Literature for family M14

(Topics flags: S Structure, I Inhibitor, P Specificity, V Review. To select only the references relevant to a single topic, click the link above. See explanation.)

2026
1. Zhao,Z., Kaluba,F.C. and Lyons,P.J.
   Surface loops may provide additional function necessary for enzyme-to-pseudoenzyme transition in the fungal metallocarboxypeptidase family
   FEBS J (2026) PubMed  Europe PubMed DOI
2018
2. Akparov,V.K., Timofeev,V.I., Khaliullin,I.G., Konstantinova,G.E., Kuranova,I.P., Rakitina,T.V. and Svedas,V.K.
   Mobile loop in the active site of metallocarboxypeptidases as an underestimated determinant of substrate specificity
   Biochemistry (Mosc) (2018) 83, 1594-1602. PubMed  Europe PubMed DOI  P  S
2014
3. Rimsa,V., Eadsforth,T.C., Joosten,R.P. and Hunter,W.N.
   High-resolution structure of the M14-type cytosolic carboxypeptidase from Burkholderia cenocepacia refined exploiting PDB_REDO strategies
   Acta Crystallogr D Biol Crystallogr (2014) 70, 279-289. PubMed  Europe PubMed DOI  S
2013
4. Fernandez,D., Pallares,I., Covaleda,G., Aviles,F.X. and Vendrell,J.
   Metallocarboxypeptidases and their Inhibitors: Recent Developments in Biomedically Relevant Protein and Organic Ligands
   Curr Med Chem (2013) 20, 1595-1608. PubMed  Europe PubMed  V  S  I
2012
5. Auld,D.S.
   Catalytic mechanisms for metallopeptidases
   [ISSN:978-0-12-407744-7] (2012) 3, 370-396. DOI
6. Otero,A., Rodriguez de la Vega,M., Tanco,S., Lorenzo,J., Aviles,F.X. and Reverter,D.
   The novel structure of a cytosolic M14 metallocarboxypeptidase (CCP) from Pseudomonas aeruginosa: a model for mammalian CCPs
   FASEB J (2012) 26, 3754-3764. PubMed  Europe PubMed DOI  S
2010
7. Fernandez,D., Pallares,I., Vendrell,J. and Aviles,F.X.
   Progress in metallocarboxypeptidases and their small molecular weight inhibitors
   Biochimie (2010) 92, 1484-1500. PubMed  Europe PubMed DOI  I
2009
8. Isoe,J., Zamora,J. and Miesfeld,R.L.
   Molecular analysis of the Aedes aegypti carboxypeptidase gene family
   Insect Biochem Mol Biol (2009) 39, 68-73. PubMed  Europe PubMed DOI  PMC  EPMC
2008
9. Gomis-Ruth,F.X.
   Structure and mechanism of metallocarboxypeptidases
   Crit Rev Biochem Mol Biol (2008) 43, 319-345. PubMed  Europe PubMed DOI
2007
10. Rodriguez de la Vega,M., Sevilla,R.G., Hermoso,A., Lorenzo,J., Tanco,S., Diez,A., Fricker,L.D., Bautista,J.M. and Aviles,F.X.
    Nna1-like proteins are active metallocarboxypeptidases of a new and diverse M14 subfamily
    FASEB J (2007) 21, 851-865. PubMed  Europe PubMed DOI
2004
11. Auld,D.S.
    Catalytic mechanisms of metallopeptidases
    [ISSN:0-12-079610-4] (2004) 2, 268-289.  V
2001
12. Reznik,S.E. and Fricker,L.D.
    Carboxypeptidases from A to Z: implications in embryonic development and Wnt binding
    Cell Mol Life Sci (2001) 58, 1790-1804. PubMed  Europe PubMed  V
2000
13. Harris,A., Morgan,J.I., Pecot,M., Soumare,A., Osborne,A. and Soares,H.D.
    Regenerating motor neurons express Nna1, a novel ATP/GTP-binding protein related to zinc carboxypeptidases
    Mol Cell Neurosci (2000) 16, 578-596. PubMed  Europe PubMed DOI
14. [YEAR:7-3-2000]Vendrell,J., Querol,E. and Aviles,F.X.
    Metallocarboxypeptidases and their protein inhibitors. Structure, function and biomedical properties
    Biochim Biophys Acta (7-3-2000) 1477, 284-298. PubMed  Europe PubMed DOI  V
1999
15. [YEAR:10-9-1999]Makarova,K.S. and Grishin,N.V.
    The Zn-peptidase superfamily: functional convergence after evolutionary divergence
    J Mol Biol (10-9-1999) 292, 11-17. PubMed  Europe PubMed DOI
1996
16. Skidgel,R.A.
    Structure and function of mammalian zinc carboxypeptidases
    (1996) , 241-283.
1995
17. Stepanov,V.M.
    Carboxypeptidase T
    Methods Enzymol (1995) 248, 675-683. PubMed  Europe PubMed DOI  V
1993
18. Aviles,F.X., Vendrell,J., Guasch,A., Coll,M. and Huber,R.
    Advances in metallo-procarboxypeptidases. Emerging details on the inhibition mechanism and on the activation process
    Eur J Biochem (1993) 211, 381-389. PubMed  Europe PubMed DOI