PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
2775217-7	1989	As purified human plasma carboxypeptidase N and pancreatic carboxypeptidase B were also activated more at pH 5.5, we conclude that the increased activation by CoCl2 is due to the enhanced dissociation of Zn2+ below the pKa of the ligands that co-ordinate the cofactor in the protein.	cobaltous chloride	159-164	carboxypeptidase B1	Homo sapiens	48-77
2584774-5	1989	LPO were significantly decreased since the initiation of CPB (1.669 +/- 0.208 versus pre-CPB 1.785 +/- 0.158 log nmol MDA/gm protein, p less than 0.05) to the post CPB 30 minutes, except around 60 minutes after initiation of CPB (1.735 +/- 0.242 log nmol MDA/gm protein, p greater than 0.05).	Lipid Peroxides	0-3	carboxypeptidase B1	Homo sapiens	89-94
2584774-7	1989	By ordinary analysis of the initial change, as to the effect of type of disease (congenital and acquired), LPO were decreased in the acquired group (1.617 +/- 0.197 versus pre-CPB 1.779 +/- 0.163 log nmol MDA/gm protein, p less than 0.05).	Lipid Peroxides	107-110	carboxypeptidase B1	Homo sapiens	176-181
2526127-5	1989	The augmented fibrin binding of rt-PA is partially abolished when the plasmin-degraded fibrin matrices are subsequently treated with carboxypeptidase B, demonstrating that this increased binding is dependent on the generation of carboxyl-terminal lysine residues in the fibrin matrix.	rt-pa	32-37	carboxypeptidase B1	Homo sapiens	133-151
2526127-5	1989	The augmented fibrin binding of rt-PA is partially abolished when the plasmin-degraded fibrin matrices are subsequently treated with carboxypeptidase B, demonstrating that this increased binding is dependent on the generation of carboxyl-terminal lysine residues in the fibrin matrix.	Lysine	247-253	carboxypeptidase B1	Homo sapiens	133-151
2775217-7	1989	As purified human plasma carboxypeptidase N and pancreatic carboxypeptidase B were also activated more at pH 5.5, we conclude that the increased activation by CoCl2 is due to the enhanced dissociation of Zn2+ below the pKa of the ligands that co-ordinate the cofactor in the protein.	Zinc	204-208	carboxypeptidase B1	Homo sapiens	48-77
2466697-3	1989	C-terminal lysine residues are involved in plasmin binding to cells, since treatment of cells with carboxypeptidase B decreases this binding by 50%.	Lysine	11-17	carboxypeptidase B1	Homo sapiens	99-117
2464136-6	1988	Arginine residue 33, which has been conserved through vertebrate evolution, is a major antigenic contributor, since a large decrease in immunoreactivity, not accompanied by a significant change in conformation, was observed upon specific removal of this residue by carboxypeptidase B.	Arginine	0-8	carboxypeptidase B1	Homo sapiens	265-283
2914904-2	1989	A membrane-bound neutral carboxypeptidase B-like enzyme was solubilized from human placental microvilli with 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS) and purified to homogeneity by ion-exchange chromatography and affinity chromatography on arginine-Sepharose.	AKOS024457464	109-167	carboxypeptidase B1	Homo sapiens	25-43
2914904-2	1989	A membrane-bound neutral carboxypeptidase B-like enzyme was solubilized from human placental microvilli with 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS) and purified to homogeneity by ion-exchange chromatography and affinity chromatography on arginine-Sepharose.	3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate	169-174	carboxypeptidase B1	Homo sapiens	25-43
2914904-2	1989	A membrane-bound neutral carboxypeptidase B-like enzyme was solubilized from human placental microvilli with 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS) and purified to homogeneity by ion-exchange chromatography and affinity chromatography on arginine-Sepharose.	Arginine	266-274	carboxypeptidase B1	Homo sapiens	25-43
2914904-2	1989	A membrane-bound neutral carboxypeptidase B-like enzyme was solubilized from human placental microvilli with 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS) and purified to homogeneity by ion-exchange chromatography and affinity chromatography on arginine-Sepharose.	Sepharose	275-284	carboxypeptidase B1	Homo sapiens	25-43
2662173-3	1989	CPB preparations are loaded onto a column of iminodiacetic acid-Sepharose that has been saturated with ZnCl2.	iminodiacetic acid	45-63	carboxypeptidase B1	Homo sapiens	0-3
2662173-3	1989	CPB preparations are loaded onto a column of iminodiacetic acid-Sepharose that has been saturated with ZnCl2.	Sepharose	64-73	carboxypeptidase B1	Homo sapiens	0-3
2662173-3	1989	CPB preparations are loaded onto a column of iminodiacetic acid-Sepharose that has been saturated with ZnCl2.	zinc chloride	103-108	carboxypeptidase B1	Homo sapiens	0-3
3214176-5	1988	The seminal plasma carboxypeptidase has a neutral pH optimum, is inhibited by o-phenanthroline and by the inhibitor of carboxypeptidase B-type enzymes, 2-mercaptomethyl-3-guanidinoethylthiopropanoic acid, and can be activated by cobalt.	2-mercaptomethyl-3-guanidinoethylthiopropionic acid	152-203	carboxypeptidase B1	Homo sapiens	119-137
3214176-5	1988	The seminal plasma carboxypeptidase has a neutral pH optimum, is inhibited by o-phenanthroline and by the inhibitor of carboxypeptidase B-type enzymes, 2-mercaptomethyl-3-guanidinoethylthiopropanoic acid, and can be activated by cobalt.	Cobalt	229-235	carboxypeptidase B1	Homo sapiens	119-137
2458720-3	1988	A synthetic peptide corresponding to the C-terminal 26 amino acid residues of AP blocked association of AP with plasmin, but this activity of the peptide was lost when its C-terminal lysine residue was removed with carboxypeptidase B.	Lysine	183-189	carboxypeptidase B1	Homo sapiens	215-233
2458720-4	1988	The essential role of this lysine residue was shown more directly by treating AP with carboxypeptidase B and observing that AP lost its ability to inhibit plasmin rapidly.	Lysine	27-33	carboxypeptidase B1	Homo sapiens	86-104
3109877-3	1987	Partial purification of the membrane fractions reveals a Co+2-stimulated carboxypeptidase B activity which is not detectable in crude homogenates.	Cobalt(2+)	57-61	carboxypeptidase B1	Homo sapiens	73-91
2963831-5	1988	Promotion by plasmin was nullified by a subsequent treatment of the clot with carboxypeptidase B, indicating that the plasmin effect was related to the exposure of carboxy terminal lysine residues on fibrin.	Lysine	181-187	carboxypeptidase B1	Homo sapiens	78-96
3667569-2	1987	Carboxypeptidase B was only slightly inhibited by SDS.	Sodium Dodecyl Sulfate	50-53	carboxypeptidase B1	Homo sapiens	0-18
3667569-6	1987	With the addition of SDS, almost only carboxypeptidase B activity was detected.	Sodium Dodecyl Sulfate	21-24	carboxypeptidase B1	Homo sapiens	38-56
3103606-5	1986	We show that digestion of plasma samples with carboxypeptidase B, which removes C-terminal basic amino acids, before electrophoresis, produces a single, sharp, distinct band for each allotype and allows identification of the biochemical basis of the multiple banding pattern previously observed in C4 phenotype determination.	Amino Acids, Basic	91-108	carboxypeptidase B1	Homo sapiens	46-64
3109177-1	1986	Carboxypeptidase B was isolated from porcine pancreas by selective heat treatment of the autolyzed tissue at 60 degrees C and pH 6.0 the presence of phosphate ions.	Phosphates	149-158	carboxypeptidase B1	Homo sapiens	0-18
3156054-1	1985	Experiments involving affinity chromatography on immobilized plasminogen columns and the concomitant use of plasmin and carboxypeptidase B indicate that the COOH-terminal lysine residues formed by plasmin-catalyzed cleavage of fibrinogen are essential for the high-affinity binding of the resulting cleavage products to plasminogen.	Lysine	171-177	carboxypeptidase B1	Homo sapiens	120-138
4005097-3	1985	Blood glucose concentration decreased by 2 mmol litre-1 +/- 0.5 (SEM) (P less than 0.01) immediately on the institution of CPB, and increased during the succeeding minutes.	Blood Glucose	0-13	carboxypeptidase B1	Homo sapiens	123-126
2579381-4	1985	These effects were abolished by cleavage of the COOH-terminal arginine by carboxypeptidase B.	Arginine	62-70	carboxypeptidase B1	Homo sapiens	74-92
2983787-4	1985	Imipramine-like activity of the extract was markedly degraded by carboxypeptidase B and leucine aminopeptidase, but was resistant to neurominidase and phospholipases A2, C, and D. The elution profile of the extract after gel chromatography on Bio-Gel P-2 showed two major peaks of serotonin uptake and imipramine binding inhibition and three additional peaks of serotonin uptake inhibitory activity that did not have a significant effect on imipramine binding.	Imipramine	0-10	carboxypeptidase B1	Homo sapiens	65-83
6335699-5	1984	The C-terminal poly(arg) tail can be readily removed by treatment with carboxypeptidase B.	Arginine	20-23	carboxypeptidase B1	Homo sapiens	71-89
3913581-5	1985	Similar experiments were attempted with high molecular weight epidermal growth factor (HMW-EGF), an analogous growth factor complex that can experience a single modification, the release of arginine by carboxypeptidase B from the carboxy terminus of its biological subunit, low molecular weight EGF (LMW-EGF).	Arginine	190-198	carboxypeptidase B1	Homo sapiens	202-220
6437858-2	1984	The C-terminal amino acid of tissue MM creatine kinase from all 3 species was shown to be lysine, a specific substrate for carboxypeptidase-N and B.	Lysine	90-96	carboxypeptidase B1	Homo sapiens	123-147
6170701-5	1981	Further, removal of the carboxyl terminal arginine by carboxypeptidase B abolished activity on the ileum but not in the skin.	carboxyl terminal arginine	24-50	carboxypeptidase B1	Homo sapiens	54-72
6548739-0	1984	Histargin, a new inhibitor of carboxypeptidase B, produced by actinomycetes.	histargin	0-9	carboxypeptidase B1	Homo sapiens	30-48
6420632-4	1984	The products of carboxypeptidase B-like activity on these substrates, 3H-benzoyl-Phe-Ala or 3H-benzoyl Phe-Leu partition quantitatively into chloroform, allowing rapid separation of product from substrate.	3h-benzoyl-phe-ala	70-88	carboxypeptidase B1	Homo sapiens	16-34
6420632-4	1984	The products of carboxypeptidase B-like activity on these substrates, 3H-benzoyl-Phe-Ala or 3H-benzoyl Phe-Leu partition quantitatively into chloroform, allowing rapid separation of product from substrate.	3h-benzoyl phe-leu	92-110	carboxypeptidase B1	Homo sapiens	16-34
6420632-4	1984	The products of carboxypeptidase B-like activity on these substrates, 3H-benzoyl-Phe-Ala or 3H-benzoyl Phe-Leu partition quantitatively into chloroform, allowing rapid separation of product from substrate.	Chloroform	141-151	carboxypeptidase B1	Homo sapiens	16-34
7118416-0	1982	Mechanistic implications of cyanide binding to carboxypeptidase B.	Cyanides	28-35	carboxypeptidase B1	Homo sapiens	47-65
7118416-2	1982	The absorption spectra of Co2+-carboxypeptidase B in the presence of cyanide pointed to a direct interaction of the ligands with the metal.	Cyanides	69-76	carboxypeptidase B1	Homo sapiens	31-49
7118416-2	1982	The absorption spectra of Co2+-carboxypeptidase B in the presence of cyanide pointed to a direct interaction of the ligands with the metal.	Metals	133-138	carboxypeptidase B1	Homo sapiens	31-49
7118416-7	1982	The dissociation constant evaluated from kinetic studies for the binding of cyanide to Co2+-carboxypeptidase B was in good agreement with that obtained from spectral measurements.	Cyanides	76-83	carboxypeptidase B1	Homo sapiens	92-110
7118417-0	1982	Tyrosyl interactions at the active site of carboxypeptidase B.	cyclo(tyrosyl-tyrosyl)	0-7	carboxypeptidase B1	Homo sapiens	43-61
7118417-1	1982	The phosphorescence emission spectra of native carboxypeptidase B and of chemically modified carboxypeptidase B (at arginyl residues) was measured in the presence and absence of peptide and ester substrates (acetyl-L-arginine and its hydroxy ester analog: acetyl-L-argininic acid).	arginyl	116-123	carboxypeptidase B1	Homo sapiens	93-111
7118417-1	1982	The phosphorescence emission spectra of native carboxypeptidase B and of chemically modified carboxypeptidase B (at arginyl residues) was measured in the presence and absence of peptide and ester substrates (acetyl-L-arginine and its hydroxy ester analog: acetyl-L-argininic acid).	acetyl-l-arginine	208-225	carboxypeptidase B1	Homo sapiens	93-111
7118417-1	1982	The phosphorescence emission spectra of native carboxypeptidase B and of chemically modified carboxypeptidase B (at arginyl residues) was measured in the presence and absence of peptide and ester substrates (acetyl-L-arginine and its hydroxy ester analog: acetyl-L-argininic acid).	hydroxy ester	234-247	carboxypeptidase B1	Homo sapiens	93-111
7118417-1	1982	The phosphorescence emission spectra of native carboxypeptidase B and of chemically modified carboxypeptidase B (at arginyl residues) was measured in the presence and absence of peptide and ester substrates (acetyl-L-arginine and its hydroxy ester analog: acetyl-L-argininic acid).	acetyl-l-argininic acid	256-279	carboxypeptidase B1	Homo sapiens	93-111
7118417-4	1982	The luminescence spectra of Zn2+- and Co2+-carboxypeptidase B in the presence of the metal coordinating ligand cyanide, used to displace the water from the metal coordination sphere, is also described.	Metals	85-90	carboxypeptidase B1	Homo sapiens	43-61
7118417-4	1982	The luminescence spectra of Zn2+- and Co2+-carboxypeptidase B in the presence of the metal coordinating ligand cyanide, used to displace the water from the metal coordination sphere, is also described.	Cyanides	111-118	carboxypeptidase B1	Homo sapiens	43-61
7118417-4	1982	The luminescence spectra of Zn2+- and Co2+-carboxypeptidase B in the presence of the metal coordinating ligand cyanide, used to displace the water from the metal coordination sphere, is also described.	Water	141-146	carboxypeptidase B1	Homo sapiens	43-61
7118417-4	1982	The luminescence spectra of Zn2+- and Co2+-carboxypeptidase B in the presence of the metal coordinating ligand cyanide, used to displace the water from the metal coordination sphere, is also described.	Metals	156-161	carboxypeptidase B1	Homo sapiens	43-61
6875538-1	1983	Native carboxypeptidase B and its Co2+-substituted derivative were oxidized by the active-site-directed agent m-chloroperbenzoic acid.	Cobalt(2+)	34-38	carboxypeptidase B1	Homo sapiens	7-25
6875538-1	1983	Native carboxypeptidase B and its Co2+-substituted derivative were oxidized by the active-site-directed agent m-chloroperbenzoic acid.	3-chloroperbenzoic acid	110-133	carboxypeptidase B1	Homo sapiens	7-25
6404277-1	1983	Biproduct analogs of lysine and arginine are potent inhibitors of enkephalin convertase, a carboxypeptidase B-like enzyme which appears to be physiologically associated with enkephalin biosynthesis.	Lysine	21-27	carboxypeptidase B1	Homo sapiens	91-109
6404277-1	1983	Biproduct analogs of lysine and arginine are potent inhibitors of enkephalin convertase, a carboxypeptidase B-like enzyme which appears to be physiologically associated with enkephalin biosynthesis.	Arginine	32-40	carboxypeptidase B1	Homo sapiens	91-109
6404277-3	1983	These dicarboxylic acid analogs of arginine are several hundred fold more potent towards enkephalin convertase than towards carboxypeptidase B or N. Kinetic analysis indicates the pure competitive nature of the inhibition.	Dicarboxylic Acids	6-23	carboxypeptidase B1	Homo sapiens	124-142
6404277-3	1983	These dicarboxylic acid analogs of arginine are several hundred fold more potent towards enkephalin convertase than towards carboxypeptidase B or N. Kinetic analysis indicates the pure competitive nature of the inhibition.	Arginine	35-43	carboxypeptidase B1	Homo sapiens	124-142
6404277-4	1983	Bromoacetyl-D-arginine, an irreversible inhibitor of carboxypeptidase B and N, is also an efficient irreversible inhibitor of enkephalin convertase.	bromoacetylarginine	0-22	carboxypeptidase B1	Homo sapiens	53-71
6985269-7	1982	Release of carboxyl-terminal arginine residue by carboxypeptidase B, converting C3a into des-Arg77-C3a, did not alter the inhibitory effect displayed by this fragment.	Arginine	29-37	carboxypeptidase B1	Homo sapiens	49-67
7410373-2	1980	Des-arg iron-cobalt hybrid hemoglobins, des-arg alpha(Co)2 beta (Fe)2, and des-arg alpha (Fe)2 beta (Co)2, in which the alpha-141 arginine residues are digested by carboxypeptidase B, were prepared, and their functional and EPR spectral properties were examined.	des-arg	0-7	carboxypeptidase B1	Homo sapiens	164-182
7287747-3	1981	The charge heterogeneity of the various species arises from the removal, by a carboxypeptidase B-like enzyme in the submaxillary gland, of this lysine residue and/or the original COOH-terminal arginine residue of the shorter Mr = 10,000 chain.	Lysine	144-150	carboxypeptidase B1	Homo sapiens	78-96
7410435-6	1980	similar changes are found in carboxypeptidase B-digested hemoglobin Ao where the COOH-terminal arginine is removed by enzymatic digestion.	Carbonic Acid	81-85	carboxypeptidase B1	Homo sapiens	29-47
7410435-6	1980	similar changes are found in carboxypeptidase B-digested hemoglobin Ao where the COOH-terminal arginine is removed by enzymatic digestion.	Arginine	95-103	carboxypeptidase B1	Homo sapiens	29-47
6448971-3	1980	Comparative experiences with the same substrate revealed that carboxypeptidase B liberated exclusively the C-terminal arginine, plasmin exclusively peptides of arginine, and trypsin, besides arginine peptides, minutes quantities of free arginine.	Arginine	118-126	carboxypeptidase B1	Homo sapiens	62-80
6448971-3	1980	Comparative experiences with the same substrate revealed that carboxypeptidase B liberated exclusively the C-terminal arginine, plasmin exclusively peptides of arginine, and trypsin, besides arginine peptides, minutes quantities of free arginine.	Arginine	160-168	carboxypeptidase B1	Homo sapiens	62-80
6448971-3	1980	Comparative experiences with the same substrate revealed that carboxypeptidase B liberated exclusively the C-terminal arginine, plasmin exclusively peptides of arginine, and trypsin, besides arginine peptides, minutes quantities of free arginine.	Arginine	160-168	carboxypeptidase B1	Homo sapiens	62-80
6448971-6	1980	3 - We could thus demonstrate that the protaminase activity of human plasma and serum in greatly enhanced by cobalt and is inhibited by cadmium and EDTA.	Cobalt	109-115	carboxypeptidase B1	Homo sapiens	39-50
6448971-6	1980	3 - We could thus demonstrate that the protaminase activity of human plasma and serum in greatly enhanced by cobalt and is inhibited by cadmium and EDTA.	Cadmium	136-143	carboxypeptidase B1	Homo sapiens	39-50
6448971-6	1980	3 - We could thus demonstrate that the protaminase activity of human plasma and serum in greatly enhanced by cobalt and is inhibited by cadmium and EDTA.	Edetic Acid	148-152	carboxypeptidase B1	Homo sapiens	39-50
6100945-1	1980	Evidence is presented to suggest that kininase activity of Bothrops jararaca plasma is due to the presence of at least three distinct enzymes: a carboxypeptidase B type enzyme, similar to that found in human plasma in that its activity is enhanced by Co2+ (1 X 10(-4) M); a carboxypeptidase B type enzyme whose activity is unaffected by Co2+, and an enzyme which cleaves bradykinin to liberate Phe-Arg as the major peptide fragment formed.	Cobalt(2+)	251-255	carboxypeptidase B1	Homo sapiens	145-163
738992-5	1978	These Sephadex derivatives contained more than 0.5 mmol of each amino acid per g dry beads and were found to be effective and specific adsorbents for carboxypeptidase B.	sephadex	6-14	carboxypeptidase B1	Homo sapiens	150-168
427123-3	1979	2-Mercaptomethyl-5-guanidinopentanoic acid (SQ 24,798) has a Ki of 4 x 10(-10) M vs. carboxypeptidase B and a Ki of 1.2 x 10(-5) M vs. carboxypeptidase A.	2-mercaptomethyl-5-guanidinopentanoic acid	0-42	carboxypeptidase B1	Homo sapiens	85-103
486428-1	1979	Carboxypeptidases A and B have been isolated individually from aqueous extracts of mammalian pancreatic acetone powders by affinity chromatography on [N-(epsilon-aminocaproyl)-p-aminobenzyl]succinyl-Sepharose 4B (CABS-Sepharose).	Acetone	104-111	carboxypeptidase B1	Homo sapiens	0-25
486428-1	1979	Carboxypeptidases A and B have been isolated individually from aqueous extracts of mammalian pancreatic acetone powders by affinity chromatography on [N-(epsilon-aminocaproyl)-p-aminobenzyl]succinyl-Sepharose 4B (CABS-Sepharose).	[n-(epsilon-aminocaproyl)-p-aminobenzyl]succinyl-sepharose 4b	150-211	carboxypeptidase B1	Homo sapiens	0-25
486428-1	1979	Carboxypeptidases A and B have been isolated individually from aqueous extracts of mammalian pancreatic acetone powders by affinity chromatography on [N-(epsilon-aminocaproyl)-p-aminobenzyl]succinyl-Sepharose 4B (CABS-Sepharose).	SCAB protocol	213-217	carboxypeptidase B1	Homo sapiens	0-25
486428-1	1979	Carboxypeptidases A and B have been isolated individually from aqueous extracts of mammalian pancreatic acetone powders by affinity chromatography on [N-(epsilon-aminocaproyl)-p-aminobenzyl]succinyl-Sepharose 4B (CABS-Sepharose).	Sepharose	199-208	carboxypeptidase B1	Homo sapiens	0-25
486428-5	1979	The ease of synthesis of the ligand from its commercially available precursor, its stability, and the mild elution conditions render CABS-Sepharose an excellent affinity support for the single-column isolation of both carboxypeptidases A and B.	SCAB protocol	133-137	carboxypeptidase B1	Homo sapiens	218-243
