Literature for family C1

Family

Summary Holotypes Alignment Tree Genomes Structure Literature H-seq M-seq Architecture

C1A

Summary Holotypes Alignment Tree Genomes Literature

C1B

Summary Holotypes Alignment Tree Genomes Literature


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

    2024
  1. Duran,S., Ustuntanir Dede,A.F., Dundar Orhan,Y. and Arslanyolu,M.
    Genome-wide identification and in-silico analysis of papain-family cysteine protease encoding genes in Tetrahymena thermophila
    Eur J Protistol92, 126033-126033. PubMed  Europe PubMed DOI
  2. Xie,Q., Yao,T., Sun,X., Liu,X. and Wang,X.
    Whole genome identification of olive flounder (Paralichthys olivaceus) cathepsin genes: Provides insights into its regulation on biotic and abiotic stresses response
    Aquat Toxicol266, 106783-106783. PubMed  Europe PubMed DOI
  3. 2023
  4. Nicolau,I., Hadade,N.D., Matache,M. and Funeriu,D.P.
    Synthetic Approaches of Epoxysuccinate Chemical Probes
    Chembiocheme202300157-e202300157. PubMed  Europe PubMed DOI  V
  5. 2022
  6. Li,Y., Li,X., Zhang,P., Chen,D., Tao,X., Cao,M., Li,C. and Fu,Q.
    Genome-Wide Identification, Evolutionary Analysis, and Expression Patterns of Cathepsin Superfamily in Black Rockfish (Sebastes schlegelii) following Aeromonas salmonicida Infection
    Mar Drugs20, PubMed  Europe PubMed DOI
  7. Petushkova,A.I., Savvateeva,L.V. and Zamyatnin,A.A., Jr.
    Structure determinants defining the specificity of papain-like cysteine proteases
    Comput Struct Biotechnol J20, 6552-6569. PubMed  Europe PubMed DOI
  8. 2021
  9. Romero,A., Novoa,B. and Figueras,A.
    Genomic and transcriptomic identification of the cathepsin superfamily in the Mediterranean mussel Mytilus galloprovincialis
    Dev Comp Immunol127, 104286-104286. PubMed  Europe PubMed DOI
  10. 2019
  11. Liu,C., Barrett,T.M., Chen,X., Ferrie,J.J. and Petersson,E.J.
    Fluorescent probes for studying thioamide positional effects on proteolysis reveal insight into resistance to cysteine proteases
    Chembiochem20, 2059-2062. PubMed  Europe PubMed DOI  I
  12. Zhang,S., Xu,Z., Sun,H., Sun,L., Shaban,M., Yang,X. and Zhu,L.
    Genome-wide identification of papain-like cysteine proteases in Gossypium hirsutum and functional characterization in response to Verticillium dahliae
    Front Plant Sci10, 134-134. PubMed  Europe PubMed DOI
  13. 2018
  14. Gong,X., Zhao,X., Zhang,W., Wang,J., Chen,X., Hameed,M.F., Zhang,N. and Ge,H.
    Structural characterization of the hypothetical protein Lpg2622, a new member of the C1 family peptidases from Legionella pneumophila
    FEBS Lett592, 2798-2810. PubMed  Europe PubMed DOI
  15. Liu,C.L., Guo,J., Zhang,X., Sukhova,G.K., Libby,P. and Shi,G.P.
    Cysteine protease cathepsins in cardiovascular disease: from basic research to clinical trials
    Nat Rev Cardiol15, 351-370. PubMed  Europe PubMed DOI
  16. Liu,H., Hu,M., Wang,Q., Cheng,L. and Zhang,Z.
    Role of papain-like cysteine proteases in plant development
    Front Plant Sci9, 1717-1717. PubMed  Europe PubMed DOI
  17. 2017
  18. Zou,Z., Xie,G. and Yang,L.
    Papain-like cysteine protease encoding genes in rubber (Hevea brasiliensis): comparative genomics, phylogenetic, and transcriptional profiling analysis
    Planta246, 999-1018. PubMed  Europe PubMed DOI
  19. 2015
  20. Riesgo,A., Maldonado,M., Lopez-Legentil,S. and Giribet,G.
    A proposal for the evolution of cathepsin and silicatein in sponges
    J Mol Evol80, 278-291. PubMed  Europe PubMed DOI
  21. Zhou,J., Zhang,Y.Y., Li,Q.Y. and Cai,Z.H.
    Evolutionary history of cathepsin L (L-like) family genes in vertebrates
    Int J Biol Sci11, 1016-1025. PubMed  Europe PubMed DOI
  22. 2014
  23. Semashko,T.A., Vorotnikova,E.A., Sharikova,V.F., Vinokurov,K.S., Smirnova,Y.A., Dunaevsky,Y.E., Belozersky,M.A., Oppert,B., Elpidina,E.N. and Filippova,I.Y.
    Selective chromogenic and fluorogenic peptide substrates for the assay of cysteine peptidases in complex mixtures
