PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
2524348-3	1989	Immune complexes with protein as antigen, such as has been reported to be diagnostic of procainamide-induced SLE, interact more with the C4A isotype of C4 than the C4B isotype.	Procainamide	88-100	complement C4B (Chido blood group)	Homo sapiens	164-167
34764957-8	2021	Second, in healthy White subject MS630, a C-nucleotide deletion at codon-755 led to frameshift mutations in his single C4B gene, which was a private mutation.	c-nucleotide	42-54	complement C4B (Chido blood group)	Homo sapiens	119-122
34764957-10	2021	Fourth, in East-Asian subject E133P with anti-NMDA receptor encephalitis, the C4B gene had a mutation that changed tryptophan-660 to a stop-codon (W660x), which was present in a haplotype with HLA-DRB1*04:06 and B*15:27.	Tryptophan	115-125	complement C4B (Chido blood group)	Homo sapiens	78-81
34356880-5	2021	In vitro, trimodulin activates complement and induces opsonophagocytosis, but also interacts with opsonins C3b, C4b and anaphylatoxin C5a in a concentration-dependent manner.	trimodulin	10-20	complement C4B (Chido blood group)	Homo sapiens	112-115
34290717-5	2021	This report demonstrates that lectin pathway (LP) recognition molecules of the complement system, such as MBL, FCN-2 and CL-11, bind to SARS-CoV-2 S- and N-proteins, with subsequent activation of LP-mediated C3b and C4b deposition.	cl-11	121-126	complement C4B (Chido blood group)	Homo sapiens	216-219
2526822-1	1989	Extracts from myelinated and unmyelinated nerves, prepared using Nonidet P-40, contained receptors for C3b/C4b (CR1).	Nonidet P-40	65-77	complement C4B (Chido blood group)	Homo sapiens	107-110
2492518-3	1989	It coprecipitates with C2 on polyethylene glycol fractionation and specifically binds, like C2, to Sepharose-bound iC4/C4b.	Sepharose	99-108	complement C4B (Chido blood group)	Homo sapiens	119-122
2785792-5	1989	[35S]Cysteine itself becomes covalently bound to C4b through the thioester site.	Sulfur-35	1-4	complement C4B (Chido blood group)	Homo sapiens	49-52
2785792-5	1989	[35S]Cysteine itself becomes covalently bound to C4b through the thioester site.	Cysteine	5-13	complement C4B (Chido blood group)	Homo sapiens	49-52
2785792-6	1989	Penicillamine and cysteine are more reactive with the C4A isotype than with the C4B isotype of the HLA class III protein C4.	Penicillamine	0-13	complement C4B (Chido blood group)	Homo sapiens	80-83
2785792-6	1989	Penicillamine and cysteine are more reactive with the C4A isotype than with the C4B isotype of the HLA class III protein C4.	Cysteine	18-26	complement C4B (Chido blood group)	Homo sapiens	80-83
2785792-7	1989	The limited amino acid sequence differences between C4A and C4B include a cysteine/serine interchange, and it is suggested that the cysteine residue in C4A contributes to the increased rate of reaction of C4A with the alpha-amino-beta-thiol compounds.	Cysteine	74-82	complement C4B (Chido blood group)	Homo sapiens	60-63
2785792-7	1989	The limited amino acid sequence differences between C4A and C4B include a cysteine/serine interchange, and it is suggested that the cysteine residue in C4A contributes to the increased rate of reaction of C4A with the alpha-amino-beta-thiol compounds.	Serine	83-89	complement C4B (Chido blood group)	Homo sapiens	60-63
2785792-7	1989	The limited amino acid sequence differences between C4A and C4B include a cysteine/serine interchange, and it is suggested that the cysteine residue in C4A contributes to the increased rate of reaction of C4A with the alpha-amino-beta-thiol compounds.	Cysteine	132-140	complement C4B (Chido blood group)	Homo sapiens	60-63
3146461-3	1988	The C4A and C4B gene products differ in reactivity with C4A being more reactive with nitrogen nucleophiles, including hydralazine and isoniazid (drugs which induce SLE), than with oxygen nucleophiles.	Nitrogen	85-93	complement C4B (Chido blood group)	Homo sapiens	12-15
3384397-2	1988	This protein migrates Mr 45,000-70,000 dalton region with a broad singlet or doublet on SDS-PAGE, specifically binds to C3b and C4b, has an acidic pI around pH 4, is rich in proline in amino acid analysis, possesses both N-linked and O-linked oligosaccharides, generates iC3b by acting as a cofactor for I-mediated C3b cleavage, and does not disassemble the C3 convertases.	Sodium Dodecyl Sulfate	88-91	complement C4B (Chido blood group)	Homo sapiens	128-131
3384397-2	1988	This protein migrates Mr 45,000-70,000 dalton region with a broad singlet or doublet on SDS-PAGE, specifically binds to C3b and C4b, has an acidic pI around pH 4, is rich in proline in amino acid analysis, possesses both N-linked and O-linked oligosaccharides, generates iC3b by acting as a cofactor for I-mediated C3b cleavage, and does not disassemble the C3 convertases.	Proline	174-181	complement C4B (Chido blood group)	Homo sapiens	128-131
3384397-2	1988	This protein migrates Mr 45,000-70,000 dalton region with a broad singlet or doublet on SDS-PAGE, specifically binds to C3b and C4b, has an acidic pI around pH 4, is rich in proline in amino acid analysis, possesses both N-linked and O-linked oligosaccharides, generates iC3b by acting as a cofactor for I-mediated C3b cleavage, and does not disassemble the C3 convertases.	Nitrogen	221-222	complement C4B (Chido blood group)	Homo sapiens	128-131
3384397-2	1988	This protein migrates Mr 45,000-70,000 dalton region with a broad singlet or doublet on SDS-PAGE, specifically binds to C3b and C4b, has an acidic pI around pH 4, is rich in proline in amino acid analysis, possesses both N-linked and O-linked oligosaccharides, generates iC3b by acting as a cofactor for I-mediated C3b cleavage, and does not disassemble the C3 convertases.	o-linked oligosaccharides	234-259	complement C4B (Chido blood group)	Homo sapiens	128-131
2553623-1	1989	The effect of arachidonic acid metabolites on the expression of the receptor for the C3b/C4b fragment of complement (CR1) by human B-lymphocytes was investigated.	Arachidonic Acid	14-30	complement C4B (Chido blood group)	Homo sapiens	89-92
3264881-4	1988	We demonstrate that human C4b binds to IgG in the fluid phase, that its covalent binding is predominantly to the heavy chain of IgG, and that the covalent linkage is by either amide or acyl ester bonds.	Amides	176-181	complement C4B (Chido blood group)	Homo sapiens	26-29
3264881-4	1988	We demonstrate that human C4b binds to IgG in the fluid phase, that its covalent binding is predominantly to the heavy chain of IgG, and that the covalent linkage is by either amide or acyl ester bonds.	Esters	190-195	complement C4B (Chido blood group)	Homo sapiens	26-29
2896160-2	1988	The gene encoding the enzyme, 21-OHB, has been mapped adjacent to the complement component C4B gene in the human HLA gene complex.	21-ohb	30-36	complement C4B (Chido blood group)	Homo sapiens	91-94
3146461-3	1988	The C4A and C4B gene products differ in reactivity with C4A being more reactive with nitrogen nucleophiles, including hydralazine and isoniazid (drugs which induce SLE), than with oxygen nucleophiles.	Hydralazine	118-129	complement C4B (Chido blood group)	Homo sapiens	12-15
3146461-3	1988	The C4A and C4B gene products differ in reactivity with C4A being more reactive with nitrogen nucleophiles, including hydralazine and isoniazid (drugs which induce SLE), than with oxygen nucleophiles.	Isoniazid	134-143	complement C4B (Chido blood group)	Homo sapiens	12-15
3568629-2	1987	High molecular weight complexes formed between C4 and IgG could be detected by the incorporation of 14C-iodoacetamide in the -SH group generated in the nascent C4b during the activation process.	14c-iodoacetamide	100-117	complement C4B (Chido blood group)	Homo sapiens	160-163
3552739-1	1987	The fourth component of complement in humans is coded for by two closely linked loci, i.e., C4A and C4B, that have been positioned within the class III region of the human major histocompatibility complex along with the genes for C2, Bf, and steroid 21-OH.	benzo(b)fluoranthene	234-236	complement C4B (Chido blood group)	Homo sapiens	100-103
3552739-1	1987	The fourth component of complement in humans is coded for by two closely linked loci, i.e., C4A and C4B, that have been positioned within the class III region of the human major histocompatibility complex along with the genes for C2, Bf, and steroid 21-OH.	Steroids	242-249	complement C4B (Chido blood group)	Homo sapiens	100-103
2433596-1	1987	Decay-accelerating factor (DAF), a glycoprotein that is anchored to the cell membrane by phosphatidylinositol, binds activated complement fragments C3b and C4b, thereby inhibiting amplification of the complement cascade on host cell membranes.	Phosphatidylinositols	89-109	complement C4B (Chido blood group)	Homo sapiens	156-159
3007562-0	1986	Gene conversion in salt-losing congenital adrenal hyperplasia with absent complement C4B protein.	Salts	19-23	complement C4B (Chido blood group)	Homo sapiens	85-88
3487454-5	1986	Among different phospholipid mixtures tested, P-glycerol/P-choline vesicles were found most effective for C4b binding.	Phospholipids	16-28	complement C4B (Chido blood group)	Homo sapiens	106-109
3487454-5	1986	Among different phospholipid mixtures tested, P-glycerol/P-choline vesicles were found most effective for C4b binding.	p-glycerol	46-56	complement C4B (Chido blood group)	Homo sapiens	106-109
3487454-5	1986	Among different phospholipid mixtures tested, P-glycerol/P-choline vesicles were found most effective for C4b binding.	Phosphorus	46-47	complement C4B (Chido blood group)	Homo sapiens	106-109
3487454-5	1986	Among different phospholipid mixtures tested, P-glycerol/P-choline vesicles were found most effective for C4b binding.	Choline	59-66	complement C4B (Chido blood group)	Homo sapiens	106-109
3487454-7	1986	C4bp was found to bind to phospholipid vesicles with a higher affinity than C4b; it was able to dissociate the vesicle-associated C3 convertase.	Phospholipids	26-38	complement C4B (Chido blood group)	Homo sapiens	0-3
3512717-2	1986	Moreover, although C4B formed predominantly ester linkages, C4A displayed a preference for amide bond formation.	Esters	44-49	complement C4B (Chido blood group)	Homo sapiens	19-22
3485688-14	1986	However, upon the addition of low doses of immune complexes, acetyl tyrosine did yield uncontrolled C1 activation, presumably by binding nascent C3b and C4b and thereby blocking their attachment to the immune complexes.	N-acetyltyrosine	61-76	complement C4B (Chido blood group)	Homo sapiens	153-156
3512717-7	1986	Irrespective of the target, C4A and C4B maintained their preference for forming amide and ester bonds, respectively.	Amides	80-85	complement C4B (Chido blood group)	Homo sapiens	36-39
3512717-7	1986	Irrespective of the target, C4A and C4B maintained their preference for forming amide and ester bonds, respectively.	Esters	90-95	complement C4B (Chido blood group)	Homo sapiens	36-39
3512717-8	1986	Interestingly, SDS-PAGE profiles of radiolabeled C4A and C4B, which had been covalently deposited on the various cells, suggested a further degree of transacylation specificity, as the two isotypic alpha-chains sometimes bound to different membrane components.	Sodium Dodecyl Sulfate	15-18	complement C4B (Chido blood group)	Homo sapiens	57-60
3012323-12	1986	We suggest that the Ser and Thr residues on the surface of Fab play an important role for binding of C4b upon activation of the complement system.	Serine	20-23	complement C4B (Chido blood group)	Homo sapiens	101-104
3459889-5	1986	A null complement allele located at the C4B locus (C4BQO) was also associated with thrombocytopenia from D-penicillamine (p less than 0.005, RR = 17.3).	Penicillamine	105-120	complement C4B (Chido blood group)	Homo sapiens	40-43
3012323-12	1986	We suggest that the Ser and Thr residues on the surface of Fab play an important role for binding of C4b upon activation of the complement system.	Threonine	28-31	complement C4B (Chido blood group)	Homo sapiens	101-104
6469387-4	1984	At relatively high concentrations, penicillins induce a conformational change in C3 and C4, leading to the C3b-like or C4b-like forms of these molecules, respectively.	Penicillins	35-46	complement C4B (Chido blood group)	Homo sapiens	119-122
2933745-1	1985	Redundant oligonucleotides were synthesized based on amino acid sequences of tryptic peptides from the purified receptor for human complement fragments C3b/C4b (CR1).	Oligonucleotides	10-26	complement C4B (Chido blood group)	Homo sapiens	156-159