486428-5	1979	The ease of synthesis of the ligand from its commercially available precursor, its stability, and the mild elution conditions render CABS-Sepharose an excellent affinity support for the single-column isolation of both carboxypeptidases A and B.	Sepharose	138-147	carboxypeptidase B1	Homo sapiens	218-243
291947-4	1979	Carboxypeptidase B released approximately 1 mol of arginine per mol of C4a.	Arginine Vasopressin	51-59	carboxypeptidase B1	Homo sapiens	0-18
568547-0	1978	The reactivity of a functional tyrosyl residue in carboxypeptidase B.	cyclo(tyrosyl-tyrosyl)	31-38	carboxypeptidase B1	Homo sapiens	50-68
568547-2	1978	Cadmium-carboxypeptidase B was nitrated with tetranitromethane.	Tetranitromethane	45-62	carboxypeptidase B1	Homo sapiens	8-26
568547-8	1978	This indicates that the state of Tyr-248 in Cd-carboxypeptidase B differs from that in zinc-carboxypeptidase B where it shows chemical hyperreactivity due to its proximity to the metal ion.	Tyrosine	33-36	carboxypeptidase B1	Homo sapiens	47-65
568547-8	1978	This indicates that the state of Tyr-248 in Cd-carboxypeptidase B differs from that in zinc-carboxypeptidase B where it shows chemical hyperreactivity due to its proximity to the metal ion.	Tyrosine	33-36	carboxypeptidase B1	Homo sapiens	92-110
568547-8	1978	This indicates that the state of Tyr-248 in Cd-carboxypeptidase B differs from that in zinc-carboxypeptidase B where it shows chemical hyperreactivity due to its proximity to the metal ion.	Metals	179-184	carboxypeptidase B1	Homo sapiens	47-65
568547-8	1978	This indicates that the state of Tyr-248 in Cd-carboxypeptidase B differs from that in zinc-carboxypeptidase B where it shows chemical hyperreactivity due to its proximity to the metal ion.	Metals	179-184	carboxypeptidase B1	Homo sapiens	92-110
656101-0	1978	Structural changes in metalloenzyme in the course of metal substitution: carboxypeptidase B.	Metals	22-27	carboxypeptidase B1	Homo sapiens	73-91
666896-7	1978	One mole of arginine or phenylalanine was released per mole of ligandin after digestion with carboxypeptidase B or A, respectively.	Arginine	12-20	carboxypeptidase B1	Homo sapiens	93-111
666896-7	1978	One mole of arginine or phenylalanine was released per mole of ligandin after digestion with carboxypeptidase B or A, respectively.	Phenylalanine	24-37	carboxypeptidase B1	Homo sapiens	93-111
667683-0	1978	Effect of the basic amino-acid side chain length and the penultimate residue on the hydrolysis of benzoldipeptides by carboxypeptidase B.	Amino Acids, Basic	14-30	carboxypeptidase B1	Homo sapiens	118-136
667683-0	1978	Effect of the basic amino-acid side chain length and the penultimate residue on the hydrolysis of benzoldipeptides by carboxypeptidase B.	benzoldipeptides	98-114	carboxypeptidase B1	Homo sapiens	118-136
667683-1	1978	The kinetic parameters Km and k cat/K m have been determined for the carboxypeptidase B (CPB, EC 3.4.12.3) catalyzed hydrolysis of benzoylglycyl-DL-homolysine and benzoylglycyl-L-homorginine.	benzoylglycyl-dl-homolysine	131-158	carboxypeptidase B1	Homo sapiens	69-87
667683-1	1978	The kinetic parameters Km and k cat/K m have been determined for the carboxypeptidase B (CPB, EC 3.4.12.3) catalyzed hydrolysis of benzoylglycyl-DL-homolysine and benzoylglycyl-L-homorginine.	benzoylglycyl-dl-homolysine	131-158	carboxypeptidase B1	Homo sapiens	89-92
667683-1	1978	The kinetic parameters Km and k cat/K m have been determined for the carboxypeptidase B (CPB, EC 3.4.12.3) catalyzed hydrolysis of benzoylglycyl-DL-homolysine and benzoylglycyl-L-homorginine.	benzoylglycyl-l-homorginine	163-190	carboxypeptidase B1	Homo sapiens	69-87
667683-1	1978	The kinetic parameters Km and k cat/K m have been determined for the carboxypeptidase B (CPB, EC 3.4.12.3) catalyzed hydrolysis of benzoylglycyl-DL-homolysine and benzoylglycyl-L-homorginine.	benzoylglycyl-l-homorginine	163-190	carboxypeptidase B1	Homo sapiens	89-92
667683-7	1978	48, 1122-1131) CPB has a higher bending affinity for a guanidino group than for an amino group at the side chain of the substrate C-terminus.	guanidino	55-64	carboxypeptidase B1	Homo sapiens	15-18
667683-8	1978	On the other hand, CPB is similar to trypsin (ibid) in that the best substrate would have a side chain length between those of lysine and arginine.	ibid	46-50	carboxypeptidase B1	Homo sapiens	19-22
667683-8	1978	On the other hand, CPB is similar to trypsin (ibid) in that the best substrate would have a side chain length between those of lysine and arginine.	Lysine	127-133	carboxypeptidase B1	Homo sapiens	19-22
667683-8	1978	On the other hand, CPB is similar to trypsin (ibid) in that the best substrate would have a side chain length between those of lysine and arginine.	Arginine	138-146	carboxypeptidase B1	Homo sapiens	19-22
667683-9	1978	Studies with Bz-MeGly-Lys and Bz-Ala-Lys showed that the former is very slowly hydrolyzed by CPB but that the latter is a good substrate with a high affinity for the enzyme, indicative of considerable participation of the Calpha-methyl group of alanine in the binding of the substrate to the enzyme.	bz-megly-lys	13-25	carboxypeptidase B1	Homo sapiens	93-96
667683-9	1978	Studies with Bz-MeGly-Lys and Bz-Ala-Lys showed that the former is very slowly hydrolyzed by CPB but that the latter is a good substrate with a high affinity for the enzyme, indicative of considerable participation of the Calpha-methyl group of alanine in the binding of the substrate to the enzyme.	Alanine	245-252	carboxypeptidase B1	Homo sapiens	93-96
1009123-6	1976	In addition, the three forms of human carboxypeptidase B differ in electrophoretic mobility in polyacrylamide gel electrophoresis and in chromatographic behavior on DEAE-cellulose.	polyacrylamide	95-109	carboxypeptidase B1	Homo sapiens	38-56
268623-2	1977	The resulting benzyloxycarbonyl derivatives of isoglutaminylarginine methyl ester and isoasparaginylarginine methyl ester were treated with trypsin for removal of the ester groups and then with porcine pancreatic carboxypeptidase B for liberation of arginine and the original benzyloxycarbonyl derivatives of isoglutamine and isoasparagine.	isoglutaminylarginine methyl ester	47-81	carboxypeptidase B1	Homo sapiens	202-231
268623-2	1977	The resulting benzyloxycarbonyl derivatives of isoglutaminylarginine methyl ester and isoasparaginylarginine methyl ester were treated with trypsin for removal of the ester groups and then with porcine pancreatic carboxypeptidase B for liberation of arginine and the original benzyloxycarbonyl derivatives of isoglutamine and isoasparagine.	isoasparaginylarginine methyl ester	86-121	carboxypeptidase B1	Homo sapiens	202-231
17398-1	1977	Carboxypeptidase B of the human pancreas was purified by chromatography on DEAE-cellulose and CM-cellulose columns.	DEAE-Cellulose	75-89	carboxypeptidase B1	Homo sapiens	0-18
17398-1	1977	Carboxypeptidase B of the human pancreas was purified by chromatography on DEAE-cellulose and CM-cellulose columns.	7,8-diacetoxy-3-(4-nitrophenyl)coumarin	94-106	carboxypeptidase B1	Homo sapiens	0-18
17398-8	1977	The N-terminal amino acid in carboxypeptidase B1 and B2 is alanine.	Alanine	59-66	carboxypeptidase B1	Homo sapiens	29-48
266705-4	1977	Like natural C3a, the synthetic C3a=(70-77) was inactivated by digestion with carboxypeptidase B [peptidyl-L-lysine(-L-arginine) hydrolase, EC 3.4.12.3], which removed the essential COOH-terminal arginine.	Carbonic Acid	182-186	carboxypeptidase B1	Homo sapiens	78-96
266705-4	1977	Like natural C3a, the synthetic C3a=(70-77) was inactivated by digestion with carboxypeptidase B [peptidyl-L-lysine(-L-arginine) hydrolase, EC 3.4.12.3], which removed the essential COOH-terminal arginine.	Arginine	119-127	carboxypeptidase B1	Homo sapiens	78-96
303770-6	1977	When the new carboxy-terminal lysine was cleaved with carboxypeptidase B, singly labeled, doubly labeled, and unlabeled lysine were recovered.	carboxy phosphate	13-20	carboxypeptidase B1	Homo sapiens	54-72
303770-6	1977	When the new carboxy-terminal lysine was cleaved with carboxypeptidase B, singly labeled, doubly labeled, and unlabeled lysine were recovered.	tyrosyl-lysine	30-36	carboxypeptidase B1	Homo sapiens	54-72
898234-4	1977	It was shown that the CPB method has considerably greater precision than the RIA method and could be employed in bioavailability and pharmacokinetic studies of both prednisolone and prednisone.	Prednisolone	165-177	carboxypeptidase B1	Homo sapiens	22-25
898234-4	1977	It was shown that the CPB method has considerably greater precision than the RIA method and could be employed in bioavailability and pharmacokinetic studies of both prednisolone and prednisone.	Prednisone	182-192	carboxypeptidase B1	Homo sapiens	22-25
1002704-7	1976	Thus, specific removal with carboxypeptidase B of Arg-141 (alpha), which is close to Val-1 (alpha) in deoxyhemoglobin, abolishes the enhancement in carbamylation.	Arginine	50-53	carboxypeptidase B1	Homo sapiens	28-46
1002704-7	1976	Thus, specific removal with carboxypeptidase B of Arg-141 (alpha), which is close to Val-1 (alpha) in deoxyhemoglobin, abolishes the enhancement in carbamylation.	Valine	85-88	carboxypeptidase B1	Homo sapiens	28-46
1009123-6	1976	In addition, the three forms of human carboxypeptidase B differ in electrophoretic mobility in polyacrylamide gel electrophoresis and in chromatographic behavior on DEAE-cellulose.	DEAE-Cellulose	165-179	carboxypeptidase B1	Homo sapiens	38-56
180518-3	1976	The tumours under study also differed by the capacity to catalyze the splitting of hippuryl-L-arginine, synthetic substrate of carboxypeptidase B.	hippuryl-L-arginine	83-102	carboxypeptidase B1	Homo sapiens	127-145
974098-5	1976	Carboxypeptidase B cleaved a C-terminal lysine from the different enzyme forms and shifted the isoelectric point of the different enzyme active bands towards the acid pH.	Lysine	40-46	carboxypeptidase B1	Homo sapiens	0-18
1214279-6	1975	On the other hand, carboxypeptidases A and B, both at 1mg/ml, suppressed the sodium and potassium conductance increases with little or no change in sodium inactivation.	Sodium	77-83	carboxypeptidase B1	Homo sapiens	19-44
1214279-6	1975	On the other hand, carboxypeptidases A and B, both at 1mg/ml, suppressed the sodium and potassium conductance increases with little or no change in sodium inactivation.	Potassium	88-97	carboxypeptidase B1	Homo sapiens	19-44
1238154-0	1975	Effect of Nepsilon-alkylation of the substrate on the hydrolysis of benzoylglycyl-L-lysine by carboxypeptidase B1.	benzoylglycyl-l-lysine	68-90	carboxypeptidase B1	Homo sapiens	94-113
1238154-1	1975	The action of carboxypeptidase B (EC 3.4.12.3) on the benzoylglycyl dipeptides Bz-Gly-Lys(X) where X = methyl, ethyl, propyl, formyl, dimethyl, isopropyl, trimethyl, and benzyl has been investigated.	benzoylglycyl dipeptides	54-78	carboxypeptidase B1	Homo sapiens	14-32
1238154-1	1975	The action of carboxypeptidase B (EC 3.4.12.3) on the benzoylglycyl dipeptides Bz-Gly-Lys(X) where X = methyl, ethyl, propyl, formyl, dimethyl, isopropyl, trimethyl, and benzyl has been investigated.	bz-gly-lys	79-89	carboxypeptidase B1	Homo sapiens	14-32
1205730-0	1975	Proceedings: Carboxypeptidase B: modification of functional arginyl residues.	arginyl	60-67	carboxypeptidase B1	Homo sapiens	13-31
1170927-1	1975	The initial rates of hydrolysis of Bz-Gly-Lys and Bz-Gly-Phe by carboxypeptidase B (CPB) are increased in the presence of the modifiers beta-phenylpropionic acid, cyclohexanol, Bz-Gly, and Bz-Gly-Gly.	bz-gly-lys	35-45	carboxypeptidase B1	Homo sapiens	64-82
1170927-1	1975	The initial rates of hydrolysis of Bz-Gly-Lys and Bz-Gly-Phe by carboxypeptidase B (CPB) are increased in the presence of the modifiers beta-phenylpropionic acid, cyclohexanol, Bz-Gly, and Bz-Gly-Gly.	bz-gly-lys	35-45	carboxypeptidase B1	Homo sapiens	84-87
1170927-1	1975	The initial rates of hydrolysis of Bz-Gly-Lys and Bz-Gly-Phe by carboxypeptidase B (CPB) are increased in the presence of the modifiers beta-phenylpropionic acid, cyclohexanol, Bz-Gly, and Bz-Gly-Gly.	N-(hippuryl)phenylalanine	50-60	carboxypeptidase B1	Homo sapiens	64-82
1170927-7	1975	Moreover, when Bz-Gly-Lys is the substrate, cyclohexanol activates its hydrolysis by CPB by increasing both the enzyme-substrate binding affinity and the rate of the catalytic step, an effect different from that observed when Bz-Gly is the modifier.	bz-gly	15-21	carboxypeptidase B1	Homo sapiens	85-88
236-1	1975	35Cl minus-nuclear magnetic resonance (NMR) studies indicate that various digests of human hemoglobin with carboxypeptidase A and B, or a combination of the two, may be used for the identification of chloride binding sites.	35cl	0-4	carboxypeptidase B1	Homo sapiens	107-131
236-1	1975	35Cl minus-nuclear magnetic resonance (NMR) studies indicate that various digests of human hemoglobin with carboxypeptidase A and B, or a combination of the two, may be used for the identification of chloride binding sites.	Chlorides	200-208	carboxypeptidase B1	Homo sapiens	107-131
1170927-1	1975	The initial rates of hydrolysis of Bz-Gly-Lys and Bz-Gly-Phe by carboxypeptidase B (CPB) are increased in the presence of the modifiers beta-phenylpropionic acid, cyclohexanol, Bz-Gly, and Bz-Gly-Gly.	N-(hippuryl)phenylalanine	50-60	carboxypeptidase B1	Homo sapiens	84-87
1170927-1	1975	The initial rates of hydrolysis of Bz-Gly-Lys and Bz-Gly-Phe by carboxypeptidase B (CPB) are increased in the presence of the modifiers beta-phenylpropionic acid, cyclohexanol, Bz-Gly, and Bz-Gly-Gly.	3-phenylpropionic acid	136-161	carboxypeptidase B1	Homo sapiens	64-82
236-4	1975	The high-affinity sites show, in the case of the simple digests, a strong oxygen linkage which is lost in the forms digested with both carboxypeptidase A and B; this linkage may thus be correlated to the presence of conformational changes.	Oxygen	74-80	carboxypeptidase B1	Homo sapiens	135-159
1170927-1	1975	The initial rates of hydrolysis of Bz-Gly-Lys and Bz-Gly-Phe by carboxypeptidase B (CPB) are increased in the presence of the modifiers beta-phenylpropionic acid, cyclohexanol, Bz-Gly, and Bz-Gly-Gly.	3-phenylpropionic acid	136-161	carboxypeptidase B1	Homo sapiens	84-87
1170927-1	1975	The initial rates of hydrolysis of Bz-Gly-Lys and Bz-Gly-Phe by carboxypeptidase B (CPB) are increased in the presence of the modifiers beta-phenylpropionic acid, cyclohexanol, Bz-Gly, and Bz-Gly-Gly.	Cyclohexanols	163-175	carboxypeptidase B1	Homo sapiens	64-82
1170927-1	1975	The initial rates of hydrolysis of Bz-Gly-Lys and Bz-Gly-Phe by carboxypeptidase B (CPB) are increased in the presence of the modifiers beta-phenylpropionic acid, cyclohexanol, Bz-Gly, and Bz-Gly-Gly.	Cyclohexanols	163-175	carboxypeptidase B1	Homo sapiens	84-87
1170927-1	1975	The initial rates of hydrolysis of Bz-Gly-Lys and Bz-Gly-Phe by carboxypeptidase B (CPB) are increased in the presence of the modifiers beta-phenylpropionic acid, cyclohexanol, Bz-Gly, and Bz-Gly-Gly.	bz-gly	35-41	carboxypeptidase B1	Homo sapiens	64-82
1170927-1	1975	The initial rates of hydrolysis of Bz-Gly-Lys and Bz-Gly-Phe by carboxypeptidase B (CPB) are increased in the presence of the modifiers beta-phenylpropionic acid, cyclohexanol, Bz-Gly, and Bz-Gly-Gly.	bz-gly	35-41	carboxypeptidase B1	Homo sapiens	84-87
1170927-1	1975	The initial rates of hydrolysis of Bz-Gly-Lys and Bz-Gly-Phe by carboxypeptidase B (CPB) are increased in the presence of the modifiers beta-phenylpropionic acid, cyclohexanol, Bz-Gly, and Bz-Gly-Gly.	bz-gly-gly	189-199	carboxypeptidase B1	Homo sapiens	64-82
1170927-1	1975	The initial rates of hydrolysis of Bz-Gly-Lys and Bz-Gly-Phe by carboxypeptidase B (CPB) are increased in the presence of the modifiers beta-phenylpropionic acid, cyclohexanol, Bz-Gly, and Bz-Gly-Gly.	bz-gly-gly	189-199	carboxypeptidase B1	Homo sapiens	84-87
1170927-2	1975	The hydrolysis of the tripeptide Bz-Gly-Gly-Phe is also activated by Bz-Gly and Bz-Gly-Gly, but none of these modifiers activate the hydrolysis of Bz-Gly-Gly-Lys, Z-Leu-Ala-Phe, or Bz-Gly-phenyllactic acid by CPB.	tripeptide K-26	22-32	carboxypeptidase B1	Homo sapiens	209-212
807247-5	1975	Human carboxypeptidase B fraction II appeared homogeneous in analytical polyacrylamide disc-gel electrophoresis, but showed two components of 23,500 and 9,200 daltons in sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	polyacrylamide	72-86	carboxypeptidase B1	Homo sapiens	6-24
807247-5	1975	Human carboxypeptidase B fraction II appeared homogeneous in analytical polyacrylamide disc-gel electrophoresis, but showed two components of 23,500 and 9,200 daltons in sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	Sodium Dodecyl Sulfate	170-192	carboxypeptidase B1	Homo sapiens	6-24
807247-5	1975	Human carboxypeptidase B fraction II appeared homogeneous in analytical polyacrylamide disc-gel electrophoresis, but showed two components of 23,500 and 9,200 daltons in sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	polyacrylamide	193-207	carboxypeptidase B1	Homo sapiens	6-24
1170927-2	1975	The hydrolysis of the tripeptide Bz-Gly-Gly-Phe is also activated by Bz-Gly and Bz-Gly-Gly, but none of these modifiers activate the hydrolysis of Bz-Gly-Gly-Lys, Z-Leu-Ala-Phe, or Bz-Gly-phenyllactic acid by CPB.	bz-gly-gly-phe	33-47	carboxypeptidase B1	Homo sapiens	209-212
1170927-2	1975	The hydrolysis of the tripeptide Bz-Gly-Gly-Phe is also activated by Bz-Gly and Bz-Gly-Gly, but none of these modifiers activate the hydrolysis of Bz-Gly-Gly-Lys, Z-Leu-Ala-Phe, or Bz-Gly-phenyllactic acid by CPB.	bz-gly	33-39	carboxypeptidase B1	Homo sapiens	209-212
1170927-2	1975	The hydrolysis of the tripeptide Bz-Gly-Gly-Phe is also activated by Bz-Gly and Bz-Gly-Gly, but none of these modifiers activate the hydrolysis of Bz-Gly-Gly-Lys, Z-Leu-Ala-Phe, or Bz-Gly-phenyllactic acid by CPB.	bz-gly-gly	33-43	carboxypeptidase B1	Homo sapiens	209-212
1170927-4	1975	Examination of Lineweaver-Burk plots in the presence of fixed concentrations of Bz-Gly has shown that activation of the hydrolysis of neutral and basic peptides by CPB, as reflected in the values of the extrapolated parameters, Km(app) and kcat, occurs by different mechanisms.	bz-gly	80-86	carboxypeptidase B1	Homo sapiens	164-167
1170927-6	1975	Cyclohexanol differs from Bz-Gly and Bz-Gly-Gly in that it displays no inhibitory mode of binding with any of the substrates examined, activates only the hydrolysis of dipeptides by CPB, and has a greater effect on the hydrolysis of the basic dipeptide than on the neurtal dipeptide.	Cyclohexanols	0-12	carboxypeptidase B1	Homo sapiens	182-185
1170927-6	1975	Cyclohexanol differs from Bz-Gly and Bz-Gly-Gly in that it displays no inhibitory mode of binding with any of the substrates examined, activates only the hydrolysis of dipeptides by CPB, and has a greater effect on the hydrolysis of the basic dipeptide than on the neurtal dipeptide.	bz-gly-gly	37-47	carboxypeptidase B1	Homo sapiens	182-185
1170927-6	1975	Cyclohexanol differs from Bz-Gly and Bz-Gly-Gly in that it displays no inhibitory mode of binding with any of the substrates examined, activates only the hydrolysis of dipeptides by CPB, and has a greater effect on the hydrolysis of the basic dipeptide than on the neurtal dipeptide.	Dipeptides	168-178	carboxypeptidase B1	Homo sapiens	182-185
1170927-7	1975	Moreover, when Bz-Gly-Lys is the substrate, cyclohexanol activates its hydrolysis by CPB by increasing both the enzyme-substrate binding affinity and the rate of the catalytic step, an effect different from that observed when Bz-Gly is the modifier.	bz-gly-lys	15-25	carboxypeptidase B1	Homo sapiens	85-88
1170927-7	1975	Moreover, when Bz-Gly-Lys is the substrate, cyclohexanol activates its hydrolysis by CPB by increasing both the enzyme-substrate binding affinity and the rate of the catalytic step, an effect different from that observed when Bz-Gly is the modifier.	Cyclohexanols	44-56	carboxypeptidase B1	Homo sapiens	85-88
1242084-2	1975	Longitudinal and transverse proton relaxation rates of water in solutions of porcine manganese carboxypeptidase B have been measured in the presence of various competitive inhibitors by pulse nuclear magnetic resonance (NMR) spectrometry.	Water	55-60	carboxypeptidase B1	Homo sapiens	95-113
240688-0	1975	On the interaction of esters and peptides with carboxypeptidase B.	Esters	22-28	carboxypeptidase B1	Homo sapiens	47-65
240688-1	1975	The specificity of porcine carboxypeptidase B towards basic and non-basic substrates was studied by employing several esters of phenyllactate.	Esters	118-124	carboxypeptidase B1	Homo sapiens	27-45
240688-1	1975	The specificity of porcine carboxypeptidase B towards basic and non-basic substrates was studied by employing several esters of phenyllactate.	3-phenyllactic acid	128-141	carboxypeptidase B1	Homo sapiens	27-45
240688-3	1975	These non-basic ester-peptide pairs as well as the basic ester-peptide pair of arginyl derivatives, permits the direct comparison of the pH dependencies of the kinetic constants for the hydrolysis of those substrates by carboxypeptidase B.	Esters	16-21	carboxypeptidase B1	Homo sapiens	220-238
240688-3	1975	These non-basic ester-peptide pairs as well as the basic ester-peptide pair of arginyl derivatives, permits the direct comparison of the pH dependencies of the kinetic constants for the hydrolysis of those substrates by carboxypeptidase B.	Esters	57-62	carboxypeptidase B1	Homo sapiens	220-238
240688-3	1975	These non-basic ester-peptide pairs as well as the basic ester-peptide pair of arginyl derivatives, permits the direct comparison of the pH dependencies of the kinetic constants for the hydrolysis of those substrates by carboxypeptidase B.	Peptides	22-29	carboxypeptidase B1	Homo sapiens	220-238
