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1962 1
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1971 24
1972 25
1973 24
1974 23
1975 32
1976 38
1977 19
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1980 28
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1986 32
1987 24
1988 36
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1994 23
1995 17
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1997 25
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1999 15
2000 25
2001 22
2002 18
2003 26
2004 21
2005 16
2006 14
2007 24
2008 23
2009 20
2010 11
2011 11
2012 17
2013 14
2014 19
2015 14
2016 21
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1,184 results

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Page 1
Both plasma basic carboxypeptidases, carboxypeptidase B2 and carboxypeptidase N, regulate vascular leakage activity in mice.
Zhou Q, Zhao L, Shao Z, Declerck P, Leung LLK, Morser J. Zhou Q, et al. J Thromb Haemost. 2022 Jan;20(1):238-244. doi: 10.1111/jth.15551. Epub 2021 Nov 7. J Thromb Haemost. 2022. PMID: 34626062 Free article.
BK binds to bradykinin receptor 2, causing vascular leakage. BK is inactivated by proteolysis by the plasma carboxypeptidase B2 and N (CPB2 and CPN). CPN is constitutively active but CPB2 is generated from its zymogen, proCPB2. ...Plasmin is the activator of proCPB2 in thi …
BK binds to bradykinin receptor 2, causing vascular leakage. BK is inactivated by proteolysis by the plasma carboxypeptidase B2 and N …
Carboxypeptidase U at the interface between coagulation and fibrinolysis.
Schatteman K, Goossens F, Leurs J, Verkerk R, Scharpé S, Michiels JJ, Hendriks D. Schatteman K, et al. Clin Appl Thromb Hemost. 2001 Apr;7(2):93-101. doi: 10.1177/107602960100700203. Clin Appl Thromb Hemost. 2001. PMID: 11292199 Free article. Review.
One decade later, the importance of carboxypeptidase U (CPU) in the regulation of fibrin clot dissolution is well documented. ...Because these C-terminal lysine residues are important for upregulating the fibrinolytic rate, CPU thus slows down fibrinolysis....
One decade later, the importance of carboxypeptidase U (CPU) in the regulation of fibrin clot dissolution is well documented. ...Beca …
Arginine and lysine product inhibition of bovine adrenomedullary carboxypeptidase H, a prohormone processing enzyme.
Hook VY. Hook VY. Life Sci. 1990;47(13):1135-9. doi: 10.1016/0024-3205(90)90173-o. Life Sci. 1990. PMID: 2122147
Carboxypeptidase H (CPH) is one of the later enzymes in the cascade of proteolytic steps required for the posttranslational processing of peptide hormone precursors, including processing of proenkephalin. In this study, CPH activity in the soluble and membrane fractions of …
Carboxypeptidase H (CPH) is one of the later enzymes in the cascade of proteolytic steps required for the posttranslational processin …
Synthesis and characterization of a novel (68)Ga-labeled p-bromobenzyl lysine-urea-ODAP PSMA inhibitor.
Sui Y, Duan X, Zhang J, Chu Y, Yang X. Sui Y, et al. Bioorg Med Chem Lett. 2023 Jul 15;91:129382. doi: 10.1016/j.bmcl.2023.129382. Epub 2023 Jun 20. Bioorg Med Chem Lett. 2023. PMID: 37348571
In this study, we synthesized seven ODAP-Urea-Lys derivatives characterized with p-bromobenzyl group conjugated to lysine. The ligands showed medium-to-high potency, with K(i) values ranging from 27.9 nM to 0.94 nM. ...
In this study, we synthesized seven ODAP-Urea-Lys derivatives characterized with p-bromobenzyl group conjugated to lysine. The ligand …
[Arginine and lysine as products of basic carboxypeptidase activity associated with fibrinolysis].
Zhloba AA, Subbotina TF, Lupan DS, Bogova VA, Kusheleva OA. Zhloba AA, et al. Biomed Khim. 2013 Sep-Oct;59(5):570-7. doi: 10.18097/pbmc20135905570. Biomed Khim. 2013. PMID: 24479347 Clinical Trial. Russian.
Blood carboxypeptidases play an important role in the regulation of fibrinolysis. We have proposed here the method for the assay of blood carboxypeptidase activity associated with coagulation/fibrinolysis using the natural substrate fibrin and the detection of basic …
Blood carboxypeptidases play an important role in the regulation of fibrinolysis. We have proposed here the method for the assay of b …
Elucidating the effects of arginine and lysine on a monoclonal antibody C-terminal lysine variation in CHO cell cultures.
Zhang X, Tang H, Sun YT, Liu X, Tan WS, Fan L. Zhang X, et al. Appl Microbiol Biotechnol. 2015 Aug;99(16):6643-52. doi: 10.1007/s00253-015-6617-y. Epub 2015 May 7. Appl Microbiol Biotechnol. 2015. PMID: 25947244
The potential roles of media arginine (Arg) and lysine (Lys) in mAb heavy chain C-terminal lysine processing were investigated by monitoring the lysine variant levels under various Arg and Lys concentrations. Both Arg and Lys were found to significantly affec …
The potential roles of media arginine (Arg) and lysine (Lys) in mAb heavy chain C-terminal lysine processing were investigated …
Purification and characterization of arginine carboxypeptidase produced by Porphyromonas gingivalis.
Masuda K, Yoshioka M, Hinode D, Nakamura R. Masuda K, et al. Infect Immun. 2002 Apr;70(4):1807-15. doi: 10.1128/IAI.70.4.1807-1815.2002. Infect Immun. 2002. PMID: 11895942 Free PMC article.
This sequence showed homology with mammalian carboxypeptidases (M, N, and E/H) and included a zinc-binding region signature, suggesting that the enzyme is a member of the zinc carboxypeptidase family. ...These results indicate that the arginine carboxypeptidase …
This sequence showed homology with mammalian carboxypeptidases (M, N, and E/H) and included a zinc-binding region signature, suggesti …
Rapid assay of human plasma carboxypeptidase N by high-performance liquid chromatographic separation of hippuryl-lysine and its product.
Marceau F, Drumheller A, Gendreau M, Lussier A, St-Pierre S. Marceau F, et al. J Chromatogr. 1983 Aug 26;266:173-7. doi: 10.1016/s0021-9673(01)90890-8. J Chromatogr. 1983. PMID: 6415078
A rapid and sensitive method for measuring carboxypeptidase N (CPN) activity in human plasma is described. The procedure is based on the hydrolysis of a high-specificity/low-affinity substrate, hippuryl-L-lysine, to its products hippuric acid and lysine. ...
A rapid and sensitive method for measuring carboxypeptidase N (CPN) activity in human plasma is described. The procedure is based on …
Isolation and characterization of the subunits of human plasma carboxypeptidase N (kininase i).
Levin Y, Skidgel RA, Erdös EG. Levin Y, et al. Proc Natl Acad Sci U S A. 1982 Aug;79(15):4618-22. doi: 10.1073/pnas.79.15.4618. Proc Natl Acad Sci U S A. 1982. PMID: 6750606 Free PMC article.
Carboxypeptidase N (kininase I, arginine carboxypeptidase; EC 3.4.17.3) cleaves COOH-terminal basic amino acids of kinins, anaphylatoxins, and other peptides. ...Trypsin, plasmin, and plasma or urinary kallikrein cleaved carboxypeptidase N into lower molecula …
Carboxypeptidase N (kininase I, arginine carboxypeptidase; EC 3.4.17.3) cleaves COOH-terminal basic amino acids of kinins, ana …
1,184 results