3873356-6	1985	We show that hydralazine binds more efficiently to the C4A than to the C4B gene product and suggest that C4 type may predispose patients to hydralazine-induced SLE.	Hydralazine	13-24	complement C4B (Chido blood group)	Homo sapiens	71-74
6609966-9	1984	It was further found that the thioester bond of nascent C4b of the C4A isotype preferentially transacylates onto amino group nucleophiles, whereas in the C4B isotype, acylation of hydroxyl groups is strongly preferred.	Cy5-benzyl thioester	30-39	complement C4B (Chido blood group)	Homo sapiens	56-59
6609966-9	1984	It was further found that the thioester bond of nascent C4b of the C4A isotype preferentially transacylates onto amino group nucleophiles, whereas in the C4B isotype, acylation of hydroxyl groups is strongly preferred.	Cy5-benzyl thioester	30-39	complement C4B (Chido blood group)	Homo sapiens	154-157
6585138-0	1984	An unusual "morphologic" variant of BF S. In the course of family studies of haplotypes of the alleles of the sixth chromosome loci HLA-A, C, B, D/DR, BF, C2, C4A, C4B, and glyoxalase I, we encountered an unusual BF variant.	benzo(b)fluoranthene	36-38	complement C4B (Chido blood group)	Homo sapiens	164-167
6480575-15	1984	Chymotrypsin digestion of C4b-binding protein was also monitored as a function of time by polyacrylamide gel electrophoresis and the number of subunits cleaved was found to be seven, supporting our previous ultrastructural data which suggested that C4b-binding protein contains seven identical tentacle-like subunits.	polyacrylamide	90-104	complement C4B (Chido blood group)	Homo sapiens	26-29
6149580-5	1984	Characterization of these genes by restriction mapping, nucleotide sequence analysis and hybridization with C4A and C4B specific synthetic oligonucleotides show that these genes are very similar.	Oligonucleotides	139-155	complement C4B (Chido blood group)	Homo sapiens	116-119
670886-11	1978	The C4b/C4-bp complexes have sedimentation coefficients between 15 and 17 s on sucrose gradient ultracentrifugation, and can be readily identified by crossed immunoelectrophoresis (CIE).	Sucrose	79-86	complement C4B (Chido blood group)	Homo sapiens	4-7
6875279-1	1983	C4 is composed of two tightly linked genes (C4A and C4B) lying within the major histocompatibility complex of chromosome 6 that can be demonstrated by agarose gel electrophoresis.	Sepharose	151-158	complement C4B (Chido blood group)	Homo sapiens	52-55
6223626-6	1983	Fluid-phase degradation of C4b was monitored on sodium dodecyl sulphate/polyacrylamide-slab-gel electrophoresis, and the effect on surface-bound C4b was estimated by haemolytic assay.	Sodium Dodecyl Sulfate	48-71	complement C4B (Chido blood group)	Homo sapiens	27-30
6223626-6	1983	Fluid-phase degradation of C4b was monitored on sodium dodecyl sulphate/polyacrylamide-slab-gel electrophoresis, and the effect on surface-bound C4b was estimated by haemolytic assay.	polyacrylamide	72-86	complement C4B (Chido blood group)	Homo sapiens	27-30
6923908-7	1982	Ni could also replace Mg in the formation of the C4b,2a enzyme.	Magnesium	22-24	complement C4B (Chido blood group)	Homo sapiens	49-52
6923908-10	1982	The half-life of the C4b,2a formed with Ni was two times longer than that formed with Mg.	Magnesium	86-88	complement C4B (Chido blood group)	Homo sapiens	21-24
6923908-11	1982	Decay of both C3b,Bb and C4b,2a enzymes formed either with Mg or with Ni was unaffected by EDTA.	Magnesium	59-61	complement C4B (Chido blood group)	Homo sapiens	25-28
6980883-5	1982	In contrast to results with C4, metastable C4b displays a general increased susceptibility for modification by C3 and C4 alkyl amines.	c3 and c4 alkyl amines	111-133	complement C4B (Chido blood group)	Homo sapiens	43-46
6980883-6	1982	However, C4b exhibits a distinct preference for diamines, putrescine and 1,3-diaminopropane, over monoamines of the same alkyl chain length, s-butylamine and n-propylamine.	Diamines	48-56	complement C4B (Chido blood group)	Homo sapiens	9-12
6980883-6	1982	However, C4b exhibits a distinct preference for diamines, putrescine and 1,3-diaminopropane, over monoamines of the same alkyl chain length, s-butylamine and n-propylamine.	Putrescine	58-68	complement C4B (Chido blood group)	Homo sapiens	9-12
6980883-6	1982	However, C4b exhibits a distinct preference for diamines, putrescine and 1,3-diaminopropane, over monoamines of the same alkyl chain length, s-butylamine and n-propylamine.	trimethylenediamine	73-91	complement C4B (Chido blood group)	Homo sapiens	9-12
6980883-6	1982	However, C4b exhibits a distinct preference for diamines, putrescine and 1,3-diaminopropane, over monoamines of the same alkyl chain length, s-butylamine and n-propylamine.	monoamines	98-108	complement C4B (Chido blood group)	Homo sapiens	9-12
6980883-6	1982	However, C4b exhibits a distinct preference for diamines, putrescine and 1,3-diaminopropane, over monoamines of the same alkyl chain length, s-butylamine and n-propylamine.	Butylamines	141-153	complement C4B (Chido blood group)	Homo sapiens	9-12
6980883-6	1982	However, C4b exhibits a distinct preference for diamines, putrescine and 1,3-diaminopropane, over monoamines of the same alkyl chain length, s-butylamine and n-propylamine.	Propylamines	158-171	complement C4B (Chido blood group)	Homo sapiens	9-12
6980883-8	1982	A model is proposed to explain the results of competitive binding experiments with metastable C4b in terms of two binding sites for amines on C4b, the presumptive thioester and a second site such as the free side chain carboxyl group of glutamic acid.	Amines	132-138	complement C4B (Chido blood group)	Homo sapiens	94-97
6980883-8	1982	A model is proposed to explain the results of competitive binding experiments with metastable C4b in terms of two binding sites for amines on C4b, the presumptive thioester and a second site such as the free side chain carboxyl group of glutamic acid.	Amines	132-138	complement C4B (Chido blood group)	Homo sapiens	142-145
6980883-8	1982	A model is proposed to explain the results of competitive binding experiments with metastable C4b in terms of two binding sites for amines on C4b, the presumptive thioester and a second site such as the free side chain carboxyl group of glutamic acid.	Glutamic Acid	237-250	complement C4B (Chido blood group)	Homo sapiens	94-97
6976994-1	1982	Conversion of C4 to C4b by enzymic cleavage or generation of a C4b-like form by treatment with amines, chaotropes, or freezing and thawing is accompanied by conformational alterations in the molecule.	Amines	95-101	complement C4B (Chido blood group)	Homo sapiens	20-23
6976994-1	1982	Conversion of C4 to C4b by enzymic cleavage or generation of a C4b-like form by treatment with amines, chaotropes, or freezing and thawing is accompanied by conformational alterations in the molecule.	Amines	95-101	complement C4B (Chido blood group)	Homo sapiens	63-66
7391570-5	1980	Therefore, an altered form of C4b, C4b", consisting of four disulfide-linked polypeptide chains with the same m.w.	Disulfides	60-69	complement C4B (Chido blood group)	Homo sapiens	30-33
7391573-3	1980	We find that i) C4b binds covalently to cell surface components; ii) the bond between C4b and receptive molecules is hydroxylamine sensitive; iii) the alpha-polypeptide of C4b binds to receptive molecules; and iv) C5b does not interact covalently with cell surfaces.	Hydroxylamine	117-130	complement C4B (Chido blood group)	Homo sapiens	16-19
7391573-3	1980	We find that i) C4b binds covalently to cell surface components; ii) the bond between C4b and receptive molecules is hydroxylamine sensitive; iii) the alpha-polypeptide of C4b binds to receptive molecules; and iv) C5b does not interact covalently with cell surfaces.	Hydroxylamine	117-130	complement C4B (Chido blood group)	Homo sapiens	86-89
7391573-3	1980	We find that i) C4b binds covalently to cell surface components; ii) the bond between C4b and receptive molecules is hydroxylamine sensitive; iii) the alpha-polypeptide of C4b binds to receptive molecules; and iv) C5b does not interact covalently with cell surfaces.	Hydroxylamine	117-130	complement C4B (Chido blood group)	Homo sapiens	86-89
6906228-10	1980	The decay of the C3 convertase reflects the release of C2a from the C4b x (C2b) x C2a complex, and the stabilizing effect of iodine on the C3 convertase is therefore apparently one of stabilizing the C4b-C2z interaction, which is otherwise weak.	Iodine	125-131	complement C4B (Chido blood group)	Homo sapiens	200-203
6906229-8	1980	The apparent covalent interaction between C4b and IgG and between C4b and other C4b molecules cannot be inhibited by iodoacetamide and hence cannot be catalysed by transglutaminase (factor XIII).	Iodoacetamide	117-130	complement C4B (Chido blood group)	Homo sapiens	42-45
6906229-8	1980	The apparent covalent interaction between C4b and IgG and between C4b and other C4b molecules cannot be inhibited by iodoacetamide and hence cannot be catalysed by transglutaminase (factor XIII).	Iodoacetamide	117-130	complement C4B (Chido blood group)	Homo sapiens	66-69
6906229-8	1980	The apparent covalent interaction between C4b and IgG and between C4b and other C4b molecules cannot be inhibited by iodoacetamide and hence cannot be catalysed by transglutaminase (factor XIII).	Iodoacetamide	117-130	complement C4B (Chido blood group)	Homo sapiens	66-69
6980671-3	1982	Formation of the complexes upon incubation of C4bp, C4 and C1s appears to involve a single link between a subunit of C4bp and the alpha" chain of C4b, as observed by SDS-polyacrylamide gel electrophoresis in reducing conditions (160 000 dalton band).	Sodium Dodecyl Sulfate	166-169	complement C4B (Chido blood group)	Homo sapiens	46-49
6980671-3	1982	Formation of the complexes upon incubation of C4bp, C4 and C1s appears to involve a single link between a subunit of C4bp and the alpha" chain of C4b, as observed by SDS-polyacrylamide gel electrophoresis in reducing conditions (160 000 dalton band).	polyacrylamide	170-184	complement C4B (Chido blood group)	Homo sapiens	46-49
6980671-6	1982	The link between C4b and C4bp is partially destroyed by 1 M hydroxylamine at pH 9.0; its formation is strongly inhibited by 3.5 mM hydroxylamine or 60 mM methylamine at pH 9.0.	Hydroxylamine	60-73	complement C4B (Chido blood group)	Homo sapiens	17-20
6980671-6	1982	The link between C4b and C4bp is partially destroyed by 1 M hydroxylamine at pH 9.0; its formation is strongly inhibited by 3.5 mM hydroxylamine or 60 mM methylamine at pH 9.0.	Hydroxylamine	131-144	complement C4B (Chido blood group)	Homo sapiens	17-20
6980671-6	1982	The link between C4b and C4bp is partially destroyed by 1 M hydroxylamine at pH 9.0; its formation is strongly inhibited by 3.5 mM hydroxylamine or 60 mM methylamine at pH 9.0.	methylamine	154-165	complement C4B (Chido blood group)	Homo sapiens	17-20
6980671-7	1982	These findings suggest an ester or amide bond between the activated carboxyl group of the thioester bridge in the alpha" or alpha chain of nascent C4b or C4b-like C4 and a hydroxyl or amino group of C4bp.	Esters	26-31	complement C4B (Chido blood group)	Homo sapiens	147-150
6980671-7	1982	These findings suggest an ester or amide bond between the activated carboxyl group of the thioester bridge in the alpha" or alpha chain of nascent C4b or C4b-like C4 and a hydroxyl or amino group of C4bp.	Esters	26-31	complement C4B (Chido blood group)	Homo sapiens	154-157
6980671-7	1982	These findings suggest an ester or amide bond between the activated carboxyl group of the thioester bridge in the alpha" or alpha chain of nascent C4b or C4b-like C4 and a hydroxyl or amino group of C4bp.	Amides	35-40	complement C4B (Chido blood group)	Homo sapiens	147-150
6980671-7	1982	These findings suggest an ester or amide bond between the activated carboxyl group of the thioester bridge in the alpha" or alpha chain of nascent C4b or C4b-like C4 and a hydroxyl or amino group of C4bp.	Amides	35-40	complement C4B (Chido blood group)	Homo sapiens	154-157
6976993-0	1982	The fourth component of human complement treated with amines or chaotropes or frozen-thawed (C4b-like C4): interaction with C4 binding protein and cleavage by C3b/C4b inactivator.	Amines	54-60	complement C4B (Chido blood group)	Homo sapiens	93-96