20240553-0	1947	The action of proteolytic enzymes and protaminase on salmine sulfate.	salmine sulfate	53-68	carboxypeptidase B1	Homo sapiens	38-49
4530307-4	1974	On the other hand, the same reaction for NES-des-Arg hemoglobin (hemoglobin reacted with N-ethylmaleimide and carboxypeptidase B) in the presence of inositol hexaphosphate is homogeneous and slow, and shows isosbesty.	Phytic Acid	149-171	carboxypeptidase B1	Homo sapiens	110-128
4857892-0	1974	Affinity labelling of carboxypeptidase B: modification of a methionyl residue.	methionyl	60-69	carboxypeptidase B1	Homo sapiens	22-40
4516202-0	1973	The role of a tyrosyl residue in the mechanism of action of carboxypeptidase B: luminescence studies.	cyclo(tyrosyl-tyrosyl)	14-21	carboxypeptidase B1	Homo sapiens	60-78
4516202-1	1973	The luminescence spectra of carboxypeptidase B indicate specific differences between the zinc and apoenzyme due to the state of tyrosyl residues presumably at the active site.	cyclo(tyrosyl-tyrosyl)	128-135	carboxypeptidase B1	Homo sapiens	28-46
4516202-3	1973	An interpretation of the role of that tyrosyl residue in the mechanism of action of carboxypeptidase B is presented.	cyclo(tyrosyl-tyrosyl)	38-45	carboxypeptidase B1	Homo sapiens	84-102
4098172-6	1970	These observations indicate that the anaphylatoxin inactivator constitutes a metal-dependent enzyme resembling in specificity pancreatic carboxypeptidase B.	Metals	77-82	carboxypeptidase B1	Homo sapiens	126-155
5353090-0	1969	The carboxypeptidase B-catalyzed hydrolysis of poly-episilon-N-methyl-L-lysine and poly-episilon-N, episilon-N-dimethyl-L-lysine.	poly-episilon-n-methyl-l-lysine	47-78	carboxypeptidase B1	Homo sapiens	4-22
5353090-0	1969	The carboxypeptidase B-catalyzed hydrolysis of poly-episilon-N-methyl-L-lysine and poly-episilon-N, episilon-N-dimethyl-L-lysine.	poly-episilon-n, episilon-n-dimethyl-l-lysine	83-128	carboxypeptidase B1	Homo sapiens	4-22
5657466-0	1968	Studies on the action of carboxypeptidase B on polylysine.	Polylysine	47-57	carboxypeptidase B1	Homo sapiens	25-43
14190467-5	1964	Spectrophotometric studies of the hydrolysis of hippuryl-L-arginine confirmed the presence of a carboxypeptidase B-like activity in brain.	hippuryl-L-arginine	48-67	carboxypeptidase B1	Homo sapiens	96-114
14190467-7	1964	Previous incubation of carboxypeptidase B with phenothiazines and zinc ions greatly reduced the enzymatic inhibition by the phenothiazines, which indicated a possible chelating action by these inhibitors on the metalo-enzyme carboxypeptidase B.	Phenothiazines	47-61	carboxypeptidase B1	Homo sapiens	23-41
14190467-7	1964	Previous incubation of carboxypeptidase B with phenothiazines and zinc ions greatly reduced the enzymatic inhibition by the phenothiazines, which indicated a possible chelating action by these inhibitors on the metalo-enzyme carboxypeptidase B.	Phenothiazines	47-61	carboxypeptidase B1	Homo sapiens	225-243
14190467-7	1964	Previous incubation of carboxypeptidase B with phenothiazines and zinc ions greatly reduced the enzymatic inhibition by the phenothiazines, which indicated a possible chelating action by these inhibitors on the metalo-enzyme carboxypeptidase B.	Phenothiazines	124-138	carboxypeptidase B1	Homo sapiens	23-41
14190467-7	1964	Previous incubation of carboxypeptidase B with phenothiazines and zinc ions greatly reduced the enzymatic inhibition by the phenothiazines, which indicated a possible chelating action by these inhibitors on the metalo-enzyme carboxypeptidase B.	Phenothiazines	124-138	carboxypeptidase B1	Homo sapiens	225-243
5065066-0	1972	Chemical evidence for a functional arginine residue in carboxypeptidase B.	Arginine	35-43	carboxypeptidase B1	Homo sapiens	55-73
13700531-0	1961	Influence of cobalt and cadmium on the peptidase and esterase activities of carboxypeptidase B.	Cobalt	13-19	carboxypeptidase B1	Homo sapiens	76-94
13700531-0	1961	Influence of cobalt and cadmium on the peptidase and esterase activities of carboxypeptidase B.	Cadmium	24-31	carboxypeptidase B1	Homo sapiens	76-94
13499436-0	1957	Release of C-terminal S-(beta-aminoethyl)-cysteine residues by carboxypeptidase-B.	S-2-aminoethyl cysteine	22-50	carboxypeptidase B1	Homo sapiens	63-81
33444116-2	2021	In this randomized, open-label, phase II study, we characterized the efficacy and safety of bevacizumab in combination with carboplatin plus paclitaxel (CPB) in patients with previously untreated advanced MM.	Paclitaxel	141-151	carboxypeptidase B1	Homo sapiens	153-156
34002533-4	2021	Here, we introduced a multifunctional micromotor to implement the adsorption and degradation roles simultaneously by integrating the poly (aspartic acid) (PASP) adsorbent with a MnO 2 -based catalyst.	polyaspartate	133-153	carboxypeptidase B1	Homo sapiens	155-159
34002533-4	2021	Here, we introduced a multifunctional micromotor to implement the adsorption and degradation roles simultaneously by integrating the poly (aspartic acid) (PASP) adsorbent with a MnO 2 -based catalyst.	mno 2	178-183	carboxypeptidase B1	Homo sapiens	155-159
34002533-7	2021	Combining the attractive adsorption capability of poly (aspartic acid) (PASP), the composite micromotors offer an efficient removal of heavy metal ions in short time.	polyaspartate	50-70	carboxypeptidase B1	Homo sapiens	72-76
34002533-7	2021	Combining the attractive adsorption capability of poly (aspartic acid) (PASP), the composite micromotors offer an efficient removal of heavy metal ions in short time.	Metals	141-146	carboxypeptidase B1	Homo sapiens	72-76
32834561-4	2020	Therefore, this work aims to evaluate the filtration performance of cellulose acetate (CA) nanofibers and cationic surfactant cetylpyridinium bromide (CPB) produced by electrospinning technique for retention of aerosol nanoparticles.	hexadecylpyridinium bromide	126-149	carboxypeptidase B1	Homo sapiens	151-154
33530942-2	2021	Therefore, we performed this study to investigate if there is a dose dependent in-vivo effect of TXA on fibrinolysis parameters by measurement of fibrinolysis markers in adults undergoing cardiac surgery with CPB.	txa	97-100	carboxypeptidase B1	Homo sapiens	209-212
33430312-1	2021	Namodenoson, an A3 adenosine-receptor agonist, showed promising results in advanced hepatocellular carcinoma (HCC) and moderate hepatic dysfunction (Child-Pugh B; CPB) in a phase I/II clinical study.	2-chloro-N(6)-(3-iodobenzyl)adenosine-5'-N-methyluronamide	0-11	carboxypeptidase B1	Homo sapiens	163-166
33430312-14	2021	In conclusion, namodenoson demonstrated a favorable safety profile and a preliminary efficacy signal in HCC CPB.	2-chloro-N(6)-(3-iodobenzyl)adenosine-5'-N-methyluronamide	15-26	carboxypeptidase B1	Homo sapiens	108-111
33624836-5	2021	To resolve this product quality issue, we developed an enzyme treatment method by introducing carboxypeptidase B (CpB) to clip the C-terminal lysine, leading to significantly increased main peak and an acceptable and more homogenous product quality for all the intensified processes.	Lysine	142-148	carboxypeptidase B1	Homo sapiens	94-112
33624836-5	2021	To resolve this product quality issue, we developed an enzyme treatment method by introducing carboxypeptidase B (CpB) to clip the C-terminal lysine, leading to significantly increased main peak and an acceptable and more homogenous product quality for all the intensified processes.	Lysine	142-148	carboxypeptidase B1	Homo sapiens	114-117
33061517-1	2020	Purpose: To assess the safety, efficacy and prognostic impact of clinical factors related to lenvatinib treatment in Child-Pugh class A (CP-A) and class B (CP-B) patients with unresectable hepatocellular carcinoma (u-HCC).	lenvatinib	93-103	carboxypeptidase B1	Homo sapiens	156-160
33061517-5	2020	Frequency of lenvatinib-related adverse events, including decreased appetite (P=0.034), diarrhea (P=0.040), elevated serum bilirubin (P=0.016) and vomiting (P=0.009), were higher in CP-B than in CP-A patients.	lenvatinib	13-23	carboxypeptidase B1	Homo sapiens	182-186
32717373-2	2020	Here, sixteen dipeptidyl nitrile derivatives were synthesized, tested against CPB, and analyzed using matched molecular pairs to determine the effects of stereochemistry and p-phenyl substitution on enzyme inhibition.	dipeptidyl nitrile	14-32	carboxypeptidase B1	Homo sapiens	78-81
32994399-3	2020	An innovative material, poly (aspartic acid)-polyethylene glycol (PASP-PEG), was designed and synthesized to construct a mineralizing and anti-adhesive surface that could be applied to repair demineralized enamel.	poly (aspartic acid)-polyethylene glycol	24-64	carboxypeptidase B1	Homo sapiens	66-70
32994399-5	2020	Adsorption results demonstrated that PASP-PEG possesses a high binding affinity to the hydroxyapatite (HA)/tooth surface.	Durapatite	87-101	carboxypeptidase B1	Homo sapiens	37-41
32994399-5	2020	Adsorption results demonstrated that PASP-PEG possesses a high binding affinity to the hydroxyapatite (HA)/tooth surface.	Durapatite	103-105	carboxypeptidase B1	Homo sapiens	37-41
32515589-3	2020	Herein, we report an O18-labeling assisted LC-MS method, which takes advantage of the carboxypeptidase B-catalyzed Lys removal and O18-labeling, to achieve improved accuracy of C-term Lys quantitation.	Lysine	115-118	carboxypeptidase B1	Homo sapiens	86-104
32702881-6	2020	The median duration of regorafenib treatment in patients with CP-A and CP-B were 4.1 months and 2.0 months, respectively, with no significant difference.	regorafenib	23-34	carboxypeptidase B1	Homo sapiens	71-75
32515589-3	2020	Herein, we report an O18-labeling assisted LC-MS method, which takes advantage of the carboxypeptidase B-catalyzed Lys removal and O18-labeling, to achieve improved accuracy of C-term Lys quantitation.	Lysine	184-187	carboxypeptidase B1	Homo sapiens	86-104
32170329-11	2020	Factors impacting the need for a blood transfusion during CPB included redo surgery [odds ratio (OR) 4.61, p = 0.001] and the highest lactate level on CPB (OR 1.65, p = 0.006).	Lactic Acid	134-141	carboxypeptidase B1	Homo sapiens	151-154
33463260-4	2020	This multifunctional nanovesicle was constructed by fluorinated cationic polymer C9F17-PAsp(DET) with PEG-conjugated protoporphyrin IX (PEG-PpIX) modification, which could yield the simultaneous loading of perfluorohexane (PFH) and oxygen.	polymer c9f17	73-86	carboxypeptidase B1	Homo sapiens	87-91
33463260-5	2020	We found that the PAsp(DET)-PpIX-PEG@PFH nanovesicles could not only generate the reactive oxygen species (ROS) under ultrasound irradiation after intravenous (i.v.)	Reactive Oxygen Species	107-110	carboxypeptidase B1	Homo sapiens	18-22
33463260-4	2020	This multifunctional nanovesicle was constructed by fluorinated cationic polymer C9F17-PAsp(DET) with PEG-conjugated protoporphyrin IX (PEG-PpIX) modification, which could yield the simultaneous loading of perfluorohexane (PFH) and oxygen.	Polyethylene Glycols	102-105	carboxypeptidase B1	Homo sapiens	87-91
33463260-7	2020	Furthermore, oxygen-loaded PAsp(DET)-PpIX-PEG nanovesicles could not only reduce therapeutic resistance by relieving tumor hypoxia but also increase ROS production for enhanced sonodynamic therapy.	Oxygen	13-19	carboxypeptidase B1	Homo sapiens	27-31
33463260-4	2020	This multifunctional nanovesicle was constructed by fluorinated cationic polymer C9F17-PAsp(DET) with PEG-conjugated protoporphyrin IX (PEG-PpIX) modification, which could yield the simultaneous loading of perfluorohexane (PFH) and oxygen.	protoporphyrin IX	117-134	carboxypeptidase B1	Homo sapiens	87-91
33463260-7	2020	Furthermore, oxygen-loaded PAsp(DET)-PpIX-PEG nanovesicles could not only reduce therapeutic resistance by relieving tumor hypoxia but also increase ROS production for enhanced sonodynamic therapy.	protoporphyrin IX	37-41	carboxypeptidase B1	Homo sapiens	27-31
33463260-7	2020	Furthermore, oxygen-loaded PAsp(DET)-PpIX-PEG nanovesicles could not only reduce therapeutic resistance by relieving tumor hypoxia but also increase ROS production for enhanced sonodynamic therapy.	Polyethylene Glycols	42-45	carboxypeptidase B1	Homo sapiens	27-31
33463260-4	2020	This multifunctional nanovesicle was constructed by fluorinated cationic polymer C9F17-PAsp(DET) with PEG-conjugated protoporphyrin IX (PEG-PpIX) modification, which could yield the simultaneous loading of perfluorohexane (PFH) and oxygen.	peg-ppix	136-144	carboxypeptidase B1	Homo sapiens	87-91
33463260-7	2020	Furthermore, oxygen-loaded PAsp(DET)-PpIX-PEG nanovesicles could not only reduce therapeutic resistance by relieving tumor hypoxia but also increase ROS production for enhanced sonodynamic therapy.	Reactive Oxygen Species	149-152	carboxypeptidase B1	Homo sapiens	27-31
33463260-4	2020	This multifunctional nanovesicle was constructed by fluorinated cationic polymer C9F17-PAsp(DET) with PEG-conjugated protoporphyrin IX (PEG-PpIX) modification, which could yield the simultaneous loading of perfluorohexane (PFH) and oxygen.	perflexane	206-221	carboxypeptidase B1	Homo sapiens	87-91
33463260-4	2020	This multifunctional nanovesicle was constructed by fluorinated cationic polymer C9F17-PAsp(DET) with PEG-conjugated protoporphyrin IX (PEG-PpIX) modification, which could yield the simultaneous loading of perfluorohexane (PFH) and oxygen.	perflexane	223-226	carboxypeptidase B1	Homo sapiens	87-91
33463260-4	2020	This multifunctional nanovesicle was constructed by fluorinated cationic polymer C9F17-PAsp(DET) with PEG-conjugated protoporphyrin IX (PEG-PpIX) modification, which could yield the simultaneous loading of perfluorohexane (PFH) and oxygen.	Oxygen	232-238	carboxypeptidase B1	Homo sapiens	87-91
33463260-5	2020	We found that the PAsp(DET)-PpIX-PEG@PFH nanovesicles could not only generate the reactive oxygen species (ROS) under ultrasound irradiation after intravenous (i.v.)	Polyethylene Glycols	33-36	carboxypeptidase B1	Homo sapiens	18-22
33463260-5	2020	We found that the PAsp(DET)-PpIX-PEG@PFH nanovesicles could not only generate the reactive oxygen species (ROS) under ultrasound irradiation after intravenous (i.v.)	perflexane	37-40	carboxypeptidase B1	Homo sapiens	18-22
33463260-5	2020	We found that the PAsp(DET)-PpIX-PEG@PFH nanovesicles could not only generate the reactive oxygen species (ROS) under ultrasound irradiation after intravenous (i.v.)	Reactive Oxygen Species	82-105	carboxypeptidase B1	Homo sapiens	18-22
30893304-11	2019	CONCLUSION: Echocardiography-derived PASP is negatively correlated with global MFR measured by 13N-NH3 dynamic PET.	13n-nh3	95-102	carboxypeptidase B1	Homo sapiens	37-41
32073726-9	2020	This interaction was prevented by epsilon-aminocaproic acid or carboxypeptidase B treatment suggesting that plasminogen/DIP-plasmin binds to FIXagamma/FIXadelta through newly generated C-terminal Lys316 and Lys413.	Carbon	185-186	carboxypeptidase B1	Homo sapiens	63-81
32201841-6	2020	PPA is a valuable intermediate for the synthesis of carboxypeptidase B enzyme inhibitors, antimuscarinic drugs, or potential anticancer agents in the pharmaceutical industry.	3-phenylpropylamine	0-3	carboxypeptidase B1	Homo sapiens	52-70
31268075-3	2019	A novel copolymer mPEG-C[double bond, length as m-dash]N-PAsp(MEA)-CA was synthesized and self-assembled into a dual-sensitive interlayer-crosslinked micelle (ICM).	copolymer	8-17	carboxypeptidase B1	Homo sapiens	57-61
31268075-3	2019	A novel copolymer mPEG-C[double bond, length as m-dash]N-PAsp(MEA)-CA was synthesized and self-assembled into a dual-sensitive interlayer-crosslinked micelle (ICM).	mpeg-c	18-24	carboxypeptidase B1	Homo sapiens	57-61
30832916-1	2019	Carboxypeptidase B (CPB) is a protease that specifically hydrolyzes C-terminal alkaline amino acid of a peptide, which plays an important role in biological analysis.	alkaline amino acid	79-98	carboxypeptidase B1	Homo sapiens	0-18
30832916-1	2019	Carboxypeptidase B (CPB) is a protease that specifically hydrolyzes C-terminal alkaline amino acid of a peptide, which plays an important role in biological analysis.	alkaline amino acid	79-98	carboxypeptidase B1	Homo sapiens	20-23
30832916-4	2019	We assembled the peptides composing of alkaline amino acids into the nanochannels to detect the activity of CPB based on its hydrolysis characteristic.	alkaline amino acids	39-59	carboxypeptidase B1	Homo sapiens	108-111
30939489-0	2019	Elbasvir/Grazoprevir in People With Hepatitis C Genotype 1 Infection and Child-Pugh Class B Cirrhosis: The C-SALT Study.	elbasvir/grazoprevir	0-20	carboxypeptidase B1	Homo sapiens	73-91
30939489-2	2019	The C-SALT study assessed elbasvir (EBR) plus grazoprevir (GZR) in individuals with HCV genotype 1 infection and Child-Pugh class B (CP-B) cirrhosis.	2-(pyrrolidin-2-yl)-5-(2-(4-(5-(pyrrolidin-2-yl)-1H-imidazol-2-yl)phenyl)benzofuran-5-yl)-1H-imidazole	26-34	carboxypeptidase B1	Homo sapiens	113-131
30939489-2	2019	The C-SALT study assessed elbasvir (EBR) plus grazoprevir (GZR) in individuals with HCV genotype 1 infection and Child-Pugh class B (CP-B) cirrhosis.	2-(pyrrolidin-2-yl)-5-(2-(4-(5-(pyrrolidin-2-yl)-1H-imidazol-2-yl)phenyl)benzofuran-5-yl)-1H-imidazole	26-34	carboxypeptidase B1	Homo sapiens	133-137
30939489-2	2019	The C-SALT study assessed elbasvir (EBR) plus grazoprevir (GZR) in individuals with HCV genotype 1 infection and Child-Pugh class B (CP-B) cirrhosis.	2-(pyrrolidin-2-yl)-5-(2-(4-(5-(pyrrolidin-2-yl)-1H-imidazol-2-yl)phenyl)benzofuran-5-yl)-1H-imidazole	36-39	carboxypeptidase B1	Homo sapiens	113-131
30939489-2	2019	The C-SALT study assessed elbasvir (EBR) plus grazoprevir (GZR) in individuals with HCV genotype 1 infection and Child-Pugh class B (CP-B) cirrhosis.	grazoprevir	46-57	carboxypeptidase B1	Homo sapiens	113-131
30939489-2	2019	The C-SALT study assessed elbasvir (EBR) plus grazoprevir (GZR) in individuals with HCV genotype 1 infection and Child-Pugh class B (CP-B) cirrhosis.	grazoprevir	59-62	carboxypeptidase B1	Homo sapiens	113-131
30341499-5	2019	RESULTS: For the approved combination of glecaprevir 300 mg with pibrentasvir 120 mg, glecaprevir AUC was increased by 33% (CP-A), to 2.0-fold (CP-B), and to 11-fold (CP-C) relative to normal subjects; pibrentasvir AUC was <= 26% different (CP-A or CP-B) and increased to 2.1-fold (CP-C).	glecaprevir	41-52	carboxypeptidase B1	Homo sapiens	144-148
30705106-5	2019	We demonstrated that bile acids elevated expression of Hh pathway target genes, such as GLI1 and PTCH1, and induced SOX9 and CDX2 up-regulation in both CP-A and CP-B cells.	Bile Acids and Salts	21-31	carboxypeptidase B1	Homo sapiens	161-165
30341499-5	2019	RESULTS: For the approved combination of glecaprevir 300 mg with pibrentasvir 120 mg, glecaprevir AUC was increased by 33% (CP-A), to 2.0-fold (CP-B), and to 11-fold (CP-C) relative to normal subjects; pibrentasvir AUC was <= 26% different (CP-A or CP-B) and increased to 2.1-fold (CP-C).	glecaprevir	41-52	carboxypeptidase B1	Homo sapiens	252-256
30341499-5	2019	RESULTS: For the approved combination of glecaprevir 300 mg with pibrentasvir 120 mg, glecaprevir AUC was increased by 33% (CP-A), to 2.0-fold (CP-B), and to 11-fold (CP-C) relative to normal subjects; pibrentasvir AUC was <= 26% different (CP-A or CP-B) and increased to 2.1-fold (CP-C).	pibrentasvir	65-77	carboxypeptidase B1	Homo sapiens	144-148
30341499-5	2019	RESULTS: For the approved combination of glecaprevir 300 mg with pibrentasvir 120 mg, glecaprevir AUC was increased by 33% (CP-A), to 2.0-fold (CP-B), and to 11-fold (CP-C) relative to normal subjects; pibrentasvir AUC was <= 26% different (CP-A or CP-B) and increased to 2.1-fold (CP-C).	pibrentasvir	65-77	carboxypeptidase B1	Homo sapiens	252-256
30341499-5	2019	RESULTS: For the approved combination of glecaprevir 300 mg with pibrentasvir 120 mg, glecaprevir AUC was increased by 33% (CP-A), to 2.0-fold (CP-B), and to 11-fold (CP-C) relative to normal subjects; pibrentasvir AUC was <= 26% different (CP-A or CP-B) and increased to 2.1-fold (CP-C).	glecaprevir	86-97	carboxypeptidase B1	Homo sapiens	144-148
30341499-5	2019	RESULTS: For the approved combination of glecaprevir 300 mg with pibrentasvir 120 mg, glecaprevir AUC was increased by 33% (CP-A), to 2.0-fold (CP-B), and to 11-fold (CP-C) relative to normal subjects; pibrentasvir AUC was <= 26% different (CP-A or CP-B) and increased to 2.1-fold (CP-C).	glecaprevir	86-97	carboxypeptidase B1	Homo sapiens	252-256
30341499-6	2019	For glecaprevir 200 mg with pibrentasvir 120 mg, glecaprevir AUC was increased by 80% (CP-A) or to 2.8-fold (CP-B), while pibrentasvir AUC was unaffected in the same subjects (<= 12% difference).	glecaprevir	4-15	carboxypeptidase B1	Homo sapiens	109-113
30341499-6	2019	For glecaprevir 200 mg with pibrentasvir 120 mg, glecaprevir AUC was increased by 80% (CP-A) or to 2.8-fold (CP-B), while pibrentasvir AUC was unaffected in the same subjects (<= 12% difference).	glecaprevir	49-60	carboxypeptidase B1	Homo sapiens	109-113
30341499-7	2019	Pibrentasvir 120 mg alone AUC increased 51% (CP-A), 31% (CP-B), and to 5.2-fold (CP-C).	pibrentasvir	0-12	carboxypeptidase B1	Homo sapiens	57-61
30341499-11	2019	Elevated glecaprevir and/or pibrentasvir exposures are expected in HCV-infected patients with CP-B or CP-C hepatic impairment.	glecaprevir	9-20	carboxypeptidase B1	Homo sapiens	94-98
30341499-11	2019	Elevated glecaprevir and/or pibrentasvir exposures are expected in HCV-infected patients with CP-B or CP-C hepatic impairment.	pibrentasvir	28-40	carboxypeptidase B1	Homo sapiens	94-98
29759300-0	2018	Decreased contractile response of peripheral arterioles to serotonin after CPB in patients with diabetes.	Serotonin	59-68	carboxypeptidase B1	Homo sapiens	75-78
