Families of zinc metalloproteases
暂无分享,去创建一个
[1] First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases. , 1993 .
[2] J. Frère,et al. Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 Å resolution , 1982, Nature.
[3] A. Bairoch,et al. A unique signature identifies a family of zinc‐dependent metallopeptidases , 1989, FEBS letters.
[4] R. Huber,et al. Refined 1.8 A X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin. , 1994, Journal of molecular biology.
[5] B. Roques,et al. Identification of glutamic acid 646 as a zinc-coordinating residue in endopeptidase-24.11. , 1991, The Journal of biological chemistry.
[6] N. Rawlings,et al. Thimet oligopeptidase: similarity to 'soluble angiotensin II-binding protein' and some corrections to the published amino acid sequence of the rat testis enzyme. , 1993, The Biochemical journal.
[7] D. Drayna,et al. Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. , 1991, The Journal of biological chemistry.
[8] A. Lazdunski,et al. Nucleotide sequence of the pepN gene encoding aminopeptidase N of Escherichia coli. , 1986, Gene.
[9] P. Strøman. Sequence of a gene (lap) encoding a 95.3-kDa aminopeptidase from Lactococcus lactis ssp. cremoris Wg2. , 1992, Gene.
[10] M. Cooper,et al. cDNA cloning and expression of human glutamyl aminopeptidase (aminopeptidase A). , 1993, Genomics.
[11] R. Roth,et al. Identification of glutamate-169 as the third zinc-binding residue in proteinase III, a member of the family of insulin-degrading enzymes. , 1993, The Biochemical journal.
[12] B. Roques,et al. Asp650 is crucial for catalytic activity of neutral endopeptidase 24-11. , 1994, European journal of biochemistry.
[13] S. Clarke,et al. Purification and characterization of a novel metalloendopeptidase from Saccharomyces cerevisiae. , 1993, Biochemistry.
[14] H. Jörnvall,et al. Molecular cloning and amino acid sequence of leukotriene A4 hydrolase. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[15] N. García-Álvarez,et al. Molecular cloning of soluble aminopeptidases from Saccharomyces cerevisiae. Sequence analysis of aminopeptidase yscII, a putative zinc-metallopeptidase. , 1991, European journal of biochemistry.
[16] Peter J. Lamb,et al. Persistence of Subsaharan drought , 1982, Nature.
[17] G. Venemâ,et al. Cloning and sequencing of the gene for a lactococcal endopeptidase, an enzyme with sequence similarity to mammalian enkephalinase , 1993, Journal of bacteriology.
[18] B. Vallee,et al. Short and long spacer sequences and other structural features of zinc binding sites in zinc enzymes , 1989, FEBS letters.
[19] J. Engberg,et al. Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA , 1988, FEBS letters.
[20] U. Klein,et al. Cloning, DNA sequence analysis and partial characterization of pepN, a lysyl aminopeptidase from Lactobacillus delbrückii ssp. lactis DSM7290. , 1993, European journal of biochemistry.
[21] Y. Lee,et al. Extracellular autoprocessing of a metalloprotease from Streptomyces cacaoi. , 1992, The Journal of biological chemistry.
[22] P. Seeburg,et al. Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase) , 1988, FEBS letters.
[23] J. Frère,et al. The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of streptomyces albus G. , 2005, European journal of biochemistry.
[24] N. Rawlings,et al. Evolutionary families of peptidases. , 1993, The Biochemical journal.
[25] K. Chang,et al. Surface acid proteinase (gp63) of Leishmania mexicana. A metalloenzyme capable of protecting liposome-encapsulated proteins from phagolysosomal degradation by macrophages. , 1989, The Journal of biological chemistry.
[26] W. Bode,et al. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc‐binding environments (HEXXHXXGXXH and Met‐turn) and topologies and should be grouped into a common family, the ‘metzincins’ , 1993, FEBS letters.
[27] T. A. Roberts,et al. Sequence of the gene encoding type F neurotoxin of Clostridium botulinum. , 1992, FEMS microbiology letters.
[28] H. Matsubara,et al. Cloning and sequencing of Serratia protease gene. , 1986, Nucleic acids research.
[29] Soohee Lee,et al. Molecular cloning and primary structure of Kell blood group protein. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[30] Weiping Jiang,et al. Families of metalloendopeptidases and their relationships , 1992, FEBS letters.
[31] F. Barras,et al. Cloning of genes encoding extracellular metalloproteases from Erwinia chrysanthemi EC16 , 1990, Journal of bacteriology.
[32] L. Tauc,et al. Minimal essential domains specifying toxicity of the light chains of tetanus toxin and botulinum neurotoxin type A. , 1992, The Journal of biological chemistry.
[33] T. Blundell. Metalloproteinase super–families and drug design , 1994, Nature Structural Biology.
[34] D. Steiner,et al. Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N. , 1989, The Journal of biological chemistry.
[35] William Arbuthnot Sir Lane,et al. Isolation and molecular cloning of mast cell carboxypeptidase A. A novel member of the carboxypeptidase gene family. , 1989, The Journal of biological chemistry.
[36] M. Werner-Washburne,et al. Isolation and characterization of AAP1. A gene encoding an alanine/arginine aminopeptidase in yeast. , 1993, The Journal of biological chemistry.
[37] J. Haeggström,et al. Leukotriene A4 hydrolase: determination of the three zinc-binding ligands by site-directed mutagenesis and zinc analysis. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[38] K. Tanzawa,et al. Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells. , 1994, The Journal of biological chemistry.
[39] F. Soubrier,et al. The testicular transcript of the angiotensin I‐converting enzyme encodes for the ancestral, non‐duplicated form of the enzyme , 1989, FEBS letters.
[40] E. Davie,et al. Rabbit liver microsomal endopeptidase with substrate specificity for processing proproteins is structurally related to rat testes metalloendopeptidase 24.15. , 1993, The Journal of biological chemistry.
[41] P Corvol,et al. Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. , 1988, Proceedings of the National Academy of Sciences of the United States of America.