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.)

2018
1. 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)83, 1594-1602. PubMed  Europe PubMed DOI  P  S
2014
2. 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 Crystallogr70, 279-289. PubMed  Europe PubMed DOI  S
2013
3. 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 Chem20, 1595-1608. PubMed  Europe PubMed  V  S  I
2012
4. Auld,D.S.
   Catalytic mechanisms for metallopeptidases
   [ISSN:978-0-12-407744-7]3, 370-396. DOI
5. 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 J26, 3754-3764. PubMed  Europe PubMed DOI  S
2010
6. Fernandez,D., Pallares,I., Vendrell,J. and Aviles,F.X.
   Progress in metallocarboxypeptidases and their small molecular weight inhibitors
   Biochimie92, 1484-1500. PubMed  Europe PubMed DOI  I
2009
7. Isoe,J., Zamora,J. and Miesfeld,R.L.
   Molecular analysis of the Aedes aegypti carboxypeptidase gene family
   Insect Biochem Mol Biol39, 68-73. PubMed  Europe PubMed DOI
2008
8. Gomis-Ruth,F.X.
   Structure and mechanism of metallocarboxypeptidases
   Crit Rev Biochem Mol Biol43, 319-345. PubMed  Europe PubMed DOI
2007
9. 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 J21, 851-865. PubMed  Europe PubMed DOI
2004
10. Auld,D.S.
    Catalytic mechanisms of metallopeptidases
    [ISSN:0-12-079610-4]2, 268-289.  V
2001
11. Reznik,S.E. and Fricker,L.D.
    Carboxypeptidases from A to Z: implications in embryonic development and Wnt binding
    Cell Mol Life Sci58, 1790-1804. PubMed  Europe PubMed  V
2000
12. 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 Neurosci16, 578-596. PubMed  Europe PubMed DOI
13. [YEAR:7-3-2000]Vendrell,J., Querol,E. and Aviles,F.X.
    Metallocarboxypeptidases and their protein inhibitors. Structure, function and biomedical properties
    Biochim Biophys Acta1477, 284-298. PubMed  Europe PubMed DOI  V
1999
14. [YEAR:10-9-1999]Makarova,K.S. and Grishin,N.V.
    The Zn-peptidase superfamily: functional convergence after evolutionary divergence
    J Mol Biol292, 11-17. PubMed  Europe PubMed DOI
1996
15. Skidgel,R.A.
    Structure and function of mammalian zinc carboxypeptidases
    241-283.
1995
16. Stepanov,V.M.
    Carboxypeptidase T
    Methods Enzymol248, 675-683. PubMed  Europe PubMed DOI  V
1993
17. 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 Biochem211, 381-389. PubMed  Europe PubMed DOI