30384012-0	2018	Sorafenib as first-line therapy in patients with advanced Child-Pugh B hepatocellular carcinoma-a meta-analysis.	Sorafenib	0-9	carboxypeptidase B1	Homo sapiens	58-70
29948358-0	2018	Survival and tolerance to sorafenib in Child-Pugh B patients with hepatocellular carcinoma: a prospective study.	Sorafenib	26-35	carboxypeptidase B1	Homo sapiens	39-51
29948358-2	2018	We evaluated the overall survival (OS) and tolerance to sorafenib in a large cohort of Child-Pugh B (CP-B) HCC patients as compared to CP-A HCC patients.	Sorafenib	56-65	carboxypeptidase B1	Homo sapiens	87-99
29948358-10	2018	This real-life cohort of CP-B HCC patients treated with sorafenib had a higher survival than that described in the literature, with a satisfactory safety profile.	Sorafenib	56-65	carboxypeptidase B1	Homo sapiens	25-29
29948358-11	2018	Despite the high prevalence of severe AEs in CP-B patients, there were fewer treatment interruptions in this group, indicating that Child-Pugh B patients can tolerate treatment and may benefit from sorafenib.	Sorafenib	198-207	carboxypeptidase B1	Homo sapiens	45-49
29948358-11	2018	Despite the high prevalence of severe AEs in CP-B patients, there were fewer treatment interruptions in this group, indicating that Child-Pugh B patients can tolerate treatment and may benefit from sorafenib.	Sorafenib	198-207	carboxypeptidase B1	Homo sapiens	132-144
30100044-1	2018	BACKGROUND: We have previously found that hyperkalemic cardioplegic arrest in the setting of cardiopulmonary bypass (CP/CPB) is associated with impairment of the coronary arteriolar response to phenylephrine in nondiabetic (ND) patients.	Phenylephrine	194-207	carboxypeptidase B1	Homo sapiens	120-123
30100044-7	2018	RESULTS: Phenylephrine (10-9 to 10-4 M) induced a dose-dependent contractile response in both ND and DM vessels pre- and post-CP/CPB.	Phenylephrine	9-22	carboxypeptidase B1	Homo sapiens	129-132
30100044-12	2018	CONCLUSIONS: Diabetes is associated with a decreased contractile response of coronary arterioles to phenylephrine in the setting of CP/CPB versus that observed in ND patients.	Phenylephrine	100-113	carboxypeptidase B1	Homo sapiens	135-138
29860319-3	2018	Patients and methods: We performed PK studies of a single 70 mg dose of caspofungin in patients with decompensated CP-B (n = 10) or CP-C (n = 10) cirrhosis and of multiple doses in 21 non-cirrhotic ICU patients with hypoalbuminaemia.	Caspofungin	72-83	carboxypeptidase B1	Homo sapiens	115-119
29860319-5	2018	Results: We observed a marginal reduction of caspofungin clearance in a PK study in patients with decompensated CP-B or CP-C cirrhosis.	Caspofungin	45-56	carboxypeptidase B1	Homo sapiens	112-116
28487062-6	2018	We hypothesised that surgery performed on CPB releases mtDAMPs into the circulation.	mtdamps	55-62	carboxypeptidase B1	Homo sapiens	42-45
31458549-7	2018	Our observation has suggested that after the photoexcitation of CPB NCs/CdSe QDs composite system, a charge-separated state is formed where the electrons are localized in CB of CdSe QDs and holes are localized in VB of CPB NCs.	cadmium selenide	72-76	carboxypeptidase B1	Homo sapiens	219-222
31458549-7	2018	Our observation has suggested that after the photoexcitation of CPB NCs/CdSe QDs composite system, a charge-separated state is formed where the electrons are localized in CB of CdSe QDs and holes are localized in VB of CPB NCs.	cadmium selenide	177-181	carboxypeptidase B1	Homo sapiens	64-67
28274181-0	2018	Structure of the carboxypeptidase B complex with N-sulfamoyl-L-phenylalanine - a transition state analog of non-specific substrate.	PHENYLALANINE-N-SULFONAMIDE	49-76	carboxypeptidase B1	Homo sapiens	17-35
29311398-5	2018	In multivariate analysis, octreotide was independently associated with in-hospital mortality (p = 0.028) and need for transfusion (p = 0.008) only in patients with severe liver dysfunction (CP-B/C or MELD >= 10).	Octreotide	26-36	carboxypeptidase B1	Homo sapiens	190-194
31458549-3	2018	The redox levels (i.e., conduction band (CB) and valence band (VB)) of the CPB NCs and CdSe QDs suggest the feasibility of photoexcited electron transfer from CPB NCs to CdSe QDs and photoexcited hole transfer from CdSe QDs to CPB NCs, and it has been confirmed by both steady-state and time-resolved spectroscopy.	cadmium selenide	87-91	carboxypeptidase B1	Homo sapiens	159-162
31458549-3	2018	The redox levels (i.e., conduction band (CB) and valence band (VB)) of the CPB NCs and CdSe QDs suggest the feasibility of photoexcited electron transfer from CPB NCs to CdSe QDs and photoexcited hole transfer from CdSe QDs to CPB NCs, and it has been confirmed by both steady-state and time-resolved spectroscopy.	cadmium selenide	87-91	carboxypeptidase B1	Homo sapiens	159-162
31458549-3	2018	The redox levels (i.e., conduction band (CB) and valence band (VB)) of the CPB NCs and CdSe QDs suggest the feasibility of photoexcited electron transfer from CPB NCs to CdSe QDs and photoexcited hole transfer from CdSe QDs to CPB NCs, and it has been confirmed by both steady-state and time-resolved spectroscopy.	cadmium selenide	170-174	carboxypeptidase B1	Homo sapiens	75-78
31458549-3	2018	The redox levels (i.e., conduction band (CB) and valence band (VB)) of the CPB NCs and CdSe QDs suggest the feasibility of photoexcited electron transfer from CPB NCs to CdSe QDs and photoexcited hole transfer from CdSe QDs to CPB NCs, and it has been confirmed by both steady-state and time-resolved spectroscopy.	cadmium selenide	170-174	carboxypeptidase B1	Homo sapiens	159-162
31458549-3	2018	The redox levels (i.e., conduction band (CB) and valence band (VB)) of the CPB NCs and CdSe QDs suggest the feasibility of photoexcited electron transfer from CPB NCs to CdSe QDs and photoexcited hole transfer from CdSe QDs to CPB NCs, and it has been confirmed by both steady-state and time-resolved spectroscopy.	cadmium selenide	170-174	carboxypeptidase B1	Homo sapiens	159-162
31458549-3	2018	The redox levels (i.e., conduction band (CB) and valence band (VB)) of the CPB NCs and CdSe QDs suggest the feasibility of photoexcited electron transfer from CPB NCs to CdSe QDs and photoexcited hole transfer from CdSe QDs to CPB NCs, and it has been confirmed by both steady-state and time-resolved spectroscopy.	cadmium selenide	170-174	carboxypeptidase B1	Homo sapiens	75-78
31458549-3	2018	The redox levels (i.e., conduction band (CB) and valence band (VB)) of the CPB NCs and CdSe QDs suggest the feasibility of photoexcited electron transfer from CPB NCs to CdSe QDs and photoexcited hole transfer from CdSe QDs to CPB NCs, and it has been confirmed by both steady-state and time-resolved spectroscopy.	cadmium selenide	170-174	carboxypeptidase B1	Homo sapiens	159-162
31458549-3	2018	The redox levels (i.e., conduction band (CB) and valence band (VB)) of the CPB NCs and CdSe QDs suggest the feasibility of photoexcited electron transfer from CPB NCs to CdSe QDs and photoexcited hole transfer from CdSe QDs to CPB NCs, and it has been confirmed by both steady-state and time-resolved spectroscopy.	cadmium selenide	170-174	carboxypeptidase B1	Homo sapiens	159-162
31458549-5	2018	The measured electron-transfer time from CPB NCs to CdSe QDs and hole-transfer time from CdSe QDs to CPB NCs were found to be 550 and 750 fs, respectively.	cadmium selenide	52-56	carboxypeptidase B1	Homo sapiens	41-44
31458549-5	2018	The measured electron-transfer time from CPB NCs to CdSe QDs and hole-transfer time from CdSe QDs to CPB NCs were found to be 550 and 750 fs, respectively.	cdse qds	52-60	carboxypeptidase B1	Homo sapiens	41-44
31458549-6	2018	Interestingly, the charge-transfer process found to be restricted in CPB/CdSe@CdS core-shell system where electron transfer from CPB NCs to core shell takes place, but the hole transfer from core shell to CPB NCs found to be restricted due to CdS shell making the process thermodynamically nonviable.	cadmium selenide	73-77	carboxypeptidase B1	Homo sapiens	69-72
31458549-6	2018	Interestingly, the charge-transfer process found to be restricted in CPB/CdSe@CdS core-shell system where electron transfer from CPB NCs to core shell takes place, but the hole transfer from core shell to CPB NCs found to be restricted due to CdS shell making the process thermodynamically nonviable.	cadmium selenide	73-77	carboxypeptidase B1	Homo sapiens	129-132
31458549-6	2018	Interestingly, the charge-transfer process found to be restricted in CPB/CdSe@CdS core-shell system where electron transfer from CPB NCs to core shell takes place, but the hole transfer from core shell to CPB NCs found to be restricted due to CdS shell making the process thermodynamically nonviable.	cadmium selenide	73-77	carboxypeptidase B1	Homo sapiens	129-132
31458549-6	2018	Interestingly, the charge-transfer process found to be restricted in CPB/CdSe@CdS core-shell system where electron transfer from CPB NCs to core shell takes place, but the hole transfer from core shell to CPB NCs found to be restricted due to CdS shell making the process thermodynamically nonviable.	Cadmium	73-76	carboxypeptidase B1	Homo sapiens	69-72
31458549-6	2018	Interestingly, the charge-transfer process found to be restricted in CPB/CdSe@CdS core-shell system where electron transfer from CPB NCs to core shell takes place, but the hole transfer from core shell to CPB NCs found to be restricted due to CdS shell making the process thermodynamically nonviable.	Cadmium	73-76	carboxypeptidase B1	Homo sapiens	129-132
31458549-6	2018	Interestingly, the charge-transfer process found to be restricted in CPB/CdSe@CdS core-shell system where electron transfer from CPB NCs to core shell takes place, but the hole transfer from core shell to CPB NCs found to be restricted due to CdS shell making the process thermodynamically nonviable.	Cadmium	73-76	carboxypeptidase B1	Homo sapiens	129-132
31458549-6	2018	Interestingly, the charge-transfer process found to be restricted in CPB/CdSe@CdS core-shell system where electron transfer from CPB NCs to core shell takes place, but the hole transfer from core shell to CPB NCs found to be restricted due to CdS shell making the process thermodynamically nonviable.	Cadmium	78-81	carboxypeptidase B1	Homo sapiens	69-72
31458549-6	2018	Interestingly, the charge-transfer process found to be restricted in CPB/CdSe@CdS core-shell system where electron transfer from CPB NCs to core shell takes place, but the hole transfer from core shell to CPB NCs found to be restricted due to CdS shell making the process thermodynamically nonviable.	Cadmium	78-81	carboxypeptidase B1	Homo sapiens	129-132
31458549-6	2018	Interestingly, the charge-transfer process found to be restricted in CPB/CdSe@CdS core-shell system where electron transfer from CPB NCs to core shell takes place, but the hole transfer from core shell to CPB NCs found to be restricted due to CdS shell making the process thermodynamically nonviable.	Cadmium	78-81	carboxypeptidase B1	Homo sapiens	129-132
31458549-7	2018	Our observation has suggested that after the photoexcitation of CPB NCs/CdSe QDs composite system, a charge-separated state is formed where the electrons are localized in CB of CdSe QDs and holes are localized in VB of CPB NCs.	cadmium selenide	72-76	carboxypeptidase B1	Homo sapiens	64-67
29058706-4	2018	Four types of phosphate-protein linkage exist and these generate nine different phosphoresidues-pSer, pThr, pTyr, pHis, pLys, pArg, pAsp, pGlu and pCys.	Phosphates	14-23	carboxypeptidase B1	Homo sapiens	132-136
28940421-10	2018	CONCLUSIONS: Changes in PASP strongly correlated with radiological severity of CAP and PaO2 .	cap	79-82	carboxypeptidase B1	Homo sapiens	24-28
28940421-10	2018	CONCLUSIONS: Changes in PASP strongly correlated with radiological severity of CAP and PaO2 .	pao2	87-91	carboxypeptidase B1	Homo sapiens	24-28
27604544-5	2016	Crystal structures of the anabaenopeptins B, C and F bound to the surrogate protease carboxypeptidase B revealed the binding modes of these large (~850 Da) compounds in detail and explained the observed SAR, i.e. the strong dependence of the potency on a basic (Arg, Lys) exocyclic residue that addressed the S1" binding pocket, and a broad tolerance towards substitutions in the pentacyclic ring that acted as a plug of the active site.	Lysine	267-270	carboxypeptidase B1	Homo sapiens	85-103
29188773-10	2017	Mean pharmacokinetic exposure to Sorafenib tosylate 200 mg, Ribavirn and Sofosbuvir at week 8th was 2.1, 1.5,1.2 times greater in CP B than in CP A.	Sorafenib	33-42	carboxypeptidase B1	Homo sapiens	130-134
29290908-8	2017	Majority (71%) of CP-B patients required a RBV dosage reduction during the treatment.	Ribavirin	43-46	carboxypeptidase B1	Homo sapiens	18-22
29188773-10	2017	Mean pharmacokinetic exposure to Sorafenib tosylate 200 mg, Ribavirn and Sofosbuvir at week 8th was 2.1, 1.5,1.2 times greater in CP B than in CP A.	Sofosbuvir	73-83	carboxypeptidase B1	Homo sapiens	130-134
28695201-4	2017	To prove the concept, we transformed biphenyl to 3,5-bis(N-carbazolyl)-1,1"-biphenyl, a novel isomer of 4,4"-bis(N-carbazolyl)-1,1"-biphenyl (CPB), a compound which is currently widely used as a host material for organic light-emitting diodes.	diphenyl	37-45	carboxypeptidase B1	Homo sapiens	142-145
28695201-4	2017	To prove the concept, we transformed biphenyl to 3,5-bis(N-carbazolyl)-1,1"-biphenyl, a novel isomer of 4,4"-bis(N-carbazolyl)-1,1"-biphenyl (CPB), a compound which is currently widely used as a host material for organic light-emitting diodes.	3,5-bis(n-carbazolyl)-1,1"-biphenyl	49-84	carboxypeptidase B1	Homo sapiens	142-145
28695201-4	2017	To prove the concept, we transformed biphenyl to 3,5-bis(N-carbazolyl)-1,1"-biphenyl, a novel isomer of 4,4"-bis(N-carbazolyl)-1,1"-biphenyl (CPB), a compound which is currently widely used as a host material for organic light-emitting diodes.	4,4"-bis(n-carbazolyl)-1,1"-biphenyl	104-140	carboxypeptidase B1	Homo sapiens	142-145
27604544-5	2016	Crystal structures of the anabaenopeptins B, C and F bound to the surrogate protease carboxypeptidase B revealed the binding modes of these large (~850 Da) compounds in detail and explained the observed SAR, i.e. the strong dependence of the potency on a basic (Arg, Lys) exocyclic residue that addressed the S1" binding pocket, and a broad tolerance towards substitutions in the pentacyclic ring that acted as a plug of the active site.	Arginine	262-265	carboxypeptidase B1	Homo sapiens	85-103
27038651-4	2016	It was also demonstrated that structural changes caused by Carboxypeptidase B treatment and deamidation study at pH extremes could be sensitively captured with the established method, with the results further indicating that the generic product"s basic variations of Fc/2 were un-cleaved Lysine residues, while the lack of certain acidic peaks on LC and Fd probably was due to the lower level of deamidation.	Lysine	288-294	carboxypeptidase B1	Homo sapiens	59-77
27005981-3	2016	The aim of the study was to compare the outcome of patients receiving VAD on VA-ECMO with patients who were converted to CPB at the time of VAD implantation.	VAD I protocol	140-143	carboxypeptidase B1	Homo sapiens	121-124
27005981-14	2016	CONCLUSIONS: This study demonstrates that the CPB machine can be safely omitted when a long-term VAD is implanted on VA-ECMO support.	VAD I protocol	97-100	carboxypeptidase B1	Homo sapiens	46-49
27007881-3	2016	The nanoparticle platform was composed of core-cross-linked polyion complex (PIC) micelles prepared from azide-functionalized PEG-b-poly(amino acids), that is, azido-PEG-b-poly(l-lysine) [N3-PEG-b-PLL] and azido-PEG-b-poly(aspartic acid) [N3-PEG-b-PAsp].	pic	77-80	carboxypeptidase B1	Homo sapiens	248-252
26457527-1	2015	Porcine pancreatic carboxypeptidase B (EC 3.4.23.6) was complexed with a stable transition-state analogue, N-sulfamoyl-L-arginine, in which an S atom imitates the sp(3)-hybridized carbon in the scissile-bond surrogate.	Carbon	180-186	carboxypeptidase B1	Homo sapiens	8-37
26069241-9	2016	CP/CPB induced more phosphorylation of VE-cadherin in all groups (versus pre-CP/CPB; P < 0.05, respectively) and this effect was more pronounced in the UDM group (P < 0.05 versus ND or CDM).	Chlorphenamidine	191-194	carboxypeptidase B1	Homo sapiens	0-6
26069241-11	2016	There were significant decreases in vasodilatory response to endothelial-dependent vasodilator ADP after CP/CPB (P < 0.05).	Adenosine Diphosphate	95-98	carboxypeptidase B1	Homo sapiens	105-111
26069241-14	2016	The increased tyrosine phosphorylation and deterioration of VE-cadherin indicate the damage of the cell-cell endothelial junctions in the diabetic vessels undergoing CP/CPB and cardiac surgery.	Tyrosine	14-22	carboxypeptidase B1	Homo sapiens	166-172
26253453-8	2016	The IPO group showed a significantly smaller increase of terminal deoxynucleotidyl transferase-mediated dUTP nick-end labeling-positive myocytes after CPB than CON group.	deoxyuridine triphosphate	104-108	carboxypeptidase B1	Homo sapiens	151-154
26510641-1	2015	A set of 5,15-biphenylene-bridged porphyrin wheels, namely, [n]cyclo-5,15-porphyrinylene-4,4"-biphenylenes [n]CPB, have been synthesized through the platination of 5,15-bis(4-(pinacolboranyl)phenyl) nickel(II) porphyrin and subsequent reductive elimination of Pt(II) (cod)-bridged cyclic porphyrin intermediates.	5,15-biphenylene	9-25	carboxypeptidase B1	Homo sapiens	110-113
26510641-1	2015	A set of 5,15-biphenylene-bridged porphyrin wheels, namely, [n]cyclo-5,15-porphyrinylene-4,4"-biphenylenes [n]CPB, have been synthesized through the platination of 5,15-bis(4-(pinacolboranyl)phenyl) nickel(II) porphyrin and subsequent reductive elimination of Pt(II) (cod)-bridged cyclic porphyrin intermediates.	Porphyrins	34-43	carboxypeptidase B1	Homo sapiens	110-113
26510641-1	2015	A set of 5,15-biphenylene-bridged porphyrin wheels, namely, [n]cyclo-5,15-porphyrinylene-4,4"-biphenylenes [n]CPB, have been synthesized through the platination of 5,15-bis(4-(pinacolboranyl)phenyl) nickel(II) porphyrin and subsequent reductive elimination of Pt(II) (cod)-bridged cyclic porphyrin intermediates.	Porphyrins	74-83	carboxypeptidase B1	Homo sapiens	110-113
26457527-0	2015	Structure of the complex of carboxypeptidase B and N-sulfamoyl-L-arginine.	N-sulfamoylarginine	51-73	carboxypeptidase B1	Homo sapiens	28-46
27161704-13	2016	Treatment of diluted plasma samples with carboxypeptidase B abolished the elevated levels of IgG to Pg, as well as the specific activity of the purified IgG to Pg-sepharose.	pg-sepharose	160-172	carboxypeptidase B1	Homo sapiens	41-59
26457527-10	2015	This study provides useful clues concerning how the transition state of arginine may bind to carboxypeptidase B and therefore provides an insight into the structural basis of carboxypeptidase B selectivity, which is useful for the rational design of a carboxypeptidase with improved selectivity for industrial recombinant pro-insulin processing.	Arginine	72-80	carboxypeptidase B1	Homo sapiens	93-111
26457527-1	2015	Porcine pancreatic carboxypeptidase B (EC 3.4.23.6) was complexed with a stable transition-state analogue, N-sulfamoyl-L-arginine, in which an S atom imitates the sp(3)-hybridized carbon in the scissile-bond surrogate.	N-sulfamoylarginine	107-129	carboxypeptidase B1	Homo sapiens	8-37
26457527-10	2015	This study provides useful clues concerning how the transition state of arginine may bind to carboxypeptidase B and therefore provides an insight into the structural basis of carboxypeptidase B selectivity, which is useful for the rational design of a carboxypeptidase with improved selectivity for industrial recombinant pro-insulin processing.	Arginine	72-80	carboxypeptidase B1	Homo sapiens	175-193
26457527-1	2015	Porcine pancreatic carboxypeptidase B (EC 3.4.23.6) was complexed with a stable transition-state analogue, N-sulfamoyl-L-arginine, in which an S atom imitates the sp(3)-hybridized carbon in the scissile-bond surrogate.	sp(3)	163-168	carboxypeptidase B1	Homo sapiens	8-37
26033798-7	2015	CP-B/C versus CP-A had more early treatment discontinuations (11% vs. 1%), adverse events (AEs) requiring hospitalization (22% vs. 2%), infections requiring antibiotics (20% vs. 1%), and hepatic decompensating events (20% vs. 3%; all P < 0.01).	aes	91-94	carboxypeptidase B1	Homo sapiens	0-4
25990761-2	2015	Cocrystal structures of these macrocyclic natural product inhibitors in a modified porcine carboxypeptidase B revealed their binding mode and provided the basis for the rational design of small molecule inhibitors with a previously unknown central urea motif.	Urea	248-252	carboxypeptidase B1	Homo sapiens	91-109
25789012-2	2015	At present, limited data exists with regard to the safety and efficacy of sorafenib in treating CP-B HCC patients.	Sorafenib	74-83	carboxypeptidase B1	Homo sapiens	96-100
26029452-11	2015	CONCLUSIONS: Patients with CP-A or CP-B advanced HCC should be offered sorafenib at 400 mg twice daily with optimal management of AEs in order to improve survival.	Sorafenib	71-80	carboxypeptidase B1	Homo sapiens	35-39
25789012-15	2015	The CP-A and CP-B groups experienced a similar incidence in the majority of AEs.	aes	76-79	carboxypeptidase B1	Homo sapiens	13-17
25789012-17	2015	The CP-A5, CP-A6 and CP-B7 patients tolerated sorafenib similarly, and derived comparable clinical and survival benefits.	Sorafenib	46-55	carboxypeptidase B1	Homo sapiens	21-26