70787-7	1977	Furthermore, when C2 is bound to C4b-Sepharose and then reacted with C1s, only the C2a fragment is released from the solid phase C2-C4b-Sepharose into the fluid phase, and the C2b fragment remains noncovalently bound to C4b-Sepharose.	Sepharose	136-145	complement C4B (Chido blood group)	Homo sapiens	33-36
894040-4	1977	Dextran sulfate strongly inhibited the formation of C567 sites on cells bearing C4b and C3b (EAC4b3b) as well as on unmodified E when C56 and C7 were added simultaneously to the cells.	Dextran Sulfate	0-15	complement C4B (Chido blood group)	Homo sapiens	80-83
70787-7	1977	Furthermore, when C2 is bound to C4b-Sepharose and then reacted with C1s, only the C2a fragment is released from the solid phase C2-C4b-Sepharose into the fluid phase, and the C2b fragment remains noncovalently bound to C4b-Sepharose.	Sepharose	136-145	complement C4B (Chido blood group)	Homo sapiens	33-36
70787-7	1977	Furthermore, when C2 is bound to C4b-Sepharose and then reacted with C1s, only the C2a fragment is released from the solid phase C2-C4b-Sepharose into the fluid phase, and the C2b fragment remains noncovalently bound to C4b-Sepharose.	Sepharose	37-46	complement C4B (Chido blood group)	Homo sapiens	33-36
32769120-4	2020	In this study, we present the nanobody hC4Nb8 that binds with picomolar affinity to human C4b and potently inhibits in vitro complement C3 deposition through the classical and lectin pathways in human serum and in mouse serum.	hc4nb8	39-45	complement C4B (Chido blood group)	Homo sapiens	90-93
34004375-1	2021	Membrane cofactor protein (MCP; CD46), a ubiquitously expressed complement regulatory protein, serves as a cofactor for serine protease factor I to cleave and inactivate C3b and C4b deposited on host cells.	Serine	120-126	complement C4B (Chido blood group)	Homo sapiens	178-181
33467558-5	2021	This model positions C4b near the Arg-Gly-Asp (RGD) loops of the penton base.	Arginine	34-37	complement C4B (Chido blood group)	Homo sapiens	21-24
33467558-5	2021	This model positions C4b near the Arg-Gly-Asp (RGD) loops of the penton base.	Glycyl-L-aspartic acid	38-45	complement C4B (Chido blood group)	Homo sapiens	21-24
33467558-5	2021	This model positions C4b near the Arg-Gly-Asp (RGD) loops of the penton base.	arginyl-glycyl-aspartic acid	47-50	complement C4B (Chido blood group)	Homo sapiens	21-24
33467558-5	2021	This model positions C4b near the Arg-Gly-Asp (RGD) loops of the penton base.	penton base	65-76	complement C4B (Chido blood group)	Homo sapiens	21-24
33467558-8	2021	We propose that C4b deposition on one RGD loop leads to the entanglement of C4b with additional RGD loops on the same penton base multimer and that this entanglement blocks AdV uncoating.	penton base	118-129	complement C4B (Chido blood group)	Homo sapiens	16-19
32978260-2	2020	alphaM protease inhibitors use theirs to conjugate proteases and preferentially react with primary amines (e.g. on lysine side chains), whereas those of alphaM complement components C3 and C4B have an increased hydroxyl reactivity that is conveyed by a conserved histidine residue and allows conjugation to cell surface glycans.	Lysine	115-121	complement C4B (Chido blood group)	Homo sapiens	189-192
32978260-2	2020	alphaM protease inhibitors use theirs to conjugate proteases and preferentially react with primary amines (e.g. on lysine side chains), whereas those of alphaM complement components C3 and C4B have an increased hydroxyl reactivity that is conveyed by a conserved histidine residue and allows conjugation to cell surface glycans.	Histidine	263-272	complement C4B (Chido blood group)	Homo sapiens	189-192
32978260-2	2020	alphaM protease inhibitors use theirs to conjugate proteases and preferentially react with primary amines (e.g. on lysine side chains), whereas those of alphaM complement components C3 and C4B have an increased hydroxyl reactivity that is conveyed by a conserved histidine residue and allows conjugation to cell surface glycans.	Polysaccharides	320-327	complement C4B (Chido blood group)	Homo sapiens	189-192
32769120-5	2020	The crystal structure of the C4b:hC4Nb8 complex and a three-dimensional reconstruction of the C4bC2 proconvertase obtained by electron microscopy together rationalize how hC4Nb8 prevents proconvertase assembly through recognition of a neoepitope exposed in C4b and reveals a unique C2 conformation compared with the alternative pathway proconvertase.	hc4nb8	33-39	complement C4B (Chido blood group)	Homo sapiens	29-32
32769120-5	2020	The crystal structure of the C4b:hC4Nb8 complex and a three-dimensional reconstruction of the C4bC2 proconvertase obtained by electron microscopy together rationalize how hC4Nb8 prevents proconvertase assembly through recognition of a neoepitope exposed in C4b and reveals a unique C2 conformation compared with the alternative pathway proconvertase.	hc4nb8	171-177	complement C4B (Chido blood group)	Homo sapiens	29-32
32769120-5	2020	The crystal structure of the C4b:hC4Nb8 complex and a three-dimensional reconstruction of the C4bC2 proconvertase obtained by electron microscopy together rationalize how hC4Nb8 prevents proconvertase assembly through recognition of a neoepitope exposed in C4b and reveals a unique C2 conformation compared with the alternative pathway proconvertase.	hc4nb8	171-177	complement C4B (Chido blood group)	Homo sapiens	94-97
31264677-9	2019	Furthermore, it was feasible to tune the CO2-capture ability of C4B32 by metal-doping, which regulated the Lewis acidity/basicity of the C4B32 surface.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	41-44	complement C4B (Chido blood group)	Homo sapiens	64-67
31003786-8	2019	DMRs included six nonoverlapping DMRs (three in the Netherlands Twin Register, three in the Dunedin study) in the major histocompatibility complex, which were associated with expression of genes in the major histocompatibility complex, including C4A and C4B, previously implicated in schizophrenia.	dmrs	0-4	complement C4B (Chido blood group)	Homo sapiens	254-257
32900365-2	2020	Here we present a case of anti-N-methyl- D-aspartate (NMDA) receptor encephalitis associated with homozygous C4B deficiency, who did not respond to intravenous immunoglobulin and pulse methylprednisolone but plasmapheresis and rituximab.	Methylprednisolone	185-203	complement C4B (Chido blood group)	Homo sapiens	109-112
31916313-5	2020	CD81 exosome marker-normalized ADE levels of classical pathway C4b, alternative pathway factor D and Bb, lectin pathway mannose-binding lectin (MBL), and shared neurotoxic effectors C3b and C5b-9 terminal C complex were significantly higher and those of C regulatory proteins CR1 and CD59 were lower in the first week of acute sTBI (n = 12) than in controls (n = 12).	Adenine	31-34	complement C4B (Chido blood group)	Homo sapiens	63-66
31916313-7	2020	In contrast, significant elevations of ADE levels of C4b, factor D, Bb, MBL, C3b and C5b-9 terminal C complex, and depressions of CR1 and CD59 relative to those of controls were observed after 1-4 years in early chronic mtTBI (n = 10) and persisted for decades except for normalization of Bb, MBL, and CD59 in late chronic mtTBI (n = 15).	Adenine	39-42	complement C4B (Chido blood group)	Homo sapiens	53-66
31264677-9	2019	Furthermore, it was feasible to tune the CO2-capture ability of C4B32 by metal-doping, which regulated the Lewis acidity/basicity of the C4B32 surface.	Metals	73-78	complement C4B (Chido blood group)	Homo sapiens	64-67
31032394-4	2019	Results: ADE levels of C1q and C4b of the classical pathway, factor D and fragment Bb of the alternative pathway, and C5b, C3b, and C5b-C9 of both pathways were significantly higher in patients with MCIC than those with MCIS.	Adenine	9-12	complement C4B (Chido blood group)	Homo sapiens	31-34
30204219-4	2018	Ablation treatment with endovenous NBCA was used in patients with C3 to C4b grade superficial venous insufficiency, according to the CEAP (clinical, aetiology, anatomy and pathophysiology) clinical classification, with sapheno-femoral junctional insufficiency and a reflux of 0.5 seconds and longer on duplex ultra-sonography.	Enbucrilate	35-39	complement C4B (Chido blood group)	Homo sapiens	72-75
27738201-8	2016	Our data reveal that in low NaCl concentrations, both at surfaces and in solution, C4b forms compact TED-MG1 structures.	Sodium Chloride	28-32	complement C4B (Chido blood group)	Homo sapiens	83-86
29350927-0	2018	Synthesis and Pharmacological Characterization of C4beta-Amide-Substituted 2-Aminobicyclo[3.1.0]hexane-2,6-dicarboxylates.	2-aminobicyclo(3.1.0)hexane-2,6-dicarboxylate	75-121	complement C4B (Chido blood group)	Homo sapiens	50-56
29350927-3	2018	As part of our ongoing efforts to identify potent, selective, and systemically bioavailable agonists for mGlu2 and mGlu3 receptor subtypes, a series of C4beta-N-linked variants of (1 S,2 S,5 R,6 S)-2-amino-bicyclo[3.1.0]hexane-2,6-dicarboxylic acid 1 (LY354740) were prepared and evaluated for both mGlu2 and mGlu3 receptor binding affinity and functional cellular responses.	(1 s,2 s,5 r,6 s)-2-amino-bicyclo[	180-214	complement C4B (Chido blood group)	Homo sapiens	152-158
27738201-0	2016	Domain structure of human complement C4b extends with increasing NaCl concentration: implications for its regulatory mechanism.	Sodium Chloride	65-69	complement C4B (Chido blood group)	Homo sapiens	26-40
27738201-8	2016	Our data reveal that in low NaCl concentrations, both at surfaces and in solution, C4b forms compact TED-MG1 structures.	mg1	105-108	complement C4B (Chido blood group)	Homo sapiens	83-86
27738201-4	2016	Dual polarisation interferometry of C4b immobilised at a sensor surface showed that the maximum thickness of C4b increased by 0.46 nm with an increase in NaCl concentration from 50 to 175 mM NaCl.	Sodium Chloride	154-158	complement C4B (Chido blood group)	Homo sapiens	36-39
27738201-4	2016	Dual polarisation interferometry of C4b immobilised at a sensor surface showed that the maximum thickness of C4b increased by 0.46 nm with an increase in NaCl concentration from 50 to 175 mM NaCl.	Sodium Chloride	154-158	complement C4B (Chido blood group)	Homo sapiens	109-112
27738201-4	2016	Dual polarisation interferometry of C4b immobilised at a sensor surface showed that the maximum thickness of C4b increased by 0.46 nm with an increase in NaCl concentration from 50 to 175 mM NaCl.	Sodium Chloride	191-195	complement C4B (Chido blood group)	Homo sapiens	109-112
27738201-5	2016	Analytical ultracentrifugation showed that the sedimentation coefficient s20,w of monomeric C4b of 8.41 S in 50 mM NaCl buffer decreased to 7.98 S in 137 mM NaCl buffer, indicating that C4b became more extended.	Sodium Chloride	115-119	complement C4B (Chido blood group)	Homo sapiens	92-95
27738201-5	2016	Analytical ultracentrifugation showed that the sedimentation coefficient s20,w of monomeric C4b of 8.41 S in 50 mM NaCl buffer decreased to 7.98 S in 137 mM NaCl buffer, indicating that C4b became more extended.	Sodium Chloride	115-119	complement C4B (Chido blood group)	Homo sapiens	186-189
27738201-5	2016	Analytical ultracentrifugation showed that the sedimentation coefficient s20,w of monomeric C4b of 8.41 S in 50 mM NaCl buffer decreased to 7.98 S in 137 mM NaCl buffer, indicating that C4b became more extended.	Sodium Chloride	157-161	complement C4B (Chido blood group)	Homo sapiens	92-95
27738201-5	2016	Analytical ultracentrifugation showed that the sedimentation coefficient s20,w of monomeric C4b of 8.41 S in 50 mM NaCl buffer decreased to 7.98 S in 137 mM NaCl buffer, indicating that C4b became more extended.	Sodium Chloride	157-161	complement C4B (Chido blood group)	Homo sapiens	186-189
27738201-6	2016	Small angle X-ray scattering reported similar RG values of 4.89-4.90 nm for C4b in 137-250 mM NaCl.	Sodium Chloride	94-98	complement C4B (Chido blood group)	Homo sapiens	76-79
27738201-9	2016	In solution, physiologically relevant NaCl concentrations lead to the separation of the TED and MG1 domain, making C4b less capable of binding to its complement regulators.	Sodium Chloride	38-42	complement C4B (Chido blood group)	Homo sapiens	115-118
25688346-7	2015	On one hand, drugs with free hydroxyl on amino groups (e.g., hydralazine, procainamide) could interact with C4A, C4B, or C3 and cause an SLE-like disease.	Hydroxyl Radical	29-37	complement C4B (Chido blood group)	Homo sapiens	113-123
