to react with the hydroxyl group of tyrosine and with specific Ser and Thr residues on IgG and on complement protein C4b. Esters 30-35 complement C3 Homo sapiens 10-13 1917974-6 1991 These results combined with results from hydroxylamine treatment (splits ester linkage between C3b and IgG) imply that this adduct peptide consists of a 22-kDa C3 fragment and an 18-kDa IgG fragment. Esters 73-78 complement C3 Homo sapiens 95-98 7890301-5 1995 Ester-linked complexes including tetanus toxin (TT) and C3b were prepared to analyse the influence of bound C3b on TT processing and presentation by APC. Esters 0-5 complement C3 Homo sapiens 56-59 7961863-7 1994 The C3b-peptide complex was sensitive to hydroxylamine as was C3b-IgG indicating that both were ester-linked. Esters 96-101 complement C3 Homo sapiens 4-7 7961863-7 1994 The C3b-peptide complex was sensitive to hydroxylamine as was C3b-IgG indicating that both were ester-linked. Esters 96-101 complement C3 Homo sapiens 62-65 8352545-2 1993 In particular, we discuss the antitumor activity of the esters of homo-aza steroids in which the p-N,N-bis(2-chloroethyl)aminophenoxyacetic acid is linked to the C-3 or C-17 position, while the lactam nucleus is linked to the D or A ring of the modified steroid respectively. Esters 56-62 complement C3 Homo sapiens 162-165 8341280-4 1993 C3b was covalently bound to Superose through an ester link, as indicated by lability to hydroxylamine treatment at alkaline pH. Esters 48-53 complement C3 Homo sapiens 0-3 8341280-6 1993 Two types of limited activities on the C3b-Superose model system were detected: (i) a proteolytic activity cleaving C3b into mainly a C3c-like fragment which was released and a C3d-like fragment of apparent M(r) 32 kDa which remained bound to Superose through the original ester link; (ii) an esterolytic activity cleaving the ester bond and releasing C3b. Esters 273-278 complement C3 Homo sapiens 39-42 8341280-6 1993 Two types of limited activities on the C3b-Superose model system were detected: (i) a proteolytic activity cleaving C3b into mainly a C3c-like fragment which was released and a C3d-like fragment of apparent M(r) 32 kDa which remained bound to Superose through the original ester link; (ii) an esterolytic activity cleaving the ester bond and releasing C3b. Esters 273-278 complement C3 Homo sapiens 116-119 8341280-6 1993 Two types of limited activities on the C3b-Superose model system were detected: (i) a proteolytic activity cleaving C3b into mainly a C3c-like fragment which was released and a C3d-like fragment of apparent M(r) 32 kDa which remained bound to Superose through the original ester link; (ii) an esterolytic activity cleaving the ester bond and releasing C3b. Esters 273-278 complement C3 Homo sapiens 116-119 8341280-6 1993 Two types of limited activities on the C3b-Superose model system were detected: (i) a proteolytic activity cleaving C3b into mainly a C3c-like fragment which was released and a C3d-like fragment of apparent M(r) 32 kDa which remained bound to Superose through the original ester link; (ii) an esterolytic activity cleaving the ester bond and releasing C3b. Esters 293-298 complement C3 Homo sapiens 39-42 8341280-6 1993 Two types of limited activities on the C3b-Superose model system were detected: (i) a proteolytic activity cleaving C3b into mainly a C3c-like fragment which was released and a C3d-like fragment of apparent M(r) 32 kDa which remained bound to Superose through the original ester link; (ii) an esterolytic activity cleaving the ester bond and releasing C3b. Esters 293-298 complement C3 Homo sapiens 116-119 8341280-6 1993 Two types of limited activities on the C3b-Superose model system were detected: (i) a proteolytic activity cleaving C3b into mainly a C3c-like fragment which was released and a C3d-like fragment of apparent M(r) 32 kDa which remained bound to Superose through the original ester link; (ii) an esterolytic activity cleaving the ester bond and releasing C3b. Esters 293-298 complement C3 Homo sapiens 116-119 8341280-9 1993 Kinetic studies were in favour of a good stability on the ester bond, supporting an effective role of C3b as a chaperone during the extracellular and intracellular travel of C3b-bound antigen. Esters 58-63 complement C3 Homo sapiens 102-105 8341280-9 1993 Kinetic studies were in favour of a good stability on the ester bond, supporting an effective role of C3b as a chaperone during the extracellular and intracellular travel of C3b-bound antigen. Esters 58-63 complement C3 Homo sapiens 174-177 1511449-2 1992 The chemical shifts of the resonance of GlcNAc C-3 suggest that the relative orientations of the monosaccharides at the (1----3) linkage in the esters and salts are different. Esters 144-150 complement C3 Homo sapiens 47-50 7659097-8 1995 The ester linked complexes C3b-IgG and C3b-glycerol were less stable each exhibiting a t1/2 of approximately 8 hr. Esters 4-9 complement