25601655-8	2015	Hyaluronan increased significantly in the course of the operation in all groups (maximum increases: CPB 1.2-fold, CPB+AC 1.4-fold, CPB+AC+DHCA 1.7-fold, p < 0.05).	Hyaluronic Acid	0-10	carboxypeptidase B1	Homo sapiens	100-105
22785552-12	2013	CONCLUSION: Our study demonstrates that prophylactic intravenous iloprost administration after initiation of a rewarming period during CPB in patients undergoing CABG surgery is associated with improved renal function, compared with conventional treatment in well-hydrated patients.	Iloprost	65-73	carboxypeptidase B1	Homo sapiens	135-138
24478033-7	2014	Treatment with carboxypeptidase B to assess the roles of carboxyl-terminal lysines in cellular receptors leads in most cases to decreases in plasminogen activation as well as plasminogen and apo(a) binding; however, inhibition of plasminogen activation by apo(a) was unaffected.	Lysine	75-82	carboxypeptidase B1	Homo sapiens	15-33
24488729-0	2014	Improved chemical synthesis of hydrophobic Abeta peptides using addition of C-terminal lysines later removed by carboxypeptidase B.	Lysine	87-94	carboxypeptidase B1	Homo sapiens	112-130
24488729-5	2014	These Lys residues are then removed post-purification using immobilized carboxypeptidase B (CPB).	Lysine	6-9	carboxypeptidase B1	Homo sapiens	72-90
24488729-5	2014	These Lys residues are then removed post-purification using immobilized carboxypeptidase B (CPB).	Lysine	6-9	carboxypeptidase B1	Homo sapiens	92-95
24488729-8	2014	Reversible Lys addition with CPB removal should be a generally useful method for making hydrophobic peptides that is applicable to any sequence not ending in Arg or Lys.	Arginine	158-161	carboxypeptidase B1	Homo sapiens	29-32
24488729-8	2014	Reversible Lys addition with CPB removal should be a generally useful method for making hydrophobic peptides that is applicable to any sequence not ending in Arg or Lys.	Lysine	165-168	carboxypeptidase B1	Homo sapiens	29-32
24108209-2	2014	We studied 3-epi-25(OH)D3 cross-reactivity in a competitive protein binding (CPB) assay (Roche Elecsys).	3-epi-25(oh)d3	11-25	carboxypeptidase B1	Homo sapiens	77-80
24108209-5	2014	RESULTS: The CPB assay showed approximately 51% cross-reactivity to 3-epi-25(OH)D3 at exogenous addition.	3-epi-25(oh)d3	68-82	carboxypeptidase B1	Homo sapiens	13-16
24108209-7	2014	CONCLUSIONS: The automated CPB assay displays minimal 3-epi-25(OH)D3 cross-reactivity in samples containing significant concentrations of endogenous 3-epi-25(OH)D3.	3-epi-25(oh)d3	54-68	carboxypeptidase B1	Homo sapiens	27-30
24108209-7	2014	CONCLUSIONS: The automated CPB assay displays minimal 3-epi-25(OH)D3 cross-reactivity in samples containing significant concentrations of endogenous 3-epi-25(OH)D3.	3-epi-25(oh)d3	149-163	carboxypeptidase B1	Homo sapiens	27-30
24094605-8	2014	CONCLUSION: The present data evidence that CPB activity generates fine-mesh fibrin which is more difficult to lyse by tPA, but conversely, CPB and plasmin together can stimulate fibrinolysis, possibly by enhancing plasmin diffusion.	Tetradecanoylphorbol Acetate	118-121	carboxypeptidase B1	Homo sapiens	43-46
23972649-10	2013	Post-CP/CPB levels of phospho-JNK, however, were increased in the 3 groups and were more pronounced in the myocardium of the UDM group (P < .05).	URIDINE-DIPHOSPHATE-METHYLENE-N-ACETYL-GLUCOSAMINE	125-128	carboxypeptidase B1	Homo sapiens	5-11
23972649-13	2013	The post-CP/CPB contractile responses to the thromboxane A2 analog U46619 were significantly impaired in all 3 groups compared with pre-CP/CPB contractile responses.	Thromboxanes	45-56	carboxypeptidase B1	Homo sapiens	9-15
23643001-1	2013	OBJECTIVE: To evaluate the influence of different tranexamic acid administration methods during and after cardiac surgery with cardiopulmonary bypass(CPB) on coagulation function and postoperative bleeding.	Tranexamic Acid	50-65	carboxypeptidase B1	Homo sapiens	150-153
23184394-3	2013	The biological function of this anaphylatoxin is regulated by carboxypeptidase B, a plasma protease that cleaves off the C-terminal arginine yielding C3a desArg, an inactive form.	Arginine	132-140	carboxypeptidase B1	Homo sapiens	62-80
25430617-2	2015	CPB solves various PB equations with an ACG, built from a hierarchical octree decomposition of the computational domain.	acg	40-43	carboxypeptidase B1	Homo sapiens	0-3
24297471-2	2014	Carboxypeptidase-B (CBP-B) was used to selectively remove C-terminal arginine or lysine residues from phosphorylated tryptic/Lys-C peptides prior to their MS/MS analysis by CID with a Paul-type ion trap.	Arginine	69-77	carboxypeptidase B1	Homo sapiens	0-18
24297471-2	2014	Carboxypeptidase-B (CBP-B) was used to selectively remove C-terminal arginine or lysine residues from phosphorylated tryptic/Lys-C peptides prior to their MS/MS analysis by CID with a Paul-type ion trap.	Arginine	69-77	carboxypeptidase B1	Homo sapiens	20-25
24297471-2	2014	Carboxypeptidase-B (CBP-B) was used to selectively remove C-terminal arginine or lysine residues from phosphorylated tryptic/Lys-C peptides prior to their MS/MS analysis by CID with a Paul-type ion trap.	Lysine	81-87	carboxypeptidase B1	Homo sapiens	0-18
24297471-2	2014	Carboxypeptidase-B (CBP-B) was used to selectively remove C-terminal arginine or lysine residues from phosphorylated tryptic/Lys-C peptides prior to their MS/MS analysis by CID with a Paul-type ion trap.	Lysine	81-87	carboxypeptidase B1	Homo sapiens	20-25
24010887-0	2013	Structural basis for inhibition of carboxypeptidase B by selenium-containing inhibitor: selenium coordinates to zinc in enzyme.	Selenium	57-65	carboxypeptidase B1	Homo sapiens	35-53
24010887-0	2013	Structural basis for inhibition of carboxypeptidase B by selenium-containing inhibitor: selenium coordinates to zinc in enzyme.	Selenium	88-96	carboxypeptidase B1	Homo sapiens	35-53
24010887-4	2013	Here we report the crystal structures of potent selenium-, sulfur-, and phosphinic acid-containing inhibitors bound to porcine pancreatic carboxypeptidase B (ppCPB).	Selenium	48-56	carboxypeptidase B1	Homo sapiens	127-156
24010887-4	2013	Here we report the crystal structures of potent selenium-, sulfur-, and phosphinic acid-containing inhibitors bound to porcine pancreatic carboxypeptidase B (ppCPB).	Sulfur	59-65	carboxypeptidase B1	Homo sapiens	127-156
24010887-4	2013	Here we report the crystal structures of potent selenium-, sulfur-, and phosphinic acid-containing inhibitors bound to porcine pancreatic carboxypeptidase B (ppCPB).	Phosphinic Acids	72-87	carboxypeptidase B1	Homo sapiens	127-156
22961629-1	2012	A graphene-nanoparticle (NP) hybrid biosensor that utilizes an electrical hysteresis change to detect the enzymatic activity and concentration of Carboxypeptidase B was developed.	Graphite	2-10	carboxypeptidase B1	Homo sapiens	146-164
22615006-6	2012	In particular, SPR showed that polyamide 9 ((RR) Cp/beta pair) had a 15-fold binding preference for 5"-TGCTCAT-3" over 5"-TGCACAT-3".	Nylons	31-40	carboxypeptidase B1	Homo sapiens	49-56
23044006-14	2012	It formed when the disulfide bonds between A-chain and B-chain of human insulin were cut by beta-mercaptoethanol, followed by cleavage of the B-chain by trypsin and carboxypeptidase B.	Disulfides	19-28	carboxypeptidase B1	Homo sapiens	165-183
22974122-2	2012	Kringle domains bind to lysines in fibrin, and this interaction can be studied by competition with lysine analogs and removal of C-terminal lysines by carboxypeptidase B (CPB).	Lysine	24-31	carboxypeptidase B1	Homo sapiens	151-169
22974122-2	2012	Kringle domains bind to lysines in fibrin, and this interaction can be studied by competition with lysine analogs and removal of C-terminal lysines by carboxypeptidase B (CPB).	Lysine	24-31	carboxypeptidase B1	Homo sapiens	171-174
22974122-2	2012	Kringle domains bind to lysines in fibrin, and this interaction can be studied by competition with lysine analogs and removal of C-terminal lysines by carboxypeptidase B (CPB).	Lysine	24-30	carboxypeptidase B1	Homo sapiens	151-169
22974122-2	2012	Kringle domains bind to lysines in fibrin, and this interaction can be studied by competition with lysine analogs and removal of C-terminal lysines by carboxypeptidase B (CPB).	Lysine	24-30	carboxypeptidase B1	Homo sapiens	171-174
22974122-2	2012	Kringle domains bind to lysines in fibrin, and this interaction can be studied by competition with lysine analogs and removal of C-terminal lysines by carboxypeptidase B (CPB).	Lysine	140-147	carboxypeptidase B1	Homo sapiens	171-174
22946546-7	2012	After 8 weeks of udenafil treatment, the mean 6MWD increased from 315 to 348 m (p = 0.02), and median PASP decreased from 36 to 30 mmHg (p = 0.02).	udenafil	17-25	carboxypeptidase B1	Homo sapiens	102-106
21815623-0	2011	Generation of counter ion radical (Br2( -)) and its reactions in water-in-oil (CTAB or CPB)/n-butanol/cyclohexane/water) microemulsion.	water-in-oil	65-77	carboxypeptidase B1	Homo sapiens	87-90
21445543-12	2011	CONCLUSIONS: Sorafenib efficacy and survival outcomes were worse in patients with CP B function.	Sorafenib	13-22	carboxypeptidase B1	Homo sapiens	82-86
22428577-4	2012	With an increase in temperature, PNIPAM collapsed and enclosed the PCL core, while PAsp penetrated through the PNIPAM shell, leading to the formation of negatively charged PAsp channels on the micelle surface.	poly-N-isopropylacrylamide	111-117	carboxypeptidase B1	Homo sapiens	83-87
22428577-4	2012	With an increase in temperature, PNIPAM collapsed and enclosed the PCL core, while PAsp penetrated through the PNIPAM shell, leading to the formation of negatively charged PAsp channels on the micelle surface.	poly-N-isopropylacrylamide	111-117	carboxypeptidase B1	Homo sapiens	172-176
22721519-3	2012	These drugs have an arterial and venous vasodilator effect during CPB which is dose dependent and is more pronounced for propofol.	Propofol	121-129	carboxypeptidase B1	Homo sapiens	66-69
21883324-9	2011	In the sorafenib group, median OS according to baseline AST was 11.8 (<100 U/L [n = 58]) vs. 3.9 (>=100 U/L [n = 15]) months for CP-A patients (P = 0.127), and 6.5 (<100 U/L [n = 33]) vs. 2.1 (>=100 U/L [n = 21]) months for CP-B patients (P = 0.011).	Sorafenib	7-16	carboxypeptidase B1	Homo sapiens	236-240
21883324-11	2011	CONCLUSIONS: Sorafenib was associated with improved survival in both CP-A and CP-B patients.	Sorafenib	13-22	carboxypeptidase B1	Homo sapiens	78-82
21883324-12	2011	In CP-B patients, baseline AST may be helpful in determining which patients are most likely to benefit from sorafenib.	Sorafenib	108-117	carboxypeptidase B1	Homo sapiens	3-7
21815623-0	2011	Generation of counter ion radical (Br2( -)) and its reactions in water-in-oil (CTAB or CPB)/n-butanol/cyclohexane/water) microemulsion.	1-Butanol	92-101	carboxypeptidase B1	Homo sapiens	87-90
21815623-0	2011	Generation of counter ion radical (Br2( -)) and its reactions in water-in-oil (CTAB or CPB)/n-butanol/cyclohexane/water) microemulsion.	Water	65-70	carboxypeptidase B1	Homo sapiens	87-90
21815623-5	2011	Interestingly another species, dibromide radical anion (Br(2)( -)) in CTAB and CPB microemulsions have been observed after the electron beam irradiation.	dibromide radical anion	31-54	carboxypeptidase B1	Homo sapiens	79-82
21815623-5	2011	Interestingly another species, dibromide radical anion (Br(2)( -)) in CTAB and CPB microemulsions have been observed after the electron beam irradiation.	Bromine	56-62	carboxypeptidase B1	Homo sapiens	79-82
21815623-6	2011	Assuming that the extinction coefficient of the radicals is the same as that in the aqueous solution, the yields of the radicals per 100 eV are 0.29 and 0.48 for the Br(2)( -) radical in CTAB and CPB containing microemulsions (W(0) = 40), respectively, under N(2)O saturated conditions.	br(2)( -) radical	166-183	carboxypeptidase B1	Homo sapiens	196-199
21815623-6	2011	Assuming that the extinction coefficient of the radicals is the same as that in the aqueous solution, the yields of the radicals per 100 eV are 0.29 and 0.48 for the Br(2)( -) radical in CTAB and CPB containing microemulsions (W(0) = 40), respectively, under N(2)O saturated conditions.	Nitrous Oxide	259-264	carboxypeptidase B1	Homo sapiens	196-199
21098023-1	2011	Human digestive carboxypeptidases CPA1, CPA2, and CPB1 are secreted by the pancreas as inactive proenzymes containing a 94-96-amino acid-long propeptide.	propeptide	142-152	carboxypeptidase B1	Homo sapiens	50-54
21536417-1	2011	A novel zwitterionic polypeptide derivative, denoted as His-PAsp/PAsp, was successfully synthesized by amidation of Poly (alpha,beta-L-aspartic acid) with L-histidine methyl ester.	poly (alpha,beta-l-aspartic acid)	116-149	carboxypeptidase B1	Homo sapiens	60-64
21536417-1	2011	A novel zwitterionic polypeptide derivative, denoted as His-PAsp/PAsp, was successfully synthesized by amidation of Poly (alpha,beta-L-aspartic acid) with L-histidine methyl ester.	poly (alpha,beta-l-aspartic acid)	116-149	carboxypeptidase B1	Homo sapiens	65-69
21536417-1	2011	A novel zwitterionic polypeptide derivative, denoted as His-PAsp/PAsp, was successfully synthesized by amidation of Poly (alpha,beta-L-aspartic acid) with L-histidine methyl ester.	histidine methyl ester	155-179	carboxypeptidase B1	Homo sapiens	60-64
21536417-1	2011	A novel zwitterionic polypeptide derivative, denoted as His-PAsp/PAsp, was successfully synthesized by amidation of Poly (alpha,beta-L-aspartic acid) with L-histidine methyl ester.	histidine methyl ester	155-179	carboxypeptidase B1	Homo sapiens	65-69
21536417-2	2011	Turbidity, zeta potential and 1H NMR measurements were used to study the aggregation behaviors of His-PAsp/PAsp under different pH values.	Histidine	98-101	carboxypeptidase B1	Homo sapiens	102-106
21536417-2	2011	Turbidity, zeta potential and 1H NMR measurements were used to study the aggregation behaviors of His-PAsp/PAsp under different pH values.	Histidine	98-101	carboxypeptidase B1	Homo sapiens	107-111
21078768-2	2011	The aim of this retrospective, observational study was to evaluate the effects of peri-operative glucose levels on adverse events in infants receiving open-heart surgery with CPB.	Glucose	97-104	carboxypeptidase B1	Homo sapiens	175-178
21098023-3	2011	Here, we demonstrate that subsequent cleavage of the propeptide by chymotrypsin C (CTRC) induces a nearly 10-fold increase in the activity of trypsin-activated CPA1 and CPA2, whereas CPB1 activity is unaffected.	propeptide	53-63	carboxypeptidase B1	Homo sapiens	183-187
20596557-1	2010	Construction of a 3-D supramolecular network from [Ln(cpb)(3)(H(2)O)(2)] (Ln = Nd, Tb; Hcpb = 1-(4-cyanophenyl)-1,3-butanedione) by sequential displacement of a coordinated water by DMF, dimerisation by reciprocal hydrogen bonding in solution and pi-pi stacking and interdigitation of nitriles has been monitored by in situ fourier transform infrared spectroscopy.	Terbium	83-85	carboxypeptidase B1	Homo sapiens	54-57
22097017-2	2011	Aminobenzenesulfonic acid (ABSA) was introduced at different mole ratio to PSI to generate polyaspartic acid (abridged as PASP)/ABSA graft copolymer.	Sulfanilic Acids	0-25	carboxypeptidase B1	Homo sapiens	122-126
22097017-2	2011	Aminobenzenesulfonic acid (ABSA) was introduced at different mole ratio to PSI to generate polyaspartic acid (abridged as PASP)/ABSA graft copolymer.	Sulfanilic Acids	27-31	carboxypeptidase B1	Homo sapiens	122-126
22097017-2	2011	Aminobenzenesulfonic acid (ABSA) was introduced at different mole ratio to PSI to generate polyaspartic acid (abridged as PASP)/ABSA graft copolymer.	polyaspartate	91-108	carboxypeptidase B1	Homo sapiens	122-126
22097017-3	2011	The scale inhibition behavior of resultant PASP/ABSA copolymer was evaluated by using static scale inhibition method.	absa copolymer	48-62	carboxypeptidase B1	Homo sapiens	43-47
22097017-6	2011	It was found that PASP/ABSA copolymer was able to efficiently inhibit CaCO3 and Ca3(PO4)2 scales and had good corrosion inhibition ability as well, and it also had good dispersion ability for Fe2O3.	absa copolymer	23-37	carboxypeptidase B1	Homo sapiens	18-22
22097017-6	2011	It was found that PASP/ABSA copolymer was able to efficiently inhibit CaCO3 and Ca3(PO4)2 scales and had good corrosion inhibition ability as well, and it also had good dispersion ability for Fe2O3.	Calcium Carbonate	70-75	carboxypeptidase B1	Homo sapiens	18-22
22097017-6	2011	It was found that PASP/ABSA copolymer was able to efficiently inhibit CaCO3 and Ca3(PO4)2 scales and had good corrosion inhibition ability as well, and it also had good dispersion ability for Fe2O3.	beta-tricalcium phosphate	80-89	carboxypeptidase B1	Homo sapiens	18-22
22097017-6	2011	It was found that PASP/ABSA copolymer was able to efficiently inhibit CaCO3 and Ca3(PO4)2 scales and had good corrosion inhibition ability as well, and it also had good dispersion ability for Fe2O3.	Iron(III) oxide	192-197	carboxypeptidase B1	Homo sapiens	18-22
22097017-7	2011	Besides, the inhibition efficiency of PASP/ABSA against CaCO3 and Ca3(PO4)2 scales and its dispersion capacity for Fe2O3 was highly dependent on dosage.	Calcium Carbonate	56-61	carboxypeptidase B1	Homo sapiens	38-42
22097017-7	2011	Besides, the inhibition efficiency of PASP/ABSA against CaCO3 and Ca3(PO4)2 scales and its dispersion capacity for Fe2O3 was highly dependent on dosage.	beta-tricalcium phosphate	66-75	carboxypeptidase B1	Homo sapiens	38-42
22097017-7	2011	Besides, the inhibition efficiency of PASP/ABSA against CaCO3 and Ca3(PO4)2 scales and its dispersion capacity for Fe2O3 was highly dependent on dosage.	Iron(III) oxide	115-120	carboxypeptidase B1	Homo sapiens	38-42
22097017-8	2011	The reason may lie in that PASP/ABSA copolymer simultaneously possesses carboxylic ion and sulfonic group which can chelate Ca2+ to form stabilized and dissoluble chelates, resulting in increase of solubility of calcium salts in water.	absa copolymer	32-46	carboxypeptidase B1	Homo sapiens	27-31
22097017-8	2011	The reason may lie in that PASP/ABSA copolymer simultaneously possesses carboxylic ion and sulfonic group which can chelate Ca2+ to form stabilized and dissoluble chelates, resulting in increase of solubility of calcium salts in water.	calcium salts	212-225	carboxypeptidase B1	Homo sapiens	27-31
22097017-8	2011	The reason may lie in that PASP/ABSA copolymer simultaneously possesses carboxylic ion and sulfonic group which can chelate Ca2+ to form stabilized and dissoluble chelates, resulting in increase of solubility of calcium salts in water.	Water	229-234	carboxypeptidase B1	Homo sapiens	27-31
22097017-9	2011	Also it may lie in that the introduction of acidic hydrophilic sulfonic group with a strong electrolytic capacity into PASP molecule simultaneously enhances the dispersion of the inhibitor molecules and hinders the formation of Ca3(PO4)2 scale.	beta-tricalcium phosphate	228-237	carboxypeptidase B1	Homo sapiens	119-123
20596557-1	2010	Construction of a 3-D supramolecular network from [Ln(cpb)(3)(H(2)O)(2)] (Ln = Nd, Tb; Hcpb = 1-(4-cyanophenyl)-1,3-butanedione) by sequential displacement of a coordinated water by DMF, dimerisation by reciprocal hydrogen bonding in solution and pi-pi stacking and interdigitation of nitriles has been monitored by in situ fourier transform infrared spectroscopy.	Dimethylformamide	182-185	carboxypeptidase B1	Homo sapiens	54-57
20596557-1	2010	Construction of a 3-D supramolecular network from [Ln(cpb)(3)(H(2)O)(2)] (Ln = Nd, Tb; Hcpb = 1-(4-cyanophenyl)-1,3-butanedione) by sequential displacement of a coordinated water by DMF, dimerisation by reciprocal hydrogen bonding in solution and pi-pi stacking and interdigitation of nitriles has been monitored by in situ fourier transform infrared spectroscopy.	Hydrogen	214-222	carboxypeptidase B1	Homo sapiens	54-57
20596557-1	2010	Construction of a 3-D supramolecular network from [Ln(cpb)(3)(H(2)O)(2)] (Ln = Nd, Tb; Hcpb = 1-(4-cyanophenyl)-1,3-butanedione) by sequential displacement of a coordinated water by DMF, dimerisation by reciprocal hydrogen bonding in solution and pi-pi stacking and interdigitation of nitriles has been monitored by in situ fourier transform infrared spectroscopy.	hcpb	87-91	carboxypeptidase B1	Homo sapiens	54-57
20596557-1	2010	Construction of a 3-D supramolecular network from [Ln(cpb)(3)(H(2)O)(2)] (Ln = Nd, Tb; Hcpb = 1-(4-cyanophenyl)-1,3-butanedione) by sequential displacement of a coordinated water by DMF, dimerisation by reciprocal hydrogen bonding in solution and pi-pi stacking and interdigitation of nitriles has been monitored by in situ fourier transform infrared spectroscopy.	)-1,3-butanedione	110-127	carboxypeptidase B1	Homo sapiens	54-57
20596557-1	2010	Construction of a 3-D supramolecular network from [Ln(cpb)(3)(H(2)O)(2)] (Ln = Nd, Tb; Hcpb = 1-(4-cyanophenyl)-1,3-butanedione) by sequential displacement of a coordinated water by DMF, dimerisation by reciprocal hydrogen bonding in solution and pi-pi stacking and interdigitation of nitriles has been monitored by in situ fourier transform infrared spectroscopy.	Water	173-178	carboxypeptidase B1	Homo sapiens	54-57
20158262-1	2010	A novel boron complex bearing a pyrene ligand (CPB) was synthesized and introduced as the first example of a binuclear boron complex in organic light-emitting diodes.	Boron	8-13	carboxypeptidase B1	Homo sapiens	47-50
20359509-0	2010	Introduction of stearoyl moieties into a biocompatible cationic polyaspartamide derivative, PAsp(DET), with endosomal escaping function for enhanced siRNA-mediated gene knockdown.	stearoyl	16-24	carboxypeptidase B1	Homo sapiens	92-96
20359509-0	2010	Introduction of stearoyl moieties into a biocompatible cationic polyaspartamide derivative, PAsp(DET), with endosomal escaping function for enhanced siRNA-mediated gene knockdown.	polyaspartamide	64-79	carboxypeptidase B1	Homo sapiens	92-96