25531924-0	2015	Carbon nanoscroll from C4H/C4F-type graphene superlattice: MD and MM simulation insights.	Carbon	0-6	complement C4B (Chido blood group)	Homo sapiens	27-30
25531924-0	2015	Carbon nanoscroll from C4H/C4F-type graphene superlattice: MD and MM simulation insights.	Graphite	36-44	complement C4B (Chido blood group)	Homo sapiens	27-30
25531924-2	2015	Through mixing single-side-hydrogenated graphene (C4H) with fluorinated graphene (C4F) on one single sheet, the C4H/C4F-type graphene superlattices can self-scroll at room temperature.	Graphite	40-48	complement C4B (Chido blood group)	Homo sapiens	116-119
25531924-2	2015	Through mixing single-side-hydrogenated graphene (C4H) with fluorinated graphene (C4F) on one single sheet, the C4H/C4F-type graphene superlattices can self-scroll at room temperature.	c4h	50-53	complement C4B (Chido blood group)	Homo sapiens	116-119
25531924-2	2015	Through mixing single-side-hydrogenated graphene (C4H) with fluorinated graphene (C4F) on one single sheet, the C4H/C4F-type graphene superlattices can self-scroll at room temperature.	Graphite	72-80	complement C4B (Chido blood group)	Homo sapiens	82-85
25531924-2	2015	Through mixing single-side-hydrogenated graphene (C4H) with fluorinated graphene (C4F) on one single sheet, the C4H/C4F-type graphene superlattices can self-scroll at room temperature.	Graphite	72-80	complement C4B (Chido blood group)	Homo sapiens	116-119
25531924-2	2015	Through mixing single-side-hydrogenated graphene (C4H) with fluorinated graphene (C4F) on one single sheet, the C4H/C4F-type graphene superlattices can self-scroll at room temperature.	c4h	112-115	complement C4B (Chido blood group)	Homo sapiens	82-85
25531924-2	2015	Through mixing single-side-hydrogenated graphene (C4H) with fluorinated graphene (C4F) on one single sheet, the C4H/C4F-type graphene superlattices can self-scroll at room temperature.	c4h	112-115	complement C4B (Chido blood group)	Homo sapiens	116-119
25531924-2	2015	Through mixing single-side-hydrogenated graphene (C4H) with fluorinated graphene (C4F) on one single sheet, the C4H/C4F-type graphene superlattices can self-scroll at room temperature.	Graphite	72-80	complement C4B (Chido blood group)	Homo sapiens	82-85
25531924-2	2015	Through mixing single-side-hydrogenated graphene (C4H) with fluorinated graphene (C4F) on one single sheet, the C4H/C4F-type graphene superlattices can self-scroll at room temperature.	Graphite	72-80	complement C4B (Chido blood group)	Homo sapiens	116-119
25688346-7	2015	On one hand, drugs with free hydroxyl on amino groups (e.g., hydralazine, procainamide) could interact with C4A, C4B, or C3 and cause an SLE-like disease.	Hydralazine	61-72	complement C4B (Chido blood group)	Homo sapiens	113-123
25688346-7	2015	On one hand, drugs with free hydroxyl on amino groups (e.g., hydralazine, procainamide) could interact with C4A, C4B, or C3 and cause an SLE-like disease.	Procainamide	74-86	complement C4B (Chido blood group)	Homo sapiens	113-123
25602126-2	2015	This molecule, 1S,2S,4R,5R,6S-2-amino-4-methylbicyclo[3.1.0]hexane-2,6-dicarboxylate 2 (LY541850), exhibited an unexpected mGlu2 agonist/mGlu3 antagonist pharmacological profile, whereas the C4beta-methyl diastereomer (3) possessed dual mGlu2/3 receptor agonist activity.	2-amino-4-methylbicyclo(3.1.0)hexane2,6-dicarboxylic acid	88-96	complement C4B (Chido blood group)	Homo sapiens	191-197
21699774-1	2011	BACKGROUND & AIMS: CD46 is a C3b/C4b binding complement regulator and a receptor for several human pathogens.	Adenosine Monophosphate	12-15	complement C4B (Chido blood group)	Homo sapiens	37-40
25140358-3	2014	Surprisingly, a high adsorption energy (~550 meV per molecule) of water has been unveiled on C4F via density functional theory studies, implying anomalous superhydrophilicity of C4F.	Water	66-71	complement C4B (Chido blood group)	Homo sapiens	93-96
25140358-3	2014	Surprisingly, a high adsorption energy (~550 meV per molecule) of water has been unveiled on C4F via density functional theory studies, implying anomalous superhydrophilicity of C4F.	Water	66-71	complement C4B (Chido blood group)	Homo sapiens	178-181
25140358-6	2014	Since the surface chemical inertness of CF inhibits it from being widely adopted in device fabrication, the present finding suggests that C4F can be a promising candidate in graphene-based electronic devices.	Graphite	174-182	complement C4B (Chido blood group)	Homo sapiens	138-141
25017204-6	2014	Furthermore, the upregulation of complement gene C3 and complement 4B preproprotein (C4b) in A549-P-S cells was confirmed by ELISA analysis and was identified to be correlated with recovering Pi absorption in A549 cells by the phosphomolybdic acid method by enhancing the expression of SLC34A2.	phosphomolybdic acid	227-247	complement C4B (Chido blood group)	Homo sapiens	85-88
24214979-3	2014	The PfRh4 attachment site lies within the three N-terminal complement control protein modules (CCPs 1-3) of CR1, which intriguingly also accommodate binding and regulatory sites for the key complement activation-specific proteolytic products, C3b and C4b.	pfrh4	4-9	complement C4B (Chido blood group)	Homo sapiens	251-254
22612291-0	2012	Improved synthesis of C4alpha- and C4beta-methyl analogues of 2-aminobicyclo[3.1.0]hexane-2,6-dicarboxylate.	2-aminobicyclo(3.1.0)hexane-2,6-dicarboxylate	62-107	complement C4B (Chido blood group)	Homo sapiens	35-41
22612291-1	2012	An efficient and divergent synthesis of C4alpha- and C4beta-methyl-substituted analogues of 2-aminobicyclo[3.1.0]hexane 2,6-dicarboxylate, which are important tools in the study of metabotropic glutamate receptor function, has been achieved.	2-aminobicyclo(3.1.0)hexane-2,6-dicarboxylate	92-137	complement C4B (Chido blood group)	Homo sapiens	53-59
22612291-2	2012	By taking advantage of an unanticipated facial selectivity of the bicyclo[3.1.0]hexane ring system, either the C4alpha- or C4beta-methyl substituent was introduced in a highly stereoselective and high-yielding manner.	bicyclo(3.1.0)hexane	66-86	complement C4B (Chido blood group)	Homo sapiens	123-129
21967755-7	2012	RESULTS: The ratio of ACTH-stimulated and baseline cortisol concentrations was significantly higher (P = 0 001) in the group of patients carrying the C4B*Q0 genotype compared to the rest of the patients.	Hydrocortisone	51-59	complement C4B (Chido blood group)	Homo sapiens	150-153
21967755-10	2012	In C4B*Q0 carriers, metyrapone hardly reduced the serum cortisol level, while in non-carriers it induced a highly significant (P = 0 002) decrease.	Metyrapone	20-30	complement C4B (Chido blood group)	Homo sapiens	3-6
24757030-4	2014	RESULTS: A total of 33% of the variation in serum C4 concentrations could be accounted for by both C4A and C4B GCNs (R(2) = 0.30, P <= 0.0001).	gcns	111-115	complement C4B (Chido blood group)	Homo sapiens	107-110
26580195-1	2014	Density functional theory (DFT) computations with van der Waals (vdw) correction revealed the existence of considerable C(delta+)F(delta-)   C(delta+)F(delta-) dipole-dipole interactions between two experimentally realized C4F monolayers.	dipole	160-166	complement C4B (Chido blood group)	Homo sapiens	223-226
26580195-1	2014	Density functional theory (DFT) computations with van der Waals (vdw) correction revealed the existence of considerable C(delta+)F(delta-)   C(delta+)F(delta-) dipole-dipole interactions between two experimentally realized C4F monolayers.	dipole	167-173	complement C4B (Chido blood group)	Homo sapiens	223-226
26580195-2	2014	The dipole-dipole interactions induce a subtle interlayer polarization, which results in a significantly reduced band gap for C4F bilayer as compared to the individual C4F monolayer.	dipole-dipole	4-17	complement C4B (Chido blood group)	Homo sapiens	126-129
26580195-2	2014	The dipole-dipole interactions induce a subtle interlayer polarization, which results in a significantly reduced band gap for C4F bilayer as compared to the individual C4F monolayer.	dipole-dipole	4-17	complement C4B (Chido blood group)	Homo sapiens	168-171
24174618-9	2013	Upon binding to mannan or DNA in the presence of MASP-2, the CL-L1-CL-K1 complex mediated deposition of C4b.	Mannans	16-22	complement C4B (Chido blood group)	Homo sapiens	104-107
24278177-11	2013	EV71vac elicited weak cross-neutralizing antibody responses (~20% of participants) against a C4B and Coxsackie virus A16.	ev71vac	0-7	complement C4B (Chido blood group)	Homo sapiens	93-96
22071314-6	2012	In addition, mutation of residue K342 to alanine in the CCP1 domain abolished binding to both C4 and C4b in its CCP1-CCP2 form, suggesting a key electrostatic role for this amino acid.	croconazole	33-37	complement C4B (Chido blood group)	Homo sapiens	101-104
22071314-6	2012	In addition, mutation of residue K342 to alanine in the CCP1 domain abolished binding to both C4 and C4b in its CCP1-CCP2 form, suggesting a key electrostatic role for this amino acid.	Alanine	41-48	complement C4B (Chido blood group)	Homo sapiens	101-104
20698613-2	2010	When exposed on one side the F coverage saturates at 25% (C(4)F), which is optically transparent, over 6 orders of magnitude more resistive than graphene, and readily patterned.	Graphite	145-153	complement C4B (Chido blood group)	Homo sapiens	58-64
21809649-7	2011	CONCLUSION: Innate masked C4 deficiency interfere with the normal immune defense of organism against chlamydia infection, and antigen carbohydrate pathogenicity may possibly be more significant for the development of immune response to which C4B isotype activity is necessary.	Carbohydrates	134-146	complement C4B (Chido blood group)	Homo sapiens	242-245
20877782-1	2010	A series of tribenzotriquinacene derivatives bearing three oxy-functionalised alkyl groups at the benzhydrylic bridgeheads (C-4b, C-8b and C-12b) have been synthesised.	Tribenzotriquinacene	12-32	complement C4B (Chido blood group)	Homo sapiens	124-128
19660812-5	2009	Increasing the C4b density on zymosan (14,000-431,000 C4b/Zym) increased the number of C4b bound per C4BP from 2.87 to 8.23 indicating that at high C4b density all seven alpha-chains of C4BP are engaged in C4b-binding.	Zymosan	30-37	complement C4B (Chido blood group)	Homo sapiens	54-57
20089702-1	2010	Kaposica, the complement regulator of Kaposi"s sarcoma-associated herpesvirus, inhibits complement by supporting factor I-mediated inactivation of the proteolytically activated form of C3 (C3b) and C4 (C4b) (cofactor activity [CFA]) and by accelerating the decay of classical and alternative pathway C3-convertases (decay-accelerating activity [DAA]).	3-chloro-4-fluoroaniline	227-230	complement C4B (Chido blood group)	Homo sapiens	202-205
19660812-2	2009	In the present study, role of C4b-binding protein (C4BP) in regulating the lectin pathway C3/C5 convertase assembled on zymosan and sheep erythrocytes coated with mannan (E(Man)) was examined.	Zymosan	120-127	complement C4B (Chido blood group)	Homo sapiens	30-33
18214838-1	2008	A series of 4beta-[(4-substituted)-1,2,3-triazol-1-yl]podophyllotoxin analogues have been synthesized with high regio-selectivity by employing copper(I)-catalyzed 1,3-dipolar cycloaddition of 1-O-propargyl monosaccharides with C4beta-azido podophyllotoxin and C4beta-azido-4"-O-demethyl podophyllotoxin.	4beta-[(4-substituted)-1,2,3-triazol-1-yl]podophyllotoxin	12-69	complement C4B (Chido blood group)	Homo sapiens	227-233
19660812-2	2009	In the present study, role of C4b-binding protein (C4BP) in regulating the lectin pathway C3/C5 convertase assembled on zymosan and sheep erythrocytes coated with mannan (E(Man)) was examined.	Mannans	163-169	complement C4B (Chido blood group)	Homo sapiens	30-33
19660812-5	2009	Increasing the C4b density on zymosan (14,000-431,000 C4b/Zym) increased the number of C4b bound per C4BP from 2.87 to 8.23 indicating that at high C4b density all seven alpha-chains of C4BP are engaged in C4b-binding.	Zymosan	30-37	complement C4B (Chido blood group)	Homo sapiens	15-18
19660812-5	2009	Increasing the C4b density on zymosan (14,000-431,000 C4b/Zym) increased the number of C4b bound per C4BP from 2.87 to 8.23 indicating that at high C4b density all seven alpha-chains of C4BP are engaged in C4b-binding.	Zymosan	30-37	complement C4B (Chido blood group)	Homo sapiens	54-57
