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Volumn 3, Issue 7, 1995, Pages 681-691

The crystal structure of the catalytic domain of human urokinase-type plasminogen activator

Author keywords

fibrinolysis; inhibitor protein interaction; serine protease; variable regions; X ray crystallography

Indexed keywords

CHYMOTRYPSIN; RECOMBINANT PROTEIN; THROMBIN; UROKINASE;

EID: 0029645121     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(01)00203-9     Document Type: Article
Times cited : (158)

References (57)
  • 2
    • 0025189508 scopus 로고
    • Fibrinolytic properties of single chain urokinase-type plasminogen activator (pro-urokinase)
    • (1990) Fibrinolysis , vol.4 , pp. 1-9
    • de Munk1    Rijken2
  • 6
    • 0028049194 scopus 로고
    • Urokinase-type plasminogen activator and its receptor: new targets for anti-metastatic therapy?
    • 94188973
    • (1994) Trends Pharmacol. Sci , vol.15 , pp. 25-28
    • Fazioli1    Blasi2
  • 8
    • 0027385945 scopus 로고
    • Urokinase-type plasminogen activator and malignancy
    • (1993) Fibrinolysis , vol.7 , pp. 295-302
    • Duffy1
  • 9
    • 0028295979 scopus 로고
    • Physiological consequences of loss of plasminogen activator gene function in mice
    • 94181018
    • (1994) Nature , vol.368 , pp. 419-424
    • Carmeliet1    Mulligan2
  • 14
    • 0027395147 scopus 로고
    • NMR studies of the dynamics of the multidomain protein urokinase-type plasminogen activator
    • 93120108
    • (1993) Biochemistry , vol.32 , pp. 298-309
    • Nowak1    Li2    Teuten3    Smith4    Dobson5
  • 15
    • 0028203899 scopus 로고
    • Unfolding studies of the protease domain of urokinase-type plasminogen activator: the existence of partly folded states and stable sub-domains
    • 94176488
    • (1994) Biochemistry , vol.33 , pp. 2951-2960
    • Nowak1    Cooper2    Saunders3    Smith4    Dobson5
  • 16
    • 0028606835 scopus 로고
    • 15N relaxation studies of the amino-terminal fragment of urokinase-type plasminogen activator
    • 95101635
    • (1994) Biochemistry , vol.33 , pp. 15418-15424
    • Hansen1    Petros2    Meadows3    Fesik4
  • 18
    • 0028292224 scopus 로고
    • Solution structure of the amino-terminal fragment of urokinase-type plasminogen activator
    • 94213863
    • (1994) Biochemistry , vol.33 , pp. 4847-4864
    • Hansen1    Fesik2
  • 19
    • 0024431034 scopus 로고
    • The refined 1.9 å crystal structure of human α- thrombin: interaction with D–Phe–Pro–Arg chloromethylketone and significance of the Tyr–Pro–Pro–Trp insertion segment
    • 90059942
    • (1989) EMBO J , vol.8 , pp. 3467-3475
    • Bode1    Mayr2    Baumann3    Huber4    Stone5    Hofsteenge6
  • 21
    • 0028115937 scopus 로고
    • Structure of human Factor D. A complement system protein at 2.0 å resolution
    • 94118317
    • (1994) J. Mol. Biol , vol.235 , pp. 695-708
    • Narayana1    DeLucus2
  • 23
    • 0021809359 scopus 로고
    • Structure of α-chymotrypsin refined at 1.68 å resolution
    • (1985) J. Mol. Biol , vol.184 , pp. 703-711
    • Tsukada1    Blow2
  • 24
    • 0013815214 scopus 로고
    • Stereochemical criteria for polypeptide and protein chain conformations. II. Allowed conformations for a pair of peptide units
    • (1965) Biophys. J , vol.5 , pp. 909-933
    • Ramakrishnan1    Ramachandran2
  • 26
    • 0019888748 scopus 로고
    • Comparative model-building of the mammalian serine proteases
    • 82216805
    • (1981) J. Mol. Biol , vol.153 , pp. 1027-1042
    • Greer1
  • 27
    • 0025287330 scopus 로고
    • Comparative modelling methods: applications to the family of mammalian serine proteases
    • 90341215
    • (1990) Proteins , vol.7 , pp. 317-334
    • Greer1
  • 28
    • 0025824270 scopus 로고
    • A synthetic DNA encoding a modified human urokinase resistant to inhibition by serum plasminogen activator inhibitor
    • 91217089
    • (1991) J. Biol. Chem , vol.266 , pp. 8476-8482
    • Adams1    Griffin2    Nachajko3    Reddy4    Wei5
  • 30
    • 0015855133 scopus 로고
    • Activation of chymotrypsinogen-A: an hypothesis based upon the comparison of the crystal structures of chymotrypsinogen-A and α-chymotrypsin
    • (1973) J. Mol. Biol , vol.79 , pp. 13-23
    • Wright1
  • 33
    • 0027496219 scopus 로고
    • Converting tissue plasminogen activator to a zymogen: a regulatory triad of Asp–His–Ser
    • 94023983
    • (1993) Science , vol.262 , pp. 419-421
    • Madison1    Kobe2    Gething3    Sambrook4
  • 34
    • 0027050807 scopus 로고
    • The refined 1.9 å X-ray crystal structure of D–Phe–Pro–Arg chloromethylketone-inhibited human α-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships
    • 93278276
    • (1992) Protein Sci , vol.1 , pp. 426-471
    • Bode1    Turk2    Karshikov3
  • 35
    • 0026319199 scopus 로고
    • Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
    • 92100752
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls1    Sharp2    Honig3
  • 36
    • 0016796849 scopus 로고
    • The refined crystal structure of bovine β-trypsin at 1.8 å resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7
    • (1975) J. Mol. Biol , vol.98 , pp. 693-717
    • Bode1    Schwager2
  • 37
    • 0014965504 scopus 로고
    • Three-dimensional structure of tosylelastase
    • (1970) Nature , vol.225 , pp. 811-816
    • Shotton1    Watson2
  • 38
  • 40
    • 0027270445 scopus 로고
    • Mechanism-based inactivators of trypsin-like proteinases. Selective inhibition of urokinase by functionalized cyclopeptides incorporating a bromomethyl-substituted m-aminobenzoic acid residue
    • (1993) J. Med. Chem , vol.36 , pp. 1539-1547
    • Wakselman1    Xie2    Mazaleyrat3
  • 54
    • 0026644421 scopus 로고
    • Urokinase plasminogen activator cleaves its cell surface receptor releasing the ligand-binding domain
    • 92388197
    • (1992) J. Biol. Chem , vol.25 , pp. 18224-18229
    • Hoyer-Hansen1    Dano2
  • 56
    • 0027077443 scopus 로고
    • Extracellular proteolytic cleavage by urokinase is required for activation of hepatocyte growth factor/scatter factor
    • 93099856
    • (1992) EMBO J , vol.11 , pp. 4825-4833
    • Naldini1    Comoglio2
  • 57


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.