20359509-2	2010	Previously, a cationic polyaspartamide derivative, poly{N-[N-(2-aminoethyl)-2-aminoethyl]aspartamide} (PAsp(DET)), was reported to exert high transfection efficacy for plasmid DNA with negligible cytotoxicity.	polyaspartamide	23-38	carboxypeptidase B1	Homo sapiens	103-107
20359509-2	2010	Previously, a cationic polyaspartamide derivative, poly{N-[N-(2-aminoethyl)-2-aminoethyl]aspartamide} (PAsp(DET)), was reported to exert high transfection efficacy for plasmid DNA with negligible cytotoxicity.	poly{n-[n-(2-aminoethyl)-2-aminoethyl]aspartamide	51-100	carboxypeptidase B1	Homo sapiens	103-107
20359509-4	2010	In this study, to overcome such instability, stearic acid as a hydrophobic moiety was conjugated to the side chain of PAsp(DET) with various substitution degrees.	stearic acid	45-57	carboxypeptidase B1	Homo sapiens	118-122
20158262-1	2010	A novel boron complex bearing a pyrene ligand (CPB) was synthesized and introduced as the first example of a binuclear boron complex in organic light-emitting diodes.	pyrene	32-38	carboxypeptidase B1	Homo sapiens	47-50
20158262-1	2010	A novel boron complex bearing a pyrene ligand (CPB) was synthesized and introduced as the first example of a binuclear boron complex in organic light-emitting diodes.	Boron	119-124	carboxypeptidase B1	Homo sapiens	47-50
19790060-3	2009	Thrombin-activatable carboxypeptidase B (CPB), also called thrombin-activatable fibrinolysis inhibitor, removes the C-terminal arginine from OPN-R, generating OPN-L and abrogating its enhanced cell binding.	Arginine	127-135	carboxypeptidase B1	Homo sapiens	21-39
19802820-3	2010	The present structure shows unbound PCPB in a distinct molecular packing as compared to the previous benzamidine complexed form.	benzamidine	101-112	carboxypeptidase B1	Homo sapiens	36-40
19524625-4	2009	We developed here block copolymer-coated magnetite nanoparticles for pancreatic cancer imaging, by means of a chelation between the carboxylic acid groups in poly(ethylene glycol)-poly(aspartic acid) block copolymer (PEG-PAsp) and Fe on the surface of the iron oxide nanoparticles.	copolymer	24-33	carboxypeptidase B1	Homo sapiens	221-225
19524625-4	2009	We developed here block copolymer-coated magnetite nanoparticles for pancreatic cancer imaging, by means of a chelation between the carboxylic acid groups in poly(ethylene glycol)-poly(aspartic acid) block copolymer (PEG-PAsp) and Fe on the surface of the iron oxide nanoparticles.	Ferrosoferric Oxide	41-50	carboxypeptidase B1	Homo sapiens	221-225
19524625-6	2009	The PEG-PAsp-coated nanoparticles were further shown to be potent as a contrast agent for enhanced MRI for an experimental pancreatic cancer, xenografts of the human-derived BxPC3 cell line in BALB/c nude mice, with combined administration of TGF-beta inhibitor.	Polyethylene Glycols	4-7	carboxypeptidase B1	Homo sapiens	8-12
19524625-8	2009	Use of the PEG-PAsp-coated magnetite nanoparticles, combined with the TGF-beta inhibitor, is of promising clinical importance for the detection of intractable solid cancers, including pancreatic cancer.	Polyethylene Glycols	11-14	carboxypeptidase B1	Homo sapiens	15-19
19790060-3	2009	Thrombin-activatable carboxypeptidase B (CPB), also called thrombin-activatable fibrinolysis inhibitor, removes the C-terminal arginine from OPN-R, generating OPN-L and abrogating its enhanced cell binding.	Arginine	127-135	carboxypeptidase B1	Homo sapiens	41-44
19589537-6	2009	Successful templating of silica hollow spheres is demonstrated in both HFDPC/SPFO and CPB/SPFO vesicle systems, using tetramethoxysilane (TMOS) as the silica precursor for the acid-catalyzed synthesis.	Silicon Dioxide	25-31	carboxypeptidase B1	Homo sapiens	86-94
19589537-9	2009	At the conditions investigated (TMOS/surfactant weight ratios of 0.25-1.0, pH 3), the colloidal silica particles templated from fluorinated HFDPC/SPFO vesicles are more stable than the particles templated from the corresponding mixed fluorinated CPB/SPFO system.	Silicon Dioxide	96-102	carboxypeptidase B1	Homo sapiens	246-254
19466793-5	2009	Our results show that cationic surfactants (CTAB, TTAB, and CPB) favor the formation of nanorods of copper oxalate.	Copper oxalate	100-114	carboxypeptidase B1	Homo sapiens	60-63
19717511-4	2009	CPB1 tyrosine nitration and loss of activity by the concerted action of NOS-3 and XO were also confirmed in vitro using both the NO donor 3-morpholinosydnonimine and peroxynitrite.	Tyrosine	5-13	carboxypeptidase B1	Homo sapiens	0-4
19717511-4	2009	CPB1 tyrosine nitration and loss of activity by the concerted action of NOS-3 and XO were also confirmed in vitro using both the NO donor 3-morpholinosydnonimine and peroxynitrite.	linsidomine	138-161	carboxypeptidase B1	Homo sapiens	0-4
19717511-4	2009	CPB1 tyrosine nitration and loss of activity by the concerted action of NOS-3 and XO were also confirmed in vitro using both the NO donor 3-morpholinosydnonimine and peroxynitrite.	Peroxynitrous Acid	166-179	carboxypeptidase B1	Homo sapiens	0-4
19386397-3	2009	Among various compounds displaying K(i) values in the low micromolar range, N-(3-chlorophenyl)-4-((5-(3-methoxybenzylthio)-1,3,4-oxadiazol-2-yl)methyl)thiazol-2-amine emerged as the most powerful inhibitor for human carboxypeptidase B (CPB).	CHEMBL552336	76-166	carboxypeptidase B1	Homo sapiens	216-234
19386397-3	2009	Among various compounds displaying K(i) values in the low micromolar range, N-(3-chlorophenyl)-4-((5-(3-methoxybenzylthio)-1,3,4-oxadiazol-2-yl)methyl)thiazol-2-amine emerged as the most powerful inhibitor for human carboxypeptidase B (CPB).	CHEMBL552336	76-166	carboxypeptidase B1	Homo sapiens	236-239
19386397-4	2009	According to molecular docking, this compound fits into CPB active site cleft through coordination of the catalytic zinc ion with the 1,3,4-oxadiazole moiety.	1,3,4-oxadiazole	134-150	carboxypeptidase B1	Homo sapiens	56-59
19010784-3	2009	We discovered that plasma carboxypeptidase N (CPN) and B (CPB or activated thrombin-activable fibrinolysis inhibitor, TAFIa) enhanced the bioactivity of 10-mer chemerin peptide NH(2)-YFPGQFAFSK-COOH by removing the carboxyl-terminal lysine (K).	Carbonic Acid	194-198	carboxypeptidase B1	Homo sapiens	58-61
19010784-3	2009	We discovered that plasma carboxypeptidase N (CPN) and B (CPB or activated thrombin-activable fibrinolysis inhibitor, TAFIa) enhanced the bioactivity of 10-mer chemerin peptide NH(2)-YFPGQFAFSK-COOH by removing the carboxyl-terminal lysine (K).	Lysine	233-239	carboxypeptidase B1	Homo sapiens	58-61
19131697-3	2008	By culturing of Pichia transformant on methanol medium, the human proCPB was successfully expressed and secreted into the culture supernatant.	Methanol	39-47	carboxypeptidase B1	Homo sapiens	66-72
19006313-1	2008	Polyplexes assembled from poly(aspartamide) derivatives bearing 1,2-diaminoethane side chains, [PAsp(DET)] display amplified in vitro and in vivo transfection activity with minimal cytotoxicity.	poly(aspartamide)	26-43	carboxypeptidase B1	Homo sapiens	96-100
19006313-1	2008	Polyplexes assembled from poly(aspartamide) derivatives bearing 1,2-diaminoethane side chains, [PAsp(DET)] display amplified in vitro and in vivo transfection activity with minimal cytotoxicity.	ethylenediamine	64-81	carboxypeptidase B1	Homo sapiens	96-100
19006313-8	2008	Apparently, the pH-selective membrane destabilization profile of PAsp(DET) corresponded to a protonation change in the flanking diamine unit, i.e., the monoprotonated gauche form at physiological pH and diprotonated anti form at acidic pH.	Diamines	128-135	carboxypeptidase B1	Homo sapiens	65-69
18396051-5	2008	Thus, from the analysis of their activity against the prototypical metallocarboxypeptidases A and B (CPA and CPB), we have observed that hydrophobic phosphorylated oxiranes perform better as CPB inhibitors, reaching K(i) values comparable to classical synthetic carboxypeptidase inhibitors.	Epoxy Compounds	164-172	carboxypeptidase B1	Homo sapiens	109-112
18394639-1	2008	We report on a series of polyion complexes from mixtures of poly(ethylene oxide)-block-poly(N,N-diethylaminoethylmethacrylate) (PEO-PDEAMA) and poly(ethylene oxide)-block-poly(aspartic acid) (PEO-PAsp).	polyion	25-32	carboxypeptidase B1	Homo sapiens	196-200
17296336-6	2007	In contrast, sample treatment by carboxypeptidase B, removing the carboxy-terminal lysine residues from the two heavy chains of the antibody, resulted in reduced charge heterogeneity eliminating the two most basic bands observed in IEF.	Lysine	83-89	carboxypeptidase B1	Homo sapiens	33-51
18788219-8	2008	Total fluid need during 120 min CPB was reduced by 60% when hypertonic saline/hydroxyethyl starch solution was added to the CPB prime (p < 0.01).	Sodium Chloride	71-77	carboxypeptidase B1	Homo sapiens	32-35
18788219-8	2008	Total fluid need during 120 min CPB was reduced by 60% when hypertonic saline/hydroxyethyl starch solution was added to the CPB prime (p < 0.01).	Sodium Chloride	71-77	carboxypeptidase B1	Homo sapiens	124-127
18788219-8	2008	Total fluid need during 120 min CPB was reduced by 60% when hypertonic saline/hydroxyethyl starch solution was added to the CPB prime (p < 0.01).	Hydroxyethyl starch	78-97	carboxypeptidase B1	Homo sapiens	32-35
17689692-9	2007	CP/CPB diminished contractile responses to phenylephrine in coronary and skeletal samples.	Phenylephrine	43-56	carboxypeptidase B1	Homo sapiens	0-6
17499999-11	2007	CONCLUSION(S): A single dose of PTX prior to CPB was able to reduce plasma levels of TNFalpha.	Pentoxifylline	32-35	carboxypeptidase B1	Homo sapiens	45-48
18222087-0	2008	Lysianadioic acid, a carboxypeptidase B inhibitor from Lysiana subfalcata.	lysianadioic acid	0-17	carboxypeptidase B1	Homo sapiens	21-39
18222087-1	2008	A new natural product, lysianadioic acid, was isolated from the plant Lysiana subfalcata as a carboxypeptidase B (CPB) inhibitor.	lysianadioic acid	23-40	carboxypeptidase B1	Homo sapiens	94-112
18222087-1	2008	A new natural product, lysianadioic acid, was isolated from the plant Lysiana subfalcata as a carboxypeptidase B (CPB) inhibitor.	lysianadioic acid	23-40	carboxypeptidase B1	Homo sapiens	114-117
17986743-6	2007	MEGX concentration at 60 min was significantly higher in healthy volunteers (131.2 ng/mL) as compared to patients with cirrhosis (CP A - 51.3 ng/mL; CP B - 37.1 ng/mL; CP C - 17.3 ng/mL).	monoethylglycinexylidide	0-4	carboxypeptidase B1	Homo sapiens	149-153
17243818-2	2007	Here, we provide a quantitative assessment of the relative strengths of hydrogen bonds involving phosphorylated amino acid side chains (pSer, pAsp) with several common donors (Arg, Lys, and backbone amide groups).	Hydrogen	72-80	carboxypeptidase B1	Homo sapiens	142-146
17189688-2	2007	Three series of cyclic arginine and lysine mimetic inhibitors vary significantly in their selectivity against other human basic carboxypeptidases, carboxypeptidase N and carboxypeptidase B.	cyclic arginine	16-31	carboxypeptidase B1	Homo sapiens	170-188
17189688-2	2007	Three series of cyclic arginine and lysine mimetic inhibitors vary significantly in their selectivity against other human basic carboxypeptidases, carboxypeptidase N and carboxypeptidase B.	Lysine	36-42	carboxypeptidase B1	Homo sapiens	170-188
17289481-1	2007	OBJECTIVE: To investigate the relationship between arterial carbon dioxide (PaCO(2)) and mean expired pump CO(2) during cardiopulmonary bypass (PeCPBCO(2)) in patients undergoing cardiac surgery with CPB during steady state, cooling, and rewarming phases of CPB.	Carbon Dioxide	60-74	carboxypeptidase B1	Homo sapiens	146-149
17289481-1	2007	OBJECTIVE: To investigate the relationship between arterial carbon dioxide (PaCO(2)) and mean expired pump CO(2) during cardiopulmonary bypass (PeCPBCO(2)) in patients undergoing cardiac surgery with CPB during steady state, cooling, and rewarming phases of CPB.	Carbon Dioxide	78-83	carboxypeptidase B1	Homo sapiens	146-149
17289481-15	2007	The arterial CO(2) +/- x mmHg can be predicted by the formula PaCPBCO(2) = (-2.17x + 69.2) + PeCPBCO(2), where x is temperature in degrees C. CONCLUSIONS: Monitoring the mean expired CO(2) value from the CPB oxygenator exhaust scavenging port with a capnography monitor provides a continuous and noninvasive data source to aid in sweep flow CPB circuit management during CPB.	Carbon Dioxide	13-18	carboxypeptidase B1	Homo sapiens	64-67
17289481-15	2007	The arterial CO(2) +/- x mmHg can be predicted by the formula PaCPBCO(2) = (-2.17x + 69.2) + PeCPBCO(2), where x is temperature in degrees C. CONCLUSIONS: Monitoring the mean expired CO(2) value from the CPB oxygenator exhaust scavenging port with a capnography monitor provides a continuous and noninvasive data source to aid in sweep flow CPB circuit management during CPB.	Carbon Dioxide	13-18	carboxypeptidase B1	Homo sapiens	95-98
17289481-15	2007	The arterial CO(2) +/- x mmHg can be predicted by the formula PaCPBCO(2) = (-2.17x + 69.2) + PeCPBCO(2), where x is temperature in degrees C. CONCLUSIONS: Monitoring the mean expired CO(2) value from the CPB oxygenator exhaust scavenging port with a capnography monitor provides a continuous and noninvasive data source to aid in sweep flow CPB circuit management during CPB.	Carbon Dioxide	13-18	carboxypeptidase B1	Homo sapiens	95-98
17289481-15	2007	The arterial CO(2) +/- x mmHg can be predicted by the formula PaCPBCO(2) = (-2.17x + 69.2) + PeCPBCO(2), where x is temperature in degrees C. CONCLUSIONS: Monitoring the mean expired CO(2) value from the CPB oxygenator exhaust scavenging port with a capnography monitor provides a continuous and noninvasive data source to aid in sweep flow CPB circuit management during CPB.	Carbon Dioxide	67-72	carboxypeptidase B1	Homo sapiens	95-98
17289481-15	2007	The arterial CO(2) +/- x mmHg can be predicted by the formula PaCPBCO(2) = (-2.17x + 69.2) + PeCPBCO(2), where x is temperature in degrees C. CONCLUSIONS: Monitoring the mean expired CO(2) value from the CPB oxygenator exhaust scavenging port with a capnography monitor provides a continuous and noninvasive data source to aid in sweep flow CPB circuit management during CPB.	Carbon Dioxide	67-72	carboxypeptidase B1	Homo sapiens	95-98
17456696-0	2007	Methylene blue for CPB.	Methylene Blue	0-14	carboxypeptidase B1	Homo sapiens	19-22
17243818-7	2007	A pSer hydrogen-bond acceptor tends to form more stable interactions than a pAsp acceptor.	Hydrogen	7-15	carboxypeptidase B1	Homo sapiens	76-80
17243818-8	2007	The effect of phosphate protonation state on the strengths of the hydrogen bonds is remarkably subtle, with a more pronounced effect on pAsp than on pSer.	Phosphates	14-23	carboxypeptidase B1	Homo sapiens	136-140
17243818-8	2007	The effect of phosphate protonation state on the strengths of the hydrogen bonds is remarkably subtle, with a more pronounced effect on pAsp than on pSer.	Hydrogen	66-74	carboxypeptidase B1	Homo sapiens	136-140
16963025-3	2006	Experiments carried out on carboxypeptidase B in the absence of substrate and in the presence of saturating concentrations of hippuryl-Arg result in HDX kinetics that are indistinguishable.	hippuryl-L-arginine	126-138	carboxypeptidase B1	Homo sapiens	27-45
17167091-8	2006	Carboxypeptidase B treatment decreased cell-dependent plasminogen activation by approximately 90%, suggesting that the binding of plasminogen to proteins exposing C-terminal lysines on the cell surface is required to promote plasminogen activation.	Lysine	174-181	carboxypeptidase B1	Homo sapiens	0-18
15982000-0	2005	Crystal structures of potent thiol-based inhibitors bound to carboxypeptidase B.	Sulfhydryl Compounds	29-34	carboxypeptidase B1	Homo sapiens	61-79
16939115-5	2006	Cardiac surgery with or without CPB is associated with increased tissue oxygen demands, particularly by the splanchnic bed.	Oxygen	72-78	carboxypeptidase B1	Homo sapiens	32-35
16939115-6	2006	The disparity in general and regional oxygen supply and demand results in the development of mucosal hypoxia and this cannot be attributed to CPB alone.	Oxygen	38-44	carboxypeptidase B1	Homo sapiens	142-145
15917233-3	2005	The cap is subsequently removed with carboxypeptidase B to yield mature biologically active ISG15 capable of stoichiometric ATP-dependent thiolester formation with its human UbE1L activating enzyme.	Adenosine Triphosphate	124-127	carboxypeptidase B1	Homo sapiens	37-55
16339296-8	2006	The processing of procarboxypeptidase B to its mature form also demonstrated a requirement for ATP and cytosol.	Adenosine Triphosphate	95-98	carboxypeptidase B1	Homo sapiens	18-39
16255955-7	2005	(4) AECOPD with pulmonary hypertension pulmonary artery systolic pressure (PASP) > or = 35 mm Hg (1 mm Hg = 0.133 kPa) showed a lower serum H(2)S level [(26.3 +/- 2.2), (36.2 +/- 2.5) micromol/L, P < 0.05] than that with a normal resting PASP.	Hydrogen Sulfide	143-148	carboxypeptidase B1	Homo sapiens	75-79
16255955-7	2005	(4) AECOPD with pulmonary hypertension pulmonary artery systolic pressure (PASP) > or = 35 mm Hg (1 mm Hg = 0.133 kPa) showed a lower serum H(2)S level [(26.3 +/- 2.2), (36.2 +/- 2.5) micromol/L, P < 0.05] than that with a normal resting PASP.	Hydrogen Sulfide	143-148	carboxypeptidase B1	Homo sapiens	244-248
15982000-1	2005	This paper presents the crystal structure of porcine pancreatic carboxypeptidase B (pp-CpB) in complex with a variety of thiol-based inhibitors that were developed as antagonists of activated thrombin-activatable fibrinolysis inhibitor (TAFIa).	Sulfhydryl Compounds	121-126	carboxypeptidase B1	Homo sapiens	53-82
16026053-1	2005	BACKGROUND: Previous studies suggest that normothermic cardiopulmonary bypass(CPB) impairs cerebral oxygen balance.	Oxygen	100-106	carboxypeptidase B1	Homo sapiens	78-81
16026053-2	2005	We studied the effect of normothermic CPB on cerebral oxygen balance evaluated by continuous measurement of oxygen saturation in the jugular vein (SjO2).	Oxygen	54-60	carboxypeptidase B1	Homo sapiens	38-41
16833611-5	2005	For example, the calculated atomic electronegativities show a uniform decrease from C to Pb increasing again to Uuq as verified in the experimental data for C-Pb but at variance with several other scales.	Carbon	84-85	carboxypeptidase B1	Homo sapiens	157-161
15946220-8	2005	Therefore, we constructed, expressed and characterized a TAFI mutant in which Ile182 and Ile183 were changed into the residues found in pancreas carboxypeptidase B at corresponding positions, Arg and Glu.	Arginine	192-195	carboxypeptidase B1	Homo sapiens	145-163
15946220-8	2005	Therefore, we constructed, expressed and characterized a TAFI mutant in which Ile182 and Ile183 were changed into the residues found in pancreas carboxypeptidase B at corresponding positions, Arg and Glu.	Glutamic Acid	200-203	carboxypeptidase B1	Homo sapiens	145-163
16833611-5	2005	For example, the calculated atomic electronegativities show a uniform decrease from C to Pb increasing again to Uuq as verified in the experimental data for C-Pb but at variance with several other scales.	Lead	89-91	carboxypeptidase B1	Homo sapiens	157-161
16833611-5	2005	For example, the calculated atomic electronegativities show a uniform decrease from C to Pb increasing again to Uuq as verified in the experimental data for C-Pb but at variance with several other scales.	uuq	112-115	carboxypeptidase B1	Homo sapiens	157-161
14580393-3	2003	Detroit 562 cells preferentially bound to Lys-plasminogen and this binding was inhibited in the presence of a lysine analog, epsilon-aminocaproic acid and by carboxypeptidase-B treatment suggesting that the C-terminal lysine residue of the putative pharyngeal cell receptor(s) may play an important role in plasminogen-binding.	Lysine	218-224	carboxypeptidase B1	Homo sapiens	158-176
15894352-4	2005	In some experiments the platelets were digested with carboxypeptidase B to remove C-lysines.	c-lysines	82-91	carboxypeptidase B1	Homo sapiens	53-71
14715654-1	2004	Activated thrombin-activable fibrinolysis inhibitor (TAFIa) is a carboxypeptidase B-like plasma enzyme that can slow clot lysis by removing lysine residues exposed on fibrin as it is cleaved by plasmin.	Lysine	140-146	carboxypeptidase B1	Homo sapiens	65-83
12799375-5	2003	Although the thrombin/thrombomodulin complex activated all the mutants, carboxypeptidase B activity of the activated mutants against hippuryl-arginine was reduced.	hippuryl-arginine	133-150	carboxypeptidase B1	Homo sapiens	72-90
12729605-2	2003	The enzyme substrate (biotin-RYRGLMVGGVVR-OH) is cleaved by CPB at the C terminus, causing release of the C-terminal Arg residue.	Biotin	22-28	carboxypeptidase B1	Homo sapiens	60-63
12729605-2	2003	The enzyme substrate (biotin-RYRGLMVGGVVR-OH) is cleaved by CPB at the C terminus, causing release of the C-terminal Arg residue.	ryrglmvggvvr-oh	29-44	carboxypeptidase B1	Homo sapiens	60-63
12729605-2	2003	The enzyme substrate (biotin-RYRGLMVGGVVR-OH) is cleaved by CPB at the C terminus, causing release of the C-terminal Arg residue.	Arginine	117-120	carboxypeptidase B1	Homo sapiens	60-63
12073205-1	2002	OBJECTIVE: To evaluate whether the deleterious effect of cardiopulmonary bypass (CPB) can be prevented by controlling PaO(2) in cyanotic children.	pao(2)	118-124	carboxypeptidase B1	Homo sapiens	81-84
12217710-1	2002	OBJECTIVE: The present study was designed to analyze vancomycin disposition in adult patients undergoing coronary bypass grafting during and following cardiopulmonary bypass (CPB).	Vancomycin	53-63	carboxypeptidase B1	Homo sapiens	175-178