19660812-5	2009	Increasing the C4b density on zymosan (14,000-431,000 C4b/Zym) increased the number of C4b bound per C4BP from 2.87 to 8.23 indicating that at high C4b density all seven alpha-chains of C4BP are engaged in C4b-binding.	Zymosan	30-37	complement C4B (Chido blood group)	Homo sapiens	54-57
19660812-5	2009	Increasing the C4b density on zymosan (14,000-431,000 C4b/Zym) increased the number of C4b bound per C4BP from 2.87 to 8.23 indicating that at high C4b density all seven alpha-chains of C4BP are engaged in C4b-binding.	Zymosan	30-37	complement C4B (Chido blood group)	Homo sapiens	54-57
19309011-5	2009	1x10(3) kDa, which were mainly attributed to the presence of the complexes of complement C4b and C4b-binding protein in heparin-plasma and their absence in EDTA-plasma.	Heparin	120-127	complement C4B (Chido blood group)	Homo sapiens	78-92
18680512-2	2008	The isotypic residues at position 1101-1106 of the C4A gene contain the Pro-Cys-Pro-Val-Leu-Asp sequence which has a higher affinity for binding amino group-containing antigens, while C4B contains the Leu-Ser-Pro-Val-Ileu-His sequence which has a higher affinity for hydroxyl group-containing antigens.	H-LEU-SER-OH	201-208	complement C4B (Chido blood group)	Homo sapiens	184-187
19237749-2	2009	The formation of these convertases requires the Mg(2+)-dependent binding of C2 to C4b and the subsequent cleavage of C2 by C1s or MASP2, respectively.	magnesium ion	48-54	complement C4B (Chido blood group)	Homo sapiens	82-85
17988764-1	2008	A series of 4beta-[(4-substituted)-1,2,3-triazol-1-yl] podophyllotoxin congeners have been designed and synthesized with significant regioselectivity by employing Cu(I) catalyzed 1,3-dipolar cycloaddition reaction of C4beta-azido podophyllotoxin and C4beta-azido-4"-O-demethyl podophyllotoxin with N-prop-2-yn-1-ylanilines.	4beta-[(4-substituted)-1,2,3-triazol-1-yl] podophyllotoxin	12-70	complement C4B (Chido blood group)	Homo sapiens	217-223
17988764-1	2008	A series of 4beta-[(4-substituted)-1,2,3-triazol-1-yl] podophyllotoxin congeners have been designed and synthesized with significant regioselectivity by employing Cu(I) catalyzed 1,3-dipolar cycloaddition reaction of C4beta-azido podophyllotoxin and C4beta-azido-4"-O-demethyl podophyllotoxin with N-prop-2-yn-1-ylanilines.	4beta-[(4-substituted)-1,2,3-triazol-1-yl] podophyllotoxin	12-70	complement C4B (Chido blood group)	Homo sapiens	250-256
17988764-1	2008	A series of 4beta-[(4-substituted)-1,2,3-triazol-1-yl] podophyllotoxin congeners have been designed and synthesized with significant regioselectivity by employing Cu(I) catalyzed 1,3-dipolar cycloaddition reaction of C4beta-azido podophyllotoxin and C4beta-azido-4"-O-demethyl podophyllotoxin with N-prop-2-yn-1-ylanilines.	cuprous ion	163-168	complement C4B (Chido blood group)	Homo sapiens	217-223
17988764-1	2008	A series of 4beta-[(4-substituted)-1,2,3-triazol-1-yl] podophyllotoxin congeners have been designed and synthesized with significant regioselectivity by employing Cu(I) catalyzed 1,3-dipolar cycloaddition reaction of C4beta-azido podophyllotoxin and C4beta-azido-4"-O-demethyl podophyllotoxin with N-prop-2-yn-1-ylanilines.	cuprous ion	163-168	complement C4B (Chido blood group)	Homo sapiens	250-256
18214838-1	2008	A series of 4beta-[(4-substituted)-1,2,3-triazol-1-yl]podophyllotoxin analogues have been synthesized with high regio-selectivity by employing copper(I)-catalyzed 1,3-dipolar cycloaddition of 1-O-propargyl monosaccharides with C4beta-azido podophyllotoxin and C4beta-azido-4"-O-demethyl podophyllotoxin.	4beta-[(4-substituted)-1,2,3-triazol-1-yl]podophyllotoxin	12-69	complement C4B (Chido blood group)	Homo sapiens	260-266
18214838-1	2008	A series of 4beta-[(4-substituted)-1,2,3-triazol-1-yl]podophyllotoxin analogues have been synthesized with high regio-selectivity by employing copper(I)-catalyzed 1,3-dipolar cycloaddition of 1-O-propargyl monosaccharides with C4beta-azido podophyllotoxin and C4beta-azido-4"-O-demethyl podophyllotoxin.	cuprous ion	143-152	complement C4B (Chido blood group)	Homo sapiens	227-233
18214838-1	2008	A series of 4beta-[(4-substituted)-1,2,3-triazol-1-yl]podophyllotoxin analogues have been synthesized with high regio-selectivity by employing copper(I)-catalyzed 1,3-dipolar cycloaddition of 1-O-propargyl monosaccharides with C4beta-azido podophyllotoxin and C4beta-azido-4"-O-demethyl podophyllotoxin.	cuprous ion	143-152	complement C4B (Chido blood group)	Homo sapiens	260-266
17984207-2	2008	We previously identified lipooligosaccharide on Neisseria meningitidis as an acceptor for complement C4b.	lipid-linked oligosaccharides	25-44	complement C4B (Chido blood group)	Homo sapiens	101-104
17984207-7	2008	Using N. gonorrhoeae variants that predominantly expressed individual Opa proteins, we found that all Opa proteins tested (A, B, C, D, E, F, and I) bound C4b and C3b via amide and ester linkages, respectively.	Amides	170-175	complement C4B (Chido blood group)	Homo sapiens	154-157
14734749-5	2004	C4A and C4B, purified from plasma lacking one of the isotypes, were Cs converted to C4Ab and C4Bb.	Cesium	68-70	complement C4B (Chido blood group)	Homo sapiens	8-11
17699783-4	2007	We observed that thymoquinone inhibited DNA synthesis, proliferation, and viability of cancerous (LNCaP, C4-B, DU145, and PC-3) but not noncancerous (BPH-1) prostate epithelial cells by down-regulating AR and E2F-1.	thymoquinone	17-29	complement C4B (Chido blood group)	Homo sapiens	105-109
16199260-8	2006	Genetically engineered carbohydrate-deficient mutant human IgA1 antibodies were used to assess the role of carbohydrate in accepting the C4b and C3b depositions, and these studies indicated that the carbohydrate on the Fc-region of IgA1 played a positive role.	Carbohydrates	107-119	complement C4B (Chido blood group)	Homo sapiens	137-140
16199260-8	2006	Genetically engineered carbohydrate-deficient mutant human IgA1 antibodies were used to assess the role of carbohydrate in accepting the C4b and C3b depositions, and these studies indicated that the carbohydrate on the Fc-region of IgA1 played a positive role.	Carbohydrates	107-119	complement C4B (Chido blood group)	Homo sapiens	137-140
16202066-10	2005	DXS treatment attenuated surface deposition of C1q, C4b/c, C3b/c and C5b-9 without affecting IgG or IgM deposition.	Dextran Sulfate	0-3	complement C4B (Chido blood group)	Homo sapiens	52-55
15304516-8	2004	Classical pathway regulation, both through decay acceleration and factor I cleavage of C4b, required a cluster of positively charged amino acids in CCP1 stretching into CCP2 (Arg-20, Arg-33, Arg-35, Lys-64, Lys-65, and Lys-88) as well as positively (Lys-131, Lys-133, and His-135) and negatively (Glu-99, Glu-152, and Asp-155) charged areas at opposing faces of the border region between CCPs 2 and 3.	Arginine	175-178	complement C4B (Chido blood group)	Homo sapiens	87-90
15304516-8	2004	Classical pathway regulation, both through decay acceleration and factor I cleavage of C4b, required a cluster of positively charged amino acids in CCP1 stretching into CCP2 (Arg-20, Arg-33, Arg-35, Lys-64, Lys-65, and Lys-88) as well as positively (Lys-131, Lys-133, and His-135) and negatively (Glu-99, Glu-152, and Asp-155) charged areas at opposing faces of the border region between CCPs 2 and 3.	Arginine	183-186	complement C4B (Chido blood group)	Homo sapiens	87-90
15304516-8	2004	Classical pathway regulation, both through decay acceleration and factor I cleavage of C4b, required a cluster of positively charged amino acids in CCP1 stretching into CCP2 (Arg-20, Arg-33, Arg-35, Lys-64, Lys-65, and Lys-88) as well as positively (Lys-131, Lys-133, and His-135) and negatively (Glu-99, Glu-152, and Asp-155) charged areas at opposing faces of the border region between CCPs 2 and 3.	Arginine	183-186	complement C4B (Chido blood group)	Homo sapiens	87-90
15304516-8	2004	Classical pathway regulation, both through decay acceleration and factor I cleavage of C4b, required a cluster of positively charged amino acids in CCP1 stretching into CCP2 (Arg-20, Arg-33, Arg-35, Lys-64, Lys-65, and Lys-88) as well as positively (Lys-131, Lys-133, and His-135) and negatively (Glu-99, Glu-152, and Asp-155) charged areas at opposing faces of the border region between CCPs 2 and 3.	Lysine	199-202	complement C4B (Chido blood group)	Homo sapiens	87-90
15304516-8	2004	Classical pathway regulation, both through decay acceleration and factor I cleavage of C4b, required a cluster of positively charged amino acids in CCP1 stretching into CCP2 (Arg-20, Arg-33, Arg-35, Lys-64, Lys-65, and Lys-88) as well as positively (Lys-131, Lys-133, and His-135) and negatively (Glu-99, Glu-152, and Asp-155) charged areas at opposing faces of the border region between CCPs 2 and 3.	Lysine	207-210	complement C4B (Chido blood group)	Homo sapiens	87-90
15166556-13	2004	At 1 h after CPB, the transvascular escape rate of Evans blue dye averaged 11.5 +/- 1.3%/h in patients with the 00BB C4 phenotype; this value was significantly higher (P < 0.01) than that in patients with other C4 phenotypes.	Evans Blue	51-61	complement C4B (Chido blood group)	Homo sapiens	117-119
15166556-13	2004	At 1 h after CPB, the transvascular escape rate of Evans blue dye averaged 11.5 +/- 1.3%/h in patients with the 00BB C4 phenotype; this value was significantly higher (P < 0.01) than that in patients with other C4 phenotypes.	Evans Blue	51-61	complement C4B (Chido blood group)	Homo sapiens	214-216
17623109-8	2007	One possible explanation is that glutamine-deprivation may have slowed the turnover rate of mCRPs, preventing the cells from replacing pre-existing mCRPs, as they became neutralized by covalent C4b and C3b depositions.	Glutamine	33-42	complement C4B (Chido blood group)	Homo sapiens	194-197
17234210-2	2007	Formation of these convertases requires the Mg(2+)-dependent binding of C2 to C4b, and the subsequent cleavage of C2 by C1s or MASP2, respectively.	magnesium ion	44-50	complement C4B (Chido blood group)	Homo sapiens	78-81
16760474-6	2006	The expressed soluble form of CCPH bound to C3b (KD = 19.2 microm) as well as to C4b (KD = 0.8 microm) and accelerated the decay of the classical/lectin as well as alternative pathway C3-convertases.	ccph	30-34	complement C4B (Chido blood group)	Homo sapiens	81-84
16600177-2	2006	The C-terminal 11-amino-acid of the first CRIT-extracellular domain (CRIT-H17) has a strong homology with a sequence in the C4beta chain, which is responsible for the binding of C2.	11-amino-acid	15-28	complement C4B (Chido blood group)	Homo sapiens	124-130
16098595-7	2006	In this report, the tertiary structures of C4A and C4B were compared using near and far-UV circular dichroism, ANS fluorescence, site-specific monoclonal antibodies and isoelectric focusing.	1-anilino-8-naphthalenesulfonate	111-114	complement C4B (Chido blood group)	Homo sapiens	51-54
15998580-10	2005	The results showed that there was 2-bp insertion in exon 29 of mutant C4B gene in one SLE patient carrying C4AQ0.	c4aq0	107-112	complement C4B (Chido blood group)	Homo sapiens	70-73
15932521-5	2005	In spite of this, PIP was normal in these patients, and in marked contrast to our previous observations on connective tissue diseases, PIP measurements in these patient groups correlated more strongly with levels of C4B (r = 0.51, P = 0.0000004) than C4A.	pip	135-138	complement C4B (Chido blood group)	Homo sapiens	216-219
15304516-8	2004	Classical pathway regulation, both through decay acceleration and factor I cleavage of C4b, required a cluster of positively charged amino acids in CCP1 stretching into CCP2 (Arg-20, Arg-33, Arg-35, Lys-64, Lys-65, and Lys-88) as well as positively (Lys-131, Lys-133, and His-135) and negatively (Glu-99, Glu-152, and Asp-155) charged areas at opposing faces of the border region between CCPs 2 and 3.	Lysine	207-210	complement C4B (Chido blood group)	Homo sapiens	87-90
15304516-8	2004	Classical pathway regulation, both through decay acceleration and factor I cleavage of C4b, required a cluster of positively charged amino acids in CCP1 stretching into CCP2 (Arg-20, Arg-33, Arg-35, Lys-64, Lys-65, and Lys-88) as well as positively (Lys-131, Lys-133, and His-135) and negatively (Glu-99, Glu-152, and Asp-155) charged areas at opposing faces of the border region between CCPs 2 and 3.	Lysine	207-210	complement C4B (Chido blood group)	Homo sapiens	87-90
