Literature for clan AA

Summary Alignment Structure Literature

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

    2019
  1. Ahsan,M. and Senapati,S.
    Water plays a cocatalytic role in epoxide ring opening reaction in aspartate proteases: a QM/MM study
    J Phys Chem B123, 7955-7964. PubMed  Europe PubMed DOI
  2. Windsor,I.W., Gold,B. and Raines,R.T.
    An n - >pi* interaction in the bound substrate of aspartic proteases replicates the oxyanion hole
    ACS Catal9, 1464-1471. PubMed  Europe PubMed DOI
  3. 2013
  4. Sussman,F., Villaverde,M.C., Dominguez,J.L. and Danielson,U.H.
    On the active site protonation state in aspartic proteases: implications for drug design
    Curr Pharm Des19, 4257-4275. PubMed  Europe PubMed DOI
  5. 2012
  6. Rawlings,N.D. and Barrett,A.J.
    Introduction: aspartic and glutamic peptidases and their clans
    [ISSN:978-0-12-407744-7]3, 3-19. DOI
  7. Wlodawer,A., Gustchina,A. and James,M.N.G.
    Catalytic pathways of aspartic peptidases
    [ISSN:978-0-12-407744-7]3, 19-27. DOI
  8. 2009
  9. Llorens,C., Futami,R., Renaud,G. and Moya,A.
    Bioinformatic flowchart and database to investigate the origins and diversity of Clan AA peptidases
    Biol Direct4, 3-3. PubMed  Europe PubMed DOI  V
  10. Rawlings,N.D. and Bateman,A.
    Pepsin homologues in bacteria
    BMC Genomics10, 437-437. PubMed  Europe PubMed DOI
  11. 2007
  12. Hulko,M., Lupas,A.N. and Martin,J.
    Inherent chaperone-like activity of aspartic proteases reveals a distant evolutionary relation to double-psi barrel domains of AAA-ATPases
    Protein Sci16, 644-653. PubMed  Europe PubMed DOI
  13. 2006
  14. [YEAR:3-9-2006]Sirkis,R., Gerst,J.E. and Fass,D.
    Ddi1, a eukaryotic protein with the retroviral protease fold
    J Mol Biol364, 376-387. PubMed  Europe PubMed DOI  S
  15. 2005
  16. [YEAR:23-3-2005]Cascella,M., Micheletti,C., Rothlisberger,U. and Carloni,P.
    Evolutionarily conserved functional mechanics across pepsin-like and retroviral aspartic proteases
    J Am Chem Soc127, 3734-3742. PubMed  Europe PubMed DOI
  17. 2004
  18. James,M.N.G.
    Catalytic pathway of aspartic peptidases
    [ISSN:0-12-079610-4]2, 12-19.  V
  19. Rawlings,N.D. and Barrett,A.J.
    Introduction: aspartic peptidases and their clans
    [ISSN:0-12-079610-4]2, 3-12.  V
  20. 2001
  21. Andreeva,N.S. and Rumsh,L.D.
    Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes
    Protein Sci10, 2439-2450. PubMed  Europe PubMed DOI
  22. Northrop,D.B.
    Follow the protons: a low-barrier hydrogen bond unifies the mechanisms of the aspartic proteases
    Acc Chem Res34, 790-797. PubMed  Europe PubMed DOI
  23. [YEAR:4-6-2001]Oh,S., Chang,W. and Suh,J.
    An aspartic protease analogue: intermolecular catalysis of peptide hydrolysis by carboxyl groups
    Bioorg Med Chem Lett11, 1469-1472. PubMed  Europe PubMed DOI
  24. 2000
  25. [YEAR:26-4-2000]Park,H., Suh,J. and Lee,S.
    Ab initio studies on the catalytic mechanism of aspartic proteinases. Nucleophilic versus general acid/general base mechanism
    J Am Chem Soc122, 3901-3908. DOI
  26. 1999
  27. Castillo,R.M., Mizuguchi,K., Dhanaraj,V., Albert,A., Blundell,T.L. and Murzin,A.G.
    A six-stranded double-psi beta barrel is shared by several protein superfamilies
    Structure7, 227-236. PubMed  Europe PubMed DOI
  28. 1991
  29. Rao,J.K., Erickson,J.W. and Wlodawer,A.
    Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases
    Biochemistry30, 4663-4671. PubMed  Europe PubMed
  30. 1990
  31. Rao,J.K.M. and Wlodawer,A.
    Is the pseudo-dyad in retroviral proteinase monomers structural or evolutionary?
    FEBS Lett260, 201-205. PubMed  Europe PubMed
  32. 1989
  33. Miller,M., Jaskolski,M., Rao,J.K., Leis,J. and Wlodawer,A.
    Crystal structure of a retroviral protease proves relationship to aspartic protease family
    Nature337, 576-579. PubMed  Europe PubMed DOI  S
  34. Polgar,L.
    Mechanisms of Protease Action