12217710-5	2002	The mean (SD) vancomycin clearance by the CPB machine was 9.51 (2.66) l/h, and the mean (SD) total vancomycin sequestrated by CPB was 331.7 (84) mg. A significant difference (6.3%; p = 0.001) was measured between the mean measured AUC during CPB (1088.1 +/- 253.9) and the same calculated parameter (1160.2 +/- 282).	Vancomycin	99-109	carboxypeptidase B1	Homo sapiens	126-129
12217710-5	2002	The mean (SD) vancomycin clearance by the CPB machine was 9.51 (2.66) l/h, and the mean (SD) total vancomycin sequestrated by CPB was 331.7 (84) mg. A significant difference (6.3%; p = 0.001) was measured between the mean measured AUC during CPB (1088.1 +/- 253.9) and the same calculated parameter (1160.2 +/- 282).	Vancomycin	99-109	carboxypeptidase B1	Homo sapiens	126-129
12217710-6	2002	Five minutes after starting CPB, a decrease in vancomycin level was detected; this difference was found to be nearly 11% in absolute values.	Vancomycin	47-57	carboxypeptidase B1	Homo sapiens	28-31
12217710-7	2002	CONCLUSIONS: This confirmatory study demonstrated that the vancomycin blood concentrations obtained during the study allow recommending a safety prophylactic dose of 12mg/kg in adults who undergo open-heart surgery under CPB conditions.	Vancomycin	59-69	carboxypeptidase B1	Homo sapiens	221-224
12217710-8	2002	Sequestration of vancomycin by the oxygenator or/and tubing system of the CPB machine had occurred and had been measured in this study.	Vancomycin	17-27	carboxypeptidase B1	Homo sapiens	74-77
12854477-2	2003	METHODS: Olprinone was administered as a single dose (0.1 mg.kg-1) into the venous reservoir of the CPB circuit 15 min prior to the end of emergence from CPB, followed by continuous infusion.	olprinone	9-18	carboxypeptidase B1	Homo sapiens	100-103
12854477-2	2003	METHODS: Olprinone was administered as a single dose (0.1 mg.kg-1) into the venous reservoir of the CPB circuit 15 min prior to the end of emergence from CPB, followed by continuous infusion.	olprinone	9-18	carboxypeptidase B1	Homo sapiens	154-157
12610743-5	2003	RESULTS: In subjects with CP-A, and in four of six subjects with CP-B, rosuvastatin steady-state AUC(0-24) and C(max) were similar to subjects with normal hepatic function (geometric mean values 60.7 ng h/ml and 6.02 ng/ml, respectively).	Rosuvastatin Calcium	71-83	carboxypeptidase B1	Homo sapiens	65-69
12073205-16	2002	This deleterious effect of reoxygenation can be modified by initiating CPB at a lower level of oxygen concentration.	Oxygen	29-35	carboxypeptidase B1	Homo sapiens	71-74
12073205-17	2002	Subsequent long-term studies are needed to determine the best method of decreasing the oxygen concentration of the CPB circuit.	Oxygen	87-93	carboxypeptidase B1	Homo sapiens	115-118
12182908-6	2002	Kinetic analysis showed that sc-uPA activation by Lys-plasmin competitively inhibited by ATF and CPB pretreated ATF (CPB-ATF) with an inhibitory constant (K(i)) of 3.8+/-0.31 and 12.4 +/- 1.8 microM, respectively.	atf	112-115	carboxypeptidase B1	Homo sapiens	97-100
11934586-0	2002	Anisylazoformylarginine: a superior assay substrate for carboxypeptidase B type enzymes.	anisylazoformylarginine	0-23	carboxypeptidase B1	Homo sapiens	56-74
11934586-1	2002	Anisylazoformylarginine (CH(3)OC(6)H(4)-N=N-CO-Arg-OH) is rapidly hydrolyzed at the acyl-arginine linkage by the zinc-enzyme porcine carboxypeptidase B.	anisylazoformylarginine	0-23	carboxypeptidase B1	Homo sapiens	133-151
11934586-1	2002	Anisylazoformylarginine (CH(3)OC(6)H(4)-N=N-CO-Arg-OH) is rapidly hydrolyzed at the acyl-arginine linkage by the zinc-enzyme porcine carboxypeptidase B.	Arginine	15-23	carboxypeptidase B1	Homo sapiens	133-151
12182908-6	2002	Kinetic analysis showed that sc-uPA activation by Lys-plasmin competitively inhibited by ATF and CPB pretreated ATF (CPB-ATF) with an inhibitory constant (K(i)) of 3.8+/-0.31 and 12.4 +/- 1.8 microM, respectively.	atf	112-115	carboxypeptidase B1	Homo sapiens	117-120
11854876-1	2002	OBJECTIVE: To determine the incidence of cerebral dysfunction in cardiac surgical patients exposed to heparin-bonded cardiopulmonary bypass (HB-CPB) versus nonheparin-bonded cardiopulmonary bypass (NH-CPB) circuits through neuropsychometric testing and to correlate these findings with markers of the systemic inflammatory response to CPB.	Heparin	102-109	carboxypeptidase B1	Homo sapiens	144-147
11457520-8	2001	Production of glycine-extended CCK processing products was evaluated by treatment of media with carboxypeptidase B followed by analysis with a CCK Gly RIA.	Glycine	14-21	carboxypeptidase B1	Homo sapiens	96-114
11215380-2	2000	TAFI is activated by thrombomodulin (TM)-bound thrombin and specifically removes the C-terminal Lys and Arg by its CPB activity.	Lysine	96-99	carboxypeptidase B1	Homo sapiens	115-118
11027681-1	2001	The plasminogen receptors responsible for enhancing cell surface-dependent plasminogen activation expose COOH-terminal lysines on the cell surface and are sensitive to proteolysis by carboxypeptidase B (CpB).	Lysine	119-126	carboxypeptidase B1	Homo sapiens	183-201
11027681-1	2001	The plasminogen receptors responsible for enhancing cell surface-dependent plasminogen activation expose COOH-terminal lysines on the cell surface and are sensitive to proteolysis by carboxypeptidase B (CpB).	Lysine	119-126	carboxypeptidase B1	Homo sapiens	203-206
11027681-5	2001	The cDNA for the 54-kDa protein matched the human TIP49a sequence, and encoded a COOH-terminal lysine, consistent with susceptibility to CpB.	Lysine	95-101	carboxypeptidase B1	Homo sapiens	137-140
11442827-8	2001	Carboxypeptidase B treatment and amino acid substitutions of the C-terminal lysyl residues of Eno indicated that the C-terminal lysine is pivotal for plasmin(ogen)-binding activity.	Lysine	128-134	carboxypeptidase B1	Homo sapiens	0-18
11215380-2	2000	TAFI is activated by thrombomodulin (TM)-bound thrombin and specifically removes the C-terminal Lys and Arg by its CPB activity.	Arginine	104-107	carboxypeptidase B1	Homo sapiens	115-118
10974350-6	2000	Using carboxypeptidase B digestion, the plasminogen-binding site of antithrombin III was localized to the carboxy-terminus lysine of the anticoagulant protein.	Lysine	123-129	carboxypeptidase B1	Homo sapiens	6-24
11127872-7	2000	Thus, a portion of membrane-associated alpha-enolase and annexin II expose carboxyl terminal lysines that are accessible to CpB on the peripheral blood monocyte surface, suggesting that these molecules may serve as profibrinolytic plasminogen receptors on monocytes.	carboxyl terminal lysines	75-100	carboxypeptidase B1	Homo sapiens	124-127
10885198-2	2000	Plasma samples treated with neuraminidase and carboxypeptidase-B were subjected to high-voltage agarose gel electrophoresis followed by immunofixation.	Sepharose	96-103	carboxypeptidase B1	Homo sapiens	46-64
10021925-1	1999	Anisylazoformyllysine (CH3OC6H4-N = N-CO-Lys-OH) is rapidly hydrolyzed at the acyl-lysine linkage by the zinc-enzyme porcine carboxypeptidase B.	Nitrogen	32-33	carboxypeptidase B1	Homo sapiens	125-143
10052689-4	1999	The C-terminal of the mCKs was concluded to be a lysine residue because the mCKs treated with carboxypeptidase B migrated to positions closer to the anode than did those not treated with carboxypeptidase B.	Lysine	49-55	carboxypeptidase B1	Homo sapiens	94-112
10052689-4	1999	The C-terminal of the mCKs was concluded to be a lysine residue because the mCKs treated with carboxypeptidase B migrated to positions closer to the anode than did those not treated with carboxypeptidase B.	Lysine	49-55	carboxypeptidase B1	Homo sapiens	187-205
10021925-1	1999	Anisylazoformyllysine (CH3OC6H4-N = N-CO-Lys-OH) is rapidly hydrolyzed at the acyl-lysine linkage by the zinc-enzyme porcine carboxypeptidase B.	anisylazoformyllysine	0-21	carboxypeptidase B1	Homo sapiens	125-143
10021925-1	1999	Anisylazoformyllysine (CH3OC6H4-N = N-CO-Lys-OH) is rapidly hydrolyzed at the acyl-lysine linkage by the zinc-enzyme porcine carboxypeptidase B.	ch3oc6h4	23-31	carboxypeptidase B1	Homo sapiens	125-143
11012092-7	2000	The increase in Bmax was correlated with plasmin-mediated exposure of C-terminal lysines since treatment of plasmin-modified fibrinogen surfaces with carboxypeptidase B produced a significant decrease in total binding signal as detected by ELISA (enzyme linked immunosorbent assay).	Lysine	81-88	carboxypeptidase B1	Homo sapiens	150-168
11119225-0	2000	Cisatracurium pharmacokinetics and pharmacodynamics during hypothermic CPB in infants	cisatracurium	0-13	carboxypeptidase B1	Homo sapiens	71-74
10021925-1	1999	Anisylazoformyllysine (CH3OC6H4-N = N-CO-Lys-OH) is rapidly hydrolyzed at the acyl-lysine linkage by the zinc-enzyme porcine carboxypeptidase B.	-lys-oh	40-47	carboxypeptidase B1	Homo sapiens	125-143
10021925-1	1999	Anisylazoformyllysine (CH3OC6H4-N = N-CO-Lys-OH) is rapidly hydrolyzed at the acyl-lysine linkage by the zinc-enzyme porcine carboxypeptidase B.	Lysine	15-21	carboxypeptidase B1	Homo sapiens	125-143
9832147-9	1998	Treatment of the ligands by carboxypeptidase B to eliminate the C-terminus Arg considerably decreased the [Ca2+] response.	Arginine	75-78	carboxypeptidase B1	Homo sapiens	28-46
9703961-5	1998	This CCK Gly immunoreactive peptide was similar in size to CCK 8, and after treatment with arylsulfatase and carboxypeptidase B, it co-eluted on HPLC with unsulfated CCK 8 Gly.	Glycine	9-12	carboxypeptidase B1	Homo sapiens	109-127
9930672-0	1998	Engineered human carboxypeptidase B enzymes that hydrolyse hippuryl-L-glutamic acid: reversed-polarity mutants.	hippuryl glutamic acid	59-83	carboxypeptidase B1	Homo sapiens	17-35
9930672-1	1998	Variants of human pancreatic carboxypeptidase B (HCPB), with specificity for hydrolysis of C-terminal glutamic acid and aspartic acid, were prepared by site-directed mutagenesis of the human gene and expressed in the periplasm of Escherichia coli.	Glutamic Acid	102-115	carboxypeptidase B1	Homo sapiens	18-47
9930672-1	1998	Variants of human pancreatic carboxypeptidase B (HCPB), with specificity for hydrolysis of C-terminal glutamic acid and aspartic acid, were prepared by site-directed mutagenesis of the human gene and expressed in the periplasm of Escherichia coli.	Aspartic Acid	120-133	carboxypeptidase B1	Homo sapiens	18-47
9703961-3	1998	PC1 also generated a peptide which after carboxypeptidase B treatment, was detected with an antiserum specific for CCK Gly.	Glycine	119-122	carboxypeptidase B1	Homo sapiens	41-59
9703961-5	1998	This CCK Gly immunoreactive peptide was similar in size to CCK 8, and after treatment with arylsulfatase and carboxypeptidase B, it co-eluted on HPLC with unsulfated CCK 8 Gly.	Glycine	172-175	carboxypeptidase B1	Homo sapiens	109-127
9571204-4	1998	Carboxypeptidase B digestion of the charged carboxyl terminus of the peptide through to the Ala residue--which mimics the enzymatic cleavage of a TM segment from a fusion protein--releases a highly hydrophobic peptide.	Alanine	92-95	carboxypeptidase B1	Homo sapiens	0-18
9562399-8	1998	The best fit of bone-Pb to the adjusted cumP-Pb (0.79 for T-Pb; 0.82 for C-Pb) was obtained for the terminal phase half-times of 13 and 12 years, respectively.	bone-pb	16-23	carboxypeptidase B1	Homo sapiens	73-77
9562399-8	1998	The best fit of bone-Pb to the adjusted cumP-Pb (0.79 for T-Pb; 0.82 for C-Pb) was obtained for the terminal phase half-times of 13 and 12 years, respectively.	cump-pb	40-47	carboxypeptidase B1	Homo sapiens	73-77
9402661-6	1997	For the clinical study we randomized 60 coronary artery surgery patients to receive either crystalloid cardioplegia (Bretschneider HTK) or selective continuous coronary perfusion via the aortic root with warm esmolol-enriched CPB blood.	esmolol	209-216	carboxypeptidase B1	Homo sapiens	226-229
8881706-4	1996	However, intracellular water standardized per litre TBW was significantly higher in CPB subjects (mean 27.0 (SD 7.5); P < 0.01) compared with CPA (mean 21.3 (SD 10.6)) and control subjects (mean 18.0 (SD 9.8)).	Water	23-28	carboxypeptidase B1	Homo sapiens	84-87
9153272-3	1997	A plausible mechanism for this inhibitory effect of thrombin involves TAFI (thrombin-activatable fibrinolysis inhibitor, procarboxypeptidase B) which, upon activation, may inhibit fibrinolysis by removing carboxy-terminal lysines from fibrin.	Lysine	222-229	carboxypeptidase B1	Homo sapiens	121-142
9102401-8	1997	HPRG-enhanced plasminogen activation was proportional to the quantity of HPRG immobilized and was abolished by anti-HPRG antiserum, by low concentrations of epsilon-aminocaproic acid, by methylation of lysine residues in HPRG, and by treatment of HPRG with carboxypeptidase B.	Lysine	202-208	carboxypeptidase B1	Homo sapiens	257-275
8881706-4	1996	However, intracellular water standardized per litre TBW was significantly higher in CPB subjects (mean 27.0 (SD 7.5); P < 0.01) compared with CPA (mean 21.3 (SD 10.6)) and control subjects (mean 18.0 (SD 9.8)).	tbw	52-55	carboxypeptidase B1	Homo sapiens	84-87
8881706-6	1996	These formulas gave accurate predictions of TBW and ECW, although standard errors of estimates were higher for CPB subjects (TBW < or = 2.5 and ECW < or = 2.1 l) than those for CPA (TBW < or = 2.0 and ECW < or = 1.8 l) and control (TBW 1.4 and ECW 0.9 l) subjects.	tbw	125-128	carboxypeptidase B1	Homo sapiens	111-114
8881706-6	1996	These formulas gave accurate predictions of TBW and ECW, although standard errors of estimates were higher for CPB subjects (TBW < or = 2.5 and ECW < or = 2.1 l) than those for CPA (TBW < or = 2.0 and ECW < or = 1.8 l) and control (TBW 1.4 and ECW 0.9 l) subjects.	tbw	125-128	carboxypeptidase B1	Homo sapiens	111-114
8881706-6	1996	These formulas gave accurate predictions of TBW and ECW, although standard errors of estimates were higher for CPB subjects (TBW < or = 2.5 and ECW < or = 2.1 l) than those for CPA (TBW < or = 2.0 and ECW < or = 1.8 l) and control (TBW 1.4 and ECW 0.9 l) subjects.	tbw	125-128	carboxypeptidase B1	Homo sapiens	111-114
8530448-7	1995	When u-PA or ATF was treated with immobilized carboxypeptidase B, its proadhesive effect was abolished, implicating the involvement of carboxyl-terminal lysine residues (Lys158 on u-PA and Lys135 on ATF).	atf	13-16	carboxypeptidase B1	Homo sapiens	46-64
8697097-4	1996	Carboxypeptidase B from the pancreas of the ostrich was purified by water extraction of acetone powder and aminobenzylsuccinic acid affinity and hydroxylapatite chromatography.	Water	68-73	carboxypeptidase B1	Homo sapiens	0-18
8697097-4	1996	Carboxypeptidase B from the pancreas of the ostrich was purified by water extraction of acetone powder and aminobenzylsuccinic acid affinity and hydroxylapatite chromatography.	Acetone	88-95	carboxypeptidase B1	Homo sapiens	0-18
8697097-4	1996	Carboxypeptidase B from the pancreas of the ostrich was purified by water extraction of acetone powder and aminobenzylsuccinic acid affinity and hydroxylapatite chromatography.	2-benzylaspartic acid	107-131	carboxypeptidase B1	Homo sapiens	0-18
8697097-4	1996	Carboxypeptidase B from the pancreas of the ostrich was purified by water extraction of acetone powder and aminobenzylsuccinic acid affinity and hydroxylapatite chromatography.	Durapatite	145-160	carboxypeptidase B1	Homo sapiens	0-18
8697097-8	1996	Purified ostrich carboxypeptidase B was assessed to be homogeneous by SDS-PAGE with a M(r) value of approx.	Sodium Dodecyl Sulfate	70-73	carboxypeptidase B1	Homo sapiens	17-35
8799752-4	1996	Ultrafiltration is valuable in removing excess plasma water during CPB.	Water	54-59	carboxypeptidase B1	Homo sapiens	67-70
8530448-8	1995	Moreover, when a carboxyl-terminal lysine analog was added, the proadhesive effect of carboxypeptidase B-treated u-PA or ATF was restored.	atf	121-124	carboxypeptidase B1	Homo sapiens	86-104
8530448-7	1995	When u-PA or ATF was treated with immobilized carboxypeptidase B, its proadhesive effect was abolished, implicating the involvement of carboxyl-terminal lysine residues (Lys158 on u-PA and Lys135 on ATF).	Lysine	153-159	carboxypeptidase B1	Homo sapiens	46-64
8530448-8	1995	Moreover, when a carboxyl-terminal lysine analog was added, the proadhesive effect of carboxypeptidase B-treated u-PA or ATF was restored.	Lysine	35-41	carboxypeptidase B1	Homo sapiens	86-104
7727441-6	1995	Trypsin cleaves pro-pCPB at two sites: Arg-92 and Arg-330.	Arginine	39-42	carboxypeptidase B1	Homo sapiens	20-24
8579343-5	1995	Purified R32Y-proinsulin was converted to insulin and Tyr-C-peptide by trypsin and carboxypeptidase B codigestion.	Tyrosine	54-57	carboxypeptidase B1	Homo sapiens	83-101
7782309-9	1995	2-Guanidinoethylmercaptosuccinic acid, a competitive inhibitor of CPB, completely inhibits prolongation of lysis by activated TAFI in a purified system and the prolongation induced by II activation in barium-adsorbed plasma.	guanidinoethylmercaptosuccinic acid	0-37	carboxypeptidase B1	Homo sapiens	66-69
7782309-9	1995	2-Guanidinoethylmercaptosuccinic acid, a competitive inhibitor of CPB, completely inhibits prolongation of lysis by activated TAFI in a purified system and the prolongation induced by II activation in barium-adsorbed plasma.	Barium	201-207	carboxypeptidase B1	Homo sapiens	66-69
8672321-15	1995	In the fentanyl group, the CD11b increase was greater and preceded CPB.	Fentanyl	7-15	carboxypeptidase B1	Homo sapiens	67-70
7727441-6	1995	Trypsin cleaves pro-pCPB at two sites: Arg-92 and Arg-330.	Arginine	50-53	carboxypeptidase B1	Homo sapiens	20-24
7727441-8	1995	However, cleavage at Arg-330 inactivates pCPB.	Arginine	21-24	carboxypeptidase B1	Homo sapiens	41-45
7727441-10	1995	We have found that 6-amino-n-hexanoic acid (epsilon ACA), a compeptitive inhibitor of basic carboxypeptidases, selectively limits trypsin cleavage of pro-pCPB.	Aminocaproic Acid	19-42	carboxypeptidase B1	Homo sapiens	154-158
7727441-14	1995	pCPB is more specific for substrates with C-terminal arginine than those with C-terminal lysine for all the natural and synthetic peptides tested.	Arginine	53-61	carboxypeptidase B1	Homo sapiens	0-4
7727441-14	1995	pCPB is more specific for substrates with C-terminal arginine than those with C-terminal lysine for all the natural and synthetic peptides tested.	Lysine	89-95	carboxypeptidase B1	Homo sapiens	0-4
7727441-14	1995	pCPB is more specific for substrates with C-terminal arginine than those with C-terminal lysine for all the natural and synthetic peptides tested.	Peptides	130-138	carboxypeptidase B1	Homo sapiens	0-4
7773614-3	1995	(R)-FP was released faster than (S)-FP by either CPB or CPY from both FP-Arg-OH and FP-Lys-OH.	Flurbiprofen	0-6	carboxypeptidase B1	Homo sapiens	49-52
8599281-3	1995	Contrary to the original impression, we concluded that a very low PaCO2 of 13 mmHg towards the end of CPB was the most likely cause of his damage.	paco2	66-71	carboxypeptidase B1	Homo sapiens	102-105
7773614-3	1995	(R)-FP was released faster than (S)-FP by either CPB or CPY from both FP-Arg-OH and FP-Lys-OH.	Flurbiprofen	32-38	carboxypeptidase B1	Homo sapiens	49-52
1939207-10	1991	When activated by trypsin, it hydrolyzes carboxypeptidase B substrates, hippuryl-Arg and hippuryl-Lys, but not carboxypeptidase A substrates, and it is inhibited by the specific carboxypeptidase B inhibitor (DL-5-guanidinoethyl)mercaptosuccinic acid.	hippuryl-L-arginine	72-84	carboxypeptidase B1	Homo sapiens	178-196
8112348-7	1994	Removal of lysine residues by treatment with, successively, plasmin and carboxypeptidase B, produced only a partial inhibition of t-PA binding, thus confirming the existence of both a lysine-dependent and a lysine-independent mechanism of binding of t-PA to both fibrin and FCB-2.	Lysine	11-17	carboxypeptidase B1	Homo sapiens	72-90
8112348-7	1994	Removal of lysine residues by treatment with, successively, plasmin and carboxypeptidase B, produced only a partial inhibition of t-PA binding, thus confirming the existence of both a lysine-dependent and a lysine-independent mechanism of binding of t-PA to both fibrin and FCB-2.	Lysine	184-190	carboxypeptidase B1	Homo sapiens	72-90
8112348-7	1994	Removal of lysine residues by treatment with, successively, plasmin and carboxypeptidase B, produced only a partial inhibition of t-PA binding, thus confirming the existence of both a lysine-dependent and a lysine-independent mechanism of binding of t-PA to both fibrin and FCB-2.	Lysine	184-190	carboxypeptidase B1	Homo sapiens	72-90
1340058-3	1992	Using this assay, high doses of cholecystokinin or carbachol were found to stimulate the intracellular conversion of at least three zymogens (procarboxypeptidase A1, procarboxypeptidase B, and chymotrypsinogen 2) to their active forms.	Cholecystokinin	32-47	carboxypeptidase B1	Homo sapiens	166-187
1340058-3	1992	Using this assay, high doses of cholecystokinin or carbachol were found to stimulate the intracellular conversion of at least three zymogens (procarboxypeptidase A1, procarboxypeptidase B, and chymotrypsinogen 2) to their active forms.	Carbachol	51-60	carboxypeptidase B1	Homo sapiens	166-187
1517314-6	1992	Added arginine was removed by carboxypeptidase B, but very slowly.	Arginine	6-14	carboxypeptidase B1	Homo sapiens	30-48
7525948-10	1994	When the anionic amino acids glutamate and aspartate were used to replace extracellular Cl-, the permeability ratios were calculated to be PGlut/PCl = 0.20 and PAsp/PCl = 0.17.	Glutamic Acid	29-38	carboxypeptidase B1	Homo sapiens	160-164
7525948-10	1994	When the anionic amino acids glutamate and aspartate were used to replace extracellular Cl-, the permeability ratios were calculated to be PGlut/PCl = 0.20 and PAsp/PCl = 0.17.	Aspartic Acid	43-52	carboxypeptidase B1	Homo sapiens	160-164