15304516-8	2004	Classical pathway regulation, both through decay acceleration and factor I cleavage of C4b, required a cluster of positively charged amino acids in CCP1 stretching into CCP2 (Arg-20, Arg-33, Arg-35, Lys-64, Lys-65, and Lys-88) as well as positively (Lys-131, Lys-133, and His-135) and negatively (Glu-99, Glu-152, and Asp-155) charged areas at opposing faces of the border region between CCPs 2 and 3.	Lysine	207-210	complement C4B (Chido blood group)	Homo sapiens	87-90
15304516-8	2004	Classical pathway regulation, both through decay acceleration and factor I cleavage of C4b, required a cluster of positively charged amino acids in CCP1 stretching into CCP2 (Arg-20, Arg-33, Arg-35, Lys-64, Lys-65, and Lys-88) as well as positively (Lys-131, Lys-133, and His-135) and negatively (Glu-99, Glu-152, and Asp-155) charged areas at opposing faces of the border region between CCPs 2 and 3.	Histidine	272-275	complement C4B (Chido blood group)	Homo sapiens	87-90
15304516-8	2004	Classical pathway regulation, both through decay acceleration and factor I cleavage of C4b, required a cluster of positively charged amino acids in CCP1 stretching into CCP2 (Arg-20, Arg-33, Arg-35, Lys-64, Lys-65, and Lys-88) as well as positively (Lys-131, Lys-133, and His-135) and negatively (Glu-99, Glu-152, and Asp-155) charged areas at opposing faces of the border region between CCPs 2 and 3.	Glutamic Acid	297-300	complement C4B (Chido blood group)	Homo sapiens	87-90
15304516-8	2004	Classical pathway regulation, both through decay acceleration and factor I cleavage of C4b, required a cluster of positively charged amino acids in CCP1 stretching into CCP2 (Arg-20, Arg-33, Arg-35, Lys-64, Lys-65, and Lys-88) as well as positively (Lys-131, Lys-133, and His-135) and negatively (Glu-99, Glu-152, and Asp-155) charged areas at opposing faces of the border region between CCPs 2 and 3.	Glutamic Acid	305-308	complement C4B (Chido blood group)	Homo sapiens	87-90
15304516-8	2004	Classical pathway regulation, both through decay acceleration and factor I cleavage of C4b, required a cluster of positively charged amino acids in CCP1 stretching into CCP2 (Arg-20, Arg-33, Arg-35, Lys-64, Lys-65, and Lys-88) as well as positively (Lys-131, Lys-133, and His-135) and negatively (Glu-99, Glu-152, and Asp-155) charged areas at opposing faces of the border region between CCPs 2 and 3.	Aspartic Acid	318-321	complement C4B (Chido blood group)	Homo sapiens	87-90
14734749-5	2004	C4A and C4B, purified from plasma lacking one of the isotypes, were Cs converted to C4Ab and C4Bb.	c4bb	93-97	complement C4B (Chido blood group)	Homo sapiens	8-11
11367523-18	2001	Site directed mutagenesis experiments revealed that D1106 is responsible for the effective binding of C4A to form amide bonds with immune aggregates or protein antigens, and H1106 of C4B catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens.	Esters	227-232	complement C4B (Chido blood group)	Homo sapiens	183-186
14522582-3	2003	We found that the cofactor activity of C4b-binding protein towards C4b/C3b and factor H towards C3b increase at micromolar concentrations of Zn(2+) and are abolished at 2 mM Zn(2+) and above.	Zinc	141-143	complement C4B (Chido blood group)	Homo sapiens	39-42
14522582-3	2003	We found that the cofactor activity of C4b-binding protein towards C4b/C3b and factor H towards C3b increase at micromolar concentrations of Zn(2+) and are abolished at 2 mM Zn(2+) and above.	Zinc	141-143	complement C4B (Chido blood group)	Homo sapiens	67-70
14522582-3	2003	We found that the cofactor activity of C4b-binding protein towards C4b/C3b and factor H towards C3b increase at micromolar concentrations of Zn(2+) and are abolished at 2 mM Zn(2+) and above.	Zinc	174-176	complement C4B (Chido blood group)	Homo sapiens	39-42
14522582-3	2003	We found that the cofactor activity of C4b-binding protein towards C4b/C3b and factor H towards C3b increase at micromolar concentrations of Zn(2+) and are abolished at 2 mM Zn(2+) and above.	Zinc	174-176	complement C4B (Chido blood group)	Homo sapiens	67-70
12645526-4	2003	The equilibrium affinity constant (KD) of KCP for C3b and C4b was determined by surface plasmon resonance analysis to range between 0.47-10 microM and 0.025-6.1 microM, respectively, depending on NaCl concentration and cation presence.	Sodium Chloride	196-200	complement C4B (Chido blood group)	Homo sapiens	58-61
12417021-5	2002	The C4bp mutant with deletion of SCR2 lost the C4b-binding ability, as judged on C3b/C4b-Sepharose binding assaying and ELISA.	Sepharose	89-98	complement C4B (Chido blood group)	Homo sapiens	4-7
12417021-5	2002	The C4bp mutant with deletion of SCR2 lost the C4b-binding ability, as judged on C3b/C4b-Sepharose binding assaying and ELISA.	Sepharose	89-98	complement C4B (Chido blood group)	Homo sapiens	47-50
12023363-7	2002	The codons determining the isotype, Asp(1054), Leu(1101), Ser(1102), Ile(1105) and His(1106), were characteristic of C4B gene, whereas the polymorphic sites in exon and intron 28 were indicative of C4A3a sequence.	Aspartic Acid	36-39	complement C4B (Chido blood group)	Homo sapiens	117-120
12023363-7	2002	The codons determining the isotype, Asp(1054), Leu(1101), Ser(1102), Ile(1105) and His(1106), were characteristic of C4B gene, whereas the polymorphic sites in exon and intron 28 were indicative of C4A3a sequence.	Leucine	47-50	complement C4B (Chido blood group)	Homo sapiens	117-120
12023363-7	2002	The codons determining the isotype, Asp(1054), Leu(1101), Ser(1102), Ile(1105) and His(1106), were characteristic of C4B gene, whereas the polymorphic sites in exon and intron 28 were indicative of C4A3a sequence.	Serine	58-61	complement C4B (Chido blood group)	Homo sapiens	117-120
12023363-7	2002	The codons determining the isotype, Asp(1054), Leu(1101), Ser(1102), Ile(1105) and His(1106), were characteristic of C4B gene, whereas the polymorphic sites in exon and intron 28 were indicative of C4A3a sequence.	Isoleucine	69-72	complement C4B (Chido blood group)	Homo sapiens	117-120
12023363-7	2002	The codons determining the isotype, Asp(1054), Leu(1101), Ser(1102), Ile(1105) and His(1106), were characteristic of C4B gene, whereas the polymorphic sites in exon and intron 28 were indicative of C4A3a sequence.	Histidine	83-86	complement C4B (Chido blood group)	Homo sapiens	117-120
11687244-7	2001	In the assay described here, the specific C4b-depositing capacity of the MBL pathway was determined by incubating serum diluted in buffer containing 1 M NaCl in mannan-coated microtiter wells before the addition of purified C4.	Sodium Chloride	153-157	complement C4B (Chido blood group)	Homo sapiens	42-45
11687244-7	2001	In the assay described here, the specific C4b-depositing capacity of the MBL pathway was determined by incubating serum diluted in buffer containing 1 M NaCl in mannan-coated microtiter wells before the addition of purified C4.	Mannans	161-167	complement C4B (Chido blood group)	Homo sapiens	42-45
11687244-10	2001	When 100 normal serum samples were analysed we found that the MBL level correlated with the amount of C4b deposited on the mannan-coated surface.	Mannans	123-129	complement C4B (Chido blood group)	Homo sapiens	102-105
11367523-18	2001	Site directed mutagenesis experiments revealed that D1106 is responsible for the effective binding of C4A to form amide bonds with immune aggregates or protein antigens, and H1106 of C4B catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens.	Carbohydrates	273-285	complement C4B (Chido blood group)	Homo sapiens	183-186
10383431-5	1999	The C4b binding site demonstrated herein was also found to be a specific heparin binding site.	Heparin	73-80	complement C4B (Chido blood group)	Homo sapiens	4-7
11696892-4	2000	The inhibition constants for binding of the nascent C4b to its target were determined for immunoglobulins G1, G2, G3, G4, M, and A1, as well as for ferritin, yeast mannan, capsid polysaccharides of the Neisseria meningitidis A, B, and C serotypes, diphtheria anatoxin, epinephrine, and salicylic acid.	Epinephrine	269-280	complement C4B (Chido blood group)	Homo sapiens	52-55
11696892-4	2000	The inhibition constants for binding of the nascent C4b to its target were determined for immunoglobulins G1, G2, G3, G4, M, and A1, as well as for ferritin, yeast mannan, capsid polysaccharides of the Neisseria meningitidis A, B, and C serotypes, diphtheria anatoxin, epinephrine, and salicylic acid.	Salicylic Acid	286-300	complement C4B (Chido blood group)	Homo sapiens	52-55
11696892-6	2000	Lectins of various specificities were shown to inhibit the enzymic activation of C4 by the first complement component and the subsequent C4b sorption to its target, which allowed us to suggest that some oligosaccharide fragments of the C1s and C4 molecules are spatially close to the C1s active site and to the thioester bond of C4.	Oligosaccharides	203-218	complement C4B (Chido blood group)	Homo sapiens	137-140
11696892-6	2000	Lectins of various specificities were shown to inhibit the enzymic activation of C4 by the first complement component and the subsequent C4b sorption to its target, which allowed us to suggest that some oligosaccharide fragments of the C1s and C4 molecules are spatially close to the C1s active site and to the thioester bond of C4.	Cy5-benzyl thioester	311-320	complement C4B (Chido blood group)	Homo sapiens	137-140
10845665-9	2000	Mean plasma levels of C4b/c and C3b/c were significantly decreased at 24 h post-surgery in the HEMI+ group (p=0.02 and p=0.07).	hemi+	95-100	complement C4B (Chido blood group)	Homo sapiens	22-25
11008645-4	2000	The nascent fragment C4b is covalently bound to the target activator; C4Ab binds better to the target protein (immunoglobulin), and C4Bb to the target carbohydrate (liposaccharide).	Carbohydrates	151-163	complement C4B (Chido blood group)	Homo sapiens	21-24
11008645-4	2000	The nascent fragment C4b is covalently bound to the target activator; C4Ab binds better to the target protein (immunoglobulin), and C4Bb to the target carbohydrate (liposaccharide).	liposaccharide	165-179	complement C4B (Chido blood group)	Homo sapiens	21-24
10799895-5	2000	We identified a key recognition surface for M proteins that overlaps with the C4b binding site because substitution of R64 and H67 by Gln dramatically reduces binding to both ligands.	Glutamine	134-137	complement C4B (Chido blood group)	Homo sapiens	78-81
9759862-6	1998	The C4B12 nucleotide sequence is analogous to C4B1b and C4B3 sequences, except for codon 1076, which is GCC in C4B1b and C4B3 and GGA in C4B12, which is coding for glycine in both cases.	Glycine	164-171	complement C4B (Chido blood group)	Homo sapiens	4-9
10408373-7	1999	Protein modeling together with site directed mutagenesis indicate that R39, R64 and R66 from the C4BP alpha-chain form a key binding site for heparin, suggesting that this region could be of major importance for interaction with C4b.	Heparin	142-149	complement C4B (Chido blood group)	Homo sapiens	229-232
9759862-6	1998	The C4B12 nucleotide sequence is analogous to C4B1b and C4B3 sequences, except for codon 1076, which is GCC in C4B1b and C4B3 and GGA in C4B12, which is coding for glycine in both cases.	Glycine	164-171	complement C4B (Chido blood group)	Homo sapiens	137-142
9257861-8	1997	Second, all tested GAG were found to reduce deposition of C4 and C3 on immobilized aggregated human IgG (AHG) and to reduce fluid phase formation of C4b/c and C3b/c in recalcified plasma upon incubation with AHG.	Glycosaminoglycans	19-22	complement C4B (Chido blood group)	Homo sapiens	149-152
9634200-7	1998	Additionally, the significant sharing rate of C4B*Q0 in couples with RSA could indicate the existence of a gene in linked to this allele predisposing to RSA and acting in a recessive manner if present in double copies in the fetus.	rabbit sperm membrane autoantigen	69-72	complement C4B (Chido blood group)	Homo sapiens	46-49
8993240-5	1997	Heparin coating, however, reduced maximum values of C3b/c (446 +/- 212 nmol/L versus 632 +/- 264 nmol/L with uncoated ECC; p = 0.0037) and maximum C4b/c values (92 +/- 48 nmol/L versus 172 +/- 148 nmol/L with uncoated ECC; p = 0.0069).	Heparin	0-7	complement C4B (Chido blood group)	Homo sapiens	147-150
9444979-6	1997	Reduction and subsequent alkylation of disulfide bridges of defensins greatly decreased the C1q binding ability but complement activation (C4b binding) remained high.	Disulfides	39-48	complement C4B (Chido blood group)	Homo sapiens	139-142