    Anal Biochem449, 179-187. PubMed  Europe PubMed DOI  A
  24. 2013
  25. Novinec,M. and Lenarcic,B.
    Papain-like peptidases: structure, function, and evolution
    Biomol Concepts4, 287-308. PubMed  Europe PubMed DOI
  26. 2008
  27. Mladenovic,M., Fink,R.F., Thiel,W., Schirmeister,T. and Engels,B.
    On the origin of the stabilization of the zwitterionic resting state of cysteine proteases: a theoretical study
    J Am Chem Soc130, 8696-8705. PubMed  Europe PubMed DOI
  28. 2004
  29. Papamichael,E.M., Theodorou,L.G. and Bieth,J.G.
    Insight into catalytic mechanism of papain-like cysteine proteinases: the case of D158
    Appl Biochem Biotechnol118, 171-175. PubMed  Europe PubMed DOI
  30. 2002
  31. Bromme,D. and Kaleta,J.
    Thiol-dependent cathepsins: pathophysiological implications and recent advances in inhibitor design
    Curr Pharm Des8, 1639-1658. PubMed  Europe PubMed DOI  V
  32. Leung-Toung,R., Li,W., Tam,T.F. and Karimian,K.
    Thiol-dependent enzymes and their inhibitors: a review
    Curr Med Chem9, 979-1002. PubMed  Europe PubMed  I
  33. 2000
  34. Brinkworth,R.I., Tort,J.F., Brindley,P.J. and Dalton,J.P.
    Phylogenetic relationships and theoretical model of human cathepsin W (lymphopain), a cysteine proteinase from cytotoxic T lymphocytes
    Int J Biochem Cell Biol32, 373-384. PubMed  Europe PubMed DOI
  35. 1999
  36. McGrath,M.E.
    The lysosomal cysteine proteases
    Annu Rev Biophys Biomol Struct28, 181-204. PubMed  Europe PubMed DOI  S
  37. [YEAR:13-4-1999]Nagler,D.K., Tam,W., Storer,A.C., Krupa,J.C., Mort,J.S. and Menard,R.
    Interdependency of sequence and positional specificities for cysteine proteases of the papain family
    Biochemistry38, 4868-4874. PubMed  Europe PubMed DOI
  38. 1998
  39. [YEAR:26-5-1998]Shimizu,K., Cha,J., Stucky,G.D. and Morse,D.E.
    Silicatein alpha: cathepsin L-like protein in sponge biosilica
    Proc Natl Acad Sci U S A95, 6234-6238. PubMed  Europe PubMed DOI
  40. 1997
  41. Cygler,M. and Mort,J.S.
    Proregion structure of members of the papain superfamily. Mode of inhibition of enzymatic activity
    Biochimie79, 645-652. PubMed  Europe PubMed DOI
  42. Ward,W., Alvarado,L., Rawlings,N.D., Engel,J.C., Franklin,C. and McKerrow,J.H.
    A primitive enzyme for a primitive cell: the protease required for excystation of Giardia
    Cell89, 437-444. PubMed  Europe PubMed DOI
  43. 1996
  44. Storer,A.C. and Menard,R.
    Recent insights into cysteine protease specificity: lessons for drug design
    Perspect Drug Discov Design6, 33-46.
  45. 1995
  46. Berti,P.J. and Storer,A.C.
    Alignment/phylogeny of the papain superfamily of cysteine proteases
    J Mol Biol246, 273-283. PubMed  Europe PubMed DOI
  47. 1994
  48. Storer,A.C. and Menard,R.
    Catalytic mechanism in papain family of cysteine peptidases
    Methods Enzymol244, 486-500. PubMed  Europe PubMed DOI  V
  49. 1991
  50. Keillor,J.W. and Brown,R.S.
    Reaction of a distorted amide with nucleophilic thiolate-containing zwitterions produced from thiolamines. A model for the acylation step in cysteine proteases and transglutaminases
    J Am Chem Soc113, 5114-5116.
  51. 1990
  52. Shaw,E.
    Cysteinyl proteinases and their selective inactivation
    Adv Enzymol Relat Areas Mol Biol63, 271-347. PubMed  Europe PubMed  V  I
  53. 1987
  54. Brocklehurst,K., Willenbrock,F. and Salih,E.
    Cysteine proteinases
    39-158.
  55. 1985
  56. Kamphuis,I.G., Drenth,J. and Baker,E.N.
    Thiol proteases. Comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain
    J Mol Biol182, 317-329. PubMed  Europe PubMed  S
  57. 1982
  58. Barrett,A.J., Kembhavi,A.A., Brown,M.A., Kirschke,H., Knight,C.G., Tamai,M. and Hanada,K.
    L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L
    Biochem J201, 189-198. PubMed  Europe PubMed  I
  59. 1976
  60. Lowe,G.
    The cysteine proteinases
    Tetrahedron32, 291-302.  V