8269943-6	1993	Several basic compounds (e.g. methyl guanidine) act as effective specificity probes for carboxypeptidase B while phenol and other hydrophobic substances serve this purpose in carboxypeptidase A.	Methylguanidine	30-46	carboxypeptidase B1	Homo sapiens	88-106
8428004-4	1993	However, this difference with pro-UK was nullified by carboxypeptidase B (CpB) treatment of thromb-UK to remove the C-terminal arginine on the A-chain.	Arginine	127-135	carboxypeptidase B1	Homo sapiens	54-72
8428004-4	1993	However, this difference with pro-UK was nullified by carboxypeptidase B (CpB) treatment of thromb-UK to remove the C-terminal arginine on the A-chain.	Arginine	127-135	carboxypeptidase B1	Homo sapiens	74-77
8428004-8	1993	Addition of a CpB inhibitor to the plasma enhanced fibrinogenolysis by thromb-UK and pro-UK by approximately 16%, consistent with the promotion of both forms by certain C-terminal lysines.	Lysine	180-187	carboxypeptidase B1	Homo sapiens	14-17
8428004-10	1993	The effect of CpB indicates that the C-terminal Arg of thromb-UK slightly enhances its affinity for plasminogen.	Arginine	48-51	carboxypeptidase B1	Homo sapiens	14-17
1627572-10	1992	The binding to both surfaces was inhibited by the lysine analogue AMCHA and was completely abolished upon treatment of the degraded surface with carboxypeptidase B, indicating that r-apo(a) binds to both the intrachain lysines of intact fibrin and the carboxy-terminal lysines of degraded fibrin.	Lysine	219-226	carboxypeptidase B1	Homo sapiens	145-163
1627572-10	1992	The binding to both surfaces was inhibited by the lysine analogue AMCHA and was completely abolished upon treatment of the degraded surface with carboxypeptidase B, indicating that r-apo(a) binds to both the intrachain lysines of intact fibrin and the carboxy-terminal lysines of degraded fibrin.	Lysine	269-276	carboxypeptidase B1	Homo sapiens	145-163
1939207-10	1991	When activated by trypsin, it hydrolyzes carboxypeptidase B substrates, hippuryl-Arg and hippuryl-Lys, but not carboxypeptidase A substrates, and it is inhibited by the specific carboxypeptidase B inhibitor (DL-5-guanidinoethyl)mercaptosuccinic acid.	Lysine	97-101	carboxypeptidase B1	Homo sapiens	41-59
1939207-10	1991	When activated by trypsin, it hydrolyzes carboxypeptidase B substrates, hippuryl-Arg and hippuryl-Lys, but not carboxypeptidase A substrates, and it is inhibited by the specific carboxypeptidase B inhibitor (DL-5-guanidinoethyl)mercaptosuccinic acid.	Lysine	97-101	carboxypeptidase B1	Homo sapiens	178-196
1939207-10	1991	When activated by trypsin, it hydrolyzes carboxypeptidase B substrates, hippuryl-Arg and hippuryl-Lys, but not carboxypeptidase A substrates, and it is inhibited by the specific carboxypeptidase B inhibitor (DL-5-guanidinoethyl)mercaptosuccinic acid.	dl-5-guanidinoethyl)mercaptosuccinic acid	208-249	carboxypeptidase B1	Homo sapiens	41-59
1939207-10	1991	When activated by trypsin, it hydrolyzes carboxypeptidase B substrates, hippuryl-Arg and hippuryl-Lys, but not carboxypeptidase A substrates, and it is inhibited by the specific carboxypeptidase B inhibitor (DL-5-guanidinoethyl)mercaptosuccinic acid.	dl-5-guanidinoethyl)mercaptosuccinic acid	208-249	carboxypeptidase B1	Homo sapiens	178-196
1998669-0	1991	Effect of Zn2+ on the thermal denaturation of carboxypeptidase B.	Zinc	10-14	carboxypeptidase B1	Homo sapiens	46-64
1836471-6	1991	Treatment of fragment E-2 by carboxypeptidase-B (CPB), eliminated its promotion of pro-UK and Ala-158-pro-UK-induced plasmin generation.	ala-158	94-101	carboxypeptidase B1	Homo sapiens	29-47
1939157-3	1991	The 84-residue form of bovine MGP predicted from the message structure could not be detected in the bone extracellular matrix extracts, and it therefore seems probable that the lysine at position 84 was removed by the action of a carboxypeptidase B-like enzyme prior to secretion.	Lysine	177-183	carboxypeptidase B1	Homo sapiens	230-248
1939157-4	1991	A plausible sequence of proteolytic cleavages that could generate the 79-residue form of MGP would be a trypsin-like cleavage at Arg80-Arg81 or Arg81-Gly82 followed by carboxypeptidase B-like cleavage to remove COOH-terminal arginine(s).	Carbonic Acid	211-215	carboxypeptidase B1	Homo sapiens	168-186
1939157-4	1991	A plausible sequence of proteolytic cleavages that could generate the 79-residue form of MGP would be a trypsin-like cleavage at Arg80-Arg81 or Arg81-Gly82 followed by carboxypeptidase B-like cleavage to remove COOH-terminal arginine(s).	Arginine	225-233	carboxypeptidase B1	Homo sapiens	168-186
1776140-7	1991	Removal of the C-terminal lysine of Lys-UK by CpB produced small but significant increases in the Michaelis constants for the activation of both Glu- and Lys-plasminogen.	Lysine	26-32	carboxypeptidase B1	Homo sapiens	46-49
1776140-7	1991	Removal of the C-terminal lysine of Lys-UK by CpB produced small but significant increases in the Michaelis constants for the activation of both Glu- and Lys-plasminogen.	Lysine	36-39	carboxypeptidase B1	Homo sapiens	46-49
1885771-7	1991	To examine whether T cells can produce met-enkephalin precursor peptides, T cell conditioned media were treated with trypsin and carboxypeptidase-B, which is known to release met-enkephalin from the propeptide.	propeptide	199-209	carboxypeptidase B1	Homo sapiens	129-147
2068071-9	1991	The variant COOH terminus ends with the dibasic sequence Arg-Lys that is apparently removed through stepwise cleavage by serum carboxypeptidase B to yield several forms of circulating albumin.	Arginine	57-60	carboxypeptidase B1	Homo sapiens	127-145
2068071-9	1991	The variant COOH terminus ends with the dibasic sequence Arg-Lys that is apparently removed through stepwise cleavage by serum carboxypeptidase B to yield several forms of circulating albumin.	Lysine	61-64	carboxypeptidase B1	Homo sapiens	127-145
1998669-1	1991	A differential scanning calorimetry study on the thermal denaturation of porcine pancreas carboxypeptidase B (in 20 mM pyrophosphate buffer, pH 9.0) has been carried out.	diphosphoric acid	119-132	carboxypeptidase B1	Homo sapiens	90-108
1989879-1	1991	The three-dimensional structure of the activation domain isolated from porcine pancreatic procarboxypeptidase B was determined using 1H NMR spectroscopy.	Hydrogen	133-135	carboxypeptidase B1	Homo sapiens	90-111
2096887-5	1990	The added arginine tail could be specifically removed by carboxypeptidase B.	Arginine	10-18	carboxypeptidase B1	Homo sapiens	57-75
1671525-5	1991	Digestion with carboxypeptidase B excluded the hypothesis that this latter could be dyn B-Arg14.	dyn b-arg14	84-95	carboxypeptidase B1	Homo sapiens	15-33
1825500-1	1991	CPB is a placental Ca2(+)-phospholipid binding protein, with a molecular weight of approximately 35,000, that shows about 50% homology with lipocortin.	Phospholipids	26-38	carboxypeptidase B1	Homo sapiens	0-3
1697448-5	1990	Although the optimal ACT, dose, plasma concentration, and means of reversal (e.g., protamine vs. heparinase) remains to be determined, heparinoids provide an alternate means of anticoagulation for CPB in patients unable to receive standard heparin.	Heparinoids	135-146	carboxypeptidase B1	Homo sapiens	197-200
2321755-2	1990	A sensitive assay for CPE and other carboxypeptidase B-like enzymes has been developed using 125I-acetyl-Tyr-Ala-Arg (125I-AcYAR) as the substrate.	125i-acetyl-tyr-ala-arg	93-116	carboxypeptidase B1	Homo sapiens	36-54
2110898-3	1990	The C-terminal Lys-58 in the A chain is highly susceptible to removal by a carboxypeptidase-B-like activity causing the formation of des-Lys58-beta 2-microglobulin.	Lysine	15-18	carboxypeptidase B1	Homo sapiens	75-93
2223783-1	1990	Nearly complete sequence-specific 1H NMR assignments are presented for amino acid residues 3-81 in the 81-residue globular activation domain of porcine pancreatic procarboxypeptidase B isolated after limited tryptic proteolysis of the zymogen.	Hydrogen	34-36	carboxypeptidase B1	Homo sapiens	163-184
1695691-4	1990	Urine output during CPB was not significantly different, but the total dose of furosemide administered was less in group Ul and a significant difference (p less than 0.05) was observed in the free water clearance at CPB 1 hr.	Water	197-202	carboxypeptidase B1	Homo sapiens	216-221
2329143-4	1990	Commercial enzymes (trypsin, carboxypeptidase B) were used to release methionine- and leucine-enkephalin from precursors.	methionine- and leucine-enkephalin	70-104	carboxypeptidase B1	Homo sapiens	29-47
2321755-3	1990	This peptide is poorly soluble in ethyl acetate whereas the product of carboxypeptidase B-like enzymatic activity (125I-AcYA) can be quantitatively extracted with this solvent, allowing the rapid separation of product from substrate.	125i-acya	115-124	carboxypeptidase B1	Homo sapiens	71-89
34798625-1	2021	All-inorganic dual-phase CsPbBr3-Cs4PbBr6 quantum dots (CPB QDs)-based polyacrylonitrile (PAN) fiber synthesized by supersaturated recrystallization and electrospinning technique possesses characteristics of homogeneous morphology, high crystallinity and solution sensitivity.	polyacrylonitrile	71-88	carboxypeptidase B1	Homo sapiens	56-59
33774002-7	2022	RESULTS: DCA induced a significant increase in ICAM-1 and VCAM-1 expression in HET1A, CPB, FLO1, and OE33 cells.	Deoxycholic Acid	9-12	carboxypeptidase B1	Homo sapiens	86-89
2293362-5	1990	From a preoperative value of 92 +/- 13 ng/ml, C3a des-Arg rose during CPB to a maximum of 1816 +/- 393 at the end of CPB.	Arginine	53-57	carboxypeptidase B1	Homo sapiens	70-73
34798625-3	2021	In the process of ethanol-anhydrous (EA) and water splashing, the CPB@PAN fiber presents conspicuous blue and green emission when contacting with EA and water, and maintains intense blue and green FL for more than 4 months.	Ethanol	18-25	carboxypeptidase B1	Homo sapiens	66-69
34798625-3	2021	In the process of ethanol-anhydrous (EA) and water splashing, the CPB@PAN fiber presents conspicuous blue and green emission when contacting with EA and water, and maintains intense blue and green FL for more than 4 months.	Water	45-50	carboxypeptidase B1	Homo sapiens	66-69
34798625-3	2021	In the process of ethanol-anhydrous (EA) and water splashing, the CPB@PAN fiber presents conspicuous blue and green emission when contacting with EA and water, and maintains intense blue and green FL for more than 4 months.	Water	153-158	carboxypeptidase B1	Homo sapiens	66-69
34840044-13	2021	CPB flow did not affect survival rate, hospital stay, intensive care unit stay, or serum lactate in post-operative day 1, but serum creatinine (mg/dL) level increased transiently in patients with low pump flow group(0.9 +- 0.4 vs 1.3 +- 0.7,p < 0.05).	Creatinine	132-142	carboxypeptidase B1	Homo sapiens	0-3
35550286-3	2022	METHODS: We calculated RV-PA coupling ratios in patients undergoing mitral TEER from August 2010 to March 2019 by dividing the tricuspid annular plane systolic excursion (TAPSE) by the echocardiographic estimated PA systolic pressure (PASP).	arginylvaline	23-25	carboxypeptidase B1	Homo sapiens	235-239
34761470-6	2022	The frequency of interruption of ATZ+BV treatment due to fatigue was higher in CP-B than CP-A patients (P=0.030).	Atazanavir Sulfate	33-36	carboxypeptidase B1	Homo sapiens	79-83
34553313-8	2021	While overshadowed by the regional differences, some differences by exposure to CPB/DHCA were seen as well.	dhca	84-88	carboxypeptidase B1	Homo sapiens	80-83
34553313-11	2021	CPB/DHCA also leads to metabolic differences and may have additive effects to the regional disturbances.	dhca	4-8	carboxypeptidase B1	Homo sapiens	0-3
34072265-2	2021	Here, we synthesized a copolymer PAsp(-N=C-PEG)-PCys-PAsp(DETA) consisting of a poly(aspartate) block grafted with comb-like PEG side chains via a pH-sensitive imine bond (PAsp(-N=C-PEG) block), a poly(l-cysteine) block with a thiol group (PCys block), and a cationic poly(aspartate) block grafted with diethylenetriamine (PAsp(DETA) block).	c-peg	41-46	carboxypeptidase B1	Homo sapiens	33-37
34072265-2	2021	Here, we synthesized a copolymer PAsp(-N=C-PEG)-PCys-PAsp(DETA) consisting of a poly(aspartate) block grafted with comb-like PEG side chains via a pH-sensitive imine bond (PAsp(-N=C-PEG) block), a poly(l-cysteine) block with a thiol group (PCys block), and a cationic poly(aspartate) block grafted with diethylenetriamine (PAsp(DETA) block).	c-peg	41-46	carboxypeptidase B1	Homo sapiens	53-57
34072265-2	2021	Here, we synthesized a copolymer PAsp(-N=C-PEG)-PCys-PAsp(DETA) consisting of a poly(aspartate) block grafted with comb-like PEG side chains via a pH-sensitive imine bond (PAsp(-N=C-PEG) block), a poly(l-cysteine) block with a thiol group (PCys block), and a cationic poly(aspartate) block grafted with diethylenetriamine (PAsp(DETA) block).	DEET	58-62	carboxypeptidase B1	Homo sapiens	33-37
34072265-2	2021	Here, we synthesized a copolymer PAsp(-N=C-PEG)-PCys-PAsp(DETA) consisting of a poly(aspartate) block grafted with comb-like PEG side chains via a pH-sensitive imine bond (PAsp(-N=C-PEG) block), a poly(l-cysteine) block with a thiol group (PCys block), and a cationic poly(aspartate) block grafted with diethylenetriamine (PAsp(DETA) block).	DEET	58-62	carboxypeptidase B1	Homo sapiens	53-57
34072265-2	2021	Here, we synthesized a copolymer PAsp(-N=C-PEG)-PCys-PAsp(DETA) consisting of a poly(aspartate) block grafted with comb-like PEG side chains via a pH-sensitive imine bond (PAsp(-N=C-PEG) block), a poly(l-cysteine) block with a thiol group (PCys block), and a cationic poly(aspartate) block grafted with diethylenetriamine (PAsp(DETA) block).	polyaspartate	80-94	carboxypeptidase B1	Homo sapiens	33-37
34072265-2	2021	Here, we synthesized a copolymer PAsp(-N=C-PEG)-PCys-PAsp(DETA) consisting of a poly(aspartate) block grafted with comb-like PEG side chains via a pH-sensitive imine bond (PAsp(-N=C-PEG) block), a poly(l-cysteine) block with a thiol group (PCys block), and a cationic poly(aspartate) block grafted with diethylenetriamine (PAsp(DETA) block).	Imines	160-165	carboxypeptidase B1	Homo sapiens	33-37
34072265-3	2021	The cationic polymers efficiently complexed siRNA into polyplexes, showing a sandwich-like structure with a PAsp(-N=C-PEG) out-layer, a crosslinked PCys interlayer, and a complexing core of siRNA and PAsp(DETA).	Polymers	13-21	carboxypeptidase B1	Homo sapiens	108-112
34072265-3	2021	The cationic polymers efficiently complexed siRNA into polyplexes, showing a sandwich-like structure with a PAsp(-N=C-PEG) out-layer, a crosslinked PCys interlayer, and a complexing core of siRNA and PAsp(DETA).	Polymers	13-21	carboxypeptidase B1	Homo sapiens	200-204
34072265-3	2021	The cationic polymers efficiently complexed siRNA into polyplexes, showing a sandwich-like structure with a PAsp(-N=C-PEG) out-layer, a crosslinked PCys interlayer, and a complexing core of siRNA and PAsp(DETA).	Carbon	116-117	carboxypeptidase B1	Homo sapiens	108-112
34373415-2	2021	In the present work, a fluorescent probe CPB based on coumarin was designed for recognizing Cu2+ ions.	coumarin	54-62	carboxypeptidase B1	Homo sapiens	41-44
34373415-2	2021	In the present work, a fluorescent probe CPB based on coumarin was designed for recognizing Cu2+ ions.	cupric ion	92-96	carboxypeptidase B1	Homo sapiens	41-44
34373415-3	2021	The fluorescence of CPB gradually quenched with increasing concentration of Cu2+ ions, due to the interactions between CPB and Cu2+ ions.	cupric ion	76-80	carboxypeptidase B1	Homo sapiens	20-23
34373415-3	2021	The fluorescence of CPB gradually quenched with increasing concentration of Cu2+ ions, due to the interactions between CPB and Cu2+ ions.	cupric ion	76-80	carboxypeptidase B1	Homo sapiens	119-122
34373415-3	2021	The fluorescence of CPB gradually quenched with increasing concentration of Cu2+ ions, due to the interactions between CPB and Cu2+ ions.	cupric ion	127-131	carboxypeptidase B1	Homo sapiens	20-23
34373415-3	2021	The fluorescence of CPB gradually quenched with increasing concentration of Cu2+ ions, due to the interactions between CPB and Cu2+ ions.	cupric ion	127-131	carboxypeptidase B1	Homo sapiens	119-122
34373415-4	2021	With the addition of Cu2+ ions, the emission changes of CPB exhibited a good liner relationship toward the Cu2+ ions content in solution.	cupric ion	21-25	carboxypeptidase B1	Homo sapiens	56-59
34373415-4	2021	With the addition of Cu2+ ions, the emission changes of CPB exhibited a good liner relationship toward the Cu2+ ions content in solution.	cupric ion	107-111	carboxypeptidase B1	Homo sapiens	56-59
34373415-5	2021	Additionally, CPB could highly selective recognize Cu2+ ions among other metal ions in solution.	cupric ion	51-55	carboxypeptidase B1	Homo sapiens	14-17
34373415-5	2021	Additionally, CPB could highly selective recognize Cu2+ ions among other metal ions in solution.	Metals	73-78	carboxypeptidase B1	Homo sapiens	14-17
34373415-6	2021	Bearing the selectivity and fluorescence property toward Cu2+ ions, CPB was successfully applied to monitoring Cu2+ ions in Hela cells and zebrafish.	cupric ion	57-61	carboxypeptidase B1	Homo sapiens	68-71
34373415-6	2021	Bearing the selectivity and fluorescence property toward Cu2+ ions, CPB was successfully applied to monitoring Cu2+ ions in Hela cells and zebrafish.	cupric ion	111-115	carboxypeptidase B1	Homo sapiens	68-71
35532069-10	2022	CPB/DHCA strongly affected the serum metabolic profile, with only one metabolite that differed significantly with acute kidney injury (pyroglutamic acid, a marker of oxidative stress).	Pyrrolidonecarboxylic Acid	135-152	carboxypeptidase B1	Homo sapiens	0-3
35115101-3	2022	METHODS: The study investigators calculated RV-PA coupling ratios for patients enrolled in the global TriValve registry by dividing the tricuspid annular plane systolic excursion (TAPSE) by the PA systolic pressure (PASP) from transthoracic echocardiograms performed before the procedure and 30 days after the procedure.	arginylvaline	44-46	carboxypeptidase B1	Homo sapiens	216-220
35191200-4	2022	In combination with the Zn anode, the PASP-Tempo composite electrode exhibited rapid charging/discharging and superior cyclic stability with reversible two-electron redox reaction in an aqueous electrolyte.	Zinc	24-26	carboxypeptidase B1	Homo sapiens	38-42
35191200-6	2022	Because the redox reaction process of the nitroxyl radical turning into oxoammonium was a p-type mechanism that interacts with an anion, three electrolytes with different anions were conducted in the Zn/PASP-Tempo organic radical battery.	nitroxyl	42-50	carboxypeptidase B1	Homo sapiens	203-207
35191200-6	2022	Because the redox reaction process of the nitroxyl radical turning into oxoammonium was a p-type mechanism that interacts with an anion, three electrolytes with different anions were conducted in the Zn/PASP-Tempo organic radical battery.	oxoammonium	72-83	carboxypeptidase B1	Homo sapiens	203-207
35156389-9	2022	At multivariable analysis, TAPSE/PASP ratio remained a predictor of in-hospital death after adjustments for age, oxygen partial pressure at arterial gas analysis/fraction of inspired oxygen, left ventricular ejection fraction, and computed tomography lung score.	Oxygen	113-119	carboxypeptidase B1	Homo sapiens	33-37
35156389-9	2022	At multivariable analysis, TAPSE/PASP ratio remained a predictor of in-hospital death after adjustments for age, oxygen partial pressure at arterial gas analysis/fraction of inspired oxygen, left ventricular ejection fraction, and computed tomography lung score.	Oxygen	183-189	carboxypeptidase B1	Homo sapiens	33-37
34995697-2	2022	For systemic mRNA delivery, we developed a series of cationic amphiphilic polyaspartamide derivatives (PAsp(DET/R)s) carrying various alicyclic (R) moieties with diethylenetriamine (DET) in the side chains to form mRNA-loaded polyplexes bearing stability under physiological conditions and possessing endosomal escape functionality.	polyaspartamide	74-89	carboxypeptidase B1	Homo sapiens	103-107
34995697-2	2022	For systemic mRNA delivery, we developed a series of cationic amphiphilic polyaspartamide derivatives (PAsp(DET/R)s) carrying various alicyclic (R) moieties with diethylenetriamine (DET) in the side chains to form mRNA-loaded polyplexes bearing stability under physiological conditions and possessing endosomal escape functionality.	diethylenetriamine	162-180	carboxypeptidase B1	Homo sapiens	103-107
34995697-3	2022	While the size and zeta-potential of polyplexes were comparable among various PAsp(DET/R)s, the transfection efficiencies of polyplexes were considerably varied due to difference in the R moieties of PAsp(DET/R)s and were described by an octanol-water (or buffer at pH 7.3) distribution coefficient (logD7.3).	Octanols	238-245	carboxypeptidase B1	Homo sapiens	200-204
34995697-3	2022	While the size and zeta-potential of polyplexes were comparable among various PAsp(DET/R)s, the transfection efficiencies of polyplexes were considerably varied due to difference in the R moieties of PAsp(DET/R)s and were described by an octanol-water (or buffer at pH 7.3) distribution coefficient (logD7.3).	Water	246-251	carboxypeptidase B1	Homo sapiens	200-204
34995697-7	2022	The highest mRNA expression in the lungs was achieved by a polyaspartamide derivative having a cyclohexylethyl group (PAsp(DET/CHE)), which induced more than 10-fold increase in mRNA transfection efficiency compared to commercially available lipid nanoparticles.	polyaspartamide	59-74	carboxypeptidase B1	Homo sapiens	118-122