9041627-5	1997	The binding of the C4B isotype, and most likely C3, to hydroxyl nucleophiles, however, involves a histidine residue, which attacks the thioester to form an intramolecular acyl-imidazole bond.	Histidine	98-107	complement C4B (Chido blood group)	Homo sapiens	19-22
9041627-5	1997	The binding of the C4B isotype, and most likely C3, to hydroxyl nucleophiles, however, involves a histidine residue, which attacks the thioester to form an intramolecular acyl-imidazole bond.	imidazole	176-185	complement C4B (Chido blood group)	Homo sapiens	19-22
8607674-3	1996	RESULTS: Heparin-coated extracorporeal circuits significantly reduced circulating complement activation product C3b/c and soluble C5b-9 concentrations at the end of cardiopulmonary bypass and after protamine sulfate administration compared with the uncoated circuits, but not iC3, C4b/c, or C3a concentrations.	Heparin	9-16	complement C4B (Chido blood group)	Homo sapiens	281-284
8977219-5	1997	This hypothesis was supported by evidence that enzymatic cleavage of the more accessible N-glycan resulted in enhanced Clq, C4b, and C3b deposition.	n-glycan	89-97	complement C4B (Chido blood group)	Homo sapiens	124-127
8977219-6	1997	Conversely, removal of the less accessible N-glycan expressed by the other Ab inhibited C1q, C4b, and C3b deposition.	n-glycan	43-51	complement C4B (Chido blood group)	Homo sapiens	93-96
8977443-10	1996	This mutation occurs within a disulfide loop of protein S that is believed to be responsible for binding to C4b binding protein and may result in greater affinity between protein S and C4b, consequently leading to thrombotic disease.	Disulfides	30-39	complement C4B (Chido blood group)	Homo sapiens	108-111
8851723-6	1996	C4A*12 A*91, C4B*Q0 was frequent in the Xhosa (15%) but rare in the San and Khoi (P < 0.001).	xhosa	40-45	complement C4B (Chido blood group)	Homo sapiens	13-16
8851723-7	1996	Alleles C4A*5 and C4A*6, and the C4B*2 B*92 duplication were only found in the Xhosa.	xhosa	79-84	complement C4B (Chido blood group)	Homo sapiens	33-36
7876551-0	1995	Evidence for the involvement of arginine 462 and the flanking sequence of human C4 beta-chain in mediating C5 binding to the C4b subcomponent of the classical complement pathway C5 convertase.	Arginine	32-40	complement C4B (Chido blood group)	Homo sapiens	125-128
7542207-1	1995	The histidine at position 1106 of the C4B isotype of human complement is involved in catalyzing the covalent binding of the thioester to glycerol and water.	Glycerol	137-145	complement C4B (Chido blood group)	Homo sapiens	38-41
7542207-1	1995	The histidine at position 1106 of the C4B isotype of human complement is involved in catalyzing the covalent binding of the thioester to glycerol and water.	Water	150-155	complement C4B (Chido blood group)	Homo sapiens	38-41
7542207-1	1995	The histidine at position 1106 of the C4B isotype of human complement is involved in catalyzing the covalent binding of the thioester to glycerol and water.	Histidine	4-13	complement C4B (Chido blood group)	Homo sapiens	38-41
7739573-3	1995	In the present study, we demonstrated that in fluid-phase, factor H and Factor I can cleave methylamine-treated C4(C4ma), a C4b analogue, to C4d, regardless of its isotype.	methylamine	92-103	complement C4B (Chido blood group)	Homo sapiens	124-127
8435078-5	1993	Results suggest that a Pro-to-Leu substitution in C4B is likely to account for the differences in inhibitory potency of C4B compared with C4A observed with the aromatic inhibitors.	Proline	23-26	complement C4B (Chido blood group)	Homo sapiens	50-53
8573285-3	1995	The binding of C3b and C4b by E-CR also leads to inhibition of complement activation.	e-cr	30-34	complement C4B (Chido blood group)	Homo sapiens	23-26
7841319-7	1994	On the other hand, in LA patients without a CL antibodies, the fPS deficiency is unrelated to an increase in C4b-BP levels and may be due to abnormal binding of PS to C4b-BP.	Phosphorus	64-66	complement C4B (Chido blood group)	Homo sapiens	167-170
8012361-2	1994	The common arrangement of these genes is tel-C2-Bf-RD-G11-C4A-[P450c21A-YA-XA]-C4B-[P450c21B-YB ]-+ ++TNX-cen.	tnx-cen	102-109	complement C4B (Chido blood group)	Homo sapiens	79-82
8495193-4	1993	C4A binds more efficiently than C4B to amino groups, and C4B is more effective than C4A in binding to hydroxyl groups.	Hydroxyl Radical	102-110	complement C4B (Chido blood group)	Homo sapiens	57-60
8495193-11	1993	We measured the time course of activation and binding of glycine to C4A and C4B.	Glycine	57-64	complement C4B (Chido blood group)	Homo sapiens	76-79
7870055-3	1995	Whereas both C4A and C4B isotypes formed dimers to a similar extent, C4B formed an ester-linked dimer and C4A an amide-linked dimer.	Esters	83-88	complement C4B (Chido blood group)	Homo sapiens	69-72
8133054-6	1994	We report that in a fluid phase system, SAP inhibited degradation of C4(H2O) (which is C4b-like) in a dose-dependent manner.	Water	72-75	complement C4B (Chido blood group)	Homo sapiens	87-90
8435078-5	1993	Results suggest that a Pro-to-Leu substitution in C4B is likely to account for the differences in inhibitory potency of C4B compared with C4A observed with the aromatic inhibitors.	Proline	23-26	complement C4B (Chido blood group)	Homo sapiens	120-123
8435078-5	1993	Results suggest that a Pro-to-Leu substitution in C4B is likely to account for the differences in inhibitory potency of C4B compared with C4A observed with the aromatic inhibitors.	Leucine	30-33	complement C4B (Chido blood group)	Homo sapiens	50-53
8435078-5	1993	Results suggest that a Pro-to-Leu substitution in C4B is likely to account for the differences in inhibitory potency of C4B compared with C4A observed with the aromatic inhibitors.	Leucine	30-33	complement C4B (Chido blood group)	Homo sapiens	120-123
1354409-4	1992	Moreover, patients carrying a duplicated C4B (as well as those having the B14 antigen) showed higher 17-hydroxyprogesterone levels after ACTH stimulation.	17-alpha-Hydroxyprogesterone	101-123	complement C4B (Chido blood group)	Homo sapiens	41-44
8433709-13	1993	The optimal relative NaCl concn for C4b deposition was 0.11 M. While pre-incubation of NIA with C1q blocked the subsequent C1 fixing potential of NIA, pre-incubation of NIA with rgp160 [HIV-1] or fibronectin did not interfere with the potential of NIA to fix C1.	Sodium Chloride	21-25	complement C4B (Chido blood group)	Homo sapiens	36-39
8422437-6	1993	At physiological ionic strength, up to twice as much 125I-sCR1 bound to ammonia-treated C4A as bound to ammonia-treated C4B.	Ammonia	104-111	complement C4B (Chido blood group)	Homo sapiens	120-123
8436550-0	1993	Use of amino acid N-carboxy anhydride in the synthesis of peptide prodrug derivatives (including beta-chloroalanyl) of C4-beta-aminoalkyl carbapenems.	amino acid n-carboxy anhydride	7-37	complement C4B (Chido blood group)	Homo sapiens	119-126
8436550-0	1993	Use of amino acid N-carboxy anhydride in the synthesis of peptide prodrug derivatives (including beta-chloroalanyl) of C4-beta-aminoalkyl carbapenems.	beta-chloroalanyl)	97-115	complement C4B (Chido blood group)	Homo sapiens	119-126
8436550-2	1993	Mono- and dipeptide derivatives of C4-beta-aminoalkyl carbapenems were synthesized by the use of amino acid N-carboxy anhydride for the peptide bond formation.	mono- and dipeptide	0-19	complement C4B (Chido blood group)	Homo sapiens	35-42
8436550-2	1993	Mono- and dipeptide derivatives of C4-beta-aminoalkyl carbapenems were synthesized by the use of amino acid N-carboxy anhydride for the peptide bond formation.	amino acid n-carboxy anhydride	97-127	complement C4B (Chido blood group)	Homo sapiens	35-42
1398744-9	1992	Fluorometric determinations revealed that approximately the same percentage of sialic acid was released from sialidase-treated C4A3 and C4B1.	N-Acetylneuraminic Acid	79-90	complement C4B (Chido blood group)	Homo sapiens	136-140
1569346-2	1992	C4B forms ester bonds more efficiently than C4A and so, in theory, is more likely than C4A to bind to polysaccharide capsules of encapsulated bacteria.	Esters	10-15	complement C4B (Chido blood group)	Homo sapiens	0-3
1569346-2	1992	C4B forms ester bonds more efficiently than C4A and so, in theory, is more likely than C4A to bind to polysaccharide capsules of encapsulated bacteria.	Polysaccharides	102-116	complement C4B (Chido blood group)	Homo sapiens	0-3
1573269-12	1992	These results are consistent with the sole defect in the mutants being at the C5 binding stage and strongly suggest that Arg 458 of the C4 beta-chain contributes to the C5 binding site of the molecule.	Arginine	121-124	complement C4B (Chido blood group)	Homo sapiens	136-143
1770131-8	1991	The majority, 95% (P less than 0.001) of PA couples and 83% of SA couples, had at least one C4A or C4B null in their phenotypes compared to 66% among Finnish controls.	Protactinium	41-43	complement C4B (Chido blood group)	Homo sapiens	99-102
1541053-1	1992	Serum from patients with membranoproliferative glomerulonephritis (MPGN) and acute poststreptococcal glomerulonephritis (APSGN) accelerated the decay of the cell bound C4b2a (C42) and C4b hemolytic activity relative to pooled normal human serum (pNHS) after 5 min incubation at 30 degrees C in EDTA-GVB.	Edetic Acid	294-298	complement C4B (Chido blood group)	Homo sapiens	168-171
1740458-3	1992	Within this complex C3b binds to C4b via an ester linkage.	Esters	44-49	complement C4B (Chido blood group)	Homo sapiens	33-36
1740458-4	1992	We now present evidence that the covalent C3b-binding site on human C4b is Ser at position 1217 of C4.	Serine	75-78	complement C4B (Chido blood group)	Homo sapiens	68-71
1770131-8	1991	The majority, 95% (P less than 0.001) of PA couples and 83% of SA couples, had at least one C4A or C4B null in their phenotypes compared to 66% among Finnish controls.	sa	63-65	complement C4B (Chido blood group)	Homo sapiens	99-102
1919003-1	1991	The C4A and C4B isotypes of human C4 show certain functional differences that stem from their relative preference for transacylation to amino (-NH2) vs hydroxyl (-OH) nucleophiles, respectively, on complement-activating surfaces.	amino (-nh2)	136-148	complement C4B (Chido blood group)	Homo sapiens	12-15
1919003-1	1991	The C4A and C4B isotypes of human C4 show certain functional differences that stem from their relative preference for transacylation to amino (-NH2) vs hydroxyl (-OH) nucleophiles, respectively, on complement-activating surfaces.	hydroxyl (-oh)	152-166	complement C4B (Chido blood group)	Homo sapiens	12-15
1919003-2	1991	Comparison of amino acid sequences of the alpha-chain fragment of C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 are the only consistent structural difference between isotype, i.e., Pro, Cys, Pro, Val, Leu, Asp in C4A and Leu, Ser, Pro, Val Ile, His in C4B.	Proline	208-211	complement C4B (Chido blood group)	Homo sapiens	94-97
1919003-2	1991	Comparison of amino acid sequences of the alpha-chain fragment of C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 are the only consistent structural difference between isotype, i.e., Pro, Cys, Pro, Val, Leu, Asp in C4A and Leu, Ser, Pro, Val Ile, His in C4B.	Cysteine	213-216	complement C4B (Chido blood group)	Homo sapiens	94-97
1919003-2	1991	Comparison of amino acid sequences of the alpha-chain fragment of C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 are the only consistent structural difference between isotype, i.e., Pro, Cys, Pro, Val, Leu, Asp in C4A and Leu, Ser, Pro, Val Ile, His in C4B.	Proline	218-221	complement C4B (Chido blood group)	Homo sapiens	94-97
1919003-2	1991	Comparison of amino acid sequences of the alpha-chain fragment of C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 are the only consistent structural difference between isotype, i.e., Pro, Cys, Pro, Val, Leu, Asp in C4A and Leu, Ser, Pro, Val Ile, His in C4B.	Valine	223-226	complement C4B (Chido blood group)	Homo sapiens	94-97
1919003-2	1991	Comparison of amino acid sequences of the alpha-chain fragment of C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 are the only consistent structural difference between isotype, i.e., Pro, Cys, Pro, Val, Leu, Asp in C4A and Leu, Ser, Pro, Val Ile, His in C4B.	Leucine	228-231	complement C4B (Chido blood group)	Homo sapiens	94-97
1919003-2	1991	Comparison of amino acid sequences of the alpha-chain fragment of C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 are the only consistent structural difference between isotype, i.e., Pro, Cys, Pro, Val, Leu, Asp in C4A and Leu, Ser, Pro, Val Ile, His in C4B.	Aspartic Acid	233-236	complement C4B (Chido blood group)	Homo sapiens	94-97
1919003-2	1991	Comparison of amino acid sequences of the alpha-chain fragment of C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 are the only consistent structural difference between isotype, i.e., Pro, Cys, Pro, Val, Leu, Asp in C4A and Leu, Ser, Pro, Val Ile, His in C4B.	Leucine	248-251	complement C4B (Chido blood group)	Homo sapiens	94-97
1919003-2	1991	Comparison of amino acid sequences of the alpha-chain fragment of C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 are the only consistent structural difference between isotype, i.e., Pro, Cys, Pro, Val, Leu, Asp in C4A and Leu, Ser, Pro, Val Ile, His in C4B.	Serine	253-256	complement C4B (Chido blood group)	Homo sapiens	94-97
1919003-2	1991	Comparison of amino acid sequences of the alpha-chain fragment of C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 are the only consistent structural difference between isotype, i.e., Pro, Cys, Pro, Val, Leu, Asp in C4A and Leu, Ser, Pro, Val Ile, His in C4B.	Proline	218-221	complement C4B (Chido blood group)	Homo sapiens	94-97
1919003-2	1991	Comparison of amino acid sequences of the alpha-chain fragment of C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 are the only consistent structural difference between isotype, i.e., Pro, Cys, Pro, Val, Leu, Asp in C4A and Leu, Ser, Pro, Val Ile, His in C4B.	Valine	263-266	complement C4B (Chido blood group)	Homo sapiens	94-97
1919003-2	1991	Comparison of amino acid sequences of the alpha-chain fragment of C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 are the only consistent structural difference between isotype, i.e., Pro, Cys, Pro, Val, Leu, Asp in C4A and Leu, Ser, Pro, Val Ile, His in C4B.	Isoleucine	267-270	complement C4B (Chido blood group)	Homo sapiens	94-97
1919003-2	1991	Comparison of amino acid sequences of the alpha-chain fragment of C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 are the only consistent structural difference between isotype, i.e., Pro, Cys, Pro, Val, Leu, Asp in C4A and Leu, Ser, Pro, Val Ile, His in C4B.	Histidine	272-275	complement C4B (Chido blood group)	Homo sapiens	94-97
1861081-8	1991	The LAC14 bearing the C4b dimer but not the monomer was lysed, although with relatively low efficiency, by the addition of oxyC2 and EDTA-supplemented C3-deficient serum (C3DS), and, furthermore, LAC142 possessed the ability to convert C5 into C5a and C5b.	Edetic Acid	133-137	complement C4B (Chido blood group)	Homo sapiens	22-25
1861081-8	1991	The LAC14 bearing the C4b dimer but not the monomer was lysed, although with relatively low efficiency, by the addition of oxyC2 and EDTA-supplemented C3-deficient serum (C3DS), and, furthermore, LAC142 possessed the ability to convert C5 into C5a and C5b.	lac142	196-202	complement C4B (Chido blood group)	Homo sapiens	22-25
2049934-1	1991	Comparison of amino acid sequences of the alpha-chain fragment of human C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 in which the aspartic acid-histidine substitution at position 1106 may be related to the amide and ester bond forming properties of these molecules.	Aspartic Acid	158-171	complement C4B (Chido blood group)	Homo sapiens	100-103
1711565-8	1991	The equivalent function of GPI-anchored and TM versions of a protein was not expected based on the hypothesized increased lateral mobility of GPI-anchored proteins, which should confer a functional advantage in contacting ligand, in this case, C3b or C4b, on the cell surface.	Glycosylphosphatidylinositols	27-30	complement C4B (Chido blood group)	Homo sapiens	251-254
1711565-8	1991	The equivalent function of GPI-anchored and TM versions of a protein was not expected based on the hypothesized increased lateral mobility of GPI-anchored proteins, which should confer a functional advantage in contacting ligand, in this case, C3b or C4b, on the cell surface.	Glycosylphosphatidylinositols	142-145	complement C4B (Chido blood group)	Homo sapiens	251-254
1838328-5	1991	Further incubation of BAC1,4b,2a,3b with EDTA-GVB at 37 degrees C gave particles carrying IgG and C4b,C3b (BAC4b,3b).	Edetic Acid	41-45	complement C4B (Chido blood group)	Homo sapiens	98-101
1815762-5	1991	A mixture of four monoclonal antibodies precipitating C4b-BP both in agarose gel and in solution was used to develop a highly reproducible radial immunodiffusion method for the measurement of C4b-BP in human serum.	Sepharose	69-76	complement C4B (Chido blood group)	Homo sapiens	54-57
2049934-1	1991	Comparison of amino acid sequences of the alpha-chain fragment of human C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 in which the aspartic acid-histidine substitution at position 1106 may be related to the amide and ester bond forming properties of these molecules.	Histidine	172-181	complement C4B (Chido blood group)	Homo sapiens	100-103
2049934-1	1991	Comparison of amino acid sequences of the alpha-chain fragment of human C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 in which the aspartic acid-histidine substitution at position 1106 may be related to the amide and ester bond forming properties of these molecules.	Amides	234-239	complement C4B (Chido blood group)	Homo sapiens	100-103
2049934-1	1991	Comparison of amino acid sequences of the alpha-chain fragment of human C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 in which the aspartic acid-histidine substitution at position 1106 may be related to the amide and ester bond forming properties of these molecules.	Esters	244-249	complement C4B (Chido blood group)	Homo sapiens	100-103
2395880-4	1990	The differences in covalent binding properties correlate only with amino acid changes between residues 1101 and 1106 (pro-C4 numbering)--namely, Pro-1101, Cys-1102, Leu-1105, and Asp-1106 in C4A and Leu-1101, Ser-1102, Ile-1105, and His-1106 in C4B, which are located in the C4d region of the alpha chain.	Proline	36-39	complement C4B (Chido blood group)	Homo sapiens	245-248
2148521-2	1990	It was found that nascent C3b attaches with high efficiency to C4b and that C3b in C4bC3b complexes is protected from inactivation by factors H and I. Activation of C3 by factors B and D in the presence of Mg2+ ions and excess C4b led to 35% incorporation of nascent C3b into C4bC3b complexes in the fluid phase.	magnesium ion	206-210	complement C4B (Chido blood group)	Homo sapiens	83-86
2144523-10	1990	In this regard it was important that C4BP which was bound to protein S on the phospholipid surface could interact with complement protein C4b.	Phospholipids	78-90	complement C4B (Chido blood group)	Homo sapiens	138-141
2395880-0	1990	Substitution of a single amino acid (aspartic acid for histidine) converts the functional activity of human complement C4B to C4A.	Aspartic Acid	37-50	complement C4B (Chido blood group)	Homo sapiens	108-122
2395880-0	1990	Substitution of a single amino acid (aspartic acid for histidine) converts the functional activity of human complement C4B to C4A.	Histidine	55-64	complement C4B (Chido blood group)	Homo sapiens	108-122
2147688-15	1990	Finally, the entire complex of proteins (C4BP, SAP, protein S, and C4b) could associate with membranes in the presence of calcium.	Calcium	122-129	complement C4B (Chido blood group)	Homo sapiens	67-70
2244876-9	1990	Purified C3 convertase itself is stable in dilute medium or high-ionic-strength medium such as 500 mM-NaCl, suggesting that the interactions between C4b and C2a are hydrophobic.	Sodium Chloride	102-106	complement C4B (Chido blood group)	Homo sapiens	149-152
2142342-3	1990	Free protein S antigen is measured by the same technique but after precipitation of the protein S-C4b-bp complex by PEG 8000.	polyethylene glycol 8000	116-124	complement C4B (Chido blood group)	Homo sapiens	98-101
2142570-2	1990	Accurate measurement of the hemostatically important free ProS required showing that, on each specimen, precipitation of the C4b-binding protein (C4b-BP)/protein S complex (C4b-BP/ProS) by polyethylene glycol-8,000 (PEG) was complete.	polyethylene glycol-8	189-210	complement C4B (Chido blood group)	Homo sapiens	125-128
2142570-2	1990	Accurate measurement of the hemostatically important free ProS required showing that, on each specimen, precipitation of the C4b-binding protein (C4b-BP)/protein S complex (C4b-BP/ProS) by polyethylene glycol-8,000 (PEG) was complete.	polyethylene glycol-8	189-210	complement C4B (Chido blood group)	Homo sapiens	146-149
2142570-2	1990	Accurate measurement of the hemostatically important free ProS required showing that, on each specimen, precipitation of the C4b-binding protein (C4b-BP)/protein S complex (C4b-BP/ProS) by polyethylene glycol-8,000 (PEG) was complete.	polyethylene glycol-8	189-210	complement C4B (Chido blood group)	Homo sapiens	146-149
2142570-2	1990	Accurate measurement of the hemostatically important free ProS required showing that, on each specimen, precipitation of the C4b-binding protein (C4b-BP)/protein S complex (C4b-BP/ProS) by polyethylene glycol-8,000 (PEG) was complete.	Polyethylene Glycols	216-219	complement C4B (Chido blood group)	Homo sapiens	125-128
2142570-2	1990	Accurate measurement of the hemostatically important free ProS required showing that, on each specimen, precipitation of the C4b-binding protein (C4b-BP)/protein S complex (C4b-BP/ProS) by polyethylene glycol-8,000 (PEG) was complete.	Polyethylene Glycols	216-219	complement C4B (Chido blood group)	Homo sapiens	146-149
2142570-2	1990	Accurate measurement of the hemostatically important free ProS required showing that, on each specimen, precipitation of the C4b-binding protein (C4b-BP)/protein S complex (C4b-BP/ProS) by polyethylene glycol-8,000 (PEG) was complete.	Polyethylene Glycols	216-219	complement C4B (Chido blood group)	Homo sapiens	146-149
2387864-2	1990	In the complex there is an ester bond between C3b and C4b.	Esters	27-32	complement C4B (Chido blood group)	Homo sapiens	54-57
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 C4B (Chido blood group)	Homo sapiens	59-62
1688812-2	1990	C4B* 15 was distinguished by having only faint staining when using polyclonal anti-C4 antibody on agarose immunoelectrophoresis (e.g. hypomorphic), having relatively weak hemolytic activity but being strongly reactive with monoclonal antibody to Rodgers 1.	Sepharose	98-105	complement C4B (Chido blood group)	Homo sapiens	0-3
2139734-7	1990	The presence of ZnCl2 prevented this factor I-mediated degradation of C3b and C4b, as evidenced by the unaffected agglutination of the cells by the antibodies.	zinc chloride	16-21	complement C4B (Chido blood group)	Homo sapiens	78-81
2139734-8	1990	We conclude that ZnCl2 inhibited factor I activity since: (1) release of complement-preopsonized IC from E-CR1 by purified factor I was markedly inhibited (90%) in the presence of ZnCl2, (2) preincubation of the cells with ZnCl2 caused only a moderate inhibition (32-38%) of the IC release, and (3) degradation by purified factor I of covalently cell-bound C3b and C4b was abrogated in the presence of 10 mM ZnCl2.	zinc chloride	17-22	complement C4B (Chido blood group)	Homo sapiens	365-368
2319131-4	1990	SDS-PAGE of C C4 and C4b both under reducing and nonreducing conditions was followed by a radiolabeled C4BP ligand blotting procedure.	Sodium Dodecyl Sulfate	0-3	complement C4B (Chido blood group)	Homo sapiens	21-24
1693017-3	1990	C4B*3 had approximately normal C4B hemolytic activity, a single alpha-chain of MR 94,000 by SDS-PAGE but was positive for Rg:1,2 by hemagglutination inhibition (HAI) and for Rg:1 by Western blotting.	Sodium Dodecyl Sulfate	92-95	complement C4B (Chido blood group)	Homo sapiens	0-3
2136880-3	1990	We now demonstrate that C4BP contains heparin-binding fragments, which are located within the C4b binding domain.	Heparin	38-45	complement C4B (Chido blood group)	Homo sapiens	94-97
2136880-8	1990	In addition, heparin blocked the binding of 125I-C4BP to C4b and vice versa.	Heparin	13-20	complement C4B (Chido blood group)	Homo sapiens	57-60
2136880-9	1990	It is therefore likely that the heparin-binding fragments are localized on or close to the C4b-binding site of C4BP.	Heparin	32-39	complement C4B (Chido blood group)	Homo sapiens	91-94