C3 Homo sapiens 27-30 7659097-8 1995 The ester linked complexes C3b-IgG and C3b-glycerol were less stable each exhibiting a t1/2 of approximately 8 hr. Esters 4-9 complement C3 Homo sapiens 39-42 7806998-10 1995 Furthermore, the C3 fragments bound to the M161 Ag were detached by 1 M hydroxylamine, suggesting that a covalent ester linkage sustains M161 Ag-C3b interaction. Esters 114-119 complement C3 Homo sapiens 145-148 7883753-8 1994 Most of the C3b-membrane molecule complexes were cleaved by hydroxylamine, suggesting covalent binding via an ester bond. Esters 110-115 complement C3 Homo sapiens 12-15 2605680-9 1989 These results show that the substituent at the C-3 position influences mainly the electronic structure of the conjugated pi-bond system (C3 = C4 - C4 = O) and consequently affects the feasibility of isomerization to the delta 2 ester, i.e., the stability to degradation. Esters 228-233 complement C3 Homo sapiens 47-50 2387864-2 1990 In the complex there is an ester bond between C3b and C4b. Esters 27-32 complement C3 Homo sapiens 46-49 2387864-5 1990 An Mr 17,000 fragment containing the ester linkage between C4b and C3b was purified and its amino-terminal sequence was examined. Esters 37-42 complement C3 Homo sapiens 67-70 2386510-8 1990 Anti-band 3 antibodies are preferred targets for nascent C3b which forms ester bonds with IgG and generates C3b-IgG complexes. Esters 73-78 complement C3 Homo sapiens 57-60 2404692-4 1990 When an activator of the alternative complement pathway is present, C3b becomes covalently attached to its surface via an ester or amide bond. Esters 122-127 complement C3 Homo sapiens 68-71 3818446-1 1986 A large group of ester derivatives of tylosin-related macrolides was prepared in which the hydroxyl groups at C-3 and C-4"" were acylated by either chemical or biochemical methods. Esters 17-22 complement C3 Homo sapiens 110-113 7326238-12 1981 An acyl transfer reaction takes place, leading to the binding of C3b to the receptive surfaces via an ester linkage [Law, S. K., Lichtenberg, N. A., & Levine, R. P. (1979) J. Immunol. Esters 102-107 complement C3 Homo sapiens 65-68 7326238-17 1981 In certain cases, the small molecules bind to C3b via ester linkages (e.g., glucose); in others, the bond is an amide linkage (e.g., lysine). Esters 54-59 complement C3 Homo sapiens 46-49 6903192-14 1980 These findings are consistent with the concept that native C3 contains an active carbonyl group, probably in the form of a thioester, which can either react with water to form functionally C3b-l;ike C3 or, upon enzymatic conversion of C3 to C3b, allows C3b to form an ester bond with hydroxyl groups on the target surface. Esters 127-132 complement C3 Homo sapiens 59-61 6903192-14 1980 These findings are consistent with the concept that native C3 contains an active carbonyl group, probably in the form of a thioester, which can either react with water to form functionally C3b-l;ike C3 or, upon enzymatic conversion of C3 to C3b, allows C3b to form an ester bond with hydroxyl groups on the target surface. Esters 127-132 complement C3 Homo sapiens 189-192 6903192-14 1980 These findings are consistent with the concept that native C3 contains an active carbonyl group, probably in the form of a thioester, which can either react with water to form functionally C3b-l;ike C3 or, upon enzymatic conversion of C3 to C3b, allows C3b to form an ester bond with hydroxyl groups on the target surface. Esters 127-132 complement C3 Homo sapiens 189-191 6903192-14 1980 These findings are consistent with the concept that native C3 contains an active carbonyl group, probably in the form of a thioester, which can either react with water to form functionally C3b-l;ike C3 or, upon enzymatic conversion of C3 to C3b, allows C3b to form an ester bond with hydroxyl groups on the target surface. Esters 127-132 complement C3 Homo sapiens 189-191 6903192-14 1980 These findings are consistent with the concept that native C3 contains an active carbonyl group, probably in the form of a thioester, which can either react with water to form functionally C3b-l;ike C3 or, upon enzymatic conversion of C3 to C3b, allows C3b to form an ester bond with hydroxyl groups on the target surface. Esters 127-132 complement C3 Homo sapiens 241-244 6903192-14 1980 These findings are consistent with the concept that native C3 contains an active carbonyl group, probably in the form of a thioester, which can either react with water to form functionally C3b-l;ike C3 or, upon enzymatic conversion of C3 to C3b, allows C3b to form an ester bond with hydroxyl groups on the target surface. Esters 127-132 complement C3 Homo sapiens 241-244 7316962-4 1981 Incubation of the C3b-antibody-antigen aggregates in buffers known to destroy ester linkages had little effect on the C3b-IgG complexes, which suggested that C3b and IgG might be linked by an amide bond. Esters 78-83 complement C3 Homo